Zobrazeno 1 - 10
of 21
pro vyhledávání: '"L. David Arscott"'
Publikováno v:
Biochemistry. 47:1721-1731
Thioredoxin reductase (TrxR) catalyzes the reduction of thioredoxin (Trx) by NADPH. Like other members of the pyridine nucleotide-disulfide oxidoreductase enzyme family, the enzyme from Drosophila melanogaster is a homodimer, and each catalytically a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d0d801db28e886de30d9bc43fba6f12
https://doi.org/10.1021/bi702040u
https://doi.org/10.1021/bi702040u
Autor:
Sylke Müller, David P. Ballou, Katja Becker, Paul J. McMillan, Charles H. Williams, L. David Arscott
Publikováno v:
Journal of Biological Chemistry. 281:32967-32977
High-M(r) thioredoxin reductase from the malaria parasite Plasmodium falciparum (PfTrxR) contains three redox active centers (FAD, Cys-88/Cys-93, and Cys-535/Cys-540) that are in redox communication. The catalytic mechanism of PfTrxR, which involves
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1535626c80bab9ec46171e9b85b0f67
https://doi.org/10.1074/jbc.m601141200
https://doi.org/10.1074/jbc.m601141200
Autor:
Régis Réau, Markus Meyer, Charles H. Williams, Christel Herold-Mende, Sabine Urig, Marcel Deponte, David P. Ballou, L. David Arscott, Katja Becker, Karin Fritz-Wolf, Elisabeth Davioud-Charvet, Sasa Koncarevic
Publikováno v:
The Journal of Biological Chemistry
The homodimeric flavoprotein glutathione reductase (GR) is a central player of cellular redox metabolism, connecting NADPH to the large pool of redox-active thiols. In this work, the inhibition of human GR by a novel gold-phosphole inhibitor (GoPI) h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4de0c491e887b8c1bb27117e46bd9174
https://doi.org/10.1074/jbc.m412519200
https://doi.org/10.1074/jbc.m412519200
Autor:
Vincent Massey, L. David Arscott, Holger Bauer, David P. Ballou, R. Heiner Schirmer, Charles H. Williams
Publikováno v:
Journal of Biological Chemistry. 278:33020-33028
Drosophila melanogaster thioredoxin reductase-1 (DmTrxR-1) is a key flavoenzyme in dipteran insects, where it substitutes for glutathione reductase. DmTrxR-1 belongs to the family of dimeric, high M r thioredoxin reductases, which catalyze reduction
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::261faba9cc38f73d5d6f1d4bb28179bb
https://doi.org/10.1074/jbc.m303762200
https://doi.org/10.1074/jbc.m303762200
Publikováno v:
Journal of Biological Chemistry. 275:37317-37323
The homodimeric flavoenzyme glutathione reductase (GR) maintains high intracellular concentrations of the antioxidant glutathione (GSSG + NADPH + H+ ↔ 2 GSH + NADP+). Due to its central function in cellular redox metabolism, inhibition of GR from t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dea45ad585a44328a3aa56d548abe75a
https://doi.org/10.1074/jbc.m007695200
https://doi.org/10.1074/jbc.m007695200
Publikováno v:
Biochemistry. 47(48)
Thioredoxin reductase (TrxR) catalyzes the reduction of thioredoxin (Trx) by NADPH. Because dipteran insects such as Drosophila melanogaster lack glutathione reductase, their TrxRs are particularly important for antioxidant protection; reduced Trx re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe1cdede23744f242f222dc89f14ba4f
https://pubmed.ncbi.nlm.nih.gov/18991392
https://pubmed.ncbi.nlm.nih.gov/18991392
Autor:
L. David Arscott, R. Heiner Schirmer, Sylke MüLLER, Katja Becker, George L. Kenyon, Adriano D. Andricopulo, David A. Giegel, Charles H. Williams, Michael J. McLeish, Donna M. Veine, Elisabeth Davioud-Charvet
Publikováno v:
Biochemistry. 42(45)
Thioredoxin reductase (TrxR) is the homodimeric flavoenzyme that catalyzes reduction of thioredoxin disulfide (Trx). For Plasmodium falciparum, a causative agent of tropical malaria, TrxR is an essential protein which has been validated as a drug tar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72192bef8901103ed89bed628d0c5346
https://pubmed.ncbi.nlm.nih.gov/14609342
https://pubmed.ncbi.nlm.nih.gov/14609342
Autor:
L. David Arscott, Elias S.J. Arnér, David P. Ballou, Charles H. Williams, R. Heiner Schirmer, Stephan Gromer, Susanne Rauch, Linda Johansson, Holger Bauer
Selenium, an essential trace element for mammals, is incorporated into a selected class of selenoproteins as selenocysteine. All known isoenzymes of mammalian thioredoxin (Trx) reductases (TrxRs) employ selenium in the C-terminal redox center -Gly-Cy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::895df49d571d3d11c9b8f5c893177249
https://europepmc.org/articles/PMC240667/
https://europepmc.org/articles/PMC240667/
Publikováno v:
Biochemistry. 39(16)
Glutathione reductase catalyzes the reduction of glutathione disulfide by NADPH. The FAD of the reductase is reduced by NADPH, and reducing equivalents are passed to a redox-active disulfide to complete the first half-reaction. The nascent dithiol of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10c9e71d449be7d8cb0495545beb76ad
https://pubmed.ncbi.nlm.nih.gov/10769127
https://pubmed.ncbi.nlm.nih.gov/10769127
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 94(8)
Thioredoxin reductase, lipoamide dehydrogenase, and glutathione reductase are members of the pyridine nucleotide–disulfide oxidoreductase family of dimeric flavoenzymes. The mechanisms and structures of lipoamide dehydrogenase and glutathione reduc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e266b676044885f6f8f7aeeb0d6a32b
https://pubmed.ncbi.nlm.nih.gov/9108027
https://pubmed.ncbi.nlm.nih.gov/9108027