Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function.
about
Order, Disorder, and Everything in BetweenThe contribution of intrinsically disordered regions to protein function, cellular complexity, and human diseaseFunctional roles of transiently and intrinsically disordered regions within proteinsPost-translationally-modified structures in the autophagy machinery: an integrative perspective.Intrinsic disorder here, there, and everywhere, and nowhere to escape from it.DisProt 7.0: a major update of the database of disordered proteins.Disorder in cholesterol-binding functionality of CRAC peptides: a molecular dynamics study.HdeB functions as an acid-protective chaperone in bacteriaThe activity and stability of the intrinsically disordered Cip/Kip protein family are regulated by non-receptor tyrosine kinases.Protein quality control under oxidative stress conditions.Advances in Understanding Carboxysome Assembly in Prochlorococcus and Synechococcus Implicate CsoS2 as a Critical ComponentDisorder transitions and conformational diversity cooperatively modulate biological function in proteins.Comparative proteomics reveal distinct chaperone-client interactions in supporting bacterial acid resistanceDissecting physical structure of calreticulin, an intrinsically disordered Ca2+-buffering chaperone from endoplasmic reticulum.How do disordered regions achieve comparable functions to structured domains?Asymmetric Modulation of Protein Order-Disorder Transitions by Phosphorylation and Partner Binding.The multifaceted roles of intrinsic disorder in protein complexes.Group 4 late embryogenesis abundant proteins as a model to study intrinsically disordered proteins in plants.Dancing Protein Clouds: The Strange Biology and Chaotic Physics of Intrinsically Disordered Proteins.Disorder in the lifetime of a proteinThe principle of conformational signaling.Digested disorder: Quarterly intrinsic disorder digest (July-August-September, 2013)Evolution of intrinsic disorder in eukaryotic proteins.Resolving the ambiguity: Making sense of intrinsic disorder when PDB structures disagreeUnfoldome variation upon plant-pathogen interactions: strawberry infection by Colletotrichum acutatum.Tripartite degrons confer diversity and specificity on regulated protein degradation in the ubiquitin-proteasome system.Abundance and functional roles of intrinsic disorder in the antimicrobial peptides of the NK-lysin family.Disulfide driven folding for a conditionally disordered protein.Intrinsic Disorder in Proteins with Pathogenic Repeat Expansions.Structure and function of yeast Atg20, a sorting nexin that facilitates autophagy induction.Prediction of protein disorder based on IUPred.Transiently disordered tails accelerate folding of globular proteins.Quantifying Allosteric Communication via Both Concerted Structural Changes and Conformational Disorder with CARDS.IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding.Thermodynamics of Conformational Transitions in a Disordered Protein Backbone Model
P2860
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P2860
Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function.
description
2014 nî lūn-bûn
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2014 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի փետրվարին հրատարակված գիտական հոդված
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2014年の論文
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年學術文章
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name
Conditionally and transiently ...... to regulate protein function.
@ast
Conditionally and transiently ...... to regulate protein function.
@en
type
label
Conditionally and transiently ...... to regulate protein function.
@ast
Conditionally and transiently ...... to regulate protein function.
@en
prefLabel
Conditionally and transiently ...... to regulate protein function.
@ast
Conditionally and transiently ...... to regulate protein function.
@en
P2860
P356
P1433
P1476
Conditionally and transiently ...... to regulate protein function.
@en
P2093
Richard Kriwacki
Ursula Jakob
P2860
P304
P356
10.1021/CR400459C
P577
2014-02-06T00:00:00Z