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

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Catalase (physiologie) < Catalyse (MeSH) < Cataracte (anatomopathologie)  Facettes :

List of bibliographic references indexed by Catalyse (MeSH)

Number of relevant bibliographic references: 91.
[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.
000126 (2019) Victoria I. Bunik [Russie]Redox-Driven Signaling: 2-Oxo Acid Dehydrogenase Complexes as Sensors and Transmitters of Metabolic Imbalance.
000146 (2019) Zhiguang Xiao [Australie] ; Sharon La Fontaine [Australie] ; Ashley I. Bush [Australie] ; Anthony G. Wedd [Australie]Molecular Mechanisms of Glutaredoxin Enzymes: Versatile Hubs for Thiol-Disulfide Exchange between Protein Thiols and Glutathione.
000217 (2018) Parismita Kalita [Inde] ; Harish Shukla [Inde] ; Kundlik Gadhave [Inde] ; Rajanish Giri [Inde] ; Timir Tripathi [Inde]Role of the glutaredoxin domain and FAD in the stabilization of thioredoxin glutathione reductase.
000271 (2018) Maria-Armineh Tossounian [Belgique] ; Inge Van Molle [Belgique] ; Khadija Wahni [Belgique] ; Silke Jacques [Belgique] ; Kris Gevaert [Belgique] ; Frank Van Breusegem [Belgique] ; Didier Vertommen [Belgique] ; David Young [Belgique] ; Leonardo Astolfi Rosado [Belgique] ; Joris Messens [Belgique]Disulfide bond formation protects Arabidopsis thaliana glutathione transferase tau 23 from oxidative damage.
000295 (2018) Inna Rozman Grinberg [Suède] ; Daniel Lundin [Suède] ; Margareta Sahlin [Suède] ; Mikael Crona [Suède] ; Gustav Berggren [Suède] ; Anders Hofer [Suède] ; Britt-Marie Sjöberg [Suède]A glutaredoxin domain fused to the radical-generating subunit of ribonucleotide reductase (RNR) functions as an efficient RNR reductant.
000346 (2017) Susanna Boronat [Espagne] ; Alba Domènech [Espagne] ; Mercè Carmona [Espagne] ; Sarela García-Santamarina [Espagne] ; M Carmen Ba [Espagne] ; José Ayté [Espagne] ; Elena Hidalgo [Espagne]Lack of a peroxiredoxin suppresses the lethality of cells devoid of electron donors by channelling electrons to oxidized ribonucleotide reductase.
000362 (2017) Patricia Begas [Allemagne] ; Linda Liedgens [Allemagne] ; Anna Moseler [Allemagne] ; Andreas J. Meyer [Allemagne] ; Marcel Deponte [Allemagne]Glutaredoxin catalysis requires two distinct glutathione interaction sites.
000503 (2015) Michele Scian [États-Unis] ; William M. Atkins [États-Unis]The busulfan metabolite EdAG irreversibly glutathionylates glutaredoxins.
000516 (2015) Benjaminas Valiauga [Lituanie] ; Nicolas Rouhier [France] ; Jean-Pierre Jacquot [France] ; Narimantas Nas [Lituanie]Quinone- and nitroreductase reactions of Thermotoga maritima thioredoxin reductase.
000555 (2015) James N. Vranish [États-Unis] ; William K. Russell ; Lusa E. Yu ; Rachael M. Cox ; David H. Russell ; David P. BarondeauFluorescent probes for tracking the transfer of iron-sulfur cluster and other metal cofactors in biosynthetic reaction pathways.
000561 (2015) Eun Hye Lee [Corée du Sud] ; Kitaik Lee [Corée du Sud] ; Geun-Hee Kwak [Corée du Sud] ; Yeon Seung Park [Corée du Sud] ; Kong-Joo Lee [Corée du Sud] ; Kwang Yeon Hwang [Corée du Sud] ; Hwa-Young Kim [Corée du Sud]Evidence for the dimerization-mediated catalysis of methionine sulfoxide reductase A from Clostridium oremlandii.
000712 (2013) Robert J. Hondal [États-Unis] ; Stefano M. Marino ; Vadim N. GladyshevSelenocysteine in thiol/disulfide-like exchange reactions.
000729 (2013) Carine F. Djuika [Allemagne] ; Sabine Fiedler ; Martina Schnölzer ; Cecilia Sanchez ; Michael Lanzer ; Marcel DepontePlasmodium falciparum antioxidant protein as a model enzyme for a special class of glutaredoxin/glutathione-dependent peroxiredoxins.
000731 (2013) Sylvain Boutigny [États-Unis] ; Avneesh Saini ; Edward E K. Baidoo ; Natasha Yeung ; Jay D. Keasling ; Gareth ButlandPhysical and functional interactions of a monothiol glutaredoxin and an iron sulfur cluster carrier protein with the sulfur-donating radical S-adenosyl-L-methionine enzyme MiaB.
000743 (2013) Ceren Alkim [France] ; Laurent Benbadis ; Ulku Yilmaz ; Z Petek Cakar ; Jean Marie FrançoisMechanisms other than activation of the iron regulon account for the hyper-resistance to cobalt of a Saccharomyces cerevisiae strain obtained by evolutionary engineering.
000751 (2013) Jérémy Couturier [France] ; Pascalita Prosper ; Alison M. Winger ; Arnaud Hecker ; Masakazu Hirasawa ; David B. Knaff ; Pierre Gans ; Jean-Pierre Jacquot ; Alda Navaza ; Ahmed Haouz ; Nicolas RouhierIn the absence of thioredoxins, what are the reductants for peroxiredoxins in Thermotoga maritima?
000758 (2013) Marcel Deponte [Allemagne]Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes.
000759 (2013) Christopher Horst Lillig [Allemagne] ; Carsten BerndtGlutaredoxins in thiol/disulfide exchange.
000807 (2012) Nicolas Foloppe [Royaume-Uni] ; Alexios Vlamis-Gardikas ; Lennart NilssonThe -Cys-X1-X2-Cys- motif of reduced glutaredoxins adopts a consensus structure that explains the low pK(a) of its catalytic cysteine.

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