A molecular mechanism of chaperone-client recognition.

A molecular mechanism of chaperone-client recognition.

Item
http://www.wikidata.org/entity/Q37603844
Chaperone-client interactions: Non-specificity engenders multifunctionality.Folding while bound to chaperones.A protean clamp guides membrane targeting of tail-anchored proteins.The dynamic dimer structure of the chaperone Trigger Factor.Outer membrane protein folding from an energy landscape perspective.Atomistic simulations and network-based modeling of the Hsp90-Cdc37 chaperone binding with Cdk4 client protein: A mechanism of chaperoning kinase clients by exploiting weak spots of intrinsically dynamic kinase domains.Local energetic frustration affects the dependence of green fluorescent protein folding on the chaperonin GroEL.Protein folding: Minimizing frustration.The antibiotic cyclomarin blocks arginine-phosphate-induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis.Oligomerization of a molecular chaperone modulates its activity.
P2860

A molecular mechanism of chaperone-client recognition.

Item
http://www.wikidata.org/entity/Q37603844
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年学术文章
@wuu
2016年学术文章
@zh-cn
2016年学术文章
@zh-hans
2016年学术文章
@zh-my
2016年学术文章
@zh-sg
2016年學術文章
@yue
2016年學術文章
@zh
2016年學術文章
@zh-hant
name
A molecular mechanism of chaperone-client recognition.
@en
A molecular mechanism of chaperone-client recognition.
@nl
type
label
A molecular mechanism of chaperone-client recognition.
@en
A molecular mechanism of chaperone-client recognition.
@nl
prefLabel
A molecular mechanism of chaperone-client recognition.
@en
A molecular mechanism of chaperone-client recognition.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P433
P478
P50
P577
P698
P921
P932
P356
P1433
P1476
A molecular mechanism of chaperone-client recognition
@en
P2093
P2860
P304
P31
P356
P433
P478
P50
P577
P698
P921
P932