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

Index « ISSN » - entrée « 0006-2960 »
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0006-2952 < 0006-2960 < 0006-2979  Facettes :

List of bibliographic references indexed by 0006-2960

Number of relevant bibliographic references: 41.
[20-40] [0 - 20][0 - 41][40-40][40-60]
Ident.Authors (with country if any)Title
001091 (1999) S Y Stevens [États-Unis] ; W. Hu ; T. Gladysheva ; B P Rosen ; E R Zuiderweg ; L. LeeSecondary structure and fold homology of the ArsC protein from the Escherichia coli arsenic resistance plasmid R773.
001092 (1999) W C Barrett [États-Unis] ; J P Degnore ; S. König ; H M Fales ; Y F Keng ; Z Y Zhang ; M B Yim ; P B ChockRegulation of PTP1B via glutathionylation of the active site cysteine 215.
001126 (1998) H. Ding [États-Unis] ; B. DempleThiol-mediated disassembly and reassembly of [2Fe-2S] clusters in the redox-regulated transcription factor SoxR.
001134 (1998) Y. Yang [États-Unis] ; S C Jao ; S. Nanduri ; D W Starke ; J J Mieyal ; J. QinReactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity.
001135 (1998) M J Berardi [États-Unis] ; C L Pendred ; J H BushwellerPreparation, characterization, and complete heteronuclear NMR resonance assignments of the glutaredoxin (C14S)-ribonucleotide reductase B1 737-761 (C754S) mixed disulfide.
001156 (1997) U. Srinivasan [États-Unis] ; P A Mieyal ; J J MieyalpH profiles indicative of rate-limiting nucleophilic displacement in thioltransferase catalysis.
001176 (1997) M. Ruoppolo [Italie] ; J. Lundström-Ljung ; F. Talamo ; P. Pucci ; G. MarinoEffect of glutaredoxin and protein disulfide isomerase on the glutathione-dependent folding of ribonuclease A.
001178 (1997) J J Kelley [États-Unis] ; T M Caputo ; S F Eaton ; T M Laue ; J H BushwellerComparison of backbone dynamics of reduced and oxidized Escherichia coli glutaredoxin-1 using 15N NMR relaxation measurements.
001192 (1996) D M Lemaster [États-Unis]Structural determinants of the catalytic reactivity of the buried cysteine of Escherichia coli thioredoxin.
001221 (1995) J. Liu [États-Unis] ; T B Gladysheva ; L. Lee ; B P RosenIdentification of an essential cysteinyl residue in the ArsC arsenate reductase of plasmid R773.
001244 (1994) T B Gladysheva [États-Unis] ; K L Oden ; B P RosenProperties of the arsenate reductase of plasmid R773.
001253 (1994) G. Ji ; E A Garber ; L G Armes ; C M Chen ; J A Fuchs ; S. SilverArsenate reductase of Staphylococcus aureus plasmid pI258.
001259 (1993) S A Gravina [États-Unis] ; J J MieyalThioltransferase is a specific glutathionyl mixed disulfide oxidoreductase.
001262 (1993) F. Siedler [Allemagne] ; S. Rudolph-Böhner ; M. Doi ; H J Musiol ; L. MoroderRedox potentials of active-site bis(cysteinyl) fragments of thiol-protein oxidoreductases.
001274 (1993) M. Nikkola ; A. Engström ; M. Saarinen ; M. Ingelman ; T. Joelson ; H. EklundAn elongated form of T4 glutaredoxin with four extra residues.
001280 (1992) J H Bushweller [Suède] ; F. Aslund ; K. Wüthrich ; A. HolmgrenStructural and functional characterization of the mutant Escherichia coli glutaredoxin (C14----S) and its mixed disulfide with glutathione.
001286 (1992) L B Ellis ; P. Saurugger ; C. WoodwardIdentification of the three-dimensional thioredoxin motif: related structure in the ORF3 protein of the Staphylococcus aureus mer operon.
001293 (1991) J J Mieyal [États-Unis] ; D W Starke ; S A Gravina ; C. Dothey ; J S ChungThioltransferase in human red blood cells: purification and properties.
001294 (1991) J J Mieyal [États-Unis] ; D W Starke ; S A Gravina ; B A HocevarThioltransferase in human red blood cells: kinetics and equilibrium.
001305 (1991) V A Sandberg ; B. Kren ; J A Fuchs ; C. WoodwardEscherichia coli glutaredoxin: cloning and overexpression, thermodynamic stability of the oxidized and reduced forms, and report of an N-terminal extended species.
001336 (1988) R. Kishore ; S. Raghothama ; P. BalaramSynthetic peptide models for the redox-active disulfide loop of glutaredoxin. Conformational studies.

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