Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein.
about
Metazoan Hsp70-based protein disaggregases: emergence and mechanismsHeterogeneous binding of the SH3 client protein to the DnaK molecular chaperone.Modeling Hsp70/Hsp40 interaction by multi-scale molecular simulations and coevolutionary sequence analysisAlternative modes of client binding enable functional plasticity of Hsp70.Mapping the conformation of a client protein through the Hsp70 functional cycle.Hsp70 biases the folding pathways of client proteins.Pharmacological chaperone reshapes the energy landscape for folding and aggregation of the prion proteinHow 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.The remarkable multivalency of the Hsp70 chaperones.The chaperone toolbox at the single-molecule level: From clamping to confining.Fluorescence fluctuation of an antigen-antibody complex: circular dichroism, FCS and smFRET of enhanced GFP and its antibody.Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles.Formal Models of Biological Systems.Probing Small Molecule Binding to Unfolded Polyprotein Based on its Elasticity and Refolding.X-Linked Inhibitor of Apoptosis Protein (XIAP) is a Client of Heat Shock Protein 70 (Hsp70) and a Biomarker of its Inhibition.Conformational Heterogeneity and FRET Data Interpretation for Dimensions of Unfolded Proteins.Thermodynamic Bounds on the Ultra- and Infra-affinity of Hsp70 for Its Substrates.Rapid Microfluidic Dilution for Single-Molecule Spectroscopy of Low-Affinity Biomolecular Complexes.Conserved conformational selection mechanism of Hsp70 chaperone-substrate interactions.Slow Interconversion in a Heterogeneous Unfolded-State Ensemble of Outer-Membrane Phospholipase A.Rapid Microfluidic Dilution for Single-Molecule Spectroscopy of Low-Affinity Biomolecular Complexes
P2860
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P2860
Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein.
description
2014 nî lūn-bûn
@nan
2014 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein.
@ast
Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein.
@en
Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein.
@nl
type
label
Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein.
@ast
Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein.
@en
Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein.
@nl
prefLabel
Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein.
@ast
Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein.
@en
Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein.
@nl
P2093
P2860
P356
P1476
Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein.
@en
P2093
Bengt Wunderlich
Daniel Nettels
Hagen Hofmann
Ruth Kellner
P2860
P304
13355-13360
P356
10.1073/PNAS.1407086111
P407
P577
2014-08-27T00:00:00Z