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

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Cysteine (deficiency) < Cysteine (genetics) < Cysteine (isolation & purification)  Facettes :

List of bibliographic references indexed by Cysteine (genetics)

Number of relevant bibliographic references: 28.
[0-20] [0 - 20][0 - 28][20-27][20-40]
Ident.Authors (with country if any)Title
000124 (2019) Kwan Young Ko [Corée du Sud] ; Jea Hwang Lee [États-Unis] ; Jun Ki Jang [Corée du Sud] ; Yunjung Jin [Corée du Sud] ; Hyunwoo Kang [Corée du Sud] ; Ick Young Kim [Corée du Sud]S-Glutathionylation of mouse selenoprotein W prevents oxidative stress-induced cell death by blocking the formation of an intramolecular disulfide bond.
000299 (2017) Cyril Charbonnel [France] ; Adnan K. Niazi [France] ; Emilie Elvira-Matelot [France] ; Elzbieta Nowak [Pologne] ; Matthias Zytnicki [France] ; Anne De Bures [France] ; Edouard Jobet [France] ; Alisson Opsomer [France] ; Nahid Shamandi [France] ; Marcin Nowotny [Pologne] ; Christine Carapito [France] ; Jean-Philippe Reichheld [France] ; Hervé Vaucheret [France] ; Julio Sáez-Vásquez [France]The siRNA suppressor RTL1 is redox-regulated through glutathionylation of a conserved cysteine in the double-stranded-RNA-binding domain.
000317 (2017) Avinash Chandel [Inde] ; Anand K. Bachhawat [Inde]Redox regulation of the yeast voltage-gated Ca2+ channel homolog Cch1p by glutathionylation of specific cysteine residues.
000323 (2017) Vu Van Loi [Allemagne] ; Manuela Harms [Allemagne] ; Marret Müller [Allemagne] ; Nguyen Thi Thu Huyen [Allemagne] ; Chris J. Hamilton [Royaume-Uni] ; Falko Hochgr Fe [Allemagne] ; Jan Pané-Farré [Allemagne] ; Haike Antelmann [Allemagne]Real-Time Imaging of the Bacillithiol Redox Potential in the Human Pathogen Staphylococcus aureus Using a Genetically Encoded Bacilliredoxin-Fused Redox Biosensor.
000394 (2017) Christoph Loderer [Suède] ; Venkateswara Rao Jonna [Suède] ; Mikael Crona [Suède] ; Inna Rozman Grinberg [Suède] ; Margareta Sahlin [Suède] ; Anders Hofer [Suède] ; Daniel Lundin [Suède] ; Britt-Marie Sjöberg [Suède]A unique cysteine-rich zinc finger domain present in a majority of class II ribonucleotide reductases mediates catalytic turnover.
000422 (2016) Núria Vall-Llaura [Espagne] ; Gemma Reverter-Branchat [Espagne] ; Celia Vived [Espagne] ; Naomi Weertman [Espagne] ; María José Rodríguez-Colman [Espagne] ; Elisa Cabiscol [Espagne]Reversible glutathionylation of Sir2 by monothiol glutaredoxins Grx3/4 regulates stress resistance.
000670 (2014) Faraz Ahmad [Inde] ; Prakash Nidadavolu [Inde] ; Lalitha Durgadoss [Inde] ; Vijayalakshmi Ravindranath [Inde]Critical cysteines in Akt1 regulate its activity and proteasomal degradation: implications for neurodegenerative diseases.
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.
000757 (2013) Nicola Giangregorio [Italie] ; Ferdinando Palmieri ; Cesare IndiveriGlutathione controls the redox state of the mitochondrial carnitine/acylcarnitine carrier Cys residues by glutathionylation.
000805 (2012) Elke Ströher [Australie] ; A Harvey MillarThe biological roles of glutaredoxins.
000879 (2012) Romina Durigon [Royaume-Uni] ; Qi Wang ; Efrain Ceh Pavia ; Chris M. Grant ; Hui LuCytosolic thioredoxin system facilitates the import of mitochondrial small Tim proteins.
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.
000968 (2010) Tomoyuki Terada [Japon] ; Kei-Ichi Okamoto ; Jun-Ichi Nishikawa ; Takeshi Miura ; Toru Nishinaka ; Tsutomu NishiharaSite-directed mutagenesis of rat thioltransferase: effects of essential cysteine residues for the protection against oxidative stress.
000A01 (2010) Esther Jortzik [Allemagne] ; Karin Fritz-Wolf ; Nicole Sturm ; Marieke Hipp ; Stefan Rahlfs ; Katja BeckerRedox regulation of Plasmodium falciparum ornithine δ-aminotransferase.
000A45 (2010) Geun-Hee Kwak [Corée du Sud] ; Moon-Jung Kim ; Hwa-Young KimCysteine-125 is the catalytic residue of Saccharomyces cerevisiae free methionine-R-sulfoxide reductase.
000A64 (2010) Ling Meng [États-Unis] ; Joshua H. Wong ; Lewis J. Feldman ; Peggy G. Lemaux ; Bob B. BuchananA membrane-associated thioredoxin required for plant growth moves from cell to cell, suggestive of a role in intercellular communication.
000A69 (2009) Haoran Li [États-Unis] ; Daphne T. Mapolelo ; Nin N. Dingra ; Sunil G. Naik ; Nicholas S. Lees ; Brian M. Hoffman ; Pamela J. Riggs-Gelasco ; Boi Hanh Huynh ; Michael K. Johnson ; Caryn E. OuttenThe yeast iron regulatory proteins Grx3/4 and Fra2 form heterodimeric complexes containing a [2Fe-2S] cluster with cysteinyl and histidyl ligation.
000B04 (2009) Steve Lancel [États-Unis] ; Jingmei Zhang ; Alicia Evangelista ; Mario P. Trucillo ; Xiaoyong Tong ; Deborah A. Siwik ; Richard A. Cohen ; Wilson S. ColucciNitroxyl activates SERCA in cardiac myocytes via glutathiolation of cysteine 674.
000C56 (2007) Christina Vieira Dos Santos [France] ; Edith Laugier ; Lionel Tarrago ; Vincent Massot ; Emmanuelle Issakidis-Bourguet ; Nicolas Rouhier ; Pascal ReySpecificity of thioredoxins and glutaredoxins as electron donors to two distinct classes of Arabidopsis plastidial methionine sulfoxide reductases B.
000D14 (2006) Ana Garcerá [Espagne] ; Lina Barreto ; Lidia Piedrafita ; Jordi Tamarit ; Enrique HerreroSaccharomyces cerevisiae cells have three Omega class glutathione S-transferases acting as 1-Cys thiol transferases.
000D40 (2006) Mirva J. Peltoniemi [Finlande] ; Anna-Riikka Karala ; Jaana K. Jurvansuu ; Vuokko L. Kinnula ; Lloyd W. RuddockInsights into deglutathionylation reactions. Different intermediates in the glutaredoxin and protein disulfide isomerase catalyzed reactions are defined by the gamma-linkage present in glutathione.

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