Visualizing chaperone-assisted protein folding.

Visualizing chaperone-assisted protein folding.

Item
http://www.wikidata.org/entity/Q37077645
Capturing a Dynamic Chaperone-Substrate Interaction Using NMR-Informed Molecular ModelingA molecular mechanism of chaperone-client recognition.Chaperone-client interactions: Non-specificity engenders multifunctionality.Folding while bound to chaperones.The chloroplast-localized small heat shock protein Hsp21 associates with the thylakoid membranes in heat-stressed plants.Forces Driving Chaperone ActionChaperone-client interactions between Hsp21 and client proteins monitored in solution by small angle X-ray scattering and captured by crosslinking mass spectrometry.Chaperone-substrate interactions monitored via a robust TEM-1 β-lactamase fragment complementation assay.Molecular chaperones: providing a safe place to weather a midlife protein-folding crisis.Selecting Conformational Ensembles Using Residual Electron and Anomalous Density (READ).Competing protein-protein interactions regulate binding of Hsp27 to its client protein tau
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Visualizing chaperone-assisted protein folding.

Item
http://www.wikidata.org/entity/Q37077645
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 30 May 2016
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Visualizing chaperone-assisted protein folding.
@en
Visualizing chaperone-assisted protein folding.
@nl
type
label
Visualizing chaperone-assisted protein folding.
@en
Visualizing chaperone-assisted protein folding.
@nl
prefLabel
Visualizing chaperone-assisted protein folding.
@en
Visualizing chaperone-assisted protein folding.
@nl
P1433
P1476
P2093
P2860
P2888
P304
P31
P356
P433
P478
P50
P577
P698
P921
P932
P356
P1433
P1476
Visualizing chaperone-assisted protein folding
@en
P2093
P2860
P2888
P304
P31
P356
P433
P478
P50
P577
P698
P921
P932