• Login
    View Item 
    •   Home
    • Office of Sponsored Research (OSR)
    • KAUST Funded Research
    • Publications Acknowledging KAUST Support
    • View Item
    •   Home
    • Office of Sponsored Research (OSR)
    • KAUST Funded Research
    • Publications Acknowledging KAUST Support
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of KAUSTCommunitiesIssue DateSubmit DateThis CollectionIssue DateSubmit Date

    My Account

    Login

    Quick Links

    Open Access PolicyORCID LibguideTheses and Dissertations LibguideSubmit an Item

    Statistics

    Display statistics

    Detecting mutually exclusive interactions in protein-protein interaction maps.

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Thumbnail
    Name:
    PMC3370996.pdf
    Size:
    286.8Kb
    Format:
    PDF
    Description:
    Main article
    Download
    Type
    Article
    Authors
    Sánchez Claros, Carmen
    Tramontano, Anna
    KAUST Grant Number
    KUK-I1-012-43
    Date
    2012-06-08
    Permanent link to this record
    http://hdl.handle.net/10754/596839
    
    Metadata
    Show full item record
    Abstract
    Comprehensive protein interaction maps can complement genetic and biochemical experiments and allow the formulation of new hypotheses to be tested in the system of interest. The computational analysis of the maps may help to focus on interesting cases and thereby to appropriately prioritize the validation experiments. We show here that, by automatically comparing and analyzing structurally similar regions of proteins of known structure interacting with a common partner, it is possible to identify mutually exclusive interactions present in the maps with a sensitivity of 70% and a specificity higher than 85% and that, in about three fourth of the correctly identified complexes, we also correctly recognize at least one residue (five on average) belonging to the interaction interface. Given the present and continuously increasing number of proteins of known structure, the requirement of the knowledge of the structure of the interacting proteins does not substantially impact on the coverage of our strategy that can be estimated to be around 25%. We also introduce here the Estrella server that embodies this strategy, is designed for users interested in validating specific hypotheses about the functional role of a protein-protein interaction and it also allows access to pre-computed data for seven organisms.
    Citation
    Sánchez Claros C, Tramontano A (2012) Detecting Mutually Exclusive Interactions in Protein-Protein Interaction Maps. PLoS ONE 7: e38765. Available: http://dx.doi.org/10.1371/journal.pone.0038765.
    Sponsors
    Award number KUK-I1-012-43 made by King Abdullah University of Science and Technology (KAUST). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
    Publisher
    Public Library of Science (PLoS)
    Journal
    PLoS ONE
    DOI
    10.1371/journal.pone.0038765
    PubMed ID
    22715412
    PubMed Central ID
    PMC3370996
    ae974a485f413a2113503eed53cd6c53
    10.1371/journal.pone.0038765
    Scopus Count
    Collections
    Publications Acknowledging KAUST Support

    entitlement

    Related articles

    • Oligomerisation status and evolutionary conservation of interfaces of protein structural domain superfamilies.
    • Authors: Sukhwal A, Sowdhamini R
    • Issue date: 2013 Jul
    • 3D-partner: a web server to infer interacting partners and binding models.
    • Authors: Chen YC, Lo YS, Hsu WC, Yang JM
    • Issue date: 2007 Jul
    • STRING 8--a global view on proteins and their functional interactions in 630 organisms.
    • Authors: Jensen LJ, Kuhn M, Stark M, Chaffron S, Creevey C, Muller J, Doerks T, Julien P, Roth A, Simonovic M, Bork P, von Mering C
    • Issue date: 2009 Jan
    • Adding biological meaning to human protein-protein interactions identified by yeast two-hybrid screenings: A guide through bioinformatics tools.
    • Authors: Felgueiras J, Silva JV, Fardilha M
    • Issue date: 2018 Jan 16
    • BindML/BindML+: Detecting Protein-Protein Interaction Interface Propensity from Amino Acid Substitution Patterns.
    • Authors: Wei Q, La D, Kihara D
    • Issue date: 2017
    DSpace software copyright © 2002-2023  DuraSpace
    Quick Guide | Contact Us | KAUST University Library
    Open Repository is a service hosted by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items. For anonymous users the allowed maximum amount is 50 search results.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.