Literature DB >> 25038412

A million peptide motifs for the molecular biologist.

Peter Tompa1, Norman E Davey2, Toby J Gibson3, M Madan Babu4.   

Abstract

A molecular description of functional modules in the cell is the focus of many high-throughput studies in the postgenomic era. A large portion of biomolecular interactions in virtually all cellular processes is mediated by compact interaction modules, referred to as peptide motifs. Such motifs are typically less than ten residues in length, occur within intrinsically disordered regions, and are recognized and/or posttranslationally modified by structured domains of the interacting partner. In this review, we suggest that there might be over a million instances of peptide motifs in the human proteome. While this staggering number suggests that peptide motifs are numerous and the most understudied functional module in the cell, it also holds great opportunities for new discoveries.
Copyright © 2014 Elsevier Inc. All rights reserved.

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Year:  2014        PMID: 25038412     DOI: 10.1016/j.molcel.2014.05.032

Source DB:  PubMed          Journal:  Mol Cell        ISSN: 1097-2765            Impact factor:   17.970


  157 in total

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2.  Protein dynamics: tuning disorder propensity in p53.

Authors:  Richard W Kriwacki
Journal:  Nat Chem Biol       Date:  2014-12       Impact factor: 15.040

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Journal:  J Mol Biol       Date:  2015-10-22       Impact factor: 5.469

Review 5.  Dynamic Protein Interaction Networks and New Structural Paradigms in Signaling.

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Journal:  Mol Cell       Date:  2020-07-08       Impact factor: 17.970

Review 7.  Friend or foe-Post-translational modifications as regulators of phase separation and RNP granule dynamics.

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Journal:  J Biol Chem       Date:  2018-12-26       Impact factor: 5.157

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Journal:  J Cell Sci       Date:  2017-05-05       Impact factor: 5.285

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Authors:  Julianne A Gerdes; Katelynn M Mannix; Andrew M Hudson; Lynn Cooley
Journal:  Genetics       Date:  2020-09-03       Impact factor: 4.562

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