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

Index « KwdFr.i » - entrée « Protéines (métabolisme) »
Attention, ce site est en cours de développement !
Attention, site généré par des moyens informatiques à partir de corpus bruts.
Les informations ne sont donc pas validées.
Protéines (isolement et purification) < Protéines (métabolisme) < Protéines (pharmacologie)  Facettes :

List of bibliographic references indexed by Protéines (métabolisme)

Number of relevant bibliographic references: 193.
[20-40] [0 - 20][0 - 50][40-60]
Ident.Authors (with country if any)Title
000978 (2010) Toru Sugiyama [États-Unis] ; Thomas MichelThiol-metabolizing proteins and endothelial redox state: differential modulation of eNOS and biopterin pathways.
000993 (2010) Enrique Herrero [Espagne] ; Gemma Bellí ; Celia CasaStructural and functional diversity of glutaredoxins in yeast.
000A44 (2010) Ulrich Mühlenhoff [Allemagne] ; Sabine Molik [Allemagne] ; José R. Godoy [Allemagne] ; Marta A. Uzarska [Allemagne] ; Nadine Richter [Allemagne] ; Andreas Seubert [Allemagne] ; Yan Zhang [États-Unis] ; Joanne Stubbe [États-Unis] ; Fabien Pierrel [France] ; Enrique Herrero [Espagne] ; Christopher Horst Lillig [Allemagne] ; Roland Lill [Allemagne]Cytosolic monothiol glutaredoxins function in intracellular iron sensing and trafficking via their bound iron-sulfur cluster.
000A85 (2009) Silke Essler [Allemagne] ; Nathalie Dehne ; Bernhard BrüneRole of sestrin2 in peroxide signaling in macrophages.
000B12 (2009) Jorge M. Romero [États-Unis] ; Oscar A. BizzozeroIntracellular glutathione mediates the denitrosylation of protein nitrosothiols in the rat spinal cord.
000B83 (2008) Lisa M. Landino [États-Unis]Protein thiol modification by peroxynitrite anion and nitric oxide donors.
000C10 (2008) B. Mcdonagh [Irlande (pays)] ; D. SheehanEffects of oxidative stress on protein thiols and disulphides in Mytilus edulis revealed by proteomics: actin and protein disulphide isomerase are redox targets.
000C44 (2007) V L Kinnula [Finlande] ; K. Vuorinen ; H. Ilumets ; P. Rytil ; M. Myll RniemiThiol proteins, redox modulation and parenchymal lung disease.
000D16 (2006) John E. Biaglow [États-Unis] ; Iraimoudi S. Ayene ; Stephen W. Tuttle ; Cameron J. Koch ; Jeremiah Donahue ; John J. MieyalRole of vicinal protein thiols in radiation and cytotoxic responses.
000D22 (2006) Saibal Biswas [Inde] ; Asiya Seema Chida ; Irfan RahmanRedox modifications of protein-thiols: emerging roles in cell signaling.
000D29 (2006) Aleksandra Filipovska [Royaume-Uni] ; Michael P. MurphyOverview of protein glutathionylation.
000D37 (2006) Aleksandra Filipovska [Royaume-Uni] ; Michael P. MurphyMeasurement of protein glutathionylation.
000D72 (2005) Paolo Di Simplicio [Italie] ; Simona Frosali ; Raffaella Priora ; Domenico Summa ; Francesca Cherubini Di Simplicio ; Danila Di Giuseppe ; Anna Di StefanoBiochemical and biological aspects of protein thiolation in cells and plasma.
000D80 (2005) J-E Oh [Autriche] ; K. Karlmark Raja ; J-H Shin ; M. Hengstschl Ger ; A. Pollak ; G. LubecThe neuronal differentiation process involves a series of antioxidant proteins.
000D89 (2005) Pietro Ghezzi [Italie]Regulation of protein function by glutathionylation.
000E36 (2004) Mee-Kyung Cha [Corée du Sud] ; Seung-Keun Hong ; Dong-Suk Lee ; Il-Han KimVibrio cholerae thiol peroxidase-glutaredoxin fusion is a 2-Cys TSA/AhpC subfamily acting as a lipid hydroperoxide reductase.
000E50 (2004) Gemma Bellí [Espagne] ; María Micaela Molina ; José García-Martínez ; José E. Pérez-Ortín ; Enrique HerreroSaccharomyces cerevisiae glutaredoxin 5-deficient cells subjected to continuous oxidizing conditions are affected in the expression of specific sets of genes.
000E54 (2004) Jennifer F. Caplan [Canada] ; Nolan R. Filipenko ; Sandra L. Fitzpatrick ; David M. WaismanRegulation of annexin A2 by reversible glutathionylation.
000E70 (2004) Henrik Stergaard [Danemark] ; Christine Tachibana ; Jakob R. WintherMonitoring disulfide bond formation in the eukaryotic cytosol.
000E76 (2004) Catrine Johansson [Suède] ; Christopher Horst Lillig ; Arne HolmgrenHuman mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase.
000E94 (2004) Raffaele Lopreiato [Italie] ; Sonia Facchin ; Geppo Sartori ; Giorgio Arrigoni ; Stefano Casonato ; Maria Ruzzene ; Lorenzo A. Pinna ; Giovanna CarignaniAnalysis of the interaction between piD261/Bud32, an evolutionarily conserved protein kinase of Saccharomyces cerevisiae, and the Grx4 glutaredoxin.

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Bois/explor/GlutaredoxinV1/Data/Main/Exploration
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/KwdFr.i -k "Protéines (métabolisme)" 
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/KwdFr.i  \
                -Sk "Protéines (métabolisme)" \
         | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd 

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Bois
   |area=    GlutaredoxinV1
   |flux=    Main
   |étape=   Exploration
   |type=    indexItem
   |index=    KwdFr.i
   |clé=    Protéines (métabolisme)
}}

Wicri

This area was generated with Dilib version V0.6.37.
Data generation: Wed Nov 18 15:13:42 2020. Site generation: Wed Nov 18 15:16:12 2020