Literature DB >> 26402567

Intrinsically disordered proteins: emerging interaction specialists.

Peter Tompa1, Eva Schad2, Agnes Tantos2, Lajos Kalmar2.   

Abstract

Intrinsically disordered proteins or regions of proteins (IDPs/IDRs) most often function through protein-protein interactions, when they permanently or transiently bind partner molecules with diverse functional consequences. There is a rapid advance in our understanding of the ensuing functional modes, obtained from describing atomic details of individual complexes, proteome-wide studies of interactomes and characterizing loosely assembled hydrogels and tightly packed amyloids. Here we briefly survey the most important recent methodological developments and structural-functional observations, with the aim of increasing the general appreciation of IDPs/IDRs as 'interaction specialists'.
Copyright © 2015 Elsevier Ltd. All rights reserved.

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Year:  2015        PMID: 26402567     DOI: 10.1016/j.sbi.2015.08.009

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  72 in total

1.  Structural Basis for the Interaction of a Human Small Heat Shock Protein with the 14-3-3 Universal Signaling Regulator.

Authors:  Nikolai N Sluchanko; Steven Beelen; Alexandra A Kulikova; Stephen D Weeks; Alfred A Antson; Nikolai B Gusev; Sergei V Strelkov
Journal:  Structure       Date:  2017-01-12       Impact factor: 5.006

2.  Large-scale analysis of intrinsic disorder flavors and associated functions in the protein sequence universe.

Authors:  Marco Necci; Damiano Piovesan; Silvio C E Tosatto
Journal:  Protein Sci       Date:  2016-10-25       Impact factor: 6.725

Review 3.  Features of molecular recognition of intrinsically disordered proteins via coupled folding and binding.

Authors:  Jing Yang; Meng Gao; Junwen Xiong; Zhengding Su; Yongqi Huang
Journal:  Protein Sci       Date:  2019-09-04       Impact factor: 6.725

Review 4.  The Structural and Functional Diversity of Intrinsically Disordered Regions in Transmembrane Proteins.

Authors:  Rajeswari Appadurai; Vladimir N Uversky; Anand Srivastava
Journal:  J Membr Biol       Date:  2019-05-28       Impact factor: 1.843

5.  The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins.

Authors:  John A Carver; Aidan B Grosas; Heath Ecroyd; Roy A Quinlan
Journal:  Cell Stress Chaperones       Date:  2017-04-08       Impact factor: 3.667

6.  The Intrinsically Disordered Protein CARP9 Bridges HYL1 to AGO1 in the Nucleus to Promote MicroRNA Activity.

Authors:  Ariel H Tomassi; Delfina A Re; Facundo Romani; Damian A Cambiagno; Lucía Gonzalo; Javier E Moreno; Agustin L Arce; Pablo A Manavella
Journal:  Plant Physiol       Date:  2020-07-07       Impact factor: 8.340

7.  Structural Basis for Recombinatorial Permissiveness in the Generation of Anaplasma marginale Msp2 Antigenic Variants.

Authors:  Telmo Graça; Marta G Silva; Alla S Kostyukova; Guy H Palmer
Journal:  Infect Immun       Date:  2016-09-19       Impact factor: 3.441

8.  Neuronal pathophysiology featuring PrPC and its control over Ca2+ metabolism.

Authors:  Alessandro Bertoli; M Catia Sorgato
Journal:  Prion       Date:  2018-01-05       Impact factor: 3.931

Review 9.  The Tail That Wags the Dog: How the Disordered C-Terminal Domain Controls the Transcriptional Activities of the p53 Tumor-Suppressor Protein.

Authors:  Oleg Laptenko; David R Tong; James Manfredi; Carol Prives
Journal:  Trends Biochem Sci       Date:  2016-09-23       Impact factor: 13.807

10.  Dynamical Oligomerisation of Histidine Rich Intrinsically Disordered ProteinS Is Regulated through Zinc-Histidine Interactions.

Authors:  Carolina Cragnell; Lasse Staby; Samuel Lenton; Birthe B Kragelund; Marie Skepö
Journal:  Biomolecules       Date:  2019-04-30
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