NK-lysin, a disulfide-containing effector peptide of T-lymphocytes, is reduced and inactivated by human thioredoxin reductase. Implication for a protective mechanism against NK-lysin cytotoxicity.
about
Human mitochondrial thioredoxin reductase cDNA cloning, expression and genomic organizationThioredoxin reductaseThe human selenoproteome: recent insights into functions and regulationThe mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coliSaposin fold revealed by the NMR structure of NK-lysinThioredoxins, glutaredoxins, and peroxiredoxins--molecular mechanisms and health significance: from cofactors to antioxidants to redox signalingCytoplasmic thioredoxin reductase is essential for embryogenesis but dispensable for cardiac developmentCell death by SecTRAPs: thioredoxin reductase as a prooxidant killer of cellsAnimal antimicrobial peptides: an overview.CUG start codon generates thioredoxin/glutathione reductase isoforms in mouse testes.News and views on thioredoxin reductases.Regulation and function of selenoproteins in human diseaseThioredoxin reductase is irreversibly modified by curcumin: a novel molecular mechanism for its anticancer activity.Reactive oxygen species and antioxidant mechanisms in human tissues and their relation to malignancies.No selenium required: reactions catalyzed by mammalian thioredoxin reductase that are independent of a selenocysteine residue.CRS-peptides: unique defense peptides of mouse Paneth cells.Selenium as an electron acceptor during the catalytic mechanism of thioredoxin reductaseIdentification of an anti-mycobacterial domain in NK-lysin and granulysin.Conserved structure and function in the granulysin and NK-lysin peptide family.Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds.A comparative study on the structure and function of a cytolytic alpha-helical peptide and its antimicrobial beta-sheet diastereomer.4-Hydroxynonenal induces adaptive response and enhances PC12 cell tolerance primarily through induction of thioredoxin reductase 1 via activation of Nrf2.The 58 kDa mouse selenoprotein is a BCNU-sensitive thioredoxin reductase.Selenoproteins and cardiovascular stress.Paraquat increases cyanide-insensitive respiration in murine lung epithelial cells by activating an NAD(P)H:paraquat oxidoreductase: identification of the enzyme as thioredoxin reductase.Structural and membrane-binding properties of saposin D
P2860
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P2860
NK-lysin, a disulfide-containing effector peptide of T-lymphocytes, is reduced and inactivated by human thioredoxin reductase. Implication for a protective mechanism against NK-lysin cytotoxicity.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
NK-lysin, a disulfide-containi ...... against NK-lysin cytotoxicity.
@en
NK-lysin, a disulfide-containi ...... against NK-lysin cytotoxicity.
@nl
type
label
NK-lysin, a disulfide-containi ...... against NK-lysin cytotoxicity.
@en
NK-lysin, a disulfide-containi ...... against NK-lysin cytotoxicity.
@nl
prefLabel
NK-lysin, a disulfide-containi ...... against NK-lysin cytotoxicity.
@en
NK-lysin, a disulfide-containi ...... against NK-lysin cytotoxicity.
@nl
P2093
P2860
P356
P1476
NK-lysin, a disulfide-containi ...... against NK-lysin cytotoxicity.
@en
P2093
P2860
P304
10116-10120
P356
10.1074/JBC.271.17.10116
P407
P577
1996-04-01T00:00:00Z