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Hub Promiscuity in Protein-Protein Interaction Networks

Hubs are proteins with a large number of interactions in a protein-protein interaction network. They are the principal agents in the interaction network and affect its function and stability. Their specific recognition of many different protein partners is of great interest from the structural viewp...

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Detalles Bibliográficos
Autores principales: Patil, Ashwini, Kinoshita, Kengo, Nakamura, Haruki
Formato: Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2871146/
https://www.ncbi.nlm.nih.gov/pubmed/20480050
http://dx.doi.org/10.3390/ijms11041930
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author Patil, Ashwini
Kinoshita, Kengo
Nakamura, Haruki
author_facet Patil, Ashwini
Kinoshita, Kengo
Nakamura, Haruki
author_sort Patil, Ashwini
collection PubMed
description Hubs are proteins with a large number of interactions in a protein-protein interaction network. They are the principal agents in the interaction network and affect its function and stability. Their specific recognition of many different protein partners is of great interest from the structural viewpoint. Over the last few years, the structural properties of hubs have been extensively studied. We review the currently known features that are particular to hubs, possibly affecting their binding ability. Specifically, we look at the levels of intrinsic disorder, surface charge and domain distribution in hubs, as compared to non-hubs, along with differences in their functional domains.
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spelling pubmed-28711462010-05-17 Hub Promiscuity in Protein-Protein Interaction Networks Patil, Ashwini Kinoshita, Kengo Nakamura, Haruki Int J Mol Sci Review Hubs are proteins with a large number of interactions in a protein-protein interaction network. They are the principal agents in the interaction network and affect its function and stability. Their specific recognition of many different protein partners is of great interest from the structural viewpoint. Over the last few years, the structural properties of hubs have been extensively studied. We review the currently known features that are particular to hubs, possibly affecting their binding ability. Specifically, we look at the levels of intrinsic disorder, surface charge and domain distribution in hubs, as compared to non-hubs, along with differences in their functional domains. Molecular Diversity Preservation International (MDPI) 2010-04-26 /pmc/articles/PMC2871146/ /pubmed/20480050 http://dx.doi.org/10.3390/ijms11041930 Text en © 2010 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0 This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Patil, Ashwini
Kinoshita, Kengo
Nakamura, Haruki
Hub Promiscuity in Protein-Protein Interaction Networks
title Hub Promiscuity in Protein-Protein Interaction Networks
title_full Hub Promiscuity in Protein-Protein Interaction Networks
title_fullStr Hub Promiscuity in Protein-Protein Interaction Networks
title_full_unstemmed Hub Promiscuity in Protein-Protein Interaction Networks
title_short Hub Promiscuity in Protein-Protein Interaction Networks
title_sort hub promiscuity in protein-protein interaction networks
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2871146/
https://www.ncbi.nlm.nih.gov/pubmed/20480050
http://dx.doi.org/10.3390/ijms11041930
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