A Conserved Cysteine within the ATPase Domain of the Endoplasmic Reticulum Chaperone BiP is Necessary for a Complete Complement of BiP Activities.
about
An unexpected role for the yeast nucleotide exchange factor Sil1 as a reductant acting on the molecular chaperone BiP.Disrupted hydrogen bond network and impaired ATPase activity in an Hsc70 cysteine mutant.Diminished Ost3-dependent N-glycosylation of the BiP nucleotide exchange factor Sil1 is an adaptive response to reductive ER stress.
P2860
A Conserved Cysteine within the ATPase Domain of the Endoplasmic Reticulum Chaperone BiP is Necessary for a Complete Complement of BiP Activities.
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
A Conserved Cysteine within th ...... Complement of BiP Activities.
@en
type
label
A Conserved Cysteine within th ...... Complement of BiP Activities.
@en
prefLabel
A Conserved Cysteine within th ...... Complement of BiP Activities.
@en
P2860
P1476
A Conserved Cysteine within th ...... Complement of BiP Activities.
@en
P2093
Heather M Marsh
P2860
P304
P356
10.1016/J.JMB.2016.08.011
P407
P577
2016-08-16T00:00:00Z