Degradation of HNE-modified proteins--possible role of ubiquitin.
about
Teratogen-induced oxidative stress targets glyceraldehyde-3-phosphate dehydrogenase in the organogenesis stage mouse embryo.4-hydroxy-2-nonenal-modified glyceraldehyde-3-phosphate dehydrogenase is degraded by cathepsin G in rat neutrophils.The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal.Effects of 4-hydroxynonenal on vascular endothelial and smooth muscle cell redox signaling and function in health and disease.Inhibition of arachidonate 15-lipoxygenase prevents 4-hydroxynonenal-induced protein damage in male germ cells.Proteolytic degradation of heat shock protein A2 occurs in response to oxidative stress in male germ cells of the mouse.SHP-1 inhibition by 4-hydroxynonenal activates Jun N-terminal kinase and glutamate cysteine ligase.Reactive carbonyl species in vivo: generation and dual biological effects
P2860
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P2860
Degradation of HNE-modified proteins--possible role of ubiquitin.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Degradation of HNE-modified proteins--possible role of ubiquitin.
@en
type
label
Degradation of HNE-modified proteins--possible role of ubiquitin.
@en
prefLabel
Degradation of HNE-modified proteins--possible role of ubiquitin.
@en
P2860
P356
P1433
P1476
Degradation of HNE-modified proteins--possible role of ubiquitin
@en
P2093
Diana Botzen
P2860
P356
10.1179/135100007X162130
P50
P577
2007-01-01T00:00:00Z