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

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thiobacillus < thiol < thiolate  Facettes :

List of bibliographic references indexed by thiol

Number of relevant bibliographic references: 110.
[0-20] [0 - 20][0 - 50][20-40]
Ident.Authors (with country if any)Title
000008 (2020) Inken Lorenzen [Allemagne] ; Johannes A. Eble [Allemagne] ; Eva-Maria Hanschmann [Allemagne]Thiol switches in membrane proteins - Extracellular redox regulation in cell biology.
000056 (2020) Grace Kouakou Ahuie [Canada] ; Hugo Gagnon [Canada] ; Paul E. Pace [Nouvelle-Zélande] ; Alexander V. Peskin [Nouvelle-Zélande] ; Richard J. Wagner [Canada] ; Stephen Naylor [États-Unis] ; Klaus Klarskov [Canada]Investigating protein thiol chemistry associated with dehydroascorbate, homocysteine and glutathione using mass spectrometry.
000105 (2019) M J L Pez-Grueso [Espagne] ; R. González-Ojeda [Espagne] ; R. Requejo-Aguilar [Espagne] ; B. Mcdonagh [Irlande (pays)] ; C A Fuentes-Almagro [Espagne] ; J. Muntané [Irlande (pays)] ; J A Bárcena [Espagne] ; C A Padilla [Espagne]Thioredoxin and glutaredoxin regulate metabolism through different multiplex thiol switches.
000112 (2019) Gavin Douglas Ferguson [Australie] ; Wallace John Bridge [Australie]The glutathione system and the related thiol network in Caenorhabditis elegans.
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.
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.
000177 (2019) Joseph J. Braymer [Allemagne] ; Martin Stümpfig [Allemagne] ; Stefanie Thelen [Allemagne] ; Ulrich Mühlenhoff [Allemagne] ; Roland Lill [Allemagne]Depletion of thiol reducing capacity impairs cytosolic but not mitochondrial iron-sulfur protein assembly machineries.
000203 (2018) Laura Martins [France] ; José Abraham Trujillo-Hernandez [France] ; Jean-Philippe Reichheld [France]Thiol Based Redox Signaling in Plant Nucleus.
000213 (2018) Denise Lacerda [Brésil] ; Vanessa Ortiz [Brésil] ; Patrick Türck [Brésil] ; Cristina Campos-Carraro [Brésil] ; Alexsandra Zimmer [Brésil] ; Rayane Teixeira [Brésil] ; Sara Bianchi [Brésil] ; Alexandre Luz De Castro [Brésil] ; Paulo Cavalheiro Schenkel [Brésil] ; Adriane Bell Klein [Brésil] ; Valquiria Linck Bassani [Brésil] ; Alex Sander Da Rosa Araujo [Brésil]Stilbenoid pterostilbene complexed with cyclodextrin preserves left ventricular function after myocardial infarction in rats: possible involvement of thiol proteins and modulation of phosphorylated GSK-3β.
000241 (2018) Yanfang Ouyang [République populaire de Chine] ; Yi Peng ; Jing Li ; Arne Holmgren ; Jun LuModulation of thiol-dependent redox system by metal ions via thioredoxin and glutaredoxin systems.
000257 (2018) Ashwinie A. Ukuwela [Australie] ; Ashley I. Bush [Australie] ; Anthony G. Wedd [Australie] ; Zhiguang Xiao [Australie]Glutaredoxins employ parallel monothiol-dithiol mechanisms to catalyze thiol-disulfide exchanges with protein disulfides.
000310 (2017) Kathrin Ulrich [Allemagne] ; Caroline Finkenzeller [Allemagne] ; Sabine Merker [Allemagne] ; Federico Rojas [Royaume-Uni] ; Keith Matthews [Royaume-Uni] ; Thomas Ruppert [Allemagne] ; R Luise Krauth-Siegel [Allemagne]Stress-Induced Protein S-Glutathionylation and S-Trypanothionylation in African Trypanosomes-A Quantitative Redox Proteome and Thiol Analysis.
000437 (2016) Valérie Delorme-Hinoux [France] ; Sajid A K. Bangash [Allemagne] ; Andreas J. Meyer [Allemagne] ; Jean-Philippe Reichheld [France]Nuclear thiol redox systems in plants.
000445 (2016) Marcelo A. Comini [Uruguay]Measurement and meaning of cellular thiol:disufhide redox status.
000472 (2016) Luis Eduardo S. Netto ; Marcos Antonio De Oliveira ; Carlos A. Tairum ; José Freire Da Silva NetoConferring specificity in redox pathways by enzymatic thiol/disulfide exchange reactions.
000479 (2016) Sidra M. Hoffman ; James D. Nolin ; Jane T. Jones ; Karolyn G. Lahue ; David G. Chapman [États-Unis] ; Minara Aliyeva ; Nirav Daphtary [États-Unis] ; Lennart K A. Lundblad [États-Unis] ; Sarah Abdalla ; Jennifer L. Ather [États-Unis] ; Ye-Shih Ho ; Charles G. Irvin [États-Unis] ; Vikas Anathy ; Emiel F M. Wouters [Pays-Bas] ; Matthew E. Poynter [États-Unis] ; Yvonne M W. Janssen-HeiningerAblation of the Thiol Transferase Glutaredoxin-1 Augments Protein S-Glutathionylation and Modulates Type 2 Inflammatory Responses and IL-17 in a House Dust Mite Model of Allergic Airway Disease in Mice.
000495 (2015) Vladimir L. Kolossov ; Jessica N. Beaudoin ; Nagendraprabhu Ponnuraj ; Stephen J. Diliberto ; William P. Hanafin ; Paul J A. Kenis ; H Rex GaskinsThiol-based antioxidants elicit mitochondrial oxidation via respiratory complex III.
000496 (2015) Gethin J. Mcbean [Irlande (pays)] ; Mutay Aslan [Turquie] ; Helen R. Griffiths [Royaume-Uni] ; Rita C. Torrão [Royaume-Uni]Thiol redox homeostasis in neurodegenerative disease.
000502 (2015) Lefentse N. Mashamaite [Afrique du Sud] ; Johann M. Rohwer [Afrique du Sud] ; Ché S. Pillay [Afrique du Sud]The glutaredoxin mono- and di-thiol mechanisms for deglutathionylation are functionally equivalent: implications for redox systems biology.
000521 (2015) Kaavya A. Mohanasundaram [Australie] ; Naomi L. Haworth [Australie] ; Mani P. Grover [Australie] ; Tamsyn M. Crowley [Australie] ; Andrzej Goscinski [Australie] ; Merridee A. Wouters [Australie]Potential role of glutathione in evolution of thiol-based redox signaling sites in proteins.
000539 (2015) Kerstin Kojer [Allemagne] ; Valentina Peleh [Allemagne] ; Gaetano Calabrese [Allemagne] ; Johannes M. Herrmann [Allemagne] ; Jan Riemer [Allemagne]Kinetic control by limiting glutaredoxin amounts enables thiol oxidation in the reducing mitochondrial intermembrane space.

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