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interaction network</title> <meta name="description" content="Search results for: protein interaction network"> <meta name="keywords" content="protein interaction network"> <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 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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="protein interaction network"> <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> 10543</div> </div> </div> </div> <h1 class="mt-3 mb-3 text-center" style="font-size:1.6rem;">Search results for: protein interaction network</h1> <div class="card paper-listing mb-3 mt-3"> <h5 class="card-header" style="font-size:.9rem"><span class="badge badge-info">10543</span> Computational Identification of Signalling Pathways in Protein Interaction Networks</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Angela%20U.%20Makolo">Angela U. Makolo</a>, <a href="https://publications.waset.org/abstracts/search?q=Temitayo%20A.%20Olagunju"> Temitayo A. Olagunju</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The knowledge of signaling pathways is central to understanding the biological mechanisms of organisms since it has been identified that in eukaryotic organisms, the number of signaling pathways determines the number of ways the organism will react to external stimuli. Signaling pathways are studied using protein interaction networks constructed from protein-protein interaction data obtained using high throughput experimental procedures. However, these high throughput methods are known to produce very high rates of false positive and negative interactions. In order to construct a useful protein interaction network from this noisy data, computational methods are applied to validate the protein-protein interactions. In this study, a computational technique to identify signaling pathways from a protein interaction network constructed using validated protein-protein interaction data was designed. A weighted interaction graph of the Saccharomyces cerevisiae (Baker’s Yeast) organism using the proteins as the nodes and interactions between them as edges was constructed. The weights were obtained using Bayesian probabilistic network to estimate the posterior probability of interaction between two proteins given the gene expression measurement as biological evidence. Only interactions above a threshold were accepted for the network model. A pathway was formalized as a simple path in the interaction network from a starting protein and an ending protein of interest. We were able to identify some pathway segments, one of which is a segment of the pathway that signals the start of the process of meiosis in S. cerevisiae. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Bayesian%20networks" title="Bayesian networks">Bayesian networks</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20interaction%20networks" title=" protein interaction networks"> protein interaction networks</a>, <a href="https://publications.waset.org/abstracts/search?q=Saccharomyces%20cerevisiae" title=" Saccharomyces cerevisiae"> Saccharomyces cerevisiae</a>, <a href="https://publications.waset.org/abstracts/search?q=signalling%20pathways" title=" signalling pathways"> signalling pathways</a> </p> <a href="https://publications.waset.org/abstracts/22095/computational-identification-of-signalling-pathways-in-protein-interaction-networks" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/22095.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">544</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">10542</span> An Efficient Algorithm for Global Alignment of Protein-Protein Interaction Networks</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Duc%20Dong%20Do">Duc Dong Do</a>, <a href="https://publications.waset.org/abstracts/search?q=Ngoc%20Ha%20Tran"> Ngoc Ha Tran</a>, <a href="https://publications.waset.org/abstracts/search?q=Thanh%20Hai%20Dang"> Thanh Hai Dang</a>, <a href="https://publications.waset.org/abstracts/search?q=Cao%20Cuong%20Dang"> Cao Cuong Dang</a>, <a href="https://publications.waset.org/abstracts/search?q=Xuan%20Huan%20Hoang"> Xuan Huan Hoang</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Global aligning two protein-protein interaction networks is an essentially important task in bioinformatics/computational biology field of study. It is a challenging and widely studied research topic in recent years. Accurately aligned networks allow us to identify functional modules of proteins and/ororthologous proteins from which unknown functions of a protein can be inferred. We here introduce a novel efficient heuristic global network alignment algorithm called FASTAn, including two phases: the first to construct an initial alignment and the second to improve such alignment by exerting a local optimization repeated procedure. The experimental results demonstrated that FASTAn outperformed the state-of-the-art global network alignment algorithm namely SPINAL in terms of both commonly used objective scores and the run-time. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=FASTAn" title="FASTAn">FASTAn</a>, <a href="https://publications.waset.org/abstracts/search?q=Heuristic%20algorithm" title=" Heuristic algorithm"> Heuristic algorithm</a>, <a href="https://publications.waset.org/abstracts/search?q=biological%20network%20alignment" title=" biological network alignment"> biological network alignment</a>, <a href="https://publications.waset.org/abstracts/search?q=protein-protein%20interaction%20networks" title=" protein-protein interaction networks"> protein-protein interaction networks</a> </p> <a href="https://publications.waset.org/abstracts/17228/an-efficient-algorithm-for-global-alignment-of-protein-protein-interaction-networks" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/17228.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">604</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">10541</span> The Relation Between Protein-Protein and Polysaccharide-Protein Interaction on Aroma Release from Brined Cheese Model</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mehrnaz%20Aminifar">Mehrnaz Aminifar</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The relation between textural parameters and casein network on release of aromatic compounds was investigated over 90-days of ripening. Low DE maltodextrin and WPI were used to modify the textural properties of low fat brined cheese. Hardness, brittleness and compaction of casein network were affected by addition of maltodextrin and WPI. Textural properties and aroma release from cheese texture were affected by interaction of WPI protein-cheese protein and maltodexterin-cheese protein. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=aroma%20release" title="aroma release">aroma release</a>, <a href="https://publications.waset.org/abstracts/search?q=brined%20cheese" title=" brined cheese"> brined cheese</a>, <a href="https://publications.waset.org/abstracts/search?q=maltodexterin" title=" maltodexterin"> maltodexterin</a>, <a href="https://publications.waset.org/abstracts/search?q=WPI" title=" WPI"> WPI</a> </p> <a href="https://publications.waset.org/abstracts/6193/the-relation-between-protein-protein-and-polysaccharide-protein-interaction-on-aroma-release-from-brined-cheese-model" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/6193.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">355</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">10540</span> Combining in vitro Protein Expression with AlphaLISA Technology to Study Protein-Protein Interaction</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Shayli%20Varasteh%20Moradi">Shayli Varasteh Moradi</a>, <a href="https://publications.waset.org/abstracts/search?q=Wayne%20A.%20Johnston"> Wayne A. Johnston</a>, <a href="https://publications.waset.org/abstracts/search?q=Dejan%20Gagoski"> Dejan Gagoski</a>, <a href="https://publications.waset.org/abstracts/search?q=Kirill%20Alexandrov"> Kirill Alexandrov</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The demand for a rapid and more efficient technique to identify protein-protein interaction particularly in the areas of therapeutics and diagnostics development is growing. The method described here is a rapid in vitro protein-protein interaction analysis approach based on AlphaLISA technology combined with Leishmania tarentolae cell-free protein production (LTE) system. Cell-free protein synthesis allows the rapid production of recombinant proteins in a multiplexed format. Among available in vitro expression systems, LTE offers several advantages over other eukaryotic cell-free systems. It is based on a fast growing fermentable organism that is inexpensive in cultivation and lysate production. High integrity of proteins produced in this system and the ability to co-express multiple proteins makes it a desirable method for screening protein interactions. Following the translation of protein pairs in LTE system, the physical interaction between proteins of interests is analysed by AlphaLISA assay. The assay is performed using unpurified in vitro translation reaction and therefore can be readily multiplexed. This approach can be used in various research applications such as epitope mapping, antigen-antibody analysis and protein interaction network mapping. The intra-viral protein interaction network of Zika virus was studied using the developed technique. The viral proteins were co-expressed pair-wise in LTE and all possible interactions among viral proteins were tested using AlphaLISA. The assay resulted to the identification of 54 intra-viral protein-protein interactions from which 19 binary interactions were found to be novel. The presented technique provides a powerful tool for rapid analysis of protein-protein interaction with high sensitivity and throughput. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=AlphaLISA%20technology" title="AlphaLISA technology">AlphaLISA technology</a>, <a href="https://publications.waset.org/abstracts/search?q=cell-free%20protein%20expression" title=" cell-free protein expression"> cell-free protein expression</a>, <a href="https://publications.waset.org/abstracts/search?q=epitope%20mapping" title=" epitope mapping"> epitope mapping</a>, <a href="https://publications.waset.org/abstracts/search?q=Leishmania%20tarentolae" title=" Leishmania tarentolae"> Leishmania tarentolae</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/81407/combining-in-vitro-protein-expression-with-alphalisa-technology-to-study-protein-protein-interaction" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/81407.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">237</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">10539</span> ACOPIN: An ACO Algorithm with TSP Approach for Clustering Proteins in Protein Interaction Networks</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Jamaludin%20Sallim">Jamaludin Sallim</a>, <a href="https://publications.waset.org/abstracts/search?q=Rozlina%20Mohamed"> Rozlina Mohamed</a>, <a href="https://publications.waset.org/abstracts/search?q=Roslina%20Abdul%20Hamid"> Roslina Abdul Hamid</a> </p> <p class="card-text"><strong>Abstract:</strong></p> In this paper, we proposed an Ant Colony Optimization (ACO) algorithm together with Traveling Salesman Problem (TSP) approach to investigate the clustering problem in Protein Interaction Networks (PIN). We named this combination as ACOPIN. The purpose of this work is two-fold. First, to test the efficacy of ACO in clustering PIN and second, to propose the simple generalization of the ACO algorithm that might allow its application in clustering proteins in PIN. We split this paper to three main sections. First, we describe the PIN and clustering proteins in PIN. Second, we discuss the steps involved in each phase of ACO algorithm. Finally, we present some results of the investigation with the clustering patterns. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=ant%20colony%20optimization%20algorithm" title="ant colony optimization algorithm">ant colony optimization algorithm</a>, <a href="https://publications.waset.org/abstracts/search?q=searching%20algorithm" title=" searching algorithm"> searching algorithm</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20functional%20module" title=" protein functional module"> protein functional module</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20interaction%20network" title=" protein interaction network "> protein interaction network </a> </p> <a href="https://publications.waset.org/abstracts/22367/acopin-an-aco-algorithm-with-tsp-approach-for-clustering-proteins-in-protein-interaction-networks" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/22367.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">612</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">10538</span> The Omicron Variant BA.2.86.1 of SARS- 2 CoV-2 Demonstrates an Altered Interaction Network and Dynamic Features to Enhance the Interaction with the hACE2</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Taimur%20Khan">Taimur Khan</a>, <a href="https://publications.waset.org/abstracts/search?q=Zakirullah"> Zakirullah</a>, <a href="https://publications.waset.org/abstracts/search?q=Muhammad%20Shahab"> Muhammad Shahab</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The SARS-CoV-2 variant BA.2.86 (Omicron) has emerged with unique mutations that may increase its transmission and infectivity. This study investigates how these mutations alter the Omicron receptor-binding domain's interaction network and dynamic properties (RBD) compared to the wild-type virus, focusing on its binding affinity to the human ACE2 (hACE2) receptor. Protein-protein docking and all-atom molecular dynamics simulations were used to analyze structural and dynamic differences. Despite the structural similarity to the wild-type virus, the Omicron variant exhibits a distinct interaction network involving new residues that enhance its binding capacity. The dynamic analysis reveals increased flexibility in the RBD, particularly in loop regions crucial for hACE2 interaction. Mutations significantly alter the secondary structure, leading to greater flexibility and conformational adaptability compared to the wild type. Binding free energy calculations confirm that the Omicron RBD has a higher binding affinity (-70.47 kcal/mol) to hACE2 than the wild-type RBD (-61.38 kcal/mol). These results suggest that the altered interaction network and enhanced dynamics of the Omicron variant contribute to its increased infectivity, providing insights for the development of targeted therapeutics and vaccines. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=SARS-CoV-2" title="SARS-CoV-2">SARS-CoV-2</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20dynamic%20simulation" title=" molecular dynamic simulation"> molecular dynamic simulation</a>, <a href="https://publications.waset.org/abstracts/search?q=receptor%20binding%20domain" title=" receptor binding domain"> receptor binding domain</a>, <a href="https://publications.waset.org/abstracts/search?q=vaccine" title=" vaccine"> vaccine</a> </p> <a href="https://publications.waset.org/abstracts/192479/the-omicron-variant-ba2861-of-sars-2-cov-2-demonstrates-an-altered-interaction-network-and-dynamic-features-to-enhance-the-interaction-with-the-hace2" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/192479.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">22</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">10537</span> Interaction of Dietary Protein and Vitamin E Supplementation on Gastrointestinal Nematode (Gnt) Parasitism of Naturally Infected Lambs</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ayobami%20Adeyemo">Ayobami Adeyemo</a>, <a href="https://publications.waset.org/abstracts/search?q=Michael%20%20Chimonyo"> Michael Chimonyo</a>, <a href="https://publications.waset.org/abstracts/search?q=Munyaradzi%20Marufu"> Munyaradzi Marufu</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Gastrointestinal nematode (GNT) infection significantly hinder sustainable and profitable sheep production on rangelands. While vitamin E and protein supplementation have individually proven to improve host immunity to parasitism in lambs, to our knowledge, there is no information on the interaction of dietary vitamin E and protein supplementation on lamb growth and GIN faecal egg counts in naturally infected lambs. Therefore, the current study investigated the interaction of dietary protein and vitamin E supplementation on faecal egg counts (FEC) and growth performance of lambs. Twenty four Dohne Merino lambs aged 12 months were allocated equally to each of four treatment combinations, with six lambs in each treatment group for a period of eight weeks. Treatment one lambs received dietary protein and vitamin E (PE), treatment two lambs received dietary protein and no vitamin E (PNE), treatment three received dietary vitamin E and no protein (NPE), and treatment four received no dietary protein and vitamin E supplementation (NPNE). The lambs were allowed to graze on Pennisetum clandestinum contaminated with a heavy load of nematodes. Dietary protein supplementation increased (P < 0.01) average daily gain (ADG) and body condition scores (BCS). Dietary vitamin E supplementation had no effect (P > 0.05) on ADG and BCS. There was no interaction (P > 0.05) between dietary protein and vitamin E supplementation on ADG and BCS. Combined supplementation of dietary protein and vitamin E supplementation significantly reduced (P < 0.01) faecal egg counts and larval counts, respectively. Also, dietary protein and vitamin E supplementation reduced GNT faecal egg counts over the exposure period. The current findings support the hypothesis that the interaction of dietary protein and vitamin E supplementation reduced faecal egg counts and larval counts in lambs. This necessitates future findings on the interaction of dietary protein and vitamin E supplementation on blood associated profiles. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=gastrointestinal%20nematodes" title="gastrointestinal nematodes">gastrointestinal nematodes</a>, <a href="https://publications.waset.org/abstracts/search?q=nematode%20eggs" title=" nematode eggs"> nematode eggs</a>, <a href="https://publications.waset.org/abstracts/search?q=Haemonchus" title=" Haemonchus"> Haemonchus</a>, <a href="https://publications.waset.org/abstracts/search?q=Trichostrongylus" title=" Trichostrongylus"> Trichostrongylus</a> </p> <a href="https://publications.waset.org/abstracts/88994/interaction-of-dietary-protein-and-vitamin-e-supplementation-on-gastrointestinal-nematode-gnt-parasitism-of-naturally-infected-lambs" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/88994.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">209</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">10536</span> Bio-Functional Polymeric Protein Based Materials Utilized for Soft Tissue Engineering Application </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Er-Yuan%20Chuang">Er-Yuan Chuang</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Bio-mimetic matters have biological functionalities. This might be valuable in the development of versatile biomaterials. At biological fields, protein-based materials might be components to form a 3D network of extracellular biomolecules, containing growth factors. Also, the protein-based biomaterial provides biochemical and structural assistance of adjacent cells. In this study, we try to prepare protein based biomaterial, which was harvested from living animal. We analyzed it’s chemical, physical and biological property in vitro. Besides, in vivo bio-interaction of the prepared biomimetic matrix was tested in an animal model. The protein-based biomaterial has degradability and biocompatibility. This development could be used for tissue regenerations and be served as platform technologies. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=protein%20based" title="protein based">protein based</a>, <a href="https://publications.waset.org/abstracts/search?q=in%20vitro%20study" title=" in vitro study"> in vitro study</a>, <a href="https://publications.waset.org/abstracts/search?q=in%20vivo%20study" title=" in vivo study"> in vivo study</a>, <a href="https://publications.waset.org/abstracts/search?q=biomaterials" title=" biomaterials"> biomaterials</a> </p> <a href="https://publications.waset.org/abstracts/105449/bio-functional-polymeric-protein-based-materials-utilized-for-soft-tissue-engineering-application" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/105449.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">189</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">10535</span> Protein Tertiary Structure Prediction by a Multiobjective Optimization and Neural Network Approach</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Alexandre%20Barbosa%20de%20Almeida">Alexandre Barbosa de Almeida</a>, <a href="https://publications.waset.org/abstracts/search?q=Telma%20Woerle%20de%20Lima%20Soares"> Telma Woerle de Lima Soares</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Protein structure prediction is a challenging task in the bioinformatics field. The biological function of all proteins majorly relies on the shape of their three-dimensional conformational structure, but less than 1% of all known proteins in the world have their structure solved. This work proposes a deep learning model to address this problem, attempting to predict some aspects of the protein conformations. Throughout a process of multiobjective dominance, a recurrent neural network was trained to abstract the particular bias of each individual multiobjective algorithm, generating a heuristic that could be useful to predict some of the relevant aspects of the three-dimensional conformation process formation, known as protein folding. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ab%20initio%20heuristic%20modeling" title="Ab initio heuristic modeling">Ab initio heuristic modeling</a>, <a href="https://publications.waset.org/abstracts/search?q=multiobjective%20optimization" title=" multiobjective optimization"> multiobjective optimization</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20structure%20prediction" title=" protein structure prediction"> protein structure prediction</a>, <a href="https://publications.waset.org/abstracts/search?q=recurrent%20neural%20network" title=" recurrent neural network"> recurrent neural network</a> </p> <a href="https://publications.waset.org/abstracts/141565/protein-tertiary-structure-prediction-by-a-multiobjective-optimization-and-neural-network-approach" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/141565.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">205</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">10534</span> Myeloid Zinc Finger 1/Ets-Like Protein-1/Protein Kinase C Alpha Associated with Poor Prognosis in Patients with Hepatocellular Carcinoma</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Jer-Yuh%20Liu">Jer-Yuh Liu</a>, <a href="https://publications.waset.org/abstracts/search?q=Je-Chiuan%20Ye"> Je-Chiuan Ye</a>, <a href="https://publications.waset.org/abstracts/search?q=Jin-Ming%20Hwang"> Jin-Ming Hwang</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Protein kinase C alpha (PKCα) is a key signaling molecule in human cancer development. As a therapeutic strategy, targeting PKCα is difficult because the molecule is ubiquitously expressed in non-malignant cells. PKCα is regulated by the cooperative interaction of the transcription factors myeloid zinc finger 1 (MZF-1) and Ets-like protein-1 (Elk-1) in human cancer cells. By conducting tissue array analysis, herein, we determined the protein expression of MZF-1/Elk-1/PKCα in various cancers. The data show that the expression of MZF-1/Elk-1 is correlated with that of PKCα in hepatocellular carcinoma (HCC), but not in bladder and lung cancers. In addition, the PKCα down-regulation by shRNA Elk-1 was only observed in the HCC SK-Hep-1 cells. Blocking the interaction between MZF-1 and Elk-1 through the transfection of their binding domain MZF-160–72 decreased PKCα expression. This step ultimately depressed the epithelial-mesenchymal transition potential of the HCC cells. These findings could be used to develop an alternative therapeutic strategy for patients with the PKCα-derived HCC. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=protein%20kinase%20C%20alpha" title="protein kinase C alpha">protein kinase C alpha</a>, <a href="https://publications.waset.org/abstracts/search?q=myeloid%20zinc%20finger%201" title=" myeloid zinc finger 1"> myeloid zinc finger 1</a>, <a href="https://publications.waset.org/abstracts/search?q=ets-like%20protein-1" title=" ets-like protein-1"> ets-like protein-1</a>, <a href="https://publications.waset.org/abstracts/search?q=hepatocellular%20carcinoma" title=" hepatocellular carcinoma"> hepatocellular carcinoma</a> </p> <a href="https://publications.waset.org/abstracts/78123/myeloid-zinc-finger-1ets-like-protein-1protein-kinase-c-alpha-associated-with-poor-prognosis-in-patients-with-hepatocellular-carcinoma" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/78123.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">227</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">10533</span> Quantifying the Protein-Protein Interaction between the Ion-Channel-Forming Colicin A and the Tol Proteins by Potassium Efflux in E. coli Cells</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Fadilah%20Aleanizy">Fadilah Aleanizy</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Colicins are a family of bacterial toxins that kill Escherichia coli and other closely related species. The mode of action of colicins involves binding to an outer membrane receptor and translocation across the cell envelope, leading to cytotoxicity through specific targets. The mechanism of colicin cytotoxicity includes a non-specific endonuclease activity or depolarization of the cytoplasmic membrane by pore-forming activity. For Group A colicins, translocation requires an interaction between the N-terminal domain of the colicin and a series of membrane- bound and periplasmic proteins known as the Tol system (TolB, TolR, TolA, TolQ, and Pal and the active domain must be translocated through the outer membranes. Protein-protein interactions are intrinsic to virtually every cellular process. The transient protein-protein interactions of the colicin include the interaction with much more complicated assemblies during colicin translocation across the cellular membrane to its target. The potassium release assay detects variation in the K+ content of bacterial cells (K+in). This assays is used to measure the effect of pore-forming colicins such as ColA on an indicator organism by measuring the changes of the K+ concentration in the external medium (K+out ) that are caused by cell killing with a K+ selective electrode. One of the goals of this work is to employ a quantifiable in-vivo method to spot which Tol protein are more implicated in the interaction with colicin A as it is translocated to its target. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=K%2B%20efflux" title="K+ efflux">K+ efflux</a>, <a href="https://publications.waset.org/abstracts/search?q=Colicin%20A" title=" Colicin A"> Colicin A</a>, <a href="https://publications.waset.org/abstracts/search?q=Tol-proteins" title=" Tol-proteins"> Tol-proteins</a>, <a href="https://publications.waset.org/abstracts/search?q=E.%20coli" title=" E. coli"> E. coli</a> </p> <a href="https://publications.waset.org/abstracts/14701/quantifying-the-protein-protein-interaction-between-the-ion-channel-forming-colicin-a-and-the-tol-proteins-by-potassium-efflux-in-e-coli-cells" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/14701.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">10532</span> Interaction of Histone H1 with Chromatin-associated Protein HMGB1 Studied by Microscale Thermophoresis</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Michal%20%C5%A0tros">Michal Štros</a>, <a href="https://publications.waset.org/abstracts/search?q=Eva%20Polansk%C3%A1"> Eva Polanská</a>, <a href="https://publications.waset.org/abstracts/search?q=%C5%A0%C3%A1rka%20Posp%C3%AD%C5%A1ilov%C3%A1"> Šárka Pospíšilová</a> </p> <p class="card-text"><strong>Abstract:</strong></p> HMGB1 is an architectural protein in chromatin, acting also as a signaling molecule outside the cell. Recent reports from several laboratories provided evidence that a number of both the intracellular and extracellular functions of HMGB1 may depend on redox-sensitive cysteine residues of the protein. MALDI-TOF analysis revealed that mild oxidization of HMGB1 resulted in a conformational change of the protein due to formation of an intramolecular disulphide bond by opposing Cys23 and Cys45 residues. We have demonstrated that redox state of HMGB1 could significantly modulate the ability of the protein to bind and bend DNA. We have also shown that reduced HMGB1 could easily displace histone H1 from DNA, while oxidized HMGB1 had limited capacity for H1 displacement. Using microscale thermophoresis (MST) we have further studied mechanism of HMGB1 interaction with histone H1 in free solution or when histone H1 was bound to DNA. Our MST analysis indicated that reduced HMGB1 exhibited in free solution > 1000 higher affinity of for H1 (KD ~ 4.5 nM) than oxidized HMGB1 (KD <10 M). Finally, we present a novel mechanism for the HMGB1-mediated modulation of histone H1 binding to DNA. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=HMGB1" title="HMGB1">HMGB1</a>, <a href="https://publications.waset.org/abstracts/search?q=histone%20H1" title=" histone H1"> histone H1</a>, <a href="https://publications.waset.org/abstracts/search?q=redox%20state" title=" redox state"> redox state</a>, <a href="https://publications.waset.org/abstracts/search?q=interaction" title=" interaction"> interaction</a>, <a href="https://publications.waset.org/abstracts/search?q=cross-linking" title=" cross-linking"> cross-linking</a>, <a href="https://publications.waset.org/abstracts/search?q=DNA%20bending" title=" DNA bending"> DNA bending</a>, <a href="https://publications.waset.org/abstracts/search?q=DNA%20end-joining" title=" DNA end-joining"> DNA end-joining</a>, <a href="https://publications.waset.org/abstracts/search?q=microscale%20thermophoresis" title=" microscale thermophoresis"> microscale thermophoresis</a> </p> <a href="https://publications.waset.org/abstracts/17609/interaction-of-histone-h1-with-chromatin-associated-protein-hmgb1-studied-by-microscale-thermophoresis" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/17609.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">335</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">10531</span> DNpro: A Deep Learning Network Approach to Predicting Protein Stability Changes Induced by Single-Site Mutations</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Xiao%20Zhou">Xiao Zhou</a>, <a href="https://publications.waset.org/abstracts/search?q=Jianlin%20Cheng"> Jianlin Cheng</a> </p> <p class="card-text"><strong>Abstract:</strong></p> A single amino acid mutation can have a significant impact on the stability of protein structure. Thus, the prediction of protein stability change induced by single site mutations is critical and useful for studying protein function and structure. Here, we presented a deep learning network with the dropout technique for predicting protein stability changes upon single amino acid substitution. While using only protein sequence as input, the overall prediction accuracy of the method on a standard benchmark is >85%, which is higher than existing sequence-based methods and is comparable to the methods that use not only protein sequence but also tertiary structure, pH value and temperature. The results demonstrate that deep learning is a promising technique for protein stability prediction. The good performance of this sequence-based method makes it a valuable tool for predicting the impact of mutations on most proteins whose experimental structures are not available. Both the downloadable software package and the user-friendly web server (DNpro) that implement the method for predicting protein stability changes induced by amino acid mutations are freely available for the community to use. <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=deep%20learning" title=" deep learning"> deep learning</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20stability%20prediction" title=" protein stability prediction"> protein stability prediction</a>, <a href="https://publications.waset.org/abstracts/search?q=biological%20data%20mining" title=" biological data mining"> biological data mining</a> </p> <a href="https://publications.waset.org/abstracts/48058/dnpro-a-deep-learning-network-approach-to-predicting-protein-stability-changes-induced-by-single-site-mutations" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/48058.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">468</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">10530</span> BiFormerDTA: Structural Embedding of Protein in Drug Target Affinity Prediction Using BiFormer</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Leila%20Baghaarabani">Leila Baghaarabani</a>, <a href="https://publications.waset.org/abstracts/search?q=Parvin%20Razzaghi"> Parvin Razzaghi</a>, <a href="https://publications.waset.org/abstracts/search?q=Mennatolla%20Magdy%20Mostafa"> Mennatolla Magdy Mostafa</a>, <a href="https://publications.waset.org/abstracts/search?q=Ahmad%20Albaqsami"> Ahmad Albaqsami</a>, <a href="https://publications.waset.org/abstracts/search?q=Al%20Warith%20Al%20Rushaidi"> Al Warith Al Rushaidi</a>, <a href="https://publications.waset.org/abstracts/search?q=Masoud%20Al%20Rawahi"> Masoud Al Rawahi</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Predicting the interaction between drugs and their molecular targets is pivotal for advancing drug development processes. Due to the time and cost limitations, computational approaches have emerged as an effective approach to drug-target interaction (DTI) prediction. Most of the introduced computational based approaches utilize the drug molecule and protein sequence as input. This study does not only utilize these inputs, it also introduces a protein representation developed using a masked protein language model. In this representation, for every individual amino acid residue within the protein sequence, there exists a corresponding probability distribution that indicates the likelihood of each amino acid being present at that particular position. Then, the similarity between each pair of amino-acids is computed to create similarity matrix. To encode the knowledge of the similarity matrix, Bi-Level Routing Attention (BiFormer) is utilized, which combines aspects of transformer-based models with protein sequence analysis and represents a significant advancement in the field of drug-protein interaction prediction. BiFormer has the ability to pinpoint the most effective regions of the protein sequence that are responsible for facilitating interactions between the protein and drugs, thereby enhancing the understanding of these critical interactions. Thus, it appears promising in its ability to capture the local structural relationship of the proteins by enhancing the understanding of how it contributes to drug protein interactions, thereby facilitating more accurate predictions. To evaluate the proposed method, it was tested on two widely recognized datasets: Davis and KIBA. A comprehensive series of experiments was conducted to illustrate its effectiveness in comparison to cuttingedge techniques. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=BiFormer" title="BiFormer">BiFormer</a>, <a href="https://publications.waset.org/abstracts/search?q=transformer" title=" transformer"> transformer</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20language%20processing" title=" protein language processing"> protein language processing</a>, <a href="https://publications.waset.org/abstracts/search?q=self-attention%20mechanism" title=" self-attention mechanism"> self-attention mechanism</a>, <a href="https://publications.waset.org/abstracts/search?q=binding%20affinity" title=" binding affinity"> binding affinity</a>, <a href="https://publications.waset.org/abstracts/search?q=drug%20target%20interaction" title=" drug target interaction"> drug target interaction</a>, <a href="https://publications.waset.org/abstracts/search?q=similarity%20matrix" title=" similarity matrix"> similarity matrix</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20masked%20representation" title=" protein masked representation"> protein masked representation</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20language%20model" title=" protein language model"> protein language model</a> </p> <a href="https://publications.waset.org/abstracts/194594/biformerdta-structural-embedding-of-protein-in-drug-target-affinity-prediction-using-biformer" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/194594.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">7</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">10529</span> Interaction between Kazal-Type Serine Proteinase Inhibitor SPIPm2 and Cyclophilin A from the Black Tiger Shrimp Penaeus monodon</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sirikwan%20Ponprateep">Sirikwan Ponprateep</a>, <a href="https://publications.waset.org/abstracts/search?q=Anchalee%20Tassanakajon"> Anchalee Tassanakajon</a>, <a href="https://publications.waset.org/abstracts/search?q=Vichien%20Rimphanitchayakit"> Vichien Rimphanitchayakit</a> </p> <p class="card-text"><strong>Abstract:</strong></p> A Kazal-type serine proteinase inhibitor, SPIPm2, was abundantly expressed in the hemocytes and secreted into shrimp plasma has anti-viral property against white spot syndrome virus (WSSV). To discover the molecular mechanism of antiviral activity, the binding assay showed that SPIPm2 bind to the components of viral particle and shrimp hemocyte. From our previous report, viral target protein of SPIPm2 was identified, namely WSV477 using yeast two-hybrid screening. WSV477 is an early gene product of WSSV and involved in viral propagation. In this study, the co-immunoprecipitation technique and Tandem Mass Spectrometry (LC-MS/MS) was used to identify the target protein of SPIPm2 from shrimp hemocyte. The target protein of SPIPm2 was cyclophilin A. In vertebrate, cyclophilin A or peptidylprolyl isomerase A was reported to be the immune suppressor interacted with cyclosporin A involved in immune defense response. The recombinant cyclophilin A from Penaeus monodon (rPmCypA) was produced in E.coli system and purified using Ni-NTA column to confirm the protein-protein interaction. In vitro pull-down assay showed the interaction between rSPIPm2 and rPmCypA. To study the biological function of these proteins, the expression analysis of immune gene in shrimp defense pathways will be investigated after rPmCypA administration. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=cyclophilin%20A" title="cyclophilin A">cyclophilin A</a>, <a href="https://publications.waset.org/abstracts/search?q=protein-protein%20interaction" title=" protein-protein interaction"> protein-protein interaction</a>, <a href="https://publications.waset.org/abstracts/search?q=Kazal-type%20serine%20proteinase%20inhibitor" title=" Kazal-type serine proteinase inhibitor"> Kazal-type serine proteinase inhibitor</a>, <a href="https://publications.waset.org/abstracts/search?q=Penaeus%20monodon" title=" Penaeus monodon"> Penaeus monodon</a> </p> <a href="https://publications.waset.org/abstracts/40707/interaction-between-kazal-type-serine-proteinase-inhibitor-spipm2-and-cyclophilin-a-from-the-black-tiger-shrimp-penaeus-monodon" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/40707.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">236</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">10528</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">10527</span> Computational Investigation of V599 Mutations of BRAF Protein and Its Control over the Therapeutic Outcome under the Malignant Condition</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mayank">Mayank</a>, <a href="https://publications.waset.org/abstracts/search?q=Navneet%20Kaur"> Navneet Kaur</a>, <a href="https://publications.waset.org/abstracts/search?q=Narinder%20Singh"> Narinder Singh</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The V599 mutations in the BRAF protein are extremely oncogenic, responsible for countless of malignant conditions. Along with wild type, V599E, V599D, and V599R are the important mutated variants of the BRAF proteins. The BRAF inhibitory anticancer agents are continuously developing, and sorafenib is a BRAF inhibitor that is under clinical use. The crystal structure of sorafenib bounded to wild type, and V599 is known, showing a similar interaction pattern in both the case. The mutated 599th residue, in both the case, is also found not interacting directly with the co-crystallized sorafenib molecule. However, the IC50 value of sorafenib was found extremely different in both the case, i.e., 22 nmol/L for wild and 38 nmol/L for V599E protein. Molecular docking study and MMGBSA binding energy results also revealed a significant difference in the binding pattern of sorafenib in both the case. Therefore, to explore the role of distinctively situated 599th residue, we have further conducted comprehensive computational studies. The molecular dynamics simulation, residue interaction network (RIN) analysis, and residue correlation study results revealed the importance of the 599th residue on the therapeutic outcome and overall dynamic of the BRAF protein. Therefore, although the position of 599th residue is very much distinctive from the ligand-binding cavity of BRAF, still it has exceptional control over the overall functional outcome of the protein. The insight obtained here may seem extremely important and guide us while designing ideal BRAF inhibitory anticancer molecules. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=BRAF" title="BRAF">BRAF</a>, <a href="https://publications.waset.org/abstracts/search?q=oncogenic" title=" oncogenic"> oncogenic</a>, <a href="https://publications.waset.org/abstracts/search?q=sorafenib" title=" sorafenib"> sorafenib</a>, <a href="https://publications.waset.org/abstracts/search?q=computational%20studies" title=" computational studies"> computational studies</a> </p> <a href="https://publications.waset.org/abstracts/117283/computational-investigation-of-v599-mutations-of-braf-protein-and-its-control-over-the-therapeutic-outcome-under-the-malignant-condition" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/117283.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">115</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">10526</span> Fluorescence Spectroscopy of Lysozyme-Silver Nanoparticles Complex </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Shahnaz%20Ashrafpour">Shahnaz Ashrafpour</a>, <a href="https://publications.waset.org/abstracts/search?q=Tahereh%20Tohidi%20Moghadam"> Tahereh Tohidi Moghadam</a>, <a href="https://publications.waset.org/abstracts/search?q=Bijan%20Ranjbar"> Bijan Ranjbar</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Identifying the nature of protein-nanoparticle interactions and favored binding sites is an important issue in functional characterization of biomolecules and their physiological responses. Herein, interaction of silver nanoparticles with lysozyme as a model protein has been monitored via fluorescence spectroscopy. Formation of complex between the biomolecule and silver nanoparticles (AgNPs) induced a steady state reduction in the fluorescence intensity of protein at different concentrations of nanoparticles. Tryptophan fluorescence quenching spectra suggested that silver nanoparticles act as a foreign quencher, approaching the protein via this residue. Analysis of the Stern-Volmer plot showed quenching constant of 3.73 µM−1. Moreover, a single binding site in lysozyme is suggested to play role during interaction with AgNPs, having low affinity of binding compared to gold nanoparticles. Unfolding studies of lysozyme showed that complex of lysozyme-AgNPs has not undergone structural perturbations compared to the bare protein. Results of this effort will pave the way for utilization of sensitive spectroscopic techniques for rational design of nanobiomaterials in biomedical applications. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=nanocarrier" title="nanocarrier">nanocarrier</a>, <a href="https://publications.waset.org/abstracts/search?q=nanoparticles" title=" nanoparticles"> nanoparticles</a>, <a href="https://publications.waset.org/abstracts/search?q=surface%20plasmon%20resonance" title=" surface plasmon resonance"> surface plasmon resonance</a>, <a href="https://publications.waset.org/abstracts/search?q=quenching%20fluorescence" title=" quenching fluorescence"> quenching fluorescence</a> </p> <a href="https://publications.waset.org/abstracts/14481/fluorescence-spectroscopy-of-lysozyme-silver-nanoparticles-complex" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/14481.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">330</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">10525</span> Ratio Energy and Protein of Dietary Based on Rice Straw Ammoniated on Productivity of Male Simenthal Cattle</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mardiati%20Zain">Mardiati Zain</a>, <a href="https://publications.waset.org/abstracts/search?q=Yetti%20Marlida"> Yetti Marlida</a>, <a href="https://publications.waset.org/abstracts/search?q=Elihasridas%20Elihasridas"> Elihasridas Elihasridas</a>, <a href="https://publications.waset.org/abstracts/search?q=Erpomen%20Erpomen"> Erpomen Erpomen</a>, <a href="https://publications.waset.org/abstracts/search?q=Andri%20Andri"> Andri Andri</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Background: Livestock productivity is greatly influenced by the energy and protein balance in diet. This study aimed to determine the energy and protein balance of male Simenthal cattle diet with protein and energy levels. The experimental design used was a randomized block design (RBD) 2x3x3 factorial design. There are two factors namely A level of energy diet that is 65% and 70% TDN. Factor B is a protein level of diet used were 10, 12 and 14% and each treatment is repeated three times. The weight of Simenthal cattle used ranged between 240 - 300 kg. Diet consisted of ammoniated rice straw and concentrated with ratio 40:60. Concentrate consisted of palm kernel cake, rice brain, cassava, mineral, and urea. The variables measured were digestibility of dry matter, organic matter and fiber, dry matter intake, daily gain, feed efficiency and blood characteristic. Results: There was no interaction between protein and energy level of diet on the nutrients intake (DM intake, OM intake, CP intake), weight gain and efficiency (P < 0.01). There was an interaction between protein and energy level of diet on digestibility (DM, OM, CP and allantoin urine (P > 0.01) Nutrients intake decreases with increasing levels of energy and protein diet, while nutrient digestibility, Avarage daily gain and feed efficiency increases with increasing levels of energy and protein diet. Conclusions: The result can be concluded that the best treatment was A2B1 which is energy level 70% TDN and protein 10%, where are dry matter intake 7.66 kg/d, daily gain 1.25 kg/d, feed efficiency 16.12%, and dry matter and organic matter digestibility 64.08 and 69.42% respectively. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=energy%20and%20protein%20ratio" title="energy and protein ratio">energy and protein ratio</a>, <a href="https://publications.waset.org/abstracts/search?q=simenthal%20cattle" title=" simenthal cattle"> simenthal cattle</a>, <a href="https://publications.waset.org/abstracts/search?q=rice%20straw%20ammoniated" title=" rice straw ammoniated"> rice straw ammoniated</a>, <a href="https://publications.waset.org/abstracts/search?q=digestibility" title=" digestibility"> digestibility</a> </p> <a href="https://publications.waset.org/abstracts/87342/ratio-energy-and-protein-of-dietary-based-on-rice-straw-ammoniated-on-productivity-of-male-simenthal-cattle" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/87342.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">356</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">10524</span> Predicting Potential Protein Therapeutic Candidates from the Gut Microbiome </h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Prasanna%20Ramachandran">Prasanna Ramachandran</a>, <a href="https://publications.waset.org/abstracts/search?q=Kareem%20Graham"> Kareem Graham</a>, <a href="https://publications.waset.org/abstracts/search?q=Helena%20Kiefel"> Helena Kiefel</a>, <a href="https://publications.waset.org/abstracts/search?q=Sunit%20Jain"> Sunit Jain</a>, <a href="https://publications.waset.org/abstracts/search?q=Todd%20DeSantis"> Todd DeSantis</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Microbes that reside inside the mammalian GI tract, commonly referred to as the gut microbiome, have been shown to have therapeutic effects in animal models of disease. We hypothesize that specific proteins produced by these microbes are responsible for this activity and may be used directly as therapeutics. To speed up the discovery of these key proteins from the big-data metagenomics, we have applied machine learning techniques. Using amino acid sequences of known epitopes and their corresponding binding partners, protein interaction descriptors (PID) were calculated, making a positive interaction set. A negative interaction dataset was calculated using sequences of proteins known not to interact with these same binding partners. Using Random Forest and positive and negative PID, a machine learning model was trained and used to predict interacting versus non-interacting proteins. Furthermore, the continuous variable, cosine similarity in the interaction descriptors was used to rank bacterial therapeutic candidates. Laboratory binding assays were conducted to test the candidates for their potential as therapeutics. Results from binding assays reveal the accuracy of the machine learning prediction and are subsequently used to further improve the model. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=protein-interactions" title="protein-interactions">protein-interactions</a>, <a href="https://publications.waset.org/abstracts/search?q=machine-learning" title=" machine-learning"> machine-learning</a>, <a href="https://publications.waset.org/abstracts/search?q=metagenomics" title=" metagenomics"> metagenomics</a>, <a href="https://publications.waset.org/abstracts/search?q=microbiome" title=" microbiome"> microbiome</a> </p> <a href="https://publications.waset.org/abstracts/62501/predicting-potential-protein-therapeutic-candidates-from-the-gut-microbiome" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/62501.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">376</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">10523</span> Suggestion for Malware Detection Agent Considering Network Environment</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ji-Hoon%20Hong">Ji-Hoon Hong</a>, <a href="https://publications.waset.org/abstracts/search?q=Dong-Hee%20Kim"> Dong-Hee Kim</a>, <a href="https://publications.waset.org/abstracts/search?q=Nam-Uk%20Kim"> Nam-Uk Kim</a>, <a href="https://publications.waset.org/abstracts/search?q=Tai-Myoung%20Chung"> Tai-Myoung Chung</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Smartphone users are increasing rapidly. Accordingly, many companies are running BYOD (Bring Your Own Device: Policies to bring private-smartphones to the company) policy to increase work efficiency. However, smartphones are always under the threat of malware, thus the company network that is connected smartphone is exposed to serious risks. Most smartphone malware detection techniques are to perform an independent detection (perform the detection of a single target application). In this paper, we analyzed a variety of intrusion detection techniques. Based on the results of analysis propose an agent using the network IDS. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=android%20malware%20detection" title="android malware detection">android malware detection</a>, <a href="https://publications.waset.org/abstracts/search?q=software-defined%20network" title=" software-defined network"> software-defined network</a>, <a href="https://publications.waset.org/abstracts/search?q=interaction%20environment" title=" interaction environment"> interaction environment</a>, <a href="https://publications.waset.org/abstracts/search?q=android%20malware%20detection" title=" android malware detection"> android malware detection</a>, <a href="https://publications.waset.org/abstracts/search?q=software-defined%20network" title=" software-defined network"> software-defined network</a>, <a href="https://publications.waset.org/abstracts/search?q=interaction%20environment" title=" interaction environment"> interaction environment</a> </p> <a href="https://publications.waset.org/abstracts/39330/suggestion-for-malware-detection-agent-considering-network-environment" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/39330.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">433</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">10522</span> Lentil Protein Fortification in Cranberry Squash</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Sandhya%20Devi%20A">Sandhya Devi A</a> </p> <p class="card-text"><strong>Abstract:</strong></p> The protein content of the cranberry squash (protein: 0g) may be increased by extracting protein from the lentils (9 g), which is particularly linked to a lower risk of developing heart disease. Using the technique of alkaline extraction from the lentils flour, protein may be extracted. Alkaline extraction of protein from lentil flour was optimized utilizing response surface approach in order to maximize both protein content and yield. Cranberry squash may be taken if a protein fortification syrup is prepared and processed into the squash. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=alkaline%20extraction" title="alkaline extraction">alkaline extraction</a>, <a href="https://publications.waset.org/abstracts/search?q=cranberry%20squash" title=" cranberry squash"> cranberry squash</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20fortification" title=" protein fortification"> protein fortification</a>, <a href="https://publications.waset.org/abstracts/search?q=response%20surface%20methodology" title=" response surface methodology"> response surface methodology</a> </p> <a href="https://publications.waset.org/abstracts/153178/lentil-protein-fortification-in-cranberry-squash" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/153178.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">10521</span> The Impact of Different Rhizobium leguminosarum Strains on the Protein Content of Peas and Broad Beans</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Alise%20Senberga">Alise Senberga</a>, <a href="https://publications.waset.org/abstracts/search?q=Laila%20Dubova"> Laila Dubova</a>, <a href="https://publications.waset.org/abstracts/search?q=Liene%20Strauta"> Liene Strauta</a>, <a href="https://publications.waset.org/abstracts/search?q=Ina%20Alsina"> Ina Alsina</a>, <a href="https://publications.waset.org/abstracts/search?q=Ieva%20Erdberga"> Ieva Erdberga</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Legume symbiotic relationship with nitrogen fixating bacteria Rhizobim leguminosarum is an important factor used to improve the productivity of legumes, due to the fact that rhizobia can supply plant with the necessary amount of nitrogen. R. leguminosarum strains have shown different activity in fixing nitrogen. Depending on the chosen R. leguminosarum strain, host plant biochemical content can be altered. In this study we focused particularly on the changes in protein content in beans (using two different varieties) and peas (five different varieties) due to the use of several different R. leguminosarum strains (four strains for both beans and peas). Overall, the protein content increase was observed after seed inoculation with R. leguminosarum. Strain and plant cultivar interaction specification was observed. The effect of R. leguminosarum inoculation on the content of protein was dependent on the R. leguminosarum strain used. Plant cultivar also appeared to have a decisive role in protein content formation with the help of R. leguminosaru. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=legumes" title="legumes">legumes</a>, <a href="https://publications.waset.org/abstracts/search?q=protein%20content" title=" protein content"> protein content</a>, <a href="https://publications.waset.org/abstracts/search?q=rhizobia%20strains" title=" rhizobia strains"> rhizobia strains</a>, <a href="https://publications.waset.org/abstracts/search?q=soil" title=" soil"> soil</a> </p> <a href="https://publications.waset.org/abstracts/27686/the-impact-of-different-rhizobium-leguminosarum-strains-on-the-protein-content-of-peas-and-broad-beans" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/27686.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">522</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">10520</span> Interaction Effects of Dietary Ginger, Zingiber Officinale, on Plasma Protein Fractions in Rainbow Trout, Oncorhynchus Mykiss</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ali%20Taheri%20Mirghaed">Ali Taheri Mirghaed</a>, <a href="https://publications.waset.org/abstracts/search?q=Sara%20Ahani"> Sara Ahani</a>, <a href="https://publications.waset.org/abstracts/search?q=Ashkan%20Zargar"> Ashkan Zargar</a>, <a href="https://publications.waset.org/abstracts/search?q=Seyyed%20Morteza%20Hoseini"> Seyyed Morteza Hoseini</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Diseases are the major challenges in intensive aquaculture that cause significant annual losses. Antibiotic-therapy is a common way to control bacterial disease in fish, and oxytetracycline (OTC) is the only oral antibiotic in aquaculture approved FDA. OTC has been found to have negative effects on fish, such as oxidative stress and immune-suppression, thus, it is necessary to mitigate such effects. Medicinal herbs have various benefits on fish, including antioxidant, immunostimulant, and anti-microbial effects. Therefore, we hypothesized if dietary ginger meal (GM) interacts with dietary OTC by monitoring plasma protein fractions in rainbow trout. The study was conducted as a 2 × 2 factorial design, including diets containing 0 and 1% GM and 0 and 1.66 % OTC (corresponding to 100 mg/kg fish biomass per day). After ten days treating the fish (60 g individual weight) with these feeds, blood samples were taken from al treatments (n =3). Plasma was separated by centrifugation, and protein fractions were determined by electrophoresis. The results showed that OTC and GM had interaction effects on total protein (P<0.001), albumin (P<0.001), alpha-1 fraction (P=0.010), alpha-2 fraction (P=0.001), beta-2 fraction (P=0.014), and gamma fraction (P<0.001). Beta-1 fraction was significantly (P=0.030) affected by dietary GM. GM decreased plasma total protein, albumin, and beta-2 but increased beta-1 fraction. OTC significantly decreased total protein (P<0.001), albumin (P=0.001), alpha-2 fraction (P<0.001), beta-2 fraction (P=0.004), and gamma fraction (P<0.001) but had no significant effects on alpha-1 and beta-1 fractions. Dietary GM inhibited/suppressed the effects of dietary OTC on the plasma total protein and protein fractions. In conclusion, adding 1% GM to diet can mitigate the negative effects of dietary OTC on plasma proteins. Thus, GM may boost health of rainbow trout during the period of medication with OTC. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=ginger" title="ginger">ginger</a>, <a href="https://publications.waset.org/abstracts/search?q=plasma%20protein%20electrophoresis" title=" plasma protein electrophoresis"> plasma protein electrophoresis</a>, <a href="https://publications.waset.org/abstracts/search?q=dietary%20additive" title=" dietary additive"> dietary additive</a>, <a href="https://publications.waset.org/abstracts/search?q=rainbow%20trout" title=" rainbow trout"> rainbow trout</a> </p> <a href="https://publications.waset.org/abstracts/170310/interaction-effects-of-dietary-ginger-zingiber-officinale-on-plasma-protein-fractions-in-rainbow-trout-oncorhynchus-mykiss" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/170310.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">93</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">10519</span> Encapsulation and Protection of Bioactive Nutrients Based on Ligand-Binding Property of Milk Proteins</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Hao%20Cheng">Hao Cheng</a>, <a href="https://publications.waset.org/abstracts/search?q=Yingzhou%20Ni"> Yingzhou Ni</a>, <a href="https://publications.waset.org/abstracts/search?q=Amr%20M.%20Bakry"> Amr M. Bakry</a>, <a href="https://publications.waset.org/abstracts/search?q=Li%20Liang"> Li Liang</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Functional foods containing bioactive nutrients offer benefits beyond basic nutrition and hence the possibility of delaying and preventing chronic diseases. However, many bioactive nutrients degrade rapidly under food processing and storage conditions. Encapsulation can be used to overcome these limitations. Food proteins have been widely used as carrier materials for the preparation of nano/micro-particles because of their ability to form gels and emulsions and to interact with polysaccharides. The mechanisms of interaction between bioactive nutrients and proteins must be understood in order to develop protein-based lipid-free delivery systems. Beta-lactoglobulin, a small globular protein in milk whey, exhibits an affinity to a wide range of compounds. Alfa-tocopherol, resveratrol and folic acid were respectively bound to the central cavity, the outer surface near Trp19–Arg124 and the hydrophobic pocket in the groove between the alfa-helix and the beta-barrel of the protein. Beta-lactoglobulin could thus bind the three bioactive nutrients simultaneously to form protein-multi-ligand complexes. Beta-casein, an intrinsically unstructured but major milk protein, could also interact with resveratrol and folic acid to form complexes. These results suggest the potential to develop milk-protein-based complex carrier systems for encapsulation of multiple bioactive nutrients for functional food application and also pharmaceutical and medical uses. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=milk%20protein" title="milk protein">milk protein</a>, <a href="https://publications.waset.org/abstracts/search?q=bioactive%20nutrient" title=" bioactive nutrient"> bioactive nutrient</a>, <a href="https://publications.waset.org/abstracts/search?q=interaction" title=" interaction"> interaction</a>, <a href="https://publications.waset.org/abstracts/search?q=protection" title=" protection"> protection</a> </p> <a href="https://publications.waset.org/abstracts/32528/encapsulation-and-protection-of-bioactive-nutrients-based-on-ligand-binding-property-of-milk-proteins" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/32528.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">412</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">10518</span> Hydration of Protein-RNA Recognition Sites</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Amita%20Barik">Amita Barik</a>, <a href="https://publications.waset.org/abstracts/search?q=Ranjit%20Prasad%20Bahadur"> Ranjit Prasad Bahadur</a> </p> <p class="card-text"><strong>Abstract:</strong></p> We investigate the role of water molecules in 89 protein-RNA complexes taken from the Protein Data Bank. Those with tRNA and single-stranded RNA are less hydrated than with duplex or ribosomal proteins. Protein-RNA interfaces are hydrated less than protein-DNA interfaces, but more than protein-protein interfaces. Majority of the waters at protein-RNA interfaces makes multiple H-bonds; however, a fraction does not make any. Those making Hbonds have preferences for the polar groups of RNA than its partner protein. The spatial distribution of waters makes interfaces with ribosomal proteins and single-stranded RNA relatively ‘dry’ than interfaces with tRNA and duplex RNA. In contrast to protein-DNA interfaces, mainly due to the presence of the 2’OH, the ribose in protein-RNA interfaces is hydrated more than the phosphate or the bases. The minor groove in protein-RNA interfaces is hydrated more than the major groove, while in protein-DNA interfaces it is reverse. The strands make the highest number of water-mediated H-bonds per unit interface area followed by the helices and the non-regular structures. The preserved waters at protein-RNA interfaces make higher number of H-bonds than the other waters. Preserved waters contribute toward the affinity in protein-RNA recognition and should be carefully treated while engineering protein-RNA interfaces. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=h-bonds" title="h-bonds">h-bonds</a>, <a href="https://publications.waset.org/abstracts/search?q=minor-major%20grooves" title=" minor-major grooves"> minor-major grooves</a>, <a href="https://publications.waset.org/abstracts/search?q=preserved%20water" title=" preserved water"> preserved water</a>, <a href="https://publications.waset.org/abstracts/search?q=protein-RNA%20interfaces" title=" protein-RNA interfaces"> protein-RNA interfaces</a> </p> <a href="https://publications.waset.org/abstracts/42932/hydration-of-protein-rna-recognition-sites" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/42932.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">302</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">10517</span> Bioinformatic Prediction of Hub Genes by Analysis of Signaling Pathways, Transcriptional Regulatory Networks and DNA Methylation Pattern in Colon Cancer</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Ankan%20Roy">Ankan Roy</a>, <a href="https://publications.waset.org/abstracts/search?q=Niharika"> Niharika</a>, <a href="https://publications.waset.org/abstracts/search?q=Samir%20Kumar%20Patra"> Samir Kumar Patra</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Anomalous nexus of complex topological assemblies and spatiotemporal epigenetic choreography at chromosomal territory may forms the most sophisticated regulatory layer of gene expression in cancer. Colon cancer is one of the leading malignant neoplasms of the lower gastrointestinal tract worldwide. There is still a paucity of information about the complex molecular mechanisms of colonic cancerogenesis. Bioinformatics prediction and analysis helps to identify essential genes and significant pathways for monitoring and conquering this deadly disease. The present study investigates and explores potential hub genes as biomarkers and effective therapeutic targets for colon cancer treatment. Colon cancer patient sample containing gene expression profile datasets, such as GSE44076, GSE20916, and GSE37364 were downloaded from Gene Expression Omnibus (GEO) database and thoroughly screened using the GEO2R tool and Funrich software to find out common 2 differentially expressed genes (DEGs). Other approaches, including Gene Ontology (GO) and KEGG pathway analysis, Protein-Protein Interaction (PPI) network construction and hub gene investigation, Overall Survival (OS) analysis, gene correlation analysis, methylation pattern analysis, and hub gene-Transcription factors regulatory network construction, were performed and validated using various bioinformatics tool. Initially, we identified 166 DEGs, including 68 up-regulated and 98 down-regulated genes. Up-regulated genes are mainly associated with the Cytokine-cytokine receptor interaction, IL17 signaling pathway, ECM-receptor interaction, Focal adhesion and PI3K-Akt pathway. Downregulated genes are enriched in metabolic pathways, retinol metabolism, Steroid hormone biosynthesis, and bile secretion. From the protein-protein interaction network, thirty hub genes with high connectivity are selected using the MCODE and cytoHubba plugin. Survival analysis, expression validation, correlation analysis, and methylation pattern analysis were further verified using TCGA data. Finally, we predicted COL1A1, COL1A2, COL4A1, SPP1, SPARC, and THBS2 as potential master regulators in colonic cancerogenesis. Moreover, our experimental data highlights that disruption of lipid raft and RAS/MAPK signaling cascade affects this gene hub at mRNA level. We identified COL1A1, COL1A2, COL4A1, SPP1, SPARC, and THBS2 as determinant hub genes in colon cancer progression. They can be considered as biomarkers for diagnosis and promising therapeutic targets in colon cancer treatment. Additionally, our experimental data advertise that signaling pathway act as connecting link between membrane hub and gene hub. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=hub%20genes" title="hub genes">hub genes</a>, <a href="https://publications.waset.org/abstracts/search?q=colon%20cancer" title=" colon cancer"> colon cancer</a>, <a href="https://publications.waset.org/abstracts/search?q=DNA%20methylation" title=" DNA methylation"> DNA methylation</a>, <a href="https://publications.waset.org/abstracts/search?q=epigenetic%20engineering" title=" epigenetic engineering"> epigenetic engineering</a>, <a href="https://publications.waset.org/abstracts/search?q=bioinformatic%20predictions" title=" bioinformatic predictions"> bioinformatic predictions</a> </p> <a href="https://publications.waset.org/abstracts/152788/bioinformatic-prediction-of-hub-genes-by-analysis-of-signaling-pathways-transcriptional-regulatory-networks-and-dna-methylation-pattern-in-colon-cancer" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/152788.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">128</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">10516</span> Identification of Significant Genes in Rheumatoid Arthritis, Melanoma Metastasis, Ulcerative Colitis and Crohn’s Disease</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Krishna%20Pal%20Singh">Krishna Pal Singh</a>, <a href="https://publications.waset.org/abstracts/search?q=Shailendra%20Kumar%20Gupta"> Shailendra Kumar Gupta</a>, <a href="https://publications.waset.org/abstracts/search?q=Olaf%20Wolkenhauer"> Olaf Wolkenhauer</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Background: Our study aimed to identify common genes and potential targets across the four diseases, which include rheumatoid arthritis, melanoma metastasis, ulcerative colitis, and Crohn’s disease. We used a network and systems biology approach to identify the hub gene, which can act as a potential target for all four disease conditions. The regulatory network was extracted from the PPI using the MCODE module present in Cytoscape. Our objective was to investigate the significance of hub genes in these diseases using gene ontology and KEGG pathway enrichment analysis. Methods: Our methodology involved collecting disease gene-related information from DisGeNET databases and performing protein-protein interaction (PPI) network and core genes screening. We then conducted gene ontology and KEGG pathway enrichment analysis. Results: We found that IL6 plays a critical role in all disease conditions and in different pathways that can be associated with the development of all four diseases. Conclusions: The theoretical importance of our research is that we employed various systems and structural biology techniques to identify a crucial protein that could serve as a promising target for treating multiple diseases. Our data collection and analysis procedures involved rigorous scrutiny, ensuring high-quality results. Our conclusion is that IL6 plays a significant role in all four diseases, and it can act as a potential target for treating them. Our findings may have important implications for the development of novel therapeutic interventions for these diseases. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=melanoma%20metastasis" title="melanoma metastasis">melanoma metastasis</a>, <a href="https://publications.waset.org/abstracts/search?q=rheumatoid%20arthritis" title=" rheumatoid arthritis"> rheumatoid arthritis</a>, <a href="https://publications.waset.org/abstracts/search?q=inflammatory%20bowel%20diseases" title=" inflammatory bowel diseases"> inflammatory bowel diseases</a>, <a href="https://publications.waset.org/abstracts/search?q=integrated%20bioinformatics%20analysis" title=" integrated bioinformatics analysis"> integrated bioinformatics analysis</a> </p> <a href="https://publications.waset.org/abstracts/168255/identification-of-significant-genes-in-rheumatoid-arthritis-melanoma-metastasis-ulcerative-colitis-and-crohns-disease" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/168255.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">90</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">10515</span> The Effect of Sorafenibe on Soat1 Protein by Using Molecular Docking Method</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Mahdiyeh%20Gholaminezhad">Mahdiyeh Gholaminezhad</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Context: The study focuses on the potential impact of Sorafenib on SOAT1 protein in liver cancer treatment, addressing the need for more effective therapeutic options. Research aim: To explore the effects of Sorafenib on the activity of SOAT1 protein in liver cancer cells. Methodology: Molecular docking was employed to analyze the interaction between Sorafenib and SOAT1 protein. Findings: The study revealed a significant effect of Sorafenib on the stability and activity of SOAT1 protein, suggesting its potential as a treatment for liver cancer. Theoretical importance: This research highlights the molecular mechanism underlying Sorafenib's anti-cancer properties, contributing to the understanding of its therapeutic effects. Data collection: Data on the molecular structure of Sorafenib and SOAT1 protein were obtained from computational simulations and databases. Analysis procedures: Molecular docking simulations were performed to predict the binding interactions between Sorafenib and SOAT1 protein. Question addressed: How does Sorafenib influence the activity of SOAT1 protein and what are the implications for liver cancer treatment? Conclusion: The study demonstrates the potential of Sorafenib as a targeted therapy for liver cancer by affecting the activity of SOAT1 protein. Reviewers' Comments: The study provides valuable insights into the molecular basis of Sorafenib's action on SOAT1 protein, suggesting its therapeutic potential. To enhance the methodology, the authors could consider validating the docking results with experimental data for further validation. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=liver%20cancer" title="liver cancer">liver cancer</a>, <a href="https://publications.waset.org/abstracts/search?q=sorafenib" title=" sorafenib"> sorafenib</a>, <a href="https://publications.waset.org/abstracts/search?q=SOAT1" title=" SOAT1"> SOAT1</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a> </p> <a href="https://publications.waset.org/abstracts/189263/the-effect-of-sorafenibe-on-soat1-protein-by-using-molecular-docking-method" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/189263.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">26</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">10514</span> Role of Estrogen Receptor-alpha in Mammary Carcinoma by Single Nucleotide Polymorphisms and Molecular Docking: An In-silico Analysis</h5> <div class="card-body"> <p class="card-text"><strong>Authors:</strong> <a href="https://publications.waset.org/abstracts/search?q=Asif%20Bilal">Asif Bilal</a>, <a href="https://publications.waset.org/abstracts/search?q=Fouzia%20Tanvir"> Fouzia Tanvir</a>, <a href="https://publications.waset.org/abstracts/search?q=Sibtain%20Ahmad"> Sibtain Ahmad</a> </p> <p class="card-text"><strong>Abstract:</strong></p> Estrogen receptor alpha, also known as estrogen receptor-1, is highly involved in risk of mammary carcinoma. The objectives of this study were to identify non-synonymous SNPs of estrogen receptor and their association with breast cancer and to identify the chemotherapeutic responses of phytochemicals against it via in-silico study design. For this purpose, different online tools. to identify pathogenic SNPs the tools were SIFT, Polyphen, Polyphen-2, fuNTRp, SNAP2, for finding disease associated SNPs the tools SNP&GO, PhD-SNP, PredictSNP, MAPP, SNAP, MetaSNP, PANTHER, and to check protein stability Mu-Pro, I-Mutant, and CONSURF were used. Post-translational modifications (PTMs) were detected by Musitedeep, Protein secondary structure by SOPMA, protein to protein interaction by STRING, molecular docking by PyRx. Seven SNPs having rsIDs (rs760766066, rs779180038, rs956399300, rs773683317, rs397509428, rs755020320, and rs1131692059) showing mutations on I229T, R243C, Y246H, P336R, Q375H, R394S, and R394H, respectively found to be completely deleterious. The PTMs found were 96 times Glycosylation; 30 times Ubiquitination, a single time Acetylation; and no Hydroxylation and Phosphorylation were found. The protein secondary structure consisted of Alpha helix (Hh) is (28%), Extended strand (Ee) is (21%), Beta turn (Tt) is 7.89% and Random coil (Cc) is (44.11%). Protein-protein interaction analysis revealed that it has strong interaction with Myeloperoxidase, Xanthine dehydrogenase, carboxylesterase 1, Glutathione S-transferase Mu 1, and with estrogen receptors. For molecular docking we used Asiaticoside, Ilekudinuside, Robustoflavone, Irinoticane, Withanolides, and 9-amin0-5 as ligands that extract from phytochemicals and docked with this protein. We found that there was great interaction (from -8.6 to -9.7) of these ligands of phytochemicals at ESR1 wild and two mutants (I229T and R394S). It is concluded that these SNPs found in ESR1 are involved in breast cancer and given phytochemicals are highly helpful against breast cancer as chemotherapeutic agents. Further in vitro and in vivo analysis should be performed to conduct these interactions. <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/abstracts/search?q=breast%20cancer" title="breast cancer">breast cancer</a>, <a href="https://publications.waset.org/abstracts/search?q=ESR1" title=" ESR1"> ESR1</a>, <a href="https://publications.waset.org/abstracts/search?q=phytochemicals" title=" phytochemicals"> phytochemicals</a>, <a href="https://publications.waset.org/abstracts/search?q=molecular%20docking" title=" molecular docking"> molecular docking</a> </p> <a href="https://publications.waset.org/abstracts/175362/role-of-estrogen-receptor-alpha-in-mammary-carcinoma-by-single-nucleotide-polymorphisms-and-molecular-docking-an-in-silico-analysis" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/abstracts/175362.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 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