dehydroepiandrosterone < dehydrogenase < deiodinase

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List of bibliographic references indexed by dehydrogenase

Number of relevant bibliographic references: 18.

Ident.	Authors (with country if any)	Title
000018 (2020)	K V Barinova [Russie] ; M V Serebryakova [Russie] ; M A Eldarov [Russie] ; A A Kulikova [Russie] ; V A Mitkevich [Russie] ; V I Muronetz [Russie] ; E V Schmalhausen [Russie]	S-glutathionylation of human glyceraldehyde-3-phosphate dehydrogenase and possible role of Cys152-Cys156 disulfide bridge in the active site of the protein.
000126 (2019)	Victoria I. Bunik [Russie]	Redox-Driven Signaling: 2-Oxo Acid Dehydrogenase Complexes as Sensors and Transmitters of Metabolic Imbalance.
000160 (2019)	Mirko Zaffagnini [Italie] ; Christophe H. Marchand [France] ; Marco Malferrari [Italie] ; Samuel Murail [France] ; Sara Bonacchi [Italie] ; Damiano Genovese [Italie] ; Marco Montalti [Italie] ; Giovanni Venturoli [Italie] ; Giuseppe Falini [Italie] ; Marc Baaden [France] ; Stéphane D. Lemaire [France] ; Simona Fermani [Italie] ; Paolo Trost [Italie]	Glutathionylation primes soluble glyceraldehyde-3-phosphate dehydrogenase for late collapse into insoluble aggregates.
000181 (2019)	Adnan Khan Niazi [France, Pakistan] ; Laetitia Bariat [France] ; Christophe Riondet [France] ; Christine Carapito [France] ; Amna Mhamdi [France, Belgique] ; Graham Noctor [France] ; Jean-Philippe Reichheld [France]	Cytosolic Isocitrate Dehydrogenase from Arabidopsis thaliana Is Regulated by Glutathionylation.
000327 (2017)	Marisa O'Brien [Canada] ; Julia Chalker [Canada] ; Liam Slade [Canada] ; Danielle Gardiner [Canada] ; Ryan J. Mailloux [Canada]	Protein S-glutathionylation alters superoxide/hydrogen peroxide emission from pyruvate dehydrogenase complex.
000448 (2016)	Ryan J. Mailloux [Canada] ; D. Craig Ayre [Canada] ; Sherri L. Christian [Canada]	Induction of mitochondrial reactive oxygen species production by GSH mediated S-glutathionylation of 2-oxoglutarate dehydrogenase.
000756 (2013)	Aaron L. Mclain [États-Unis] ; Peter J. Cormier [États-Unis] ; Michael Kinter [États-Unis] ; Luke I. Szweda [États-Unis]	Glutathionylation of α-ketoglutarate dehydrogenase: the chemical nature and relative susceptibility of the cofactor lipoic acid to modification.
000806 (2012)	Katarína Smolková [République tchèque] ; Petr Ježek	The Role of Mitochondrial NADPH-Dependent Isocitrate Dehydrogenase in Cancer Cells.
000857 (2012)	Mariette Bedhomme [Italie] ; Mattia Adamo ; Christophe H. Marchand ; Jérémy Couturier ; Nicolas Rouhier ; Stéphane D. Lemaire ; Mirko Zaffagnini ; Paolo Trost	Glutathionylation of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the model plant Arabidopsis thaliana is reversed by both glutaredoxins and thioredoxins in vitro.
000896 (2011)	Aaron L. Mclain [États-Unis] ; Pamela A. Szweda ; Luke I. Szweda	α-Ketoglutarate dehydrogenase: a mitochondrial redox sensor.
000913 (2011)	Linda E. Kippner [États-Unis] ; Nnenna A. Finn ; Shreya Shukla ; Melissa L. Kemp	Systemic remodeling of the redox regulatory network due to RNAi perturbations of glutaredoxin 1, thioredoxin 1, and glucose-6-phosphate dehydrogenase.
000B21 (2009)	Seoung Woo Shin [Corée du Sud] ; Chang Joo Oh ; In Sup Kil ; Jeen-Woo Park	Glutathionylation regulates cytosolic NADP+-dependent isocitrate dehydrogenase activity.
000D35 (2006)	In Sup Kil [Corée du Sud] ; Seoung Woo Shin ; Hyun Seok Yeo ; Young Sup Lee ; Jeen-Woo Park	Mitochondrial NADP+-dependent isocitrate dehydrogenase protects cadmium-induced apoptosis.
000E52 (2004)	Diyaa Rachdan [Royaume-Uni] ; Marjorie F. Lou ; John J. Harding	Revival of inactive glyceraldehyde 3-phosphate dehydrogenase in human cataract lenses by reduction.
000F12 (2003)	Amy C. Nulton-Persson [États-Unis] ; David W. Starke ; John J. Mieyal ; Luke I. Szweda	Reversible inactivation of alpha-ketoglutarate dehydrogenase in response to alterations in the mitochondrial glutathione status.
000F68 (2002)	Ian A. Cotgreave [Suède] ; Robert Gerdes ; Ina Schuppe-Koistinen ; Christina Lind	S-glutathionylation of glyceraldehyde-3-phosphate dehydrogenase: role of thiol oxidation and catalysis by glutaredoxin.
001130 (1998)	C. Lind [Suède] ; R. Gerdes ; I. Schuppe-Koistinen ; I A Cotgreave	Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: catalysis by glutaredoxin.
001236 (1994)	T. Terada [Japon]	Thioltransferase can utilize cysteamine as same as glutathione as a reductant during the restoration of cystamine-treated glucose 6-phosphate dehydrogenase activity.

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