CINXE.COM

<!DOCTYPE html> <html lang="en" dir="ltr"> <head>  <script async src="https://www.googletagmanager.com/gtag/js?id=G-P63WKM1TM1"></script> <script> window.dataLayer = window.dataLayer || []; function gtag(){dataLayer.push(arguments);} gtag('js', new Date()); gtag('config', 'G-P63WKM1TM1'); </script>  <script type="text/javascript" > (function(m,e,t,r,i,k,a){m[i]=m[i]||function(){(m[i].a=m[i].a||[]).push(arguments)}; m[i].l=1*new Date(); for (var j = 0; j < document.scripts.length; j++) {if (document.scripts[j].src === r) { return; }} k=e.createElement(t),a=e.getElementsByTagName(t)[0],k.async=1,k.src=r,a.parentNode.insertBefore(k,a)}) (window, document, "script", "https://mc.yandex.ru/metrika/tag.js", "ym"); ym(55165297, "init", { clickmap:false, trackLinks:true, accurateTrackBounce:true, webvisor:false }); </script> <noscript><div><img src="https://mc.yandex.ru/watch/55165297" style="position:absolute; left:-9999px;" alt="" /></div></noscript>    <title>Search results for: Human C-Cbl proteins</title> <meta name="description" content="Search results for: Human C-Cbl proteins"> <meta name="keywords" content="Human C-Cbl proteins"> <meta name="viewport" content="width=device-width, initial-scale=1, minimum-scale=1, maximum-scale=1, user-scalable=no"> <meta charset="utf-8"> <link href="https://cdn.waset.org/favicon.ico" type="image/x-icon" rel="shortcut icon"> <link href="https://cdn.waset.org/static/plugins/bootstrap-4.2.1/css/bootstrap.min.css" rel="stylesheet"> <link href="https://cdn.waset.org/static/plugins/fontawesome/css/all.min.css" rel="stylesheet"> <link href="https://cdn.waset.org/static/css/site.css?v=150220211555" rel="stylesheet"> </head> <body> <header> <div class="container"> <nav class="navbar navbar-expand-lg navbar-light"> <a class="navbar-brand" href="https://waset.org"> <img src="https://cdn.waset.org/static/images/wasetc.png" alt="Open Science Research Excellence" title="Open Science Research Excellence" /> </a> <button class="d-block d-lg-none navbar-toggler ml-auto" type="button" data-toggle="collapse" data-target="#navbarMenu" aria-controls="navbarMenu" aria-expanded="false" aria-label="Toggle navigation"> <span class="navbar-toggler-icon"></span> </button> <div class="w-100"> <div class="d-none d-lg-flex flex-row-reverse"> <form method="get" action="https://waset.org/search" class="form-inline my-2 my-lg-0"> <input class="form-control mr-sm-2" type="search" placeholder="Search Conferences" value="Human C-Cbl proteins" name="q" aria-label="Search"> <button class="btn btn-light my-2 my-sm-0" type="submit"><i class="fas fa-search"></i></button> </form> </div> <div class="collapse navbar-collapse mt-1" id="navbarMenu"> <ul class="navbar-nav ml-auto align-items-center" id="mainNavMenu"> <li class="nav-item"> <a class="nav-link" href="https://waset.org/conferences" title="Conferences in 2024/2025/2026">Conferences</a> </li> <li class="nav-item"> <a class="nav-link" href="https://waset.org/disciplines" title="Disciplines">Disciplines</a> </li> <li class="nav-item"> <a class="nav-link" href="https://waset.org/committees" rel="nofollow">Committees</a> </li> <li class="nav-item dropdown"> <a class="nav-link dropdown-toggle" href="#" id="navbarDropdownPublications" role="button" data-toggle="dropdown" aria-haspopup="true" aria-expanded="false"> Publications </a> <div class="dropdown-menu" aria-labelledby="navbarDropdownPublications"> <a class="dropdown-item" href="https://publications.waset.org/abstracts">Abstracts</a> <a class="dropdown-item" href="https://publications.waset.org">Periodicals</a> <a class="dropdown-item" href="https://publications.waset.org/archive">Archive</a> </div> </li> <li class="nav-item"> <a class="nav-link" href="https://waset.org/page/support" title="Support">Support</a> </li> </ul> </div> </div> </nav> </div> </header> <main> <div class="container mt-4"> <div class="row"> <div class="col-md-9 mx-auto"> <form method="get" action="https://publications.waset.org/abstracts/search"> <div id="custom-search-input"> <div class="input-group"> <i class="fas fa-search"></i> <input type="text" class="search-query" name="q" placeholder="Author, Title, Abstract, Keywords" value="Human C-Cbl proteins"> <input type="submit" class="btn_search" value="Search"> </div> </div> </form> </div> </div> <div class="row mt-3"> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Commenced</strong> in January 2007</div> </div> </div> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Frequency:</strong> Monthly</div> </div> </div> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Edition:</strong> International</div> </div> </div> <div class="col-sm-3"> <div class="card"> <div class="card-body"><strong>Paper Count:</strong> 9144</div> </div> </div> </div> <h1 class="mt-3 mb-3 text-center" style="font-size:1.6rem;">Search results for: Human C-Cbl proteins</h1> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9144</span> Human C-Cbl and Cbl-b Proteins Are More Highly Expressed in the Thymus Compared to the Testis</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mazo%20Kone">Mazo Kone</a>, <a href="https://publications.waset.org/abstracts/search?q=Rachida%20Salah"> Rachida Salah</a>, <a href="https://publications.waset.org/abstracts/search?q=Harir%20Noria"> Harir Noria</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Background and objectives: c-Cbl and Cbl-b are two members of the Cbl family proteins, with a crucial role of downregulation of tyrosine kinase receptors. They act as E3 ubiquitin ligases and are multivalent adaptor proteins, making them important in maintaining homeostasis in the body. This study investigated the expression level in thymus and testis in normal conditions. Methods: The expression level was assessed by immunochemistry of tissue microarrays of normal thymus and testis biopsies. Results: Cbl-b and c-Cbl proteins were found to be highly expressed in normal testis and thymus, indicated as yellowish brown granules in the cytomembrane and cytoplasm compared to controls. The c-Cbl appears to be more highly expressed than the Cbl-b in the thymus, while c-Cbl appears slightly stronger than Cbl-b in the testis. The thymus was found with a higher grade compared to the testis. Conclusion: In this work we concluded, that in normal condition, thymus tissue expresses more Cbl family proteins(c-Cbl and Cbl-b) than the testis tissue in humans. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Human%20C-Cbl%20proteins" title="Human C-Cbl proteins">Human C-Cbl proteins</a>, <a href="https://publications.waset.org/abstracts/search?q=Human%20Cbl-b%20protein" title=" Human Cbl-b protein"> Human Cbl-b protein</a>, <a href="https://publications.waset.org/abstracts/search?q=Testis" title=" Testis"> Testis</a>, <a href="https://publications.waset.org/abstracts/search?q=Thymus" title=" Thymus"> Thymus</a> </p> <a href="https://publications.waset.org/abstracts/72064/human-c-cbl-and-cbl-b-proteins-are-more-highly-expressed-in-the-thymus-compared-to-the-testis" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/72064.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">233</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9143</span> Prediction and Analysis of Human Transmembrane Transporter Proteins Based on SCM</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Hui-Ling%20Huang">Hui-Ling Huang</a>, <a href="https://publications.waset.org/abstracts/search?q=Tamara%20Vasylenko"> Tamara Vasylenko</a>, <a href="https://publications.waset.org/abstracts/search?q=Phasit%20Charoenkwan"> Phasit Charoenkwan</a>, <a href="https://publications.waset.org/abstracts/search?q=Shih-Hsiang%20Chiu"> Shih-Hsiang Chiu</a>, <a href="https://publications.waset.org/abstracts/search?q=Shinn-Ying%20Ho"> Shinn-Ying Ho</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The knowledge of the human transporters is still limited due to technically demanding procedure of crystallization for the structural characterization of transporters by spectroscopic methods. It is desirable to develop bioinformatics tools for effective analysis of available sequences in order to identify human transmembrane transporter proteins (HMTPs). This study proposes a scoring card method (SCM) based method for predicting HMTPs. We estimated a set of propensity scores of dipeptides to be HMTPs using SCM from the training dataset (HTS732) consisting of 366 HMTPs and 366 non-HMTPs. SCM using the estimated propensity scores of 20 amino acids and 400 dipeptides -as HMTPs, has a training accuracy of 87.63% and a test accuracy of 66.46%. The five top-ranked dipeptides include LD, NV, LI, KY, and MN with scores 996, 992, 989, 987, and 985, respectively. Five amino acids with the highest propensity scores are Ile, Phe, Met, Gly, and Leu, that hydrophobic residues are mostly highly-scored. Furthermore, obtained propensity scores were used to analyze physicochemical properties of human transporters. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=dipeptide%20composition" title="dipeptide composition">dipeptide composition</a>, <a href="https://publications.waset.org/abstracts/search?q=physicochemical%20property" title=" physicochemical property"> physicochemical property</a>, <a href="https://publications.waset.org/abstracts/search?q=human%20transmembrane%20transporter%20proteins" title=" human transmembrane transporter proteins"> human transmembrane transporter proteins</a>, <a href="https://publications.waset.org/abstracts/search?q=human%20transmembrane%20transporters%20binding%20propensity" title=" human transmembrane transporters binding propensity"> human transmembrane transporters binding propensity</a>, <a href="https://publications.waset.org/abstracts/search?q=scoring%20card%20method" title=" scoring card method"> scoring card method</a> </p> <a href="https://publications.waset.org/abstracts/31931/prediction-and-analysis-of-human-transmembrane-transporter-proteins-based-on-scm" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/31931.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">369</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9142</span> Mining the Proteome of Fusobacterium nucleatum for Potential Therapeutics Discovery </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Abdul%20Musaweer%20Habib">Abdul Musaweer Habib</a>, <a href="https://publications.waset.org/abstracts/search?q=Habibul%20Hasan%20Mazumder"> Habibul Hasan Mazumder</a>, <a href="https://publications.waset.org/abstracts/search?q=Saiful%20Islam"> Saiful Islam</a>, <a href="https://publications.waset.org/abstracts/search?q=Sohel%20Sikder"> Sohel Sikder</a>, <a href="https://publications.waset.org/abstracts/search?q=Omar%20Faruk%20Sikder"> Omar Faruk Sikder </a> </p> <p class="card-text"><strong>Abstract:</strong></p> The plethora of genome sequence information of bacteria in recent times has ushered in many novel strategies for antibacterial drug discovery and facilitated medical science to take up the challenge of the increasing resistance of pathogenic bacteria to current antibiotics. In this study, we adopted subtractive genomics approach to analyze the whole genome sequence of the Fusobacterium nucleatum, a human oral pathogen having association with colorectal cancer. Our study divulged 1499 proteins of Fusobacterium nucleatum, which has no homolog in human genome. These proteins were subjected to screening further by using the Database of Essential Genes (DEG) that resulted in the identification of 32 vitally important proteins for the bacterium. Subsequent analysis of the identified pivotal proteins, using the KEGG Automated Annotation Server (KAAS) resulted in sorting 3 key enzymes of F. nucleatum that may be good candidates as potential drug targets, since they are unique for the bacterium and absent in humans. In addition, we have demonstrated the 3-D structure of these three proteins. Finally, determination of ligand binding sites of the key proteins as well as screening for functional inhibitors that best fitted with the ligands sites were conducted to discover effective novel therapeutic compounds against Fusobacterium nucleatum. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=colorectal%20cancer" title="colorectal cancer">colorectal cancer</a>, <a href="https://publications.waset.org/abstracts/search?q=drug%20target" title=" drug target"> drug target</a>, <a href="https://publications.waset.org/abstracts/search?q=Fusobacterium%20nucleatum" title=" Fusobacterium nucleatum"> Fusobacterium nucleatum</a>, <a href="https://publications.waset.org/abstracts/search?q=homology%20modeling" title=" homology modeling"> homology modeling</a>, <a href="https://publications.waset.org/abstracts/search?q=ligands" title=" ligands"> ligands</a> </p> <a href="https://publications.waset.org/abstracts/16273/mining-the-proteome-of-fusobacterium-nucleatum-for-potential-therapeutics-discovery" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/16273.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">388</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9141</span> Cloning, Expression and N-Terminal Pegylation of Human Interferon Alpha-2b Analogs and Their Cytotoxic Evaluation against Cancer Cell Lines</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Syeda%20Kiran%20Shahzadi">Syeda Kiran Shahzadi</a>, <a href="https://publications.waset.org/abstracts/search?q=Nasir%20Mahmood"> Nasir Mahmood</a>, <a href="https://publications.waset.org/abstracts/search?q=Muhammad%20Abdul%20Qadir"> Muhammad Abdul Qadir</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In the current research, three recombinant human interferon alpha-2b proteins (two modified and one normal form) were produced and Pegylated with an aim to produce more effective drugs against viral infections and cancers. The modified recombinant human interferon alpha-2b proteins were produced by site-directed modifications of interferon alpha 2b gene, targeting the amino acids at positions ‘R23’ and ‘H34’. The resulting chemically modified and unmodified forms of human interferon alpha 2b were conjugated with methoxy-polyethylene glycol propanealdehyde (400 KDa) and methoxy-polyethylene glycol succinimidyl succinate (400 KDa). Pegylation of normal and modified forms of Interferon alpha-2b prolong their release time and enhance their efficacy. The conjugation of PEG with modified and unmodified human interferon alpha 2b protein drugs was also characterized with 1H-NMR, HPLC, and SDS-PAGE. Antiproliferative assays of modified and unmodified forms of drugs were performed in cell based bioassays using MDBK cell lines. The results indicated that experimentally produced recombinant human interferon alpha-2b proteins were biologically active and resulted in significant inhibition of cell growth. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=protein%20refolding" title="protein refolding">protein refolding</a>, <a href="https://publications.waset.org/abstracts/search?q=antiproliferative%20activities" title=" antiproliferative activities"> antiproliferative activities</a>, <a href="https://publications.waset.org/abstracts/search?q=biomedical%20applications" title=" biomedical applications"> biomedical applications</a>, <a href="https://publications.waset.org/abstracts/search?q=human%20interferon%20alpha-2b" title=" human interferon alpha-2b"> human interferon alpha-2b</a>, <a href="https://publications.waset.org/abstracts/search?q=pegylation" title=" pegylation"> pegylation</a>, <a href="https://publications.waset.org/abstracts/search?q=mPEG-propionaldehyde" title=" mPEG-propionaldehyde"> mPEG-propionaldehyde</a>, <a href="https://publications.waset.org/abstracts/search?q=site%20directed%20mutagenesis" title=" site directed mutagenesis"> site directed mutagenesis</a>, <a href="https://publications.waset.org/abstracts/search?q=E.%20coli%20expression" title=" E. coli expression"> E. coli expression</a> </p> <a href="https://publications.waset.org/abstracts/83956/cloning-expression-and-n-terminal-pegylation-of-human-interferon-alpha-2b-analogs-and-their-cytotoxic-evaluation-against-cancer-cell-lines" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/83956.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">177</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9140</span> The Effect of Resistance and Progressive Training on Hsp 70 and Glucose</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=F.%20Nameni">F. Nameni</a>, <a href="https://publications.waset.org/abstracts/search?q=H.%20Poursadra"> H. Poursadra</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The present study investigated resistance and progressive training alters the expression of chaperone proteins. These proteins function to maintain homeostasis, facilitate repair from injury, and provide protection. Nineteen training female in 2 groups taking part in the intervention volunteered to give blood samples. Levels of chaperone proteins were measured in response to resistance and progressive training. Hsp 70 levels were increased immediately after 2 h progressive training but decreased after resistance training. The data showed that human skeletal muscle responds to the stress of a single period of progressive training by up-regulating and resistance training by down-regulating expression of HSP70. Physical exercise can elevate core temperature and muscle temperatures and the expression pattern of HSP70 due to training status may be attributed to adaptive mechanisms. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=resistance%20training" title="resistance training">resistance training</a>, <a href="https://publications.waset.org/abstracts/search?q=heat%20shock%20proteins" title=" heat shock proteins"> heat shock proteins</a>, <a href="https://publications.waset.org/abstracts/search?q=leukocytes" title=" leukocytes"> leukocytes</a>, <a href="https://publications.waset.org/abstracts/search?q=Hsp%2070" title=" Hsp 70"> Hsp 70</a> </p> <a href="https://publications.waset.org/abstracts/12855/the-effect-of-resistance-and-progressive-training-on-hsp-70-and-glucose" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/12855.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">458</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9139</span> Identification and Characterization of Nuclear Envelope Protein Interactions</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mohammed%20Hakim%20Jafferali">Mohammed Hakim Jafferali</a>, <a href="https://publications.waset.org/abstracts/search?q=Balaje%20Vijayaraghavan"> Balaje Vijayaraghavan</a>, <a href="https://publications.waset.org/abstracts/search?q=Ricardo%20A.%20Figueroa"> Ricardo A. Figueroa</a>, <a href="https://publications.waset.org/abstracts/search?q=Ellinor%20Crafoord"> Ellinor Crafoord</a>, <a href="https://publications.waset.org/abstracts/search?q=Veronica%20J.%20Larsson"> Veronica J. Larsson</a>, <a href="https://publications.waset.org/abstracts/search?q=Einar%20Hallberg"> Einar Hallberg</a>, <a href="https://publications.waset.org/abstracts/search?q=Santhosh%20Gudise"> Santhosh Gudise </a> </p> <p class="card-text"><strong>Abstract:</strong></p> The nuclear envelope which surrounds the chromatin of eukaryotic cells contains more than a hundred transmembrane proteins. Mutations in some genes encoding nuclear envelope proteins give rise to human diseases including neurological disorders. The function of many nuclear envelope proteins is not well established. This is partly because nuclear envelope proteins and their interactions are difficult to study due to the inherent resistance to extraction of nuclear envelope proteins. We have developed a novel method called MCLIP, to identify interacting partners of nuclear envelope proteins in live cells. Using MCLIP, we found three new binding partners of the inner nuclear membrane protein Samp1: the intermediate filament protein Lamin B1, the LINC complex protein Sun1 and the G-protein Ran. Furthermore, using in vitro studies, we show that Samp1 binds both Emerin and Ran directly. We have also studied the interaction between Samp1 and Ran in detail. The results show that the Samp1 binds stronger to RanGTP than RanGDP. Samp1 is the first transmembrane protein known to bind Ran and it is tempting to speculate that Samp1 may provide local binding sites for RanGTP at membranes. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=MCLIP" title="MCLIP">MCLIP</a>, <a href="https://publications.waset.org/abstracts/search?q=nuclear%20envelope" title=" nuclear envelope"> nuclear envelope</a>, <a href="https://publications.waset.org/abstracts/search?q=ran" title=" ran"> ran</a>, <a href="https://publications.waset.org/abstracts/search?q=Samp1" title=" Samp1"> Samp1</a> </p> <a href="https://publications.waset.org/abstracts/42955/identification-and-characterization-of-nuclear-envelope-protein-interactions" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/42955.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">353</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9138</span> Computational Screening of Secretory Proteins with Brain-Specific Expression in Glioblastoma Multiforme</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sumera">Sumera</a>, <a href="https://publications.waset.org/abstracts/search?q=Sanila%20Amber"> Sanila Amber</a>, <a href="https://publications.waset.org/abstracts/search?q=Fatima%20Javed%20Mirza"> Fatima Javed Mirza</a>, <a href="https://publications.waset.org/abstracts/search?q=Amjad%20Ali"> Amjad Ali</a>, <a href="https://publications.waset.org/abstracts/search?q=Saadia%20Zahid"> Saadia Zahid</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Glioblastoma multiforme (GBM) is a widely spread and fatal primary brain tumor with an increased risk of relapse in spite of aggressive treatment. The current procedures for GBM diagnosis include invasive procedures i.e. resection or biopsy, to acquire tumor mass. Implementation of negligibly invasive tests as a potential diagnostic technique and biofluid-based monitoring of GBM stresses on discovering biomarkers in CSF and blood. Therefore, we performed a comprehensive in silico analysis to identify potential circulating biomarkers for GBM. Initially, six gene and protein databases were utilized to mine brain-specific proteins. The resulting proteins were filtered using a channel of five tools to predict the secretory proteins. Subsequently, the expression profile of the secreted proteins was verified in the brain and blood using two databases. Additional verification of the resulting proteins was done using Plasma Proteome Database (PPD) to confirm their presence in blood. The final set of proteins was searched in literature for their relationship with GBM, keeping a special emphasis on secretome proteome. 2145 proteins were firstly mined as brain-specific, out of which 69 proteins were identified as secretory in nature. Verification of expression profile in brain and blood eliminated 58 proteins from the 69 proteins, providing a final list of 11 proteins. Further verification of these 11 proteins further eliminated 2 proteins, giving a final set of nine secretory proteins i.e. OPCML, NPTX1, LGI1, CNTN2, LY6H, SLIT1, CREG2, GDF1 and SERPINI1. Out of these 9 proteins, 7 were found to be linked to GBM, whereas 2 proteins are not investigated in GBM so far. We propose that these secretory proteins can serve as potential circulating biomarker signatures of GBM and will facilitate the development of minimally invasive diagnostic methods and novel therapeutic interventions for GBM. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=glioblastoma%20multiforme" title="glioblastoma multiforme">glioblastoma multiforme</a>, <a href="https://publications.waset.org/abstracts/search?q=secretory%20proteins" title=" secretory proteins"> secretory proteins</a>, <a href="https://publications.waset.org/abstracts/search?q=brain%20secretome" title=" brain secretome"> brain secretome</a>, <a href="https://publications.waset.org/abstracts/search?q=biomarkers" title=" biomarkers"> biomarkers</a> </p> <a href="https://publications.waset.org/abstracts/144723/computational-screening-of-secretory-proteins-with-brain-specific-expression-in-glioblastoma-multiforme" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/144723.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">152</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9137</span> Computing the Similarity and the Diversity in the Species Based on Cronobacter Genome</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=E.%20Al%20Daoud">E. Al Daoud</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The purpose of computing the similarity and the diversity in the species is to trace the process of evolution and to find the relationship between the species and discover the unique, the special, the common and the universal proteins. The proteins of the whole genome of 40 species are compared with the cronobacter genome which is used as reference genome. More than 3 billion pairwise alignments are performed using blastp. Several findings are introduced in this study, for example, we found 172 proteins in cronobacter genome which have insignificant hits in other species, 116 significant proteins in the all tested species with very high score value and 129 common proteins in the plants but have insignificant hits in mammals, birds, fishes, and insects. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=genome" title="genome">genome</a>, <a href="https://publications.waset.org/abstracts/search?q=species" title=" species"> species</a>, <a href="https://publications.waset.org/abstracts/search?q=blastp" title=" blastp"> blastp</a>, <a href="https://publications.waset.org/abstracts/search?q=conserved%20genes" title=" conserved genes"> conserved genes</a>, <a href="https://publications.waset.org/abstracts/search?q=Cronobacter" title=" Cronobacter"> Cronobacter</a> </p> <a href="https://publications.waset.org/abstracts/82396/computing-the-similarity-and-the-diversity-in-the-species-based-on-cronobacter-genome" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/82396.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">496</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9136</span> Insights of Interaction Studies between HSP-60, HSP-70 Proteins and HSF-1 in Bubalus bubalis</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ravinder%20Singh">Ravinder Singh</a>, <a href="https://publications.waset.org/abstracts/search?q=C%20Rajesh"> C Rajesh</a>, <a href="https://publications.waset.org/abstracts/search?q=Saroj%20Badhan"> Saroj Badhan</a>, <a href="https://publications.waset.org/abstracts/search?q=Shailendra%20Mishra"> Shailendra Mishra</a>, <a href="https://publications.waset.org/abstracts/search?q=Ranjit%20Singh%20Kataria"> Ranjit Singh Kataria</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Heat shock protein 60 and 70 are crucial chaperones that guide appropriate folding of denatured proteins under heat stress conditions. HSP60 and HSP70 provide assistance in correct folding of a multitude of denatured proteins. The heat shock factors are the family of some transcription factors which controls the regulation of gene expression of proteins involved in folding of damaged or improper folded proteins during stress conditions. Under normal condition heat shock proteins bind with HSF-1 and act as its repressor as well as aids in maintaining the HSF-1’s nonactive and monomeric confirmation. The experimental protein structure for all these proteins in Bubalus bubalis is not known till date. Therefore computational approach was explored to identify three-dimensional structure analysis of all these proteins. In this study, an extensive in silico analysis has been performed including sequence comparison among species to comparative modeling of Bubalus bubalis HSP60, HSP70 and HSF-1 protein. The stereochemical properties of proteins were assessed by utilizing several scrutiny bioinformatics tools to ensure model accuracy. Further docking approach was used to study interactions between Heat shock proteins and HSF-1. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Bubalus%20bubalis" title="Bubalus bubalis">Bubalus bubalis</a>, <a href="https://publications.waset.org/abstracts/search?q=comparative%20modelling" title=" comparative modelling"> comparative modelling</a>, <a href="https://publications.waset.org/abstracts/search?q=docking" title=" docking"> docking</a>, <a href="https://publications.waset.org/abstracts/search?q=heat%20shock%20protein" title=" heat shock protein"> heat shock protein</a> </p> <a href="https://publications.waset.org/abstracts/64431/insights-of-interaction-studies-between-hsp-60-hsp-70-proteins-and-hsf-1-in-bubalus-bubalis" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/64431.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">322</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9135</span> Use RP-HPLC To Investigate Factors Influencing Sorghum Protein Extraction</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Khaled%20Khaladi">Khaled Khaladi</a>, <a href="https://publications.waset.org/abstracts/search?q=Rafika%20Bibi"> Rafika Bibi</a>, <a href="https://publications.waset.org/abstracts/search?q=Hind%20Mokrane"> Hind Mokrane</a>, <a href="https://publications.waset.org/abstracts/search?q=Boubekeur%20Nadjemi"> Boubekeur Nadjemi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Sorghum (Sorghum bicolor (L.) Moench) is an important cereal crop grown in the semi-arid tropics of Africa and Asia due to its drought tolerance. Sorghum grain has protein content varying from 6 to 18%, with an average of 11%, Sorghum proteins can be broadly classified into prolamin and non-prolamin proteins. Kafirins, the major storage proteins, are classified as prolamins, and as such, they contain high levels of proline and glutamine and are soluble in non-polar solvents such as aqueous alcohols. Kafirins account for 77 to 82% of the protein in the endosperm, whereas non-prolamin proteins (namely, albumins, globulins, and glutelins) make up about 30% of the proteins. To optimize the extraction of sorghum proteins, several variables were examined: detergent type and concentration, reducing agent type and concentration, and buffer pH and concentration. Samples were quantified and characterized by RP-HPLC. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=sorghum" title="sorghum">sorghum</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20extraction" title=" protein extraction"> protein extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=detergent" title=" detergent"> detergent</a>, <a href="https://publications.waset.org/abstracts/search?q=food%20science" title=" food science "> food science </a> </p> <a href="https://publications.waset.org/abstracts/2669/use-rp-hplc-to-investigate-factors-influencing-sorghum-protein-extraction" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/2669.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">320</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9134</span> Functional Characterization of Transcriptional Regulator WhiB Proteins of Mycobacterium Tuberculosis</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sonam%20Kumari">Sonam Kumari</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis, possesses a remarkable feature of entering into and emerging from a persistent state. The mechanism by which Mtb switches from the dormant state to the replicative form is still poorly characterized. Proteome studies have given us an insight into the role of certain proteins in giving stupendous virulence to Mtb, but numerous dotsremain unconnected and unaccounted. The WhiB family of proteins is one such protein that is associated with developmental processes in actinomycetes.Mtb has seven such proteins (WhiB1 to WhiB7).WhiB proteins are transcriptional regulators; their conserved C-terminal HTH motif is involved in DNA binding. They regulate various essential genes of Mtbby binding to their promoter DNA. Biophysical Analysis of the effect of DNA binding on WhiB proteins has not yet been appropriately characterized. Interaction with DNA induces conformational changes in the WhiB proteins, confirmed by steady-state fluorescence and circular dichroism spectroscopy. ITC has deduced thermodynamic parameters and the binding affinity of the interaction. Since these transcription factors are highly unstable in vitro, their stability and solubility were enhanced by the co-expression of molecular chaperones. The present study findings help determine the conditions under which the WhiB proteins interact with their interacting partner and the factors that influence their binding affinity. This is crucial in understanding their role in regulating gene expression in Mtbandin targeting WhiB proteins as a drug target to cure TB. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=tuberculosis" title="tuberculosis">tuberculosis</a>, <a href="https://publications.waset.org/abstracts/search?q=WhiB%20proteins" title=" WhiB proteins"> WhiB proteins</a>, <a href="https://publications.waset.org/abstracts/search?q=mycobacterium%20tuberculosis" title=" mycobacterium tuberculosis"> mycobacterium tuberculosis</a>, <a href="https://publications.waset.org/abstracts/search?q=nucleic%20acid%20binding" title=" nucleic acid binding"> nucleic acid binding</a> </p> <a href="https://publications.waset.org/abstracts/157126/functional-characterization-of-transcriptional-regulator-whib-proteins-of-mycobacterium-tuberculosis" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/157126.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">104</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9133</span> Proteomics Associated with Colonization of Human Enteric Pathogen on Solanum lycopersicum</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Neha%20Bhadauria">Neha Bhadauria</a>, <a href="https://publications.waset.org/abstracts/search?q=Indu%20Gaur"> Indu Gaur</a>, <a href="https://publications.waset.org/abstracts/search?q=Shilpi%20Shilpi"> Shilpi Shilpi</a>, <a href="https://publications.waset.org/abstracts/search?q=Susmita%20Goswami"> Susmita Goswami</a>, <a href="https://publications.waset.org/abstracts/search?q=Prabir%20K.%20Paul"> Prabir K. Paul</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The aerial surface of plants colonized by Human Enteric Pathogens ()has been implicated in outbreaks of enteric diseases in humans. Practice of organic farming primarily using animal dung as manure and sewage water for irrigation are the most significant source of enteric pathogens on the surface of leaves, fruits and vegetables. The present work aims to have an insight into the molecular mechanism of interaction of Human Enteric Pathogens or their metabolites with cell wall receptors in plants. Tomato plants grown under aseptic conditions at 12 hours L/D photoperiod, 25±1°C and 75% RH were inoculated individually with S. fonticola and K. pneumonia. The leaves from treated plants were sampled after 24 and 48 hours of incubation. The cell wall and cytoplasmic proteins were extracted and isocratically separated on 1D SDS-PAGE. The sampled leaves were also subjected to formaldehyde treatment prior to isolation of cytoplasmic proteins to study protein-protein interactions induced by Human Enteric Pathogens. Protein bands extracted from the gel were subjected to MALDI-TOF-TOF MS analysis. The foremost interaction of Human Enteric Pathogens on the plant surface was found to be cell wall bound receptors which possibly set ups a wave a critical protein-protein interaction in cytoplasm. The study revealed the expression and suppression of specific cytoplasmic and cell wall-bound proteins, some of them being important components of signaling pathways. The results also demonstrated HEP induced rearrangement of signaling pathways which possibly are crucial for adaptation of these pathogens to plant surface. At the end of the study, it can be concluded that controlling the over-expression or suppression of these specific proteins rearrange the signaling pathway thus reduces the outbreaks of food-borne illness. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=cytoplasmic%20protein" title="cytoplasmic protein">cytoplasmic protein</a>, <a href="https://publications.waset.org/abstracts/search?q=cell%20wall-bound%20protein" title=" cell wall-bound protein"> cell wall-bound protein</a>, <a href="https://publications.waset.org/abstracts/search?q=Human%20Enteric%20Pathogen%20%28HEP%29" title=" Human Enteric Pathogen (HEP)"> Human Enteric Pathogen (HEP)</a>, <a href="https://publications.waset.org/abstracts/search?q=protein-protein%20interaction" title=" protein-protein interaction "> protein-protein interaction </a> </p> <a href="https://publications.waset.org/abstracts/60905/proteomics-associated-with-colonization-of-human-enteric-pathogen-on-solanum-lycopersicum" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/60905.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">277</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9132</span> Effects from Maillard Reactions on the Alleginicity of Peanuts</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Khadija%20Radhi">Khadija Radhi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Food allergy is a serious public health problem, especially in developed countries. As one of the most significant allergies, peanut allergy was investigated in this research. Peanut was mixed with treacle under different heating conditions. The results of glycation analyses revealed that proteins from peanuts interacted with the carbohydrates. Further studies also indicated that Millard reactions were determined by different heating treatment. It is noted that denatured peanut proteins accelerated the first stage of Millard reactions but prevented the third one. From the ELISA results, it was found that Millard reactions between proteins with sugars had no effects on the allergenicity of peanuts. Besides, there was no significant difference in allergenicity between digested and non-digested peanut proteins. However, pre-boiled peanut with denatured proteins displayed lower allergenicity after mixing with sugars. Such results indicated that denaturation is the key factor to reduce the allergenicity of the peanut proteins and it seemed that the second-staged Maillard products had less allergenicity. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=allergenicity" title="allergenicity">allergenicity</a>, <a href="https://publications.waset.org/abstracts/search?q=heating%20treatment" title=" heating treatment"> heating treatment</a>, <a href="https://publications.waset.org/abstracts/search?q=peanut" title=" peanut"> peanut</a>, <a href="https://publications.waset.org/abstracts/search?q=Maillard%20reaction" title=" Maillard reaction"> Maillard reaction</a> </p> <a href="https://publications.waset.org/abstracts/18275/effects-from-maillard-reactions-on-the-alleginicity-of-peanuts" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/18275.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">333</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9131</span> Recovery of Value-Added Whey Proteins from Dairy Effluent Using Aqueous Two-Phase System</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Perumalsamy%20Muthiah">Perumalsamy Muthiah</a>, <a href="https://publications.waset.org/abstracts/search?q=Murugesan%20Thanapalan"> Murugesan Thanapalan</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The remains of cheese production contain nutritional value added proteins viz., α-Lactalbumin, β-Lactoglobulin representing 80- 90% of the total volume of milk entering the process. Although several possibilities for cheese-whey exploitation have been assayed, approximately half of world cheese-whey production is not treated but is discarded as effluent. It is necessary to develop an effective and environmentally benign extraction process for the recovery of value added cheese whey proteins. Recently aqueous two phase system (ATPS) have emerged as potential separation process, particularly in the field of biotechnology due to the mild conditions of the process, short processing time, and ease of scale-up. In order to design an ATPS process for the recovery of cheese whey proteins, development of phase diagram and the effect of system parameters such as pH, types and the concentrations of the phase forming components, temperature, etc., on the partitioning of proteins were addressed in order to maximize the recovery of proteins. Some of the practical problems encountered in the application of aqueous two-phase systems for the recovery of Cheese whey proteins were also discussed. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=aqueous%20two-phase%20system" title="aqueous two-phase system">aqueous two-phase system</a>, <a href="https://publications.waset.org/abstracts/search?q=phase%20diagram" title=" phase diagram"> phase diagram</a>, <a href="https://publications.waset.org/abstracts/search?q=extraction" title=" extraction"> extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=cheese%20whey" title=" cheese whey"> cheese whey</a> </p> <a href="https://publications.waset.org/abstracts/71016/recovery-of-value-added-whey-proteins-from-dairy-effluent-using-aqueous-two-phase-system" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/71016.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">410</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9130</span> LGR5 and Downstream Intracellular Signaling Proteins Play Critical Roles in the Cell Proliferation of Neuroblastoma, Meningioma and Pituitary Adenoma</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Jin%20Hwan%20Cheong">Jin Hwan Cheong</a>, <a href="https://publications.waset.org/abstracts/search?q=Mina%20Hwang"> Mina Hwang</a>, <a href="https://publications.waset.org/abstracts/search?q=Myung%20Hoon%20Han"> Myung Hoon Han</a>, <a href="https://publications.waset.org/abstracts/search?q=Je%20Il%20Ryu"> Je Il Ryu</a>, <a href="https://publications.waset.org/abstracts/search?q=Young%20ha%20Oh"> Young ha Oh</a>, <a href="https://publications.waset.org/abstracts/search?q=Seong%20Ho%20Koh"> Seong Ho Koh</a>, <a href="https://publications.waset.org/abstracts/search?q=Wu%20Duck%20Won"> Wu Duck Won</a>, <a href="https://publications.waset.org/abstracts/search?q=Byung%20Jin%20Ha"> Byung Jin Ha</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Leucine-rich repeat-containing G-protein coupled receptor 5 (LGR5) has been reported to play critical roles in the proliferation of various cancer cells. However, the roles of LGR5 in brain tumors and the specific intracellular signaling proteins directly associated with it remain unknown. Expression of LGR5 was first measured in normal brain tissue, meningioma, and pituitary adenoma of humans. To identify the downstream signaling pathways of LGR5, siRNA-mediated knockdown of LGR5 was performed in SH-SY5Y neuroblastoma cells followed by proteomics analysis with 2-dimensional polyacrylamide gel electrophoresis (2D-PAGE). In addition, the expression of LGR5-associated proteins was evaluated in LGR5-inꠓhibited neuroblastoma cells and in human normal brain, meningioma, and pituitary adenoma tissue. Proteomics analysis showed 12 protein spots were significantly different in expression level (more than two-fold change) and subsequently identified by peptide mass fingerprinting. A protein association network was constructed from the 12 identified proteins altered by LGR5 knockdown. Direct and indirect interactions were identified among the 12 proteins. HSP 90-beta was one of the proteins whose expression was altered by LGR5 knockdown. Likewise, we observed decreased expression of proteins in the hnRNP subfamily following LGR5 knockdown. In addition, we have for the first time identified significantly higher hnRNP family expression in meningioma and pituitary adenoma compared to normal brain tissue. Taken together, LGR5 and its downstream sigꠓnaling play critical roles in neuroblastoma and brain tumors such as meningioma and pituitary adenoma. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=LGR5" title="LGR5">LGR5</a>, <a href="https://publications.waset.org/abstracts/search?q=neuroblastoma" title=" neuroblastoma"> neuroblastoma</a>, <a href="https://publications.waset.org/abstracts/search?q=meningioma" title=" meningioma"> meningioma</a>, <a href="https://publications.waset.org/abstracts/search?q=pituitary%20adenoma" title=" pituitary adenoma"> pituitary adenoma</a>, <a href="https://publications.waset.org/abstracts/search?q=hnRNP" title=" hnRNP"> hnRNP</a> </p> <a href="https://publications.waset.org/abstracts/180812/lgr5-and-downstream-intracellular-signaling-proteins-play-critical-roles-in-the-cell-proliferation-of-neuroblastoma-meningioma-and-pituitary-adenoma" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/180812.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">56</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9129</span> Proteomic Analysis of Excretory Secretory Antigen (ESA) from Entamoeba histolytica HM1: IMSS</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=N.%20Othman">N. Othman</a>, <a href="https://publications.waset.org/abstracts/search?q=J.%20Ujang"> J. Ujang</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20N.%20Ismail"> M. N. Ismail</a>, <a href="https://publications.waset.org/abstracts/search?q=R.%20Noordin"> R. Noordin</a>, <a href="https://publications.waset.org/abstracts/search?q=B.%20H.%20Lim"> B. H. Lim</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Amoebiasis is caused by the Entamoeba histolytica and still endemic in many parts of the tropical region, worldwide. Currently, there is no available vaccine against amoebiasis. Hence, there is an urgent need to develop a vaccine. The excretory secretory antigen (ESA) of E. histolytica is a suitable biomarker for the vaccine candidate since it can modulate the host immune response. Hence, the objective of this study is to identify the proteome of the ESA towards finding suitable biomarker for the vaccine candidate. The non-gel based and gel-based proteomics analyses were performed to identify proteins. Two kinds of mass spectrometry with different ionization systems were utilized i.e. LC-MS/MS (ESI) and MALDI-TOF/TOF. Then, the functional proteins classification analysis was performed using PANTHER software. Combination of the LC -MS/MS for the non-gel based and MALDI-TOF/TOF for the gel-based approaches identified a total of 273 proteins from the ESA. Both systems identified 29 similar proteins whereby 239 and 5 more proteins were identified by LC-MS/MS and MALDI-TOF/TOF, respectively. Functional classification analysis showed the majority of proteins involved in the metabolic process (24%), primary metabolic process (19%) and protein metabolic process (10%). Thus, this study has revealed the proteome the E. histolytica ESA and the identified proteins merit further investigations as a vaccine candidate. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=E.%20histolytica" title="E. histolytica">E. histolytica</a>, <a href="https://publications.waset.org/abstracts/search?q=ESA" title=" ESA"> ESA</a>, <a href="https://publications.waset.org/abstracts/search?q=proteomics" title=" proteomics"> proteomics</a>, <a href="https://publications.waset.org/abstracts/search?q=biomarker" title=" biomarker "> biomarker </a> </p> <a href="https://publications.waset.org/abstracts/34707/proteomic-analysis-of-excretory-secretory-antigen-esa-from-entamoeba-histolytica-hm1-imss" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/34707.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">343</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9128</span> A Greener Approach for the Recovery of Proteins from Meat Industries</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Jesus%20Hernandez">Jesus Hernandez</a>, <a href="https://publications.waset.org/abstracts/search?q=Zead%20Elzoeiry"> Zead Elzoeiry</a>, <a href="https://publications.waset.org/abstracts/search?q=Md.%20S.%20Islam"> Md. S. Islam</a>, <a href="https://publications.waset.org/abstracts/search?q=Abel%20E.%20Navarro"> Abel E. Navarro</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The adsorption of bovine serum albumin (BSA) and human hemoglobin (Hb) on naturally-occurring adsorbents was studied to evaluate the potential recovery of proteins from meat industry residues. Spent peppermint tea (PM), powdered purple corn cob (PC), natural clay (NC) and chemically-modified clay (MC) were investigated to elucidate the effects of pH, adsorbent dose, initial protein concentration, presence of salts and heavy metals. Equilibrium data were fitted according to isotherm models, reporting a maximum adsorption capacity at pH 8 of 318 and 344 mg BSA/g of PM and NC, respectively. Moreover, Hb displayed maximum adsorption capacity at pH 5 of 125 and 143 mg/g of PM and PC, respectively. Hofmeister salt effect was only observed for PM/Hb system. Salts tend to decrease protein adsorption, and the presence of Cu(II) ions had negligible impacts on the adsorption onto NC and PC. Desorption experiments confirmed that more than 85% of both proteins can be recovered with diluted acids and bases. SEM, EDX, and TGA analyses demonstrated that the adsorbents have favorable morphological and mechanical properties. The long-term goal of this study aims to recover soluble proteins from industrial wastewaters to produce animal food or any protein-based product. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=adsorption" title="adsorption">adsorption</a>, <a href="https://publications.waset.org/abstracts/search?q=albumin" title=" albumin"> albumin</a>, <a href="https://publications.waset.org/abstracts/search?q=clay" title=" clay"> clay</a>, <a href="https://publications.waset.org/abstracts/search?q=hemoglobin" title=" hemoglobin"> hemoglobin</a>, <a href="https://publications.waset.org/abstracts/search?q=spent%20peppermint%20leaf" title=" spent peppermint leaf"> spent peppermint leaf</a> </p> <a href="https://publications.waset.org/abstracts/113481/a-greener-approach-for-the-recovery-of-proteins-from-meat-industries" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/113481.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">103</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9127</span> An Insight into the Interaction Study of a WhiB Protein and its Binding Partner</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sonam%20Kumari">Sonam Kumari</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Tuberculosis is the deadliest disease worldwide. Millions of people lose their lives every year due to this disease. It has turned lethal due to the erratic nature of its causative organism, Mycobacterium tuberculosis (Mtb). Mtb tends to enter into an inactive, dormant state and emerge to replicating state upon encountering favorable conditions. The mechanism by which Mtb switches from the dormant state to the replicative form is still poorly characterized. Proteome studies have given us an insight into the role of certain proteins in giving stupendous virulence to Mtb, but numerous dotsremain unconnected and unaccounted. The WhiB family of proteins is one such protein that is associated with developmental processes in actinomycetes. Mtb has seven such proteins (WhiB1 to WhiB7). WhiB proteins are transcriptional regulators; they regulate various essential genes of Mtbby binding to their promoter DNA. Biophysical parameters of the effect of DNA binding on WhiB proteins has not yet been appropriately characterized. Interaction with DNA induces conformational changes in the WhiB proteins, confirmed by steady-state fluorescence and circular dichroism spectroscopy. ITC has deduced thermodynamic parameters and the binding affinity of the interaction. Since these transcription factors are highly unstable in vitro, their stability and solubility were enhanced by the co-expression of molecular chaperones. The present study findings help determine the conditions under which the WhiB proteins interact with their interacting partner and the factors that influence their binding affinity. This is crucial in understanding their role in regulating gene expression in Mtbandin targeting WhiB proteins as a drug target to cure TB. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=mycobacterium%20tuberculosis" title="mycobacterium tuberculosis">mycobacterium tuberculosis</a>, <a href="https://publications.waset.org/abstracts/search?q=TB" title=" TB"> TB</a>, <a href="https://publications.waset.org/abstracts/search?q=whiB%20proteins" title=" whiB proteins"> whiB proteins</a>, <a href="https://publications.waset.org/abstracts/search?q=ITC" title=" ITC"> ITC</a> </p> <a href="https://publications.waset.org/abstracts/157140/an-insight-into-the-interaction-study-of-a-whib-protein-and-its-binding-partner" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/157140.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">97</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9126</span> CAP-Glycine Protein Governs Growth, Differentiation, and the Pathogenicity of Global Meningoencephalitis Fungi</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Kyung-Tae%20Lee">Kyung-Tae Lee</a>, <a href="https://publications.waset.org/abstracts/search?q=Li%20Li%20Wang"> Li Li Wang</a>, <a href="https://publications.waset.org/abstracts/search?q=Kwang-Woo%20Jung"> Kwang-Woo Jung</a>, <a href="https://publications.waset.org/abstracts/search?q=Yong-Sun%20Bahn"> Yong-Sun Bahn</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Microtubules are involved in mechanical support, cytoplasmic organization as well as in a number of cellular processes by interacting with diverse microtubule-associated proteins (MAPs), such as plus-end tracking proteins, motor proteins, and tubulin-folding cofactors. A common feature of these proteins is the presence of a cytoskeleton-associated protein-glycine-rich (CAP-Gly) domain, which is evolutionarily conserved and generally considered to bind to α-tubulin to regulate functions of microtubules. However, there has been a dearth of research on CAP-Gly proteins in fungal pathogens, including Cryptococcus neoformans, which causes fatal meningoencephalitis globally. In this study, we identified five CAP-Gly proteins encoding genes in C. neoformans. Among these, Cgp1, encoded by CNAG_06352, has a unique domain structure that has not been reported before in other eukaryotes. Supporting the role of Cpg1 in microtubule-related functions, we demonstrate that deletion or overexpression of CGP1 alters cellular susceptibility to thiabendazole, a microtubule destabilizer, and Cgp1 is co-localized with cytoplasmic microtubules. Related to the cellular functions of microtubules, Cgp1 also governs maintenance of membrane stability and genotoxic stress responses. Furthermore, we demonstrate that Cgp1 uniquely regulates sexual differentiation of C. neoformans with distinct roles in the early and late stage of mating. Our domain analysis reveals that the CAP-Gly domain plays major roles in all the functions of Cgp1. Finally, the cgp1Δ mutant is attenuated in virulence. In conclusion, this novel CAP-Gly protein, Cgp1, has pleotropic roles in regulating growth, stress responses, differentiation and pathogenicity of C. neoformans. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=human%20fungal%20pathogen" title="human fungal pathogen">human fungal pathogen</a>, <a href="https://publications.waset.org/abstracts/search?q=CAP-Glycine%20protein" title=" CAP-Glycine protein"> CAP-Glycine protein</a>, <a href="https://publications.waset.org/abstracts/search?q=microtubule" title=" microtubule"> microtubule</a>, <a href="https://publications.waset.org/abstracts/search?q=meningoencephalitis" title=" meningoencephalitis"> meningoencephalitis</a> </p> <a href="https://publications.waset.org/abstracts/63213/cap-glycine-protein-governs-growth-differentiation-and-the-pathogenicity-of-global-meningoencephalitis-fungi" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/63213.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">315</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9125</span> Mechanical Properties of Young and Senescence Fibroblast Cells Using Passive Microrheology</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Samira%20Khalaji">Samira Khalaji</a>, <a href="https://publications.waset.org/abstracts/search?q="> </a>, <a href="https://publications.waset.org/abstracts/search?q=Fenneke%20Klein%20Jan"> Fenneke Klein Jan</a>, <a href="https://publications.waset.org/abstracts/search?q=Kay-E.%20Gottschalk"> Kay-E. Gottschalk</a>, <a href="https://publications.waset.org/abstracts/search?q=Eugenia%20Makrantonaki"> Eugenia Makrantonaki</a>, <a href="https://publications.waset.org/abstracts/search?q=Karin%20Scharffetter-Kochanek"> Karin Scharffetter-Kochanek </a> </p> <p class="card-text"><strong>Abstract:</strong></p> Biological aging is a multi-dimensional process that takes place over a whole range of scales from the nanoscopic alterations within individual cells, over transformations in tissues and organs and to changes of the whole organism. On the single cell level, aging involves mutation of genes, differences in gene expression levels as well as altered posttranslational modifications of proteins. A variety of proteins is affected, including proteins of the cell cytoskeleton and migration machinery. Previous work quantified the expression of cytoskeleton proteins on the gene and protein levels in senescent and young fibroblasts. Their results show that senescent skin fibroblasts have an upregulated expression of the intermediate filament (IF) protein vimentin in contrast to actin and tubulin, which are downregulated. IFs play an important role in providing mechanical stability of cells. However, the mechanical properties of IFs depending on cellular senescence or age of the donor has not been studied so far. Hence, we employed passive microrheology on primary human dermal fibroblasts from female donors with age of 28 years (young) and 86 years (old) as model of in vivo aging and human normal dermal fibroblast from 11-year old male with CPD 17-35 (young) and CPD 58-59 (senescence) as a model of in vitro replicative senescence. In contrast to the expectations, our primary results show no significant differences in the viscoelastic properties of fibroblasts depending on age of the donor or cellular replicative senescence. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=aging" title="aging">aging</a>, <a href="https://publications.waset.org/abstracts/search?q=cytoskeleton" title=" cytoskeleton"> cytoskeleton</a>, <a href="https://publications.waset.org/abstracts/search?q=fibroblast" title=" fibroblast"> fibroblast</a>, <a href="https://publications.waset.org/abstracts/search?q=mechanical%20properties" title=" mechanical properties"> mechanical properties</a> </p> <a href="https://publications.waset.org/abstracts/46654/mechanical-properties-of-young-and-senescence-fibroblast-cells-using-passive-microrheology" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/46654.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">320</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9124</span> Manipulating The PAAR Proteins of Acinetobacter Baumannii</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Irene%20Alevizos">Irene Alevizos</a>, <a href="https://publications.waset.org/abstracts/search?q=Jessica%20Lewis"> Jessica Lewis</a>, <a href="https://publications.waset.org/abstracts/search?q=Marina%20Harper"> Marina Harper</a>, <a href="https://publications.waset.org/abstracts/search?q=John%20Boyce"> John Boyce</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Acinetobacter baumannii causes a range of severe nosocomial-acquired infections, and many strains are multi-drug resistant. A. baumannii possesses survival mechanisms allowing it to thrive in competitive polymicrobial environments, including a Type VI Secretion System (T6SS) that injects effector proteins into other bacteria to give a competitive advantage. The effects of T6SS firing are broad and depend entirely on the effector that is delivered. Effects can include toxicity against prokaryotic or eukaryotic cells and the acquisition of essential nutrients. The T6SS of some species can deliver ‘specialised effectors’ that are fused directly to T6SS components, such as PAAR proteins. PAAR proteins are predicted to form the piercing tip of the T6SS and are essential for T6SS function. Although no specialised effectors have been identified in A. baumannii, many strains encode multiple PAAR proteins. Analysis of PAAR proteins across the species identified 12 families of PAAR proteins with distinct C-terminal extensions. A. baumannii AB307-0294 encodes two PAAR proteins, one of which has a C-terminal extension. Mutation of one or both of the PAAR-encoding genes in this strain showed that expression of either PAAR protein was sufficient for T6SS function. We employed a heterologous expression approach and determined that PAAR proteins from different A. baumannii strains, as well as the closely related A. baylyi species, could complement the A. baumannii ∆paar mutant and restore T6SS function. Furthermore, we showed that PAAR fusions could be used to deliver artificially cloned protein fragments by generating Histidine- and Streptavidin- tagged PAAR specialised effectors, which restored T6SS activity. This provides evidence that the fusion of protein fragments onto PAAR proteins in A. baumannii is compatible with a functional T6SS. Successful delivery by this mechanism extends the scope of what the T6SS can deliver, including user designed proteins. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=A.%20baumannii" title="A. baumannii">A. baumannii</a>, <a href="https://publications.waset.org/abstracts/search?q=effectors" title=" effectors"> effectors</a>, <a href="https://publications.waset.org/abstracts/search?q=PAAR" title=" PAAR"> PAAR</a>, <a href="https://publications.waset.org/abstracts/search?q=T6SS" title=" T6SS"> T6SS</a> </p> <a href="https://publications.waset.org/abstracts/175739/manipulating-the-paar-proteins-of-acinetobacter-baumannii" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/175739.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">97</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9123</span> Role of ABC Transporters in Non-Target Site Herbicide Resistance in Black Grass (Alopecurus myosuroides)</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Alina%20Goldberg%20Cavalleri">Alina Goldberg Cavalleri</a>, <a href="https://publications.waset.org/abstracts/search?q=Sara%20Franco%20Ortega"> Sara Franco Ortega</a>, <a href="https://publications.waset.org/abstracts/search?q=Nawaporn%20Onkokesung"> Nawaporn Onkokesung</a>, <a href="https://publications.waset.org/abstracts/search?q=Richard%20Dale"> Richard Dale</a>, <a href="https://publications.waset.org/abstracts/search?q=Melissa%20Brazier-Hicks"> Melissa Brazier-Hicks</a>, <a href="https://publications.waset.org/abstracts/search?q=Robert%20%20Edwards"> Robert Edwards</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Non-target site based resistance (NTSR) to herbicides in weeds is a polygenic trait associated with the upregulation of proteins involved in xenobiotic detoxification and translocation we have termed the xenome. Among the xenome proteins, ABC transporters play a key role in enhancing herbicide metabolism by effluxing conjugated xenobiotics from the cytoplasm into the vacuole. The importance of ABC transporters is emphasized by the fact that they often contribute to multidrug resistance in human cells and antibiotic resistance in bacteria. They also play a key role in insecticide resistance in major vectors of human diseases and crop pests. By surveying available databases, transcripts encoding ABCs have been identified as being enhanced in populations exhibiting NTSR in several weed species. Based on a transcriptomics data in black grass (Alopecurus myosuroides, Am), we have identified three proteins from the ABC-C subfamily that are upregulated in NTSR populations. ABC-C transporters are poorly characterized proteins in plants, but in Arabidopsis localize to the vacuolar membrane and have functional roles in transporting glutathionylated (GSH)-xenobiotic conjugates. We found that the up-regulation of AmABCs strongly correlates with the up-regulation of a glutathione transferase termed AmGSTU2, which can conjugate GSH to herbicides. The expression profile of the ABC transcripts was profiled in populations of black grass showing different degree of resistance to herbicides. This, together with a phylogenetic analysis, revealed that AmABCs cluster in different groups which might indicate different substrate and roles in the herbicide resistance phenotype in the different populations <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=black%20grass" title="black grass">black grass</a>, <a href="https://publications.waset.org/abstracts/search?q=herbicide" title=" herbicide"> herbicide</a>, <a href="https://publications.waset.org/abstracts/search?q=resistance" title=" resistance"> resistance</a>, <a href="https://publications.waset.org/abstracts/search?q=transporters" title=" transporters "> transporters </a> </p> <a href="https://publications.waset.org/abstracts/124743/role-of-abc-transporters-in-non-target-site-herbicide-resistance-in-black-grass-alopecurus-myosuroides" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/124743.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">156</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9122</span> Extracellular Protein Secreted by Bacillus subtilis ATCC21332 in the Presence of Streptomycin Sulfate</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=M.%20N.%20Hanina">M. N. Hanina</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20Hairul%20Shahril"> M. Hairul Shahril</a>, <a href="https://publications.waset.org/abstracts/search?q=I.%20Ismatul%20Nurul%20Asyikin"> I. Ismatul Nurul Asyikin</a>, <a href="https://publications.waset.org/abstracts/search?q=A.%20K.%20Abdul%20Jalil"> A. K. Abdul Jalil</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20R.%20Salina"> M. R. Salina</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20R.%20Maryam"> M. R. Maryam</a>, <a href="https://publications.waset.org/abstracts/search?q=M.%20Rosfarizan"> M. Rosfarizan</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The extracellular proteins secreted by bacteria may be increased in stressful surroundings, such as in the presence of antibiotics. It appears that many antibiotics, when used at low concentrations, have in common the ability to activate or repress gene transcription, which is distinct from their inhibitory effect. There have been comparatively few studies on the potential of antibiotics as a specific chemical signal that can trigger a variety of biological functions. Therefore, this study was carried out to determine the effect of Streptomycin Sulfate in regulating extracellular proteins secreted by Bacillus subtilis ATCC21332. Results of Microdilution assay showed that the Minimum Inhibition Concentration (MIC) of Streptomycin Sulfate on B. subtilis ATCC21332 was 2.5 mg/ml. The bacteria cells were then exposed to Streptomycin Sulfate at concentration of 0.01 MIC before being further incubated for 48h to 72 h. The extracellular proteins secreted were then isolated and analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Proteins profile revealed that three additional bands with approximate sizes of 30 kDa, 22 kDa and 23 kDa were appeared for the treated bacteria with Streptomycin Sulfate. Thus, B. subtilis ATCC21332 in stressful condition with the presence of Streptomycin Sulfate at low concentration could induce the extracellular proteins secretion. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Bacillus%20subtilis%20ATCC21332" title="Bacillus subtilis ATCC21332">Bacillus subtilis ATCC21332</a>, <a href="https://publications.waset.org/abstracts/search?q=streptomycin%20sulfate" title=" streptomycin sulfate"> streptomycin sulfate</a>, <a href="https://publications.waset.org/abstracts/search?q=extracellular%20proteins" title=" extracellular proteins"> extracellular proteins</a>, <a href="https://publications.waset.org/abstracts/search?q=antibiotics" title=" antibiotics"> antibiotics</a> </p> <a href="https://publications.waset.org/abstracts/11187/extracellular-protein-secreted-by-bacillus-subtilis-atcc21332-in-the-presence-of-streptomycin-sulfate" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/11187.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">284</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9121</span> Characterization of Transmembrane Proteins with Five Alpha-Helical Regions</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Misty%20Attwood">Misty Attwood</a>, <a href="https://publications.waset.org/abstracts/search?q=Helgi%20Schioth"> Helgi Schioth</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Transmembrane proteins are important components in many essential cell processes such as signal transduction, cell-cell signalling, transport of solutes, structural adhesion activities, and protein trafficking. Due to their involvement in diverse critical activities, transmembrane proteins are implicated in different disease pathways and hence are the focus of intense interest in understanding functional activities, their pathogenesis in disease, and their potential as pharmaceutical targets. Further, as the structure and function of proteins are correlated, investigating a group of proteins with the same tertiary structure, i.e., the same number of transmembrane regions, may give understanding about their functional roles and potential as therapeutic targets. In this in silico bioinformatics analysis, we identify and comprehensively characterize the previously unstudied group of proteins with five transmembrane-spanning regions (5TM). We classify nearly 60 5TM proteins in which 31 are members of ten families that contain two or more family members and all members are predicted to contain the 5TM architecture. Furthermore, nine singlet proteins that contain the 5TM architecture without paralogues detected in humans were also identifying, indicating the evolution of single unique proteins with the 5TM structure. Interestingly, more than half of these proteins function in localization activities through movement or tethering of cell components and more than one-third are involved in transport activities, particularly in the mitochondria. Surprisingly, no receptor activity was identified within this family in sharp contrast with other TM families. Three major 5TM families were identified and include the Tweety family, which are pore-forming subunits of the swelling-dependent volume regulated anion channel in astrocytes; the sidoreflexin family that acts as mitochondrial amino acid transporters; and the Yip1 domain family engaged in vesicle budding and intra-Golgi transport. About 30% of the proteins have enhanced expression in the brain, liver, or testis. Importantly, 60% of these proteins are identified as cancer prognostic markers, where they are associated with clinical outcomes of various tumour types, indicating further investigation into the function and expression of these proteins is important. This study provides the first comprehensive analysis of proteins with 5TM regions and provides details of the unique characteristics and application in pharmaceutical development. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=5TM" title="5TM">5TM</a>, <a href="https://publications.waset.org/abstracts/search?q=cancer%20prognostic%20marker" title=" cancer prognostic marker"> cancer prognostic marker</a>, <a href="https://publications.waset.org/abstracts/search?q=drug%20targets" title=" drug targets"> drug targets</a>, <a href="https://publications.waset.org/abstracts/search?q=transmembrane%20protein" title=" transmembrane protein"> transmembrane protein</a> </p> <a href="https://publications.waset.org/abstracts/125485/characterization-of-transmembrane-proteins-with-five-alpha-helical-regions" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/125485.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">111</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9120</span> A Novel Epitope Prediction for Vaccine Designing against Ebola Viral Envelope Proteins</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Manju%20Kanu">Manju Kanu</a>, <a href="https://publications.waset.org/abstracts/search?q=Subrata%20Sinha"> Subrata Sinha</a>, <a href="https://publications.waset.org/abstracts/search?q=Surabhi%20Johari"> Surabhi Johari</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Viral proteins of Ebola viruses belong to one of the best studied viruses; however no effective prevention against EBOV has been developed. Epitope-based vaccines provide a new strategy for prophylactic and therapeutic application of pathogen-specific immunity. A critical requirement of this strategy is the identification and selection of T-cell epitopes that act as vaccine targets. This study describes current methodologies for the selection process, with Ebola virus as a model system. Hence great challenge in the field of ebola virus research is to design universal vaccine. A combination of publicly available bioinformatics algorithms and computational tools are used to screen and select antigen sequences as potential T-cell epitopes of supertypes Human Leukocyte Antigen (HLA) alleles. MUSCLE and MOTIF tools were used to find out most conserved peptide sequences of viral proteins. Immunoinformatics tools were used for prediction of immunogenic peptides of viral proteins in zaire strains of Ebola virus. Putative epitopes for viral proteins (VP) were predicted from conserved peptide sequences of VP. Three tools NetCTL 1.2, BIMAS and Syfpeithi were used to predict the Class I putative epitopes while three tools, ProPred, IEDB-SMM-align and NetMHCII 2.2 were used to predict the Class II putative epitopes. B cell epitopes were predicted by BCPREDS 1.0. Immunogenic peptides were identified and selected manually by putative epitopes predicted from online tools individually for both MHC classes. Finally sequences of predicted peptides for both MHC classes were looked for common region which was selected as common immunogenic peptide. The immunogenic peptides were found for viral proteins of Ebola virus: epitopes FLESGAVKY, SSLAKHGEY. These predicted peptides could be promising candidates to be used as target for vaccine design. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=epitope" title="epitope">epitope</a>, <a href="https://publications.waset.org/abstracts/search?q=b%20cell" title=" b cell"> b cell</a>, <a href="https://publications.waset.org/abstracts/search?q=immunogenicity" title=" immunogenicity"> immunogenicity</a>, <a href="https://publications.waset.org/abstracts/search?q=ebola" title=" ebola"> ebola</a> </p> <a href="https://publications.waset.org/abstracts/36701/a-novel-epitope-prediction-for-vaccine-designing-against-ebola-viral-envelope-proteins" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/36701.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">314</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9119</span> Human LACE1 Functions Pro-Apoptotic and Interacts with Mitochondrial YME1L Protease</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Lukas%20Stiburek">Lukas Stiburek</a>, <a href="https://publications.waset.org/abstracts/search?q=Jana%20Cesnekova"> Jana Cesnekova</a>, <a href="https://publications.waset.org/abstracts/search?q=Josef%20Houstek"> Josef Houstek</a>, <a href="https://publications.waset.org/abstracts/search?q=Jiri%20Zeman"> Jiri Zeman</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Cellular function depends on mitochondrial function and integrity that is therefore maintained by several classes of proteins possessing chaperone and/or proteolytic activities. In this work, we focused on characterization of LACE1 (lactation elevated 1) function in mitochondrial protein homeostasis maintenance. LACE1 is the human homologue of yeast mitochondrial Afg1 ATPase, a member of SEC18-NSF, PAS1, CDC48-VCP, TBP family. Yeast Afg1 was shown to be involved in mitochondrial complex IV biogenesis, and based on its similarity with CDC48 (p97/VCP) it was suggested to facilitate extraction of polytopic membrane proteins. Here we show that LACE1, which is a mitochondrial integral membrane protein, exists as part of three complexes of approx. 140, 400 and 500 kDa and is essential for maintenance of fused mitochondrial reticulum and lamellar cristae morphology. Using affinity purification of LACE1-FLAG expressed in LACE1 knockdown background we show that the protein physically interacts with mitochondrial inner membrane protease YME1L. We further show that human LACE1 exhibits significant pro-apoptotic activity and that the protein is required for normal function of the mitochondrial respiratory chain. Thus, our work establishes LACE1 as a novel factor with the crucial role in mitochondrial homeostasis maintenance. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=LACE1" title="LACE1">LACE1</a>, <a href="https://publications.waset.org/abstracts/search?q=mitochondria" title=" mitochondria"> mitochondria</a>, <a href="https://publications.waset.org/abstracts/search?q=apoptosis" title=" apoptosis"> apoptosis</a>, <a href="https://publications.waset.org/abstracts/search?q=protease" title=" protease"> protease</a> </p> <a href="https://publications.waset.org/abstracts/46195/human-lace1-functions-pro-apoptotic-and-interacts-with-mitochondrial-yme1l-protease" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/46195.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">313</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9118</span> Deleterious SNP’s Detection Using Machine Learning</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Hamza%20Zidoum">Hamza Zidoum</a> </p> <p class="card-text"><strong>Abstract:</strong></p> This paper investigates the impact of human genetic variation on the function of human proteins using machine-learning algorithms. Single-Nucleotide Polymorphism represents the most common form of human genome variation. We focus on the single amino-acid polymorphism located in the coding region as they can affect the protein function leading to pathologic phenotypic change. We use several supervised Machine Learning methods to identify structural properties correlated with increased risk of the missense mutation being damaging. SVM associated with Principal Component Analysis give the best performance. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=single-nucleotide%20polymorphism" title="single-nucleotide polymorphism">single-nucleotide polymorphism</a>, <a href="https://publications.waset.org/abstracts/search?q=machine%20learning" title=" machine learning"> machine learning</a>, <a href="https://publications.waset.org/abstracts/search?q=feature%20selection" title=" feature selection"> feature selection</a>, <a href="https://publications.waset.org/abstracts/search?q=SVM" title=" SVM"> SVM</a> </p> <a href="https://publications.waset.org/abstracts/45046/deleterious-snps-detection-using-machine-learning" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/45046.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">378</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9117</span> Improved 3D Structure Prediction of Beta-Barrel Membrane Proteins by Using Evolutionary Coupling Constraints, Reduced State Space and an Empirical Potential Function</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Wei%20Tian">Wei Tian</a>, <a href="https://publications.waset.org/abstracts/search?q=Jie%20Liang"> Jie Liang</a>, <a href="https://publications.waset.org/abstracts/search?q=Hammad%20Naveed"> Hammad Naveed</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Beta-barrel membrane proteins are found in the outer membrane of gram-negative bacteria, mitochondria, and chloroplasts. They carry out diverse biological functions, including pore formation, membrane anchoring, enzyme activity, and bacterial virulence. In addition, beta-barrel membrane proteins increasingly serve as scaffolds for bacterial surface display and nanopore-based DNA sequencing. Due to difficulties in experimental structure determination, they are sparsely represented in the protein structure databank and computational methods can help to understand their biophysical principles. We have developed a novel computational method to predict the 3D structure of beta-barrel membrane proteins using evolutionary coupling (EC) constraints and a reduced state space. Combined with an empirical potential function, we can successfully predict strand register at > 80% accuracy for a set of 49 non-homologous proteins with known structures. This is a significant improvement from previous results using EC alone (44%) and using empirical potential function alone (73%). Our method is general and can be applied to genome-wide structural prediction. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=beta-barrel%20membrane%20proteins" title="beta-barrel membrane proteins">beta-barrel membrane proteins</a>, <a href="https://publications.waset.org/abstracts/search?q=structure%20prediction" title=" structure prediction"> structure prediction</a>, <a href="https://publications.waset.org/abstracts/search?q=evolutionary%20constraints" title=" evolutionary constraints"> evolutionary constraints</a>, <a href="https://publications.waset.org/abstracts/search?q=reduced%20state%20space" title=" reduced state space"> reduced state space</a> </p> <a href="https://publications.waset.org/abstracts/40565/improved-3d-structure-prediction-of-beta-barrel-membrane-proteins-by-using-evolutionary-coupling-constraints-reduced-state-space-and-an-empirical-potential-function" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/40565.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">618</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9116</span> Identification and Characterization of Small Peptides Encoded by Small Open Reading Frames using Mass Spectrometry and Bioinformatics</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Su%20Mon%20Saw">Su Mon Saw</a>, <a href="https://publications.waset.org/abstracts/search?q=Joe%20Rothnagel"> Joe Rothnagel</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Short open reading frames (sORFs) located in 5’UTR of mRNAs are known as uORFs. Characterization of uORF-encoded peptides (uPEPs) i.e., a subset of short open reading frame encoded peptides (sPEPs) and their translation regulation lead to understanding of causes of genetic disease, proteome complexity and development of treatments. Existence of uORFs within cellular proteome could be detected by LC-MS/MS. The ability of uORF to be translated into uPEP and achievement of uPEP identification will allow uPEP’s characterization, structures, functions, subcellular localization, evolutionary maintenance (conservation in human and other species) and abundance in cells. It is hypothesized that a subset of sORFs are translatable and that their encoded sPEPs are functional and are endogenously expressed contributing to the eukaryotic cellular proteome complexity. This project aimed to investigate whether sORFs encode functional peptides. Liquid chromatography-mass spectrometry (LC-MS) and bioinformatics were thus employed. Due to probable low abundance of sPEPs and small in sizes, the need for efficient peptide enrichment strategies for enriching small proteins and depleting the sub-proteome of large and abundant proteins is crucial for identifying sPEPs. Low molecular weight proteins were extracted using SDS-PAGE from Human Embryonic Kidney (HEK293) cells and Strong Cation Exchange Chromatography (SCX) from secreted HEK293 cells. Extracted proteins were digested by trypsin to peptides, which were detected by LC-MS/MS. The MS/MS data obtained was searched against Swiss-Prot using MASCOT version 2.4 to filter out known proteins, and all unmatched spectra were re-searched against human RefSeq database. ProteinPilot v5.0.1 was used to identify sPEPs by searching against human RefSeq, Vanderperre and Human Alternative Open Reading Frame (HaltORF) databases. Potential sPEPs were analyzed by bioinformatics. Since SDS PAGE electrophoresis could not separate proteins <20kDa, this could not identify sPEPs. All MASCOT-identified peptide fragments were parts of main open reading frame (mORF) by ORF Finder search and blastp search. No sPEP was detected and existence of sPEPs could not be identified in this study. 13 translated sORFs in HEK293 cells by mass spectrometry in previous studies were characterized by bioinformatics. Identified sPEPs from previous studies were <100 amino acids and <15 kDa. Bioinformatics results showed that sORFs are translated to sPEPs and contribute to proteome complexity. uPEP translated from uORF of SLC35A4 was strongly conserved in human and mouse while uPEP translated from uORF of MKKS was strongly conserved in human and Rhesus monkey. Cross-species conserved uORFs in association with protein translation strongly suggest evolutionary maintenance of coding sequence and indicate probable functional expression of peptides encoded within these uORFs. Translation of sORFs was confirmed by mass spectrometry and sPEPs were characterized with bioinformatics. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=bioinformatics" title="bioinformatics">bioinformatics</a>, <a href="https://publications.waset.org/abstracts/search?q=HEK293%20cells" title=" HEK293 cells"> HEK293 cells</a>, <a href="https://publications.waset.org/abstracts/search?q=liquid%20chromatography-mass%20spectrometry" title=" liquid chromatography-mass spectrometry"> liquid chromatography-mass spectrometry</a>, <a href="https://publications.waset.org/abstracts/search?q=ProteinPilot" title=" ProteinPilot"> ProteinPilot</a>, <a href="https://publications.waset.org/abstracts/search?q=Strong%20Cation%20Exchange%20Chromatography" title=" Strong Cation Exchange Chromatography"> Strong Cation Exchange Chromatography</a>, <a href="https://publications.waset.org/abstracts/search?q=SDS-PAGE" title=" SDS-PAGE"> SDS-PAGE</a>, <a href="https://publications.waset.org/abstracts/search?q=sPEPs" title=" sPEPs"> sPEPs</a> </p> <a href="https://publications.waset.org/abstracts/55031/identification-and-characterization-of-small-peptides-encoded-by-small-open-reading-frames-using-mass-spectrometry-and-bioinformatics" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/55031.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">188</span> </span> </div> </div> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">9115</span> Comparative Study on Productivity, Chemical Composition and Yield Quality of Some Alternative Crops in Romanian Organic Farming</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Maria%20Toader">Maria Toader</a>, <a href="https://publications.waset.org/abstracts/search?q=Gheorghe%20Valentin%20Roman"> Gheorghe Valentin Roman</a>, <a href="https://publications.waset.org/abstracts/search?q=Alina%20Maria%20Ionescu"> Alina Maria Ionescu</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Crops diversity and maintaining and enhancing the fertility of agricultural lands are basic principles of organic farming. With a wider range of crops in agroecosystem can improve the ability to control weeds, pests and diseases, and the performance of crops rotation and food safety. In this sense, the main objective of the research was to study the productivity and chemical composition of some alternative crops and their adaptability to soil and climatic conditions of the agricultural area in Southern Romania and to cultivation in the organic farming system. The alternative crops were: lentil (7 genotypes); five species of grain legumes (5 genotypes); four species of oil crops (5 genotypes). The seed production was, on average: 1343 kg/ha of lentil; 2500 kg/ha of field beans; 2400 kg/ha of chick peas and blackeyed peas; more than 2000 kg/ha of atzuki beans, over 1250 kg/ha of fenugreek; 2200 kg/ha of safflower; 570 kg/ha of oil pumpkin; 2150 kg/ha of oil flax; 1518 kg/ha of camelina. Regarding chemical composition, lentil seeds contained: 22.18% proteins, 3.03% lipids, 33.29% glucides, 4.00% minerals, and 259.97 kcal energy values. For field beans: 21.50% proteins, 4.40% lipids, 63.90% glucides, 5.85% minerals, 395.36 kcal energetic value. For chick peas: 21.23% proteins, 4.55% lipids, 53.00% glucides, 3.67% minerals, 348.22 kcal energetic value. For blackeyed peas: 23.30% proteins, 2.10% lipids, 68.10% glucides, 3.93% minerals, 350.14 kcal energetic value. For adzuki beans: 21.90% proteins, 2.60% lipids, 69.30% glucides, 4.10% minerals, 402.48 kcal energetic value. For fenugreek: 21.30% proteins, 4.65% lipids, 63.83% glucides, 5.69% minerals, 396.54 kcal energetic value. For safflower: 12.60% proteins, 28.37% lipids, 46.41% glucides, 3.60% minerals, 505.78 kcal energetic value. For camelina: 20.29% proteins, 31.68% lipids, 36.28% glucides, 4.29% minerals, 526.63 kcal energetic value. For oil pumpkin: 29.50% proteins, 36.92% lipids, 18.50% glucides, 5.41% minerals, 540.15 kcal energetic value. For oil flax: 22.56% proteins, 34.10% lipids, 27.73% glucides, 5.25% minerals, 558.45 kcal energetic value. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=adaptability" title="adaptability">adaptability</a>, <a href="https://publications.waset.org/abstracts/search?q=alternative%20crops" title=" alternative crops"> alternative crops</a>, <a href="https://publications.waset.org/abstracts/search?q=chemical%20composition" title=" chemical composition"> chemical composition</a>, <a href="https://publications.waset.org/abstracts/search?q=organic%20farming%20productivity" title=" organic farming productivity"> organic farming productivity</a> </p> <a href="https://publications.waset.org/abstracts/28059/comparative-study-on-productivity-chemical-composition-and-yield-quality-of-some-alternative-crops-in-romanian-organic-farming" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/28059.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">516</span> </span> </div> </div> <ul class="pagination"> <li class="page-item disabled"><span class="page-link">&lsaquo;</span></li> <li class="page-item active"><span class="page-link">1</span></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=Human%20C-Cbl%20proteins&page=2">2</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=Human%20C-Cbl%20proteins&page=3">3</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=Human%20C-Cbl%20proteins&page=4">4</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=Human%20C-Cbl%20proteins&page=5">5</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=Human%20C-Cbl%20proteins&page=6">6</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=Human%20C-Cbl%20proteins&page=7">7</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=Human%20C-Cbl%20proteins&page=8">8</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=Human%20C-Cbl%20proteins&page=9">9</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=Human%20C-Cbl%20proteins&page=10">10</a></li> <li class="page-item disabled"><span class="page-link">...</span></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=Human%20C-Cbl%20proteins&page=304">304</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=Human%20C-Cbl%20proteins&page=305">305</a></li> <li class="page-item"><a class="page-link" href="https://publications.waset.org/abstracts/search?q=Human%20C-Cbl%20proteins&page=2" rel="next">&rsaquo;</a></li> </ul> </div> </main> <footer> <div id="infolinks" class="pt-3 pb-2"> <div class="container"> <div style="background-color:#f5f5f5;" class="p-3"> <div class="row"> <div class="col-md-2"> <ul class="list-unstyled"> About <li><a href="https://waset.org/page/support">About Us</a></li> <li><a href="https://waset.org/page/support#legal-information">Legal</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/WASET-16th-foundational-anniversary.pdf">WASET celebrates its 16th foundational anniversary</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Account <li><a href="https://waset.org/profile">My Account</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Explore <li><a href="https://waset.org/disciplines">Disciplines</a></li> <li><a href="https://waset.org/conferences">Conferences</a></li> <li><a href="https://waset.org/conference-programs">Conference Program</a></li> <li><a href="https://waset.org/committees">Committees</a></li> <li><a href="https://publications.waset.org">Publications</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Research <li><a href="https://publications.waset.org/abstracts">Abstracts</a></li> <li><a href="https://publications.waset.org">Periodicals</a></li> <li><a href="https://publications.waset.org/archive">Archive</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Open Science <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Open-Science-Philosophy.pdf">Open Science Philosophy</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Open-Science-Award.pdf">Open Science Award</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Open-Society-Open-Science-and-Open-Innovation.pdf">Open Innovation</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Postdoctoral-Fellowship-Award.pdf">Postdoctoral Fellowship Award</a></li> <li><a target="_blank" rel="nofollow" href="https://publications.waset.org/static/files/Scholarly-Research-Review.pdf">Scholarly Research Review</a></li> </ul> </div> <div class="col-md-2"> <ul class="list-unstyled"> Support <li><a href="https://waset.org/page/support">Support</a></li> <li><a href="https://waset.org/profile/messages/create">Contact Us</a></li> <li><a href="https://waset.org/profile/messages/create">Report Abuse</a></li> </ul> </div> </div> </div> </div> </div> <div class="container text-center"> <hr style="margin-top:0;margin-bottom:.3rem;"> <a href="https://creativecommons.org/licenses/by/4.0/" target="_blank" class="text-muted small">Creative Commons Attribution 4.0 International License</a> <div id="copy" class="mt-2">© 2024 World Academy of Science, Engineering and Technology</div> </div> </footer> <a href="javascript:" id="return-to-top"><i class="fas fa-arrow-up"></i></a> <div class="modal" id="modal-template"> <div class="modal-dialog"> <div class="modal-content"> <div class="row m-0 mt-1"> <div class="col-md-12"> <button type="button" class="close" data-dismiss="modal" aria-label="Close"><span aria-hidden="true">×</span></button> </div> </div> <div class="modal-body"></div> </div> </div> </div> <script src="https://cdn.waset.org/static/plugins/jquery-3.3.1.min.js"></script> <script src="https://cdn.waset.org/static/plugins/bootstrap-4.2.1/js/bootstrap.bundle.min.js"></script> <script src="https://cdn.waset.org/static/js/site.js?v=150220211556"></script> <script> jQuery(document).ready(function() { /*jQuery.get("https://publications.waset.org/xhr/user-menu", function (response) { jQuery('#mainNavMenu').append(response); });*/ jQuery.get({ url: "https://publications.waset.org/xhr/user-menu", cache: false }).then(function(response){ jQuery('#mainNavMenu').append(response); }); }); </script> </body> </html>