Conserved, disordered C terminus of DnaK enhances cellular survival upon stress and DnaK in vitro chaperone activity
about
Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced ActivityInsights into the molecular mechanism of allostery in Hsp70s.Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functionsAllosteric opening of the polypeptide-binding site when an Hsp70 binds ATPThe C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activationAllostery in the Hsp70 chaperone proteinsKey features of an Hsp70 chaperone allosteric landscape revealed by ion-mobility native mass spectrometry and double electron-electron resonanceConditional disorder in chaperone action.Alternative modes of client binding enable functional plasticity of Hsp70.ATPase subdomain IA is a mediator of interdomain allostery in Hsp70 molecular chaperones.Targeting intrinsically disordered proteins in rational drug discovery.The crystal structure of Erwinia amylovora AmyR, a member of the YbjN protein family, shows similarity to type III secretion chaperones but suggests different cellular functions.How bacteria survive an acid trip.Essential functions linked with structural disorder in organisms of minimal genomePrinciples of self-organization in biological pathways: a hypothesis on the autogenous association of alpha-synucleinHow hsp70 molecular machines interact with their substrates to mediate diverse physiological functions.Conformational heterogeneity in the Hsp70 chaperone-substrate ensemble: identified from analysis of NMR-detected titration data.Chaperone-client interactions: Non-specificity engenders multifunctionality.Tyrosine 601 of Bacillus subtilis DnaK Undergoes Phosphorylation and Is Crucial for Chaperone Activity and Heat Shock Survival.Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles.Tracking the interplay between bound peptide and the lid domain of DnaK, using molecular dynamics.Interplay between recombinant Hsp70 and proteasomes: proteasome activity modulation and ubiquitin-independent cleavage of Hsp70.Activation of the DnaK-ClpB Complex is Regulated by the Properties of the Bound Substrate.The toxin GraT inhibits ribosome biogenesis.A phasin with extra talents: a polyhydroxyalkanoate granule-associated protein has chaperone activity.
P2860
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P2860
Conserved, disordered C terminus of DnaK enhances cellular survival upon stress and DnaK in vitro chaperone activity
description
2011 nî lūn-bûn
@nan
2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Conserved, disordered C termin ...... aK in vitro chaperone activity
@ast
Conserved, disordered C termin ...... aK in vitro chaperone activity
@en
type
label
Conserved, disordered C termin ...... aK in vitro chaperone activity
@ast
Conserved, disordered C termin ...... aK in vitro chaperone activity
@en
prefLabel
Conserved, disordered C termin ...... aK in vitro chaperone activity
@ast
Conserved, disordered C termin ...... aK in vitro chaperone activity
@en
P2093
P2860
P356
P1476
Conserved, disordered C termin ...... aK in vitro chaperone activity
@en
P2093
Lila M Gierasch
Mandy E Blackburn
Robert G Smock
P2860
P304
31821-31829
P356
10.1074/JBC.M111.265835
P407
P577
2011-07-18T00:00:00Z