Literature DB >> 22012032

Intrinsic protein disorder in human pathways.

Jessica H Fong1, Benjamin A Shoemaker, Anna R Panchenko.   

Abstract

We analyze human-specific KEGG pathways trying to understand the functional role of intrinsic disorder in proteins. Pathways provide a comprehensive picture of biological processes and allow better understanding of a protein's function within the specific context of its surroundings. Our study pinpoints a few specific pathways significantly enriched in disorder-containing proteins and identifies the role of these proteins within the framework of pathway relationships. Three major categories of relations are shown to be significantly enriched in disordered proteins: gene expression, protein binding and to a lesser degree, protein phosphorylation. Finally we find that relations involving protein activation and to some extent inhibition are characterized by low disorder content.

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Year:  2011        PMID: 22012032      PMCID: PMC3584708          DOI: 10.1039/c1mb05274h

Source DB:  PubMed          Journal:  Mol Biosyst        ISSN: 1742-2051


  48 in total

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8.  Intrinsic protein disorder in complete genomes.

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9.  The importance of intrinsic disorder for protein phosphorylation.

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  10 in total

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5.  An N-terminal, 830 residues intrinsically disordered region of the cytoskeleton-regulatory protein supervillin contains Myosin II- and F-actin-binding sites.

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7.  A critical evaluation of in silico methods for detection of membrane protein intrinsic disorder.

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9.  Intrinsic disorder in PTEN and its interactome confers structural plasticity and functional versatility.

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10.  Predicting Protein-Protein Interactions Using BiGGER: Case Studies.

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  10 in total

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