Serveur d'exploration sur la glutarédoxine - Exploration (Accueil)

Index « KwdFr.i » - entrée « Glutathion (composition chimique) »
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Glutathion (biosynthèse) < Glutathion (composition chimique) < Glutathion (déficit)  Facettes :

List of bibliographic references indexed by Glutathion (composition chimique)

Number of relevant bibliographic references: 78.
[0-20] [0 - 20][0 - 50][20-40]
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.
000027 (2020) Linda Liedgens [Allemagne] ; Jannik Zimmermann [Allemagne] ; Lucas W Schenbach [Allemagne] ; Fabian Geissel [Allemagne] ; Hugo Laporte [Allemagne] ; Holger Gohlke [Allemagne] ; Bruce Morgan [Allemagne] ; Marcel Deponte [Allemagne]Quantitative assessment of the determinant structural differences between redox-active and inactive glutaredoxins.
000157 (2019) Shadi Maghool [Australie] ; Sharon La Fontaine [Australie] ; Megan J. Maher [Australie]High-resolution crystal structure of the reduced Grx1 from Saccharomyces cerevisiae.
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.
000180 (2019) Grace Ahuié Kouakou [Canada] ; Hugo Gagnon [Canada] ; Vincent Lacasse [Canada] ; J Richard Wagner [Canada] ; Stephen Naylor [États-Unis] ; Klaus Klarskov [Canada]Dehydroascorbic acid S-Thiolation of peptides and proteins: Role of homocysteine and glutathione.
000243 (2018) Christina Brandstaedter [Allemagne] ; Karin Fritz-Wolf [Allemagne] ; Stine Weder [Allemagne] ; Marina Fischer [Allemagne] ; Beate Hecker [Allemagne] ; Stefan Rahlfs [Allemagne] ; Katja Becker [Allemagne]Kinetic characterization of wild-type and mutant human thioredoxin glutathione reductase defines its reaction and regulatory mechanisms.
000247 (2018) Sambuddha Sen [États-Unis] ; Claudia Bonfio [Italie] ; Sheref S. Mansy [Italie] ; J A Cowan [États-Unis]Investigation of glutathione-derived electrostatic and hydrogen-bonding interactions and their role in defining Grx5 [2Fe-2S] cluster optical spectra and transfer chemistry.
000307 (2017) Alexandra Müller [Allemagne] ; Jannis F. Schneider [Allemagne] ; Adriana Degrossoli [Allemagne] ; Nataliya Lupilova [Allemagne] ; Tobias P. Dick [Allemagne] ; Lars I. Leichert [Allemagne]Systematic in vitro assessment of responses of roGFP2-based probes to physiologically relevant oxidant species.
000314 (2017) Sambuddha Sen [États-Unis] ; J A Cowan [États-Unis]Role of protein-glutathione contacts in defining glutaredoxin-3 [2Fe-2S] cluster chirality, ligand exchange and transfer chemistry.
000315 (2017) Ashwinie A. Ukuwela [Australie] ; Ashley I. Bush [Australie] ; Anthony G. Wedd [Australie] ; Zhiguang Xiao [Australie]Reduction potentials of protein disulfides and catalysis of glutathionylation and deglutathionylation by glutaredoxin enzymes.
000318 (2017) Reiko Matsui [États-Unis] ; Yosuke Watanabe [Japon] ; Colin E. Murdoch [Royaume-Uni]Redox regulation of ischemic limb neovascularization - What we have learned from animal studies.
000450 (2016) Alexander V. Peskin ; Paul E. Pace ; Jessica B. Behring [États-Unis] ; Louise N. Paton ; Marjolein Soethoudt ; Markus M. Bachschmid [États-Unis] ; Christine C. Winterbourn [Nouvelle-Zélande]Glutathionylation of the Active Site Cysteines of Peroxiredoxin 2 and Recycling by Glutaredoxin.
000466 (2016) Lucia Coppo [Suède] ; Sergio J. Montano [Suède] ; Alicia C. Padilla [Espagne] ; Arne Holmgren [Suède]Determination of glutaredoxin enzyme activity and protein S-glutathionylation using fluorescent eosin-glutathione.
000469 (2016) Mohnad Abdalla [République populaire de Chine] ; Ya Nan Dai [République populaire de Chine] ; Chang Biao Chi [République populaire de Chine] ; Wang Cheng [République populaire de Chine] ; Dong Dong Cao [République populaire de Chine] ; Kang Zhou [République populaire de Chine] ; Wafa Ali [République populaire de Chine] ; Yuxing Chen [République populaire de Chine] ; Cong Zhao Zhou [République populaire de Chine]Crystal structure of yeast monothiol glutaredoxin Grx6 in complex with a glutathione-coordinated [2Fe-2S] cluster.
000499 (2015) Jérémy Couturier [France] ; Jonathan Przybyla-Toscano [France] ; Thomas Roret [France] ; Claude Didierjean [France] ; Nicolas Rouhier [France]The roles of glutaredoxins ligating Fe-S clusters: Sensing, transfer or repair functions?
000560 (2015) Samia Boukhenouna [France] ; Hortense Mazon ; Guy Branlant ; Christophe Jacob ; Michel B. Toledano ; Sophie Rahuel-ClermontEvidence that glutathione and the glutathione system efficiently recycle 1-cys sulfiredoxin in vivo.
000573 (2015) Constantine Chrysostomou [États-Unis] ; Erik M. Quandt [États-Unis] ; Nicholas M. Marshall [États-Unis] ; Everett Stone [États-Unis] ; George Georgiou [États-Unis]An alternate pathway of arsenate resistance in E. coli mediated by the glutathione S-transferase GstB.
000595 (2014) James D. Nolin [États-Unis] ; Jane E. Tully [États-Unis] ; Sidra M. Hoffman [États-Unis] ; Amy S. Guala [États-Unis] ; Jos L. Van Der Velden [États-Unis] ; Matthew E. Poynter [États-Unis] ; Albert Van Der Vliet [États-Unis] ; Vikas Anathy [États-Unis] ; Yvonne M W. Janssen-Heininger [États-Unis]The glutaredoxin/S-glutathionylation axis regulates interleukin-17A-induced proinflammatory responses in lung epithelial cells in association with S-glutathionylation of nuclear factor κB family proteins.
000597 (2014) Eun Hye Lee [Corée du Sud] ; Hwa-Young Kim [Corée du Sud] ; Kwang Yeon Hwang [Corée du Sud]The GSH- and GSSG-bound structures of glutaredoxin from Clostridium oremlandii.
000599 (2014) Jun Ye [République populaire de Chine] ; S Venkadesh Nadar [États-Unis] ; Jiaojiao Li [États-Unis] ; Barry P. Rosen [États-Unis]Structure of Escherichia coli Grx2 in complex with glutathione: a dual-function hybrid of glutaredoxin and glutathione S-transferase.
000612 (2014) Jens Brose [Australie] ; Sharon La Fontaine ; Anthony G. Wedd ; Zhiguang XiaoRedox sulfur chemistry of the copper chaperone Atox1 is regulated by the enzyme glutaredoxin 1, the reduction potential of the glutathione couple GSSG/2GSH and the availability of Cu(I).

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