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Protein Folding and Mechanisms of ProteostasisPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Coping with low pH: molecular strategies in neutralophilic bacteriaComparing protein folding in vitro and in vivo: foldability meets the fitness challengeThiol-based redox switchesConditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function.Recent development and application of constant pH molecular dynamicsHdeB functions as an acid-protective chaperone in bacteriaMitochondrial peroxiredoxin functions as crucial chaperone reservoir in Leishmania infantum.Protein quality control under oxidative stress conditions.Multiscale modeling of a conditionally disordered pH-sensing chaperone.Energy landscapes of functional proteins are inherently risky.Dynamics of the BH3-Only Protein Binding Interface of Bcl-xL.HdeB chaperone activity is coupled to its intrinsic dynamic properties.From sequence and forces to structure, function, and evolution of intrinsically disordered proteinsProtein unfolding as a switch from self-recognition to high-affinity client bindingCoupled folding and binding with 2D Window-Exchange Umbrella Sampling.Conformational dynamics of a membrane protein chaperone enables spatially regulated substrate capture and release.How bacteria survive an acid trip.Comparative proteomics reveal distinct chaperone-client interactions in supporting bacterial acid resistanceSuper Spy variants implicate flexibility in chaperone action.NMR-monitored titration of acid-stress bacterial chaperone HdeA reveals that Asp and Glu charge neutralization produces a loosened dimer structure in preparation for protein unfolding and chaperone activation.CHARMM-GUI 10 years for biomolecular modeling and simulation.Binding and folding of the small bacterial chaperone HdeA.Is catalytic activity of chaperones a selectable trait for the emergence of heat shock response?Folding Optimization In Vivo Uncovers New Chaperones.¹³C, ¹⁵N and ¹H backbone and side chain chemical shift assignment of acid-stress bacterial chaperone HdeA at pH 6.Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.The Mechanism of HdeA Unfolding and Chaperone Activation.Stress-Activated Chaperones: A First Line of Defense.Structural insight into a partially unfolded state preceding aggregation in an intracellular lipid-binding protein.Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo.Amyloid β-Sheet Secondary Structure Identified in UV-Induced Cataracts of Porcine Lenses using 2D IR Spectroscopy.Roles of structural plasticity in chaperone HdeA activity are revealed by 19F NMR.
P2860
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P2860
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
Chaperone activation by unfolding.
@en
type
label
Chaperone activation by unfolding.
@en
prefLabel
Chaperone activation by unfolding.
@en
P2093
P2860
P356
P1476
Chaperone activation by unfolding.
@en
P2093
Bin W Zhang
Charles L Brooks
James C A Bardwell
Jenny S George
Linda Foit
P2860
P304
P356
10.1073/PNAS.1222458110
P407
P577
2013-03-04T00:00:00Z