Allosteric Coupling between the Lid and Interdomain Linker in DnaK Revealed by Inhibitor Binding Studies
about
Crystal structure of the stress-inducible human heat shock protein 70 substrate-binding domain in complex with peptide substrateCrystallographic and Molecular Dynamics Analysis of Loop Motions Unmasking the Peptidoglycan-Binding Site in Stator Protein MotB of Flagellar MotorAllosteric opening of the polypeptide-binding site when an Hsp70 binds ATPFunctional analysis of Hsp70 inhibitorsNew conformational state of NHERF1-CXCR2 signaling complex captured by crystal lattice trappingThe C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activationClose and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiPRole of the loop L4,5 in allosteric regulation in mtHsp70s: in vivo significance of domain communication and its implications in protein translocationATPase subdomain IA is a mediator of interdomain allostery in Hsp70 molecular chaperones.Novel apidaecin 1b analogs with superior serum stabilities for treatment of infections by gram-negative pathogens.Proline-rich antimicrobial peptides: converging to a non-lytic mechanism of action.Mechanism of Escherichia coli resistance to Pyrrhocoricin.Immunogenicity and pharmacokinetics of short, proline-rich antimicrobial peptides.HSPA5 Gene encoding Hsp70 chaperone BiP in the endoplasmic reticulum.Intracellular toxicity of proline-rich antimicrobial peptides shuttled into mammalian cells by the cell-penetrating peptide penetratin.BiPPred: Combined sequence- and structure-based prediction of peptide binding to the Hsp70 chaperone BiP.Novel Entropically Driven Conformation-specific Interactions with Tomm34 Protein Modulate Hsp70 Protein Folding and ATPase Activities.Insect-derived proline-rich antimicrobial peptides kill bacteria by inhibiting bacterial protein translation at the 70S ribosome.Tracking the interplay between bound peptide and the lid domain of DnaK, using molecular dynamics.Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop.The four hydrophobic residues on the Hsp70 inter-domain linker have two distinct roles.
P2860
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P2860
Allosteric Coupling between the Lid and Interdomain Linker in DnaK Revealed by Inhibitor Binding Studies
description
2009 nî lūn-bûn
@nan
2009 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի մարտին հրատարակված գիտական հոդված
@hy
2009年の論文
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2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
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2009年論文
@zh-tw
2009年论文
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name
Allosteric Coupling between th ...... d by Inhibitor Binding Studies
@ast
Allosteric Coupling between th ...... d by Inhibitor Binding Studies
@en
Allosteric Coupling between th ...... d by Inhibitor Binding Studies
@nl
type
label
Allosteric Coupling between th ...... d by Inhibitor Binding Studies
@ast
Allosteric Coupling between th ...... d by Inhibitor Binding Studies
@en
Allosteric Coupling between th ...... d by Inhibitor Binding Studies
@nl
prefLabel
Allosteric Coupling between th ...... d by Inhibitor Binding Studies
@ast
Allosteric Coupling between th ...... d by Inhibitor Binding Studies
@en
Allosteric Coupling between th ...... d by Inhibitor Binding Studies
@nl
P2860
P356
P1476
Allosteric Coupling between th ...... d by Inhibitor Binding Studies
@en
P2093
Anna Roujeinikova
Markus Liebscher
P2860
P304
P356
10.1128/JB.01131-08
P407
P577
2009-03-01T00:00:00Z