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

Index « KwdFr.i » - entrée « Protein-disulfide reductase (glutathione) (composition chimique) »
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.
Protein-disulfide reductase (glutathione) (classification) < Protein-disulfide reductase (glutathione) (composition chimique) < Protein-disulfide reductase (glutathione) (génétique)  Facettes :

List of bibliographic references indexed by Protein-disulfide reductase (glutathione) (composition chimique)

Number of relevant bibliographic references: 10.
Ident.Authors (with country if any)Title
000196 (2018) Subhash C. Bihani [Inde] ; Lata Panicker [Inde] ; Yogendra S. Rajpurohit [Inde] ; Hari S. Misra [Inde] ; Vinay Kumar [Inde]drFrnE Represents a Hitherto Unknown Class of Eubacterial Cytoplasmic Disulfide Oxido-Reductases.
000415 (2016) Deepa Yenugudhati [États-Unis] ; Divya Prakash [États-Unis] ; Adepu K. Kumar [États-Unis] ; R Siva Sai Kumar [États-Unis] ; Neela H. Yennawar [États-Unis] ; Hemant P. Yennawar [États-Unis] ; James G. Ferry [États-Unis]Structural and Biochemical Characterizations of Methanoredoxin from Methanosarcina acetivorans, a Glutaredoxin-Like Enzyme with Coenzyme M-Dependent Protein Disulfide Reductase Activity.
000A71 (2009) Yvonne Carius [Allemagne] ; Dagmar Rother ; Cornelius G. Friedrich ; Axel J. ScheidigThe structure of the periplasmic thiol-disulfide oxidoreductase SoxS from Paracoccus pantotrophus indicates a triple Trx/Grx/DsbC functionality in chemotrophic sulfur oxidation.
000C67 (2007) Toshimitsu Niwa [Japon]Protein glutathionylation and oxidative stress.
000D11 (2006) Kenji Maeda [Danemark] ; Per H Gglund ; Christine Finnie ; Birte Svensson ; Anette HenriksenStructural basis for target protein recognition by the protein disulfide reductase thioredoxin.
000F55 (2003) Yasuhiro Kashima [Japon] ; Kazuhiko IshikawaA hyperthermostable novel protein-disulfide oxidoreductase is reduced by thioredoxin reductase from hyperthermophilic archaeon Pyrococcus horikoshii.
001056 (2000) R A Fabianek [Suisse] ; H. Hennecke ; L. Thöny-MeyerPeriplasmic protein thiol:disulfide oxidoreductases of Escherichia coli.
001089 (1999) J S Fetrow [États-Unis] ; N. Siew ; J. SkolnickStructure-based functional motif identifies a potential disulfide oxidoreductase active site in the serine/threonine protein phosphatase-1 subfamily.
001139 (1998) J S Fetrow [États-Unis] ; J. SkolnickMethod for prediction of protein function from sequence using the sequence-to-structure-to-function paradigm with application to glutaredoxins/thioredoxins and T1 ribonucleases.
001144 (1998) J S Fetrow [États-Unis] ; A. Godzik ; J. SkolnickFunctional analysis of the Escherichia coli genome using the sequence-to-structure-to-function paradigm: identification of proteins exhibiting the glutaredoxin/thioredoxin disulfide oxidoreductase activity.

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 "Protein-disulfide reductase (glutathione) (composition chimique)" 
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/KwdFr.i  \
                -Sk "Protein-disulfide reductase (glutathione) (composition chimique)" \
         | 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=    Protein-disulfide reductase (glutathione) (composition chimique)
}}

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