Allostery within a transcription coactivator is predominantly mediated through dissociation rate constants - Wikidata - wikimedia - TriplyDB

Allostery within a transcription coactivator is predominantly mediated through dissociation rate constants

Allostery within a transcription coactivator is predominantly mediated through dissociation rate constants

http://www.wikidata.org/entity/Q34082986

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Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies Binding Mechanisms of Intrinsically Disordered Proteins: Theory, Simulation, and Experiment The contribution of intrinsically disordered regions to protein function, cellular complexity, and human disease Conserved Helix-Flanking Prolines Modulate Intrinsically Disordered Protein:Target Affinity by Altering the Lifetime of the Bound Complex Prepaying the entropic cost for allosteric regulation in KIX Interplay between partner and ligand facilitates the folding and binding of an intrinsically disordered protein Intrinsically disordered proteins in cellular signalling and regulation.Identification of two-step chemical mechanisms using small temperature oscillations and a single tagged species.Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding Functional advantages of dynamic protein disorder.Role of non-native electrostatic interactions in the coupled folding and binding of PUMA with Mcl-1 Molecular Recognition by Templated Folding of an Intrinsically Disordered Protein Role of Intrinsic Protein Disorder in the Function and Interactions of the Transcriptional Coactivators CREB-binding Protein (CBP) and p300 Peptide- and proton-driven allosteric clamps catalyze anthrax toxin translocation across membranes.Disorder drives cooperative folding in a multidomain protein Globular and disordered-the non-identical twins in protein-protein interactions.Targeting transcription is no longer a quixotic quest Plasticity of an ultrafast interaction between nucleoporins and nuclear transport receptors.From Fuzzy to Function: The New Frontier of Protein-Protein Interactions.pKID Binds to KIX via an Unstructured Transition State with Nonnative Interactions.Phosphorylation of the IDP KID Modulates Affinity for KIX by Increasing the Lifetime of the Complex.Deciphering the promiscuous interactions between intrinsically disordered transactivation domains and the KIX domain.How Robust Is the Mechanism of Folding-Upon-Binding for an Intrinsically Disordered Protein?Expanding the Paradigm: Intrinsically Disordered Proteins and Allosteric Regulation Conservation of coactivator engagement mechanism enables small-molecule allosteric modulators

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P2860

Allostery within a transcription coactivator is predominantly mediated through dissociation rate constants

http://www.wikidata.org/entity/Q34082986

description

2014 nî lūn-bûn

@nan

2014 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2014年の論文

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2014年論文

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2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Allostery within a transcripti ...... gh dissociation rate constants

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Allostery within a transcripti ...... gh dissociation rate constants

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Allostery within a transcripti ...... gh dissociation rate constants

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type

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Allostery within a transcripti ...... gh dissociation rate constants

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Allostery within a transcripti ...... gh dissociation rate constants

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Allostery within a transcripti ...... gh dissociation rate constants

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Allostery within a transcripti ...... gh dissociation rate constants

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Allostery within a transcripti ...... gh dissociation rate constants

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P356

PNAS.1405815111

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Allostery within a transcripti ...... gh dissociation rate constants

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P2093

Alexandra J Travis

http://www.w3.org/2001/XMLSchema#string

Jane Clarke

http://www.w3.org/2001/XMLSchema#string

Sarah L Shammas

http://www.w3.org/2001/XMLSchema#string

P2860

Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life

Conformational transitions of adenylate kinase: switching by cracking

Structural and energetic basis of allostery

Ordering a Dynamic Protein Via a Small-Molecule Stabilizer

Allosteric Communication in the KIX Domain Proceeds through Dynamic Repacking of the Hydrophobic Core

Structures of KIX domain of CBP in complex with two FOXO3a transactivation domains reveal promiscuity and plasticity in coactivator recruitment

CBP/p300 in cell growth, transformation, and development

Cooperativity in transcription factor binding to the coactivator CREB-binding protein (CBP). The mixed lineage leukemia protein (MLL) activation domain binds to an allosteric site on the KIX domain

Flexible nets. The roles of intrinsic disorder in protein interaction networks.

Direct observation of the dynamic process underlying allosteric signal transmission.

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12055-12060

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scholarly article

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10.1073/PNAS.1405815111

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33

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111

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2014-08-04T00:00:00Z

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264501423

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25092343

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4143058

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