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

Index « AbsEn.i » - entrée « catalysis »
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catalysing < catalysis < catalyst  Facettes :

List of bibliographic references indexed by catalysis

Number of relevant bibliographic references: 68.
[0-20] [0 - 20][0 - 50][20-40]
Ident.Authors (with country if any)Title
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.
000040 (2020) Jannik Zimmermann [Allemagne] ; Julian Oestreicher [Allemagne] ; Steffen Hess [Allemagne] ; Johannes M. Herrmann [Allemagne] ; Marcel Deponte [Allemagne] ; Bruce Morgan [Allemagne]One cysteine is enough: A monothiol Grx can functionally replace all cytosolic Trx and dithiol Grx.
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.
000234 (2018) Anju Sreelatha [États-Unis] ; Samantha S. Yee [États-Unis] ; Victor A. Lopez [États-Unis] ; Brenden C. Park [États-Unis] ; Lisa N. Kinch [États-Unis] ; Sylwia Pilch [Pologne] ; Kelly A. Servage [États-Unis] ; Junmei Zhang [États-Unis] ; Jenny Jiou [États-Unis] ; Monika Karasiewicz-Urba Ska [Pologne] ; Małgorzata Łobocka [Pologne] ; Nick V. Grishin [États-Unis] ; Kim Orth [États-Unis] ; Roza Kucharczyk [Pologne] ; Krzysztof Pawłowski [Pologne] ; Diana R. Tomchick [États-Unis] ; Vincent S. Tagliabracci [États-Unis]Protein AMPylation by an Evolutionarily Conserved Pseudokinase.
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.
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.
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.
000589 (2014) Rajib Sengupta [Suède] ; Arne Holmgren [Suède]Thioredoxin and glutaredoxin-mediated redox regulation of ribonucleotide reductase.
000598 (2014) Yajun Tang [République populaire de Chine] ; Jiahai Zhang ; Jiang Yu ; Ling Xu ; Jihui Wu ; Cong-Zhao Zhou ; Yunyu ShiStructure-guided activity enhancement and catalytic mechanism of yeast grx8.
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).
000626 (2014) Shuyan Li [République populaire de Chine] ; Yan Sun [République populaire de Chine] ; Xiaodan Qi [République populaire de Chine] ; Yan Shi [République populaire de Chine] ; Han Gao [République populaire de Chine] ; Qi Wu [République populaire de Chine] ; Xiucai Liu [République populaire de Chine] ; Haitao Yu [République populaire de Chine] ; Chunjing Zhang [République populaire de Chine]Protective effect and mechanism of glutaredoxin 1 on coronary arteries endothelial cells damage induced by high glucose.
000672 (2014) Jong Gyu Lim [Corée du Sud] ; Ye-Ji Bang [Corée du Sud] ; Sang Ho Choi [Corée du Sud]Characterization of the Vibrio vulnificus 1-Cys peroxiredoxin Prx3 and regulation of its expression by the Fe-S cluster regulator IscR in response to oxidative stress and iron starvation.
000756 (2013) Aaron L. Mclain [États-Unis] ; Peter J. Cormier [États-Unis] ; Michael Kinter [États-Unis] ; Luke I. Szweda [États-Unis]Glutathionylation of α-ketoglutarate dehydrogenase: the chemical nature and relative susceptibility of the cofactor lipoic acid to modification.
000758 (2013) Marcel Deponte [Allemagne]Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes.
000779 (2013) Christina L. Grek ; Jie Zhang ; Yefim Manevich ; Danyelle M. Townsend ; Kenneth D. TewCauses and consequences of cysteine S-glutathionylation.
000810 (2012) Olena Dobrovolska [Norvège] ; Elena Shumilina ; Vadim N. Gladyshev ; Alexander DikiyStructural analysis of glutaredoxin domain of Mus musculus thioredoxin glutathione reductase.
000820 (2012) Sang Gon Kim [États-Unis] ; Jung-Sung Chung ; R Bryan Sutton ; Jong-Sun Lee ; Luis L Pez-Maury ; Sang Yeol Lee ; Francisco J. Florencio ; Teresa Lin ; Masoud Zabet-Moghaddam ; Matthew J. Wood ; Kamakshi Nayak ; Vivek Madem ; Jatindra N. Tripathy ; Sung-Kun Kim ; David B. KnaffRedox, mutagenic and structural studies of the glutaredoxin/arsenate reductase couple from the cyanobacterium Synechocystis sp. PCC 6803.
000826 (2012) L. Tarrago [États-Unis] ; V N GladyshevRecharging oxidative protein repair: catalysis by methionine sulfoxide reductases towards their amino acid, protein, and model substrates.
000831 (2012) Bradford G. Hill [États-Unis] ; Aruni BhatnagarProtein S-glutathiolation: redox-sensitive regulation of protein function.
000837 (2012) Chiaki Inadomi [Japon] ; Hiroaki Murata ; Yoshito Ihara ; Shinji Goto ; Yoshishige Urata ; Junji Yodoi ; Takahito Kondo ; Koji SumikawaOverexpression of glutaredoxin protects cardiomyocytes against nitric oxide-induced apoptosis with suppressing the S-nitrosylation of proteins and nuclear translocation of GAPDH.
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.

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