Oligomerization of the cysteinyl-rich oligopeptidase EP24.15 is triggered by S-glutathionylation.
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Redox modulation of thimet oligopeptidase activity by hydrogen peroxideCys-141 glutathionylation of human p53: Studies using specific polyclonal antibodies in cancer samples and cell lines.The cysteine-rich protein thimet oligopeptidase as a model of the structural requirements for S-glutathiolation and oxidative oligomerization.Recycling of the high valence States of heme proteins by cysteine residues of THIMET-oligopeptidase.Reversible and irreversible protein glutathionylation: biological and clinical aspects.Protein S-glutathiolation: redox-sensitive regulation of protein function.Protective role of bacillithiol in superoxide stress and Fe-S metabolism in Bacillus subtilis.S-glutathionylation of cysteine 99 in the APE1 protein impairs abasic endonuclease activity.Glutathione complexed Fe-S centers.Hydrogen bond residue positioning in the 599-611 loop of thimet oligopeptidase is required for substrate selectionS-glutathiolation in life and death decisions of the cell.The Arabidopsis oligopeptidases TOP1 and TOP2 are salicylic acid targets that modulate SA-mediated signaling and the immune response.Conferring specificity in redox pathways by enzymatic thiol/disulfide exchange reactions.Analysis of intracellular substrates and products of thimet oligopeptidase in human embryonic kidney 293 cells.Intracellular peptides as natural regulators of cell signaling.N-Acetylcysteine infusion does not affect glucose disposal during prolonged moderate-intensity exercise in humans.Inhibition of thimet oligopeptidase by siRNA alters specific intracellular peptides and potentiates isoproterenol signal transduction.
P2860
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P2860
Oligomerization of the cysteinyl-rich oligopeptidase EP24.15 is triggered by S-glutathionylation.
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
Oligomerization of the cystein ...... ggered by S-glutathionylation.
@en
type
label
Oligomerization of the cystein ...... ggered by S-glutathionylation.
@en
prefLabel
Oligomerization of the cystein ...... ggered by S-glutathionylation.
@en
P2093
P1476
Oligomerization of the cystein ...... ggered by S-glutathionylation.
@en
P2093
Emer S Ferro
Gilberto M Piassa Filho
Juliana C Ferreira
Marilene Demasi
Vanessa Rioli
P304
P356
10.1016/J.FREERADBIOMED.2007.12.012
P577
2007-12-23T00:00:00Z