Glutathione Reductase (isolation & purification) < Glutathione Reductase (metabolism) < Glutathione Reductase (physiology)

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List of bibliographic references indexed by Glutathione Reductase (metabolism)

Number of relevant bibliographic references: 69.
[0-20] [0 - 20][0 - 50][20-40]

Ident.	Authors (with country if any)	Title
000039 (2020)	Anil Kumar [Inde] ; Arvind Kumar Dubey [Inde] ; Varun Kumar [Inde] ; Mohd Akram Ansari [Inde] ; Shiv Narayan [Inde] ; Meenakshi [Inde] ; Sanoj Kumar [Inde] ; Vivek Pandey [Inde] ; Pramod Arvind Shirke [Inde] ; Veena Pande [Inde] ; Indraneel Sanyal [Inde]	Over-expression of chickpea glutaredoxin (CaGrx) provides tolerance to heavy metals by reducing metal accumulation and improved physiological and antioxidant defence system.
000099 (2019)	N Y Rusetskaya [Russie] ; I V Fedotov [Russie] ; V A Koftina [Russie] ; V B Borodulin [Russie]	[Selenium compounds in redox regulation of inflammation and apoptosis].
000202 (2018)	Haijie Ma [République populaire de Chine] ; Mingshuang Wang [République populaire de Chine] ; Yunpeng Gai [République populaire de Chine] ; Huilan Fu [République populaire de Chine] ; Bin Zhang [République populaire de Chine] ; Ruoxin Ruan [République populaire de Chine] ; Kuang-Ren Chung [Taïwan] ; Hongye Li [Taïwan, République populaire de Chine]	Thioredoxin and Glutaredoxin Systems Required for Oxidative Stress Resistance, Fungicide Sensitivity, and Virulence of Alternaria alternata.
000232 (2018)	Donatella Pietraforte [Italie] ; Eleonora Paulicelli [Italie] ; Clarice Patrono [Italie] ; Lucrezia Gambardella [Italie] ; Giuseppe Scorza [Italie] ; Antonella Testa [Italie] ; Paola Fattibene [Italie]	Protein oxidative damage and redox imbalance induced by ionising radiation in CHO cells.
000297 (2017)	E A Stepovaya [Russie] ; E V Shakhristova [Russie] ; O L Nosareva [Russie] ; E V Rudikov [Russie] ; M Y Egorova [Russie] ; D Y Egorova [Russie] ; V V Novitsky [Russie]	[Redox-dependent mechanisms of regulation of breast epithelial cell proliferation].
000358 (2017)	Justin R. Prigge [États-Unis] ; Lucia Coppo [Suède] ; Sebastin S. Martin [Suède] ; Fernando Ogata [Suède] ; Colin G. Miller [États-Unis] ; Michael D. Bruschwein [États-Unis] ; David J. Orlicky [États-Unis] ; Colin T. Shearn [États-Unis] ; Jean A. Kundert [États-Unis] ; Julia Lytchier [Suède] ; Alix E. Herr [États-Unis] ; Se Mattsson [Suède] ; Matthew P. Taylor [États-Unis] ; Tomas N. Gustafsson [Suède] ; Elias S J. Arnér [Suède] ; Arne Holmgren [Suède] ; Edward E. Schmidt [États-Unis]	Hepatocyte Hyperproliferation upon Liver-Specific Co-disruption of Thioredoxin-1, Thioredoxin Reductase-1, and Glutathione Reductase.
000395 (2017)	Agustín Plancarte [Mexique] ; Gabriela Nava [Mexique] ; Javier A. Munguía [Mexique]	A new thioredoxin reductase with additional glutathione reductase activity in Haemonchus contortus.
000425 (2016)	Long-Bin Zhang [République populaire de Chine] ; Li Tang [République populaire de Chine] ; Sheng-Hua Ying [République populaire de Chine] ; Ming-Guang Feng [République populaire de Chine]	Regulative roles of glutathione reductase and four glutaredoxins in glutathione redox, antioxidant activity, and iron homeostasis of Beauveria bassiana.
000435 (2016)	Pankaj Kumar Verma [Inde] ; Shikha Verma [Inde] ; Alok Kumar Meher [Inde] ; Veena Pande [Inde] ; Shekhar Mallick [Inde] ; Amit Kumar Bansiwal [Inde] ; Rudra Deo Tripathi [Inde] ; Om Parkash Dhankher [États-Unis] ; Debasis Chakrabarty [Inde]	Overexpression of rice glutaredoxins (OsGrxs) significantly reduces arsenite accumulation by maintaining glutathione pool and modulating aquaporins in yeast.
000463 (2016)	Ruixia Dong [République populaire de Chine] ; Dongxu Wang [République populaire de Chine] ; Xiaoxiao Wang [République populaire de Chine] ; Ke Zhang [République populaire de Chine] ; Pingping Chen [République populaire de Chine] ; Chung S. Yang [République populaire de Chine] ; Jinsong Zhang [République populaire de Chine]	Epigallocatechin-3-gallate enhances key enzymatic activities of hepatic thioredoxin and glutathione systems in selenium-optimal mice but activates hepatic Nrf2 responses in selenium-deficient mice.
000533 (2015)	Narin Changklungmoa [Oman] ; Pornanan Kueakhai ; Kant Sangpairoj ; Pannigan Chaichanasak ; Wipaphorn Jaikua ; Suda Riengrojpitak ; Prasert Sobhon ; Kulathida Chaithirayanon	Molecular cloning and characterization of Fasciola gigantica thioredoxin-glutathione reductase.
000581 (2014)	O O Honchar ; I M Man'Kovs'Ka	[Mitochondrial thiol-disulfide system under acute hypoxia and hypoxic-hyperoxic adaptation].
000676 (2014)	Pamela Lopert [États-Unis] ; Manisha Patel [États-Unis]	Brain mitochondria from DJ-1 knockout mice show increased respiration-dependent hydrogen peroxide consumption.
000698 (2013)	Yatao Du [Suède] ; Huihui Zhang ; Xu Zhang ; Jun Lu ; Arne Holmgren	Thioredoxin 1 is inactivated due to oxidation induced by peroxiredoxin under oxidative stress and reactivated by the glutaredoxin system.
000758 (2013)	Marcel Deponte [Allemagne]	Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes.
000796 (2012)	Esther Jortzik [Allemagne] ; Katja Becker	Thioredoxin and glutathione systems in Plasmodium falciparum.
000798 (2012)	Karouk Said [Suède] ; Hans Glaumann ; Mikael Björnstedt ; Annika Bergquist	The value of thioredoxin family proteins and proliferation markers in dysplastic and malignant gallbladders in patients with primary sclerosing cholangitis.
000872 (2012)	Yuta Hatori [États-Unis] ; Sara Clasen ; Nesrin M. Hasan ; Amanda N. Barry ; Svetlana Lutsenko	Functional partnership of the copper export machinery and glutathione balance in human cells.
000873 (2012)	Viswanadham Duppatla [Allemagne] ; Maja Gjorgjevikj ; Werner Schmitz ; Mathias Kottmair ; Thomas D. Mueller ; Walter Sebald	Enzymatic deglutathionylation to generate interleukin-4 cysteine muteins with free thiol.
000877 (2012)	Ye Yuan [États-Unis] ; Matthew B. Wheeler ; Rebecca L. Krisher	Disrupted redox homeostasis and aberrant redox gene expression in porcine oocytes contribute to decreased developmental competence.
000904 (2011)	Yu Yu [Australie] ; Yohan Suryo Rahmanto ; Clare L. Hawkins ; Des R. Richardson	The potent and novel thiosemicarbazone chelators di-2-pyridylketone-4,4-dimethyl-3-thiosemicarbazone and 2-benzoylpyridine-4,4-dimethyl-3-thiosemicarbazone affect crucial thiol systems required for ribonucleotide reductase activity.

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