Degradation of PsbO by the Deg protease HhoA Is thioredoxin dependent.
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Crystal structure of the zinc-bound HhoA protease from Synechocystis sp. PCC 6803Proteomic evidences for rex regulation of metabolism in toxin-producing Bacillus cereus ATCC 14579.Conditional, temperature-induced proteolytic regulation of cyanobacterial RNA helicase expressionInsights into the Cyanobacterial Deg/HtrA ProteasesThe conservative cysteines in transmembrane domain of AtVKOR/LTO1 are critical for photosynthetic growth and photosystem II activity in Arabidopsis.Molecular Basis Underlying Leaf Variegation of a Moth Orchid Mutant (Phalaenopsis aphrodite subsp. formosana).The Role of Light-Dark Regulation of the Chloroplast ATP Synthase.A Deg-protease family protein in marine Synechococcus is involved in outer membrane protein organization
P2860
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P2860
Degradation of PsbO by the Deg protease HhoA Is thioredoxin dependent.
description
2012 nî lūn-bûn
@nan
2012 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Degradation of PsbO by the Deg protease HhoA Is thioredoxin dependent.
@ast
Degradation of PsbO by the Deg protease HhoA Is thioredoxin dependent.
@en
Degradation of PsbO by the Deg protease HhoA Is thioredoxin dependent.
@nl
type
label
Degradation of PsbO by the Deg protease HhoA Is thioredoxin dependent.
@ast
Degradation of PsbO by the Deg protease HhoA Is thioredoxin dependent.
@en
Degradation of PsbO by the Deg protease HhoA Is thioredoxin dependent.
@nl
prefLabel
Degradation of PsbO by the Deg protease HhoA Is thioredoxin dependent.
@ast
Degradation of PsbO by the Deg protease HhoA Is thioredoxin dependent.
@en
Degradation of PsbO by the Deg protease HhoA Is thioredoxin dependent.
@nl
P2093
P2860
P1433
P1476
Degradation of PsbO by the Deg protease HhoA Is thioredoxin dependent.
@en
P2093
Christiane Funk
Helder Miranda
Irma N Roberts
Xuan Tam Lam
P2860
P304
P356
10.1371/JOURNAL.PONE.0045713
P407
P577
2012-09-19T00:00:00Z