Mapping temperature-induced conformational changes in the Escherichia coli heat shock transcription factor sigma 32 by amide hydrogen exchange.
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Structural insights into tail-anchored protein binding and membrane insertion by Get3Lipids Trigger a Conformational Switch That Regulates Signal Recognition Particle (SRP)-mediated Protein TargetingSynchronizing nuclear import of ribosomal proteins with ribosome assemblyHead-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregationConvergence of Molecular, Modeling, and Systems Approaches for an Understanding of the Escherichia coli Heat Shock ResponseLocal unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry.Molecular insights into frataxin-mediated iron supply for heme biosynthesis in Bacillus subtilisInsights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity.Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding.Analyzing protein dynamics using hydrogen exchange mass spectrometry.The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110.A chaperone network controls the heat shock response in E. coliDifferences in conformational dynamics within the Hsp90 chaperone family reveal mechanistic insightsThe B1 Protein Guides the Biosynthesis of a Lasso Peptide.Dynamics of the regulation of Hsp90 by the co-chaperone Sti1.Analysis of subsecond protein dynamics by amide hydrogen exchange and mass spectrometry using a quenched-flow setupSpatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine.Mutant Analysis Reveals Allosteric Regulation of ClpB DisaggregaseRole of DnaJ G/F-rich domain in conformational recognition and binding of protein substrates.Structural analysis of the ribosome-associated complex (RAC) reveals an unusual Hsp70/Hsp40 interaction.Conserved residues in the N-domain of the AAA+ chaperone ClpA regulate substrate recognition and unfolding.Hsp110 is a nucleotide-activated exchange factor for Hsp70.The stress sigma factor of RNA polymerase RpoS/σS is a solvent exposed open molecule in solution.A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins.A tightly regulated molecular toggle controls AAA+ disaggregase.Formation of active inclusion bodies in the periplasm of Escherichia coli.Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation.Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domainCochaperones enable Hsp70 to use ATP energy to stabilize native proteins out of the folding equilibrium
P2860
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P2860
Mapping temperature-induced conformational changes in the Escherichia coli heat shock transcription factor sigma 32 by amide hydrogen exchange.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
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2003年學術文章
@zh-hant
name
Mapping temperature-induced co ...... 32 by amide hydrogen exchange.
@en
Mapping temperature-induced co ...... 32 by amide hydrogen exchange.
@nl
type
label
Mapping temperature-induced co ...... 32 by amide hydrogen exchange.
@en
Mapping temperature-induced co ...... 32 by amide hydrogen exchange.
@nl
prefLabel
Mapping temperature-induced co ...... 32 by amide hydrogen exchange.
@en
Mapping temperature-induced co ...... 32 by amide hydrogen exchange.
@nl
P2860
P50
P356
P1476
Mapping temperature-induced co ...... 32 by amide hydrogen exchange
@en
P2093
Peter Roepstorff
P2860
P304
51415-51421
P356
10.1074/JBC.M307160200
P407
P577
2003-09-22T00:00:00Z