Mutations in the FAD binding domain cause stress-induced misoxidation of the endoplasmic reticulum oxidoreductase Ero1beta.
about
Biochemical evidence that regulation of Ero1β activity in human cells does not involve the isoform-specific cysteine 262.Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulumEro1alpha requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM).
P2860
Mutations in the FAD binding domain cause stress-induced misoxidation of the endoplasmic reticulum oxidoreductase Ero1beta.
description
2006 nî lūn-bûn
@nan
2006 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Mutations in the FAD binding d ...... culum oxidoreductase Ero1beta.
@ast
Mutations in the FAD binding d ...... culum oxidoreductase Ero1beta.
@en
Mutations in the FAD binding d ...... culum oxidoreductase Ero1beta.
@nl
type
label
Mutations in the FAD binding d ...... culum oxidoreductase Ero1beta.
@ast
Mutations in the FAD binding d ...... culum oxidoreductase Ero1beta.
@en
Mutations in the FAD binding d ...... culum oxidoreductase Ero1beta.
@nl
prefLabel
Mutations in the FAD binding d ...... culum oxidoreductase Ero1beta.
@ast
Mutations in the FAD binding d ...... culum oxidoreductase Ero1beta.
@en
Mutations in the FAD binding d ...... culum oxidoreductase Ero1beta.
@nl
P2860
P50
P356
P1476
Mutations in the FAD binding d ...... iculum oxidoreductase Ero1beta
@en
P2093
Ritu Kataky
Sanjika Dias-Gunasekara
P2860
P304
25018-25025
P356
10.1074/JBC.M602354200
P407
P577
2006-07-05T00:00:00Z