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

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List of bibliographic references indexed by active

Number of relevant bibliographic references: 44.
[0-20] [0 - 20][0 - 44][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.
000044 (2020) Daniel Trnka [Allemagne] ; Anna D. Engelke [Allemagne] ; Manuela Gellert [Allemagne] ; Anna Moseler [Allemagne, France] ; Md Faruq Hossain [Allemagne] ; Tobias T. Lindenberg [Allemagne] ; Luca Pedroletti [Allemagne] ; Benjamin Odermatt [Allemagne] ; João V. De Souza [Royaume-Uni] ; Agnieszka K. Bronowska [Royaume-Uni] ; Tobias P. Dick [Allemagne] ; Uli Mühlenhoff [Allemagne] ; Andreas J. Meyer [Allemagne] ; Carsten Berndt [Allemagne] ; Christopher Horst Lillig [Allemagne]Molecular basis for the distinct functions of redox-active and FeS-transfering glutaredoxins.
000152 (2019) Bruno Manta [Uruguay] ; Matías N. Möller ; Mariana Bonilla [Uruguay] ; Matías Deambrosi [Uruguay] ; Karin Grunberg [Uruguay] ; Massimo Bellanda [Italie] ; Marcelo A. Comini [Uruguay] ; Gerardo Ferrer-Sueta [Uruguay]Kinetic studies reveal a key role of a redox-active glutaredoxin in the evolution of the thiol-redox metabolism of trypanosomatid parasites.
000348 (2017) Jack D. Stopa [États-Unis] ; Katherine M. Baker [États-Unis] ; Steven P. Grover [États-Unis] ; Robert Flaumenhaft [États-Unis] ; Bruce Furie [États-Unis]Kinetic-based trapping by intervening sequence variants of the active sites of protein-disulfide isomerase identifies platelet protein substrates.
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.
000632 (2014) Hsu-Han Chuang [Taïwan] ; Chu-Ying Cheng ; Yu-Ting Chen ; Jei-Fu ShawNovel highly active recombinant glutaredoxin from Chlorella sorokiniana T-89.
000641 (2014) Olof Björnberg [Danemark] ; Petr Efler [Danemark] ; Epie Denis Ebong [Danemark] ; Birte Svensson [Danemark] ; Per H Gglund [Danemark]Lactococcus lactis TrxD represents a subgroup of thioredoxins prevalent in Gram-positive bacteria containing WCXDC active site motifs.
000702 (2013) Marcus Cebula [Suède] ; Naazneen Moolla ; Alexio Capovilla ; Elias S J. ArnérThe rare TXNRD1_v3 ("v3") splice variant of human thioredoxin reductase 1 protein is targeted to membrane rafts by N-acylation and induces filopodia independently of its redox active site integrity.
000866 (2012) Katsunobu Hagihara [Japon] ; Miho Kazui ; Atsushi Kurihara ; Toshihiko Ikeda ; Takashi IzumiGlutaredoxin is involved in the formation of the pharmacologically active metabolite of clopidogrel from its GSH conjugate.
000887 (2012) Kamel Chibani [France] ; Lionel Tarrago ; José Manuel Gualberto ; Gunnar Wingsle ; Pascal Rey ; Jean-Pierre Jacquot ; Nicolas RouhierAtypical thioredoxins in poplar: the glutathione-dependent thioredoxin-like 2.1 supports the activity of target enzymes possessing a single redox active cysteine.
000946 (2011) Katsunobu Hagihara [Japon] ; Miho Kazui ; Atsushi Kurihara ; Kazuishi Kubota ; Toshihiko IkedaGlutaredoxin and thioredoxin can be involved in producing the pharmacologically active metabolite of a thienopyridine antiplatelet agent, prasugrel.
000A00 (2010) Rocío G Mez-Pastor [Espagne] ; Roberto Pérez-Torrado ; Elisa Cabiscol ; Joaquim Ros ; Emilia MatallanaReduction of oxidative cellular damage by overexpression of the thioredoxin TRX2 gene improves yield and quality of wine yeast dry active biomass.
000A11 (2010) Elena Garre [Espagne] ; Françoise Raginel ; Antonio Palacios ; Anne Julien ; Emilia MatallanaOxidative stress responses and lipid peroxidation damage are induced during dehydration in the production of dry active wine yeasts.
000A62 (2010) Talia Shekhter [Israël] ; Norman Metanis ; Philip E. Dawson ; Ehud KeinanA residue outside the active site CXXC motif regulates the catalytic efficiency of Glutaredoxin 3.
000A77 (2009) Mirva J. Saaranen [Finlande] ; Kirsi E H. Salo ; Maria K. Latva-Ranta ; Vuokko L. Kinnula ; Lloyd W. RuddockThe C-terminal active site cysteine of Escherichia coli glutaredoxin 1 determines the glutathione specificity of the second step of peptide deglutathionylation.
000A78 (2009) Jeremy Couturier [France] ; Cha San Koh ; Mirko Zaffagnini ; Alison M. Winger ; Jose Manuel Gualberto ; Catherine Corbier ; Paulette Decottignies ; Jean-Pierre Jacquot ; Stéphane D. Lemaire ; Claude Didierjean ; Nicolas RouhierStructure-function relationship of the chloroplastic glutaredoxin S12 with an atypical WCSYS active site.
000C60 (2007) Catrine Johansson [Royaume-Uni] ; Kathryn L. Kavanagh ; Opher Gileadi ; Udo OppermannReversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria.
000D10 (2006) Yingang Feng [République populaire de Chine] ; Nan Zhong ; Nicolas Rouhier ; Toshiharu Hase ; Masami Kusunoki ; Jean-Pierre Jacquot ; Changwen Jin ; Bin XiaStructural insight into poplar glutaredoxin C1 with a bridging iron-sulfur cluster at the active site.
000D67 (2006) V V Lyakhovich [Russie] ; V A Vavilin ; N K Zenkov ; E B MenshchikovaActive defense under oxidative stress. The antioxidant responsive element.
000E61 (2004) George Hoppe [États-Unis] ; Yuh-Cherng Chai ; John W. Crabb ; Jonathan SearsProtein s-glutathionylation in retinal pigment epithelium converts heat shock protein 70 to an active chaperone.

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