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

Index « MedMesh.i » - entrée « Biocatalysis »
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.
Binding, Competitive < Biocatalysis < Biodegradation, Environmental  Facettes :

List of bibliographic references

Number of relevant bibliographic references: 19.
Ident.Authors (with country if any)Title
000278 (2018) Ji Liu ; Shuke Wu ; Zhi LiRecent advances in enzymatic oxidation of alcohols.
000282 (2018) Christina Brandstaedter ; Karin Fritz-Wolf ; Stine Weder ; Marina Fischer ; Beate Hecker ; Stefan Rahlfs ; Katja BeckerKinetic characterization of wild-type and mutant human thioredoxin glutathione reductase defines its reaction and regulatory mechanisms.
000330 (2017) Leonardo Astolfi Rosado ; Khadija Wahni ; Giulia Degiacomi ; Brandán Pedre ; David Young ; Alfonso G. De La Rubia ; Francesca Boldrin ; Edo Martens ; Laura Marcos-Pascual ; Enea Sancho-Vaello ; David Albesa-Jové ; Roberta Provvedi ; Charlotte Martin ; Vadim Makarov ; Wim Versées ; Guido Verniest ; Marcelo E. Guerin ; Luis M. Mateos ; Riccardo Manganelli ; Joris MessensThe antibacterial prodrug activator Rv2466c is a mycothiol-dependent reductase in the oxidative stress response of Mycobacterium tuberculosis.
000497 (2015) Ankita Gupta ; Tripti Pandey ; Bijay Kumar ; Timir TripathiPreferential regeneration of thioredoxin from parasitic flatworm Fasciola gigantica using glutathione system.
000604 (2014) Vanina E. Márquez ; Diego G. Arias ; Maria L. Chiribao ; Paula Faral-Tello ; Carlos Robello ; Alberto A. Iglesias ; Sergio A. GuerreroRedox metabolism in Trypanosoma cruzi. Biochemical characterization of dithiol glutaredoxin dependent cellular pathways.
000611 (2014) Ulrich Schweizer ; Christine Schlicker ; Doreen Braun ; Josef Köhrle ; Clemens SteegbornCrystal structure of mammalian selenocysteine-dependent iodothyronine deiodinase suggests a peroxiredoxin-like catalytic mechanism.
000639 (2014) Kristine Steen Jensen ; Jeppe T. Pedersen ; Jakob R. Winther ; Kaare TeilumThe pKa value and accessibility of cysteine residues are key determinants for protein substrate discrimination by glutaredoxin.
000643 (2014) Yajun Tang ; Jiahai Zhang ; Jiang Yu ; Ling Xu ; Jihui Wu ; Cong-Zhao Zhou ; Yunyu ShiStructure-guided activity enhancement and catalytic mechanism of yeast grx8.
000662 (2014) Mackenzie J. Parker ; Xuling Zhu ; Joanne StubbeBacillus subtilis class Ib ribonucleotide reductase: high activity and dynamic subunit interactions.
000668 (2014) Martín Hugo ; Koen Van Laer ; Aníbal M. Reyes ; Didier Vertommen ; Joris Messens ; Rafael Radi ; Madia TrujilloMycothiol/mycoredoxin 1-dependent reduction of the peroxiredoxin AhpE from Mycobacterium tuberculosis.
000877 (2012) Sang Gon Kim ; 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.
000918 (2011) Hsin-Hung Huang ; Latasha Day ; Cynthia L. Cass ; David P. Ballou ; Charles H. Williams ; David L. WilliamsInvestigations of the catalytic mechanism of thioredoxin glutathione reductase from Schistosoma mansoni.
000A94 (2009) Ji Won Park ; John J. Mieyal ; Sue Goo Rhee ; P Boon ChockDeglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin.
000A95 (2009) Scott W. Aesif ; Vikas Anathy ; Marije Havermans ; Amy S. Guala ; Karina Ckless ; Douglas J. Taatjes ; Yvonne M W. Janssen-HeiningerIn situ analysis of protein S-glutathionylation in lung tissue using glutaredoxin-1-catalyzed cysteine derivatization.
000B06 (2009) Adam P. Lothrop ; Erik L. Ruggles ; Robert J. HondalNo selenium required: reactions catalyzed by mammalian thioredoxin reductase that are independent of a selenocysteine residue.
000B08 (2009) Mirva J. Saaranen ; Kirsi E H. Salo ; Maria K. Latva-Ranta ; Vuokko L. Kinnula ; Lloyd W. RuddockThe C-terminal active site cysteine of Escherichia coli glutaredoxin 1 determines the glutathione specificity of the second step of peptide deglutathionylation.
000B11 (2009) Zai-Rong Zhang ; Sarah PerrettNovel glutaredoxin activity of the yeast prion protein Ure2 reveals a native-like dimer within fibrils.
000B31 (2009) Elisabeth Eckers ; Melanie Bien ; Vincent Stroobant ; Johannes M. Herrmann ; Marcel DeponteBiochemical characterization of dithiol glutaredoxin 8 from Saccharomyces cerevisiae: the catalytic redox mechanism redux.
000B32 (2009) Markus Eser ; Lluis Masip ; Hiroshi Kadokura ; George Georgiou ; Jonathan BeckwithDisulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E. coli periplasm.

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Bois/explor/GlutaredoxinV1/Data/Main/Corpus
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Corpus/MedMesh.i -k "Biocatalysis" 
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Corpus/MedMesh.i  \
                -Sk "Biocatalysis" \
         | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd 

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Bois
   |area=    GlutaredoxinV1
   |flux=    Main
   |étape=   Corpus
   |type=    indexItem
   |index=    MedMesh.i
   |clé=    Biocatalysis
}}

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