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

Index « MedMesh.i » - entrée « Hydrogen Bonding »
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List of bibliographic references

Number of relevant bibliographic references: 18.
Ident.Authors (with country if any)Title
000093 (2020) Soumila Mondal ; Vinod Kumar ; Shailendra P. SinghPhylogenetic distribution and structural analyses of cyanobacterial glutaredoxins (Grxs).
000276 (2018) Sambuddha Sen ; Claudia Bonfio ; Sheref S. Mansy ; J A CowanInvestigation of glutathione-derived electrostatic and hydrogen-bonding interactions and their role in defining Grx5 [2Fe-2S] cluster optical spectra and transfer chemistry.
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.
000687 (2014) Koen Van Laer ; Margarida Oliveira ; Khadija Wahni ; Joris MessensThe concerted action of a positive charge and hydrogen bonds dynamically regulates the pKa of the nucleophilic cysteine in the NrdH-redoxin family.
000738 (2013) Swastik Phulera ; Shekhar C. MandeThe crystal structure of Mycobacterium tuberculosis NrdH at 0.87 Å suggests a possible mode of its activity.
000838 (2012) Saurabh Yadav ; Hemant Ritturaj Kushwaha ; Kamal Kumar ; Praveen Kumar VermaComparative structural modeling of a monothiol GRX from chickpea: insight in iron-sulfur cluster assembly.
000A45 (2010) Talia Shekhter ; Norman Metanis ; Philip E. Dawson ; Ehud KeinanA residue outside the active site CXXC motif regulates the catalytic efficiency of Glutaredoxin 3.
000A99 (2009) Thomas Iwema ; Antoine Picciocchi ; Daouda A K. Traore ; Jean-Luc Ferrer ; Franck Chauvat ; Lilian JacquametStructural basis for delivery of the intact [Fe2S2] cluster by monothiol glutaredoxin.
000B18 (2009) Luca Federici ; Michele Masulli ; Stefano Gianni ; Carmine Di Ilio ; Nerino AllocatiA conserved hydrogen-bond network stabilizes the structure of Beta class glutathione S-transferases.
000B33 (2009) Jeremy Couturier ; Cha San Koh ; Mirko Zaffagnini ; Alison M. Winger ; Jose Manuel Gualberto ; Catherine Corbier ; Paulette Decottignies ; Jean-Pierre Jacquot ; Stéphane D. Lemaire ; Claude Didierjean ; Nicolas RouhierStructure-function relationship of the chloroplastic glutaredoxin S12 with an atypical WCSYS active site.
000E16 (2005) Malin Fladvad ; Massimo Bellanda ; Aristi Potamitou Fernandes ; Stefano Mammi ; Alexios Vlamis-Gardikas ; Arne Holmgren ; Maria SunnerhagenMolecular mapping of functionalities in the solution structure of reduced Grx4, a monothiol glutaredoxin from Escherichia coli.
000F79 (2002) Bin Xia ; Vickie Tsui ; David A. Case ; H Jane Dyson ; Peter E. WrightComparison of protein solution structures refined by molecular dynamics simulation in vacuum, with a generalized Born model, and with explicit water.
001027 (2001) N. Foloppe ; J. Sagemark ; K. Nordstrand ; K D Berndt ; L. NilssonStructure, dynamics and electrostatics of the active site of glutaredoxin 3 from Escherichia coli: comparison with functionally related proteins.
001056 (2000) K. Nordstrand ; A. Sandström ; F. Aslund ; A. Holmgren ; G. Otting ; K D BerndtNMR structure of oxidized glutaredoxin 3 from Escherichia coli.
001108 (1999) K. Nordstrand ; F. Aslund ; S. Meunier ; A. Holmgren ; G. Otting ; K D BerndtDirect NMR observation of the Cys-14 thiol proton of reduced Escherichia coli glutaredoxin-3 supports the presence of an active site thiol-thiolate hydrogen bond.
001253 (1994) J H Bushweller ; M. Billeter ; A. Holmgren ; K. WüthrichThe nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin(C14S) and glutathione.
001275 (1992) H. Eklund ; M. Ingelman ; B O Söderberg ; T. Uhlin ; P. Nordlund ; M. Nikkola ; U. Sonnerstam ; T. Joelson ; K. PetratosStructure of oxidized bacteriophage T4 glutaredoxin (thioredoxin). Refinement of native and mutant proteins.
001312 (1990) O. Nilsson ; O. Tapia ; W F Van GunsterenStructure and fluctuations of bacteriophage T4 glutaredoxin modelled by molecular dynamics.

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