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thioredoxin peroxidase
Known as:
Peroxiredoxins [Chemical/Ingredient]
, Thiol Specific Antioxidant Protein
, Alkyl Hydroperoxide Reductase
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A family of ubiquitously-expressed peroxidases that play a role in the reduction of a broad spectrum of PEROXIDES like HYDROGEN PEROXIDE; LIPID…
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National Institutes of Health
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Related topics
Related topics
25 relations
Narrower (17)
Alkyl Hydroperoxide Reductase C
Alkyl Hydroperoxide Reductase D
BAS1 protein, Arabidopsis
PAMM protein, mouse
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In Blood
Peroxidase
Process of secretion
antagonists & inhibitors
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2005
Highly Cited
2005
Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II
Min Hee Choi
,
I. Lee
,
+11 authors
S. Kang
Nature
2005
Corpus ID: 4391206
Platelet-derived growth factor (PDGF) is a potent mitogenic and migratory factor that regulates the tyrosine phosphorylation of a…
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Highly Cited
2004
Highly Cited
2004
Two Enzymes in One Two Yeast Peroxiredoxins Display Oxidative Stress-Dependent Switching from a Peroxidase to a Molecular Chaperone Function
H. Jang
,
Kyun Oh Lee
,
+15 authors
Sang Yeol Lee
Cell
2004
Corpus ID: 16512529
Highly Cited
2004
Highly Cited
2004
Protein Disulfide Bond Formation in the Cytoplasm during Oxidative Stress*
R. Cumming
,
N. Andon
,
P. Haynes
,
Minkyu Park
,
W. Fischer
,
D. Schubert
Journal of Biological Chemistry
2004
Corpus ID: 19773478
The majority of disulfide-linked cytosolic proteins are thought to be enzymes that transiently form disulfide bonds while…
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Highly Cited
2003
Highly Cited
2003
ATP-dependent reduction of cysteine–sulphinic acid by S. cerevisiae sulphiredoxin
B. Biteau
,
J. Labarre
,
M. Tolédano
Nature
2003
Corpus ID: 2804619
Proteins contain thiol-bearing cysteine residues that are sensitive to oxidation, and this may interfere with biological function…
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Highly Cited
2003
Highly Cited
2003
Reversing the Inactivation of Peroxiredoxins Caused by Cysteine Sulfinic Acid Formation
H. Woo
,
H. Chae
,
+4 authors
S. Rhee
Science
2003
Corpus ID: 46481752
The active-site cysteine of peroxiredoxins is selectively oxidized to cysteine sulfinic acid during catalysis, which leads to…
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Highly Cited
2002
Highly Cited
2002
Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes
M. Fratelli
,
H. Demol
,
+11 authors
P. Ghezzi
Proceedings of the National Academy of Sciences…
2002
Corpus ID: 14456934
Formation of mixed disulfides between glutathione and the cysteines of some proteins (glutathionylation) has been suggested as a…
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Highly Cited
2002
Highly Cited
2002
Proteomics Analysis of Cellular Response to Oxidative Stress
T. Rabilloud
,
M. Heller
,
+6 authors
J. Lunardi
Journal of Biological Chemistry
2002
Corpus ID: 1966941
The proteomics analysis reported here shows that a major cellular response to oxidative stress is the modification of several…
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Highly Cited
1998
Highly Cited
1998
Mammalian Peroxiredoxin Isoforms Can Reduce Hydrogen Peroxide Generated in Response to Growth Factors and Tumor Necrosis Factor-α*
Sang Won Kang
,
H. Chae
,
M. Seo
,
Kanghwa Kim
,
I. Baines
,
S. Rhee
Journal of Biological Chemistry
1998
Corpus ID: 2658501
Mammalian tissues express three immunologically distinct peroxiredoxin (Prx) proteins (Prx I, II, and III), which are the…
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Highly Cited
1997
Highly Cited
1997
Thioredoxin Peroxidase Is a Novel Inhibitor of Apoptosis with a Mechanism Distinct from That of Bcl-2*
Ping Zhang
,
Bin Liu
,
Sangmin Kang
,
M. Seo
,
S. Rhee
,
L. Obeid
Journal of Biological Chemistry
1997
Corpus ID: 37659566
Thioredoxin peroxidase (TPx) is a member of a newly discovered family of proteins that are conserved from yeast to mammals and to…
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Highly Cited
1994
Highly Cited
1994
Thioredoxin-dependent peroxide reductase from yeast.
H. Chae
,
Sangjin Chung
,
S. Rhee
Journal of Biological Chemistry
1994
Corpus ID: 33189396
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