Remarkably fast coupled folding and binding of the intrinsically disordered transactivation domain of cMyb to CBP KIX.
about
Insights into Coupled Folding and Binding Mechanisms from Kinetic StudiesBinding Mechanisms of Intrinsically Disordered Proteins: Theory, Simulation, and ExperimentThe contribution of intrinsically disordered regions to protein function, cellular complexity, and human diseasePrepaying the entropic cost for allosteric regulation in KIXAllostery within a transcription coactivator is predominantly mediated through dissociation rate constantsDissecting allosteric effects of activator-coactivator complexes using a covalent small molecule ligand.Coupled folding and binding of the disordered protein PUMA does not require particular residual structure.Interplay between partner and ligand facilitates the folding and binding of an intrinsically disordered proteinThe binding mechanisms of intrinsically disordered proteins.Intrinsically disordered proteins in cellular signalling and regulation.Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and foldingFunctional advantages of dynamic protein disorder.Multivalent IDP assemblies: Unique properties of LC8-associated, IDP duplex scaffoldsRole of non-native electrostatic interactions in the coupled folding and binding of PUMA with Mcl-1Impact of the amino acid sequence on the conformation of side chain lactam-bridged octapeptides.Role of Intrinsic Protein Disorder in the Function and Interactions of the Transcriptional Coactivators CREB-binding Protein (CBP) and p300Order-Disorder Transitions in the Cardiac Troponin Complex.Deciphering the mechanisms of binding induced folding at nearly atomic resolution: The Φ value analysis applied to IDPs.A Quantitative Fluorescence-Based Assay for Assessing LIM Domain-Peptide Interactions.Plasticity of an ultrafast interaction between nucleoporins and nuclear transport receptors.Digested disorder, Quarterly intrinsic disorder digest (October-November-December, 2013).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.Kinetic mechanism of controlled Fab-arm exchange for the formation of bispecific immunoglobulin G1 antibodies.Affinity of IDPs to their targets is modulated by ion-specific changes in kinetics and residual structure.Fuzzy regions in an intrinsically disordered protein impair protein-protein interactions.Disparate binding kinetics by an intrinsically disordered domain enables temporal regulation of transcriptional complex formation.Conservation of coactivator engagement mechanism enables small-molecule allosteric modulatorsTunable order-disorder continuum in protein-DNA interactions
P2860
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P2860
Remarkably fast coupled folding and binding of the intrinsically disordered transactivation domain of cMyb to CBP KIX.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
Remarkably fast coupled foldin ...... ion domain of cMyb to CBP KIX.
@en
Remarkably fast coupled foldin ...... ion domain of cMyb to CBP KIX.
@nl
type
label
Remarkably fast coupled foldin ...... ion domain of cMyb to CBP KIX.
@en
Remarkably fast coupled foldin ...... ion domain of cMyb to CBP KIX.
@nl
prefLabel
Remarkably fast coupled foldin ...... ion domain of cMyb to CBP KIX.
@en
Remarkably fast coupled foldin ...... ion domain of cMyb to CBP KIX.
@nl
P2093
P2860
P356
P1476
Remarkably fast coupled foldin ...... ion domain of cMyb to CBP KIX.
@en
P2093
Alexandra J Travis
Jane Clarke
Sarah L Shammas
P2860
P304
13346-13356
P356
10.1021/JP404267E
P407
P577
2013-08-15T00:00:00Z