Forces Driving Chaperone Action

Forces Driving Chaperone Action

Item
http://www.wikidata.org/entity/Q41832929
Capturing a Dynamic Chaperone-Substrate Interaction Using NMR-Informed Molecular ModelingStructural model of dodecameric heat-shock protein Hsp21: Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity.A 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.Harnessing an RNA-mediated chaperone for the assembly of influenza hemagglutinin in an immunologically relevant conformation.Chaperone-client interactions between Hsp21 and client proteins monitored in solution by small angle X-ray scattering and captured by crosslinking mass spectrometry.Stress-Activated Chaperones: A First Line of Defense.Chaperone-substrate interactions monitored via a robust TEM-1 β-lactamase fragment complementation assay.Oligomerization of a molecular chaperone modulates its activity.
P2860

Forces Driving Chaperone Action

Item
http://www.wikidata.org/entity/Q41832929
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
2016年论文
@zh
2016年论文
@zh-cn
name
Forces Driving Chaperone Action
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type
label
Forces Driving Chaperone Action
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prefLabel
Forces Driving Chaperone Action
@en
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Forces Driving Chaperone Action
@en
P2093
P2860
P304
P31
P356
10.1016/J.CELL.2016.05.054
P407
P433
P478
P50
P577
P698
P921
P932