Chromatographie sur DEAE-cellulose < Chromatographie sur gel < Chromobacterium

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List of bibliographic references indexed by Chromatographie sur gel

Number of relevant bibliographic references: 18.

Ident.	Authors (with country if any)	Title
000113 (2019)	Haoran Li [États-Unis] ; Caryn E. Outten [États-Unis]	The conserved CDC motif in the yeast iron regulator Aft2 mediates iron-sulfur cluster exchange and protein-protein interactions with Grx3 and Bol2.
000637 (2014)	Catherine B. Poor [États-Unis] ; Seraphine V. Wegner ; Haoran Li ; Adrienne C. Dlouhy ; Jonathan P. Schuermann ; Ruslan Sanishvili ; James R. Hinshaw ; Pamela J. Riggs-Gelasco ; Caryn E. Outten ; Chuan He	Molecular mechanism and structure of the Saccharomyces cerevisiae iron regulator Aft2.
000708 (2013)	Xi Liu [République populaire de Chine] ; Shian Liu ; Yingang Feng ; Jian-Zhong Liu ; Yuling Chen ; Khanh Pham ; Haiteng Deng ; Kendal D. Hirschi ; Xinquan Wang ; Ninghui Cheng	Structural insights into the N-terminal GIY-YIG endonuclease activity of Arabidopsis glutaredoxin AtGRXS16 in chloroplasts.
000911 (2011)	N. Yeung [États-Unis] ; B. Gold ; N L Liu ; R. Prathapam ; H J Sterling ; E R Willams ; G. Butland	The E. coli monothiol glutaredoxin GrxD forms homodimeric and heterodimeric FeS cluster containing complexes.
000946 (2011)	Katsunobu Hagihara [Japon] ; Miho Kazui ; Atsushi Kurihara ; Kazuishi Kubota ; Toshihiko Ikeda	Glutaredoxin and thioredoxin can be involved in producing the pharmacologically active metabolite of a thienopyridine antiplatelet agent, prasugrel.
000B59 (2008)	Nikola Mesecke [Allemagne] ; Sarah Mittler ; Elisabeth Eckers ; Johannes M. Herrmann ; Marcel Deponte	Two novel monothiol glutaredoxins from Saccharomyces cerevisiae provide further insight into iron-sulfur cluster binding, oligomerization, and enzymatic activity of glutaredoxins.
000C19 (2008)	Michael Filser [Allemagne] ; Marcelo A. Comini ; Maria M. Molina-Navarro ; Natalie Dirdjaja ; Enrique Herrero ; R Luise Krauth-Siegel	Cloning, functional analysis, and mitochondrial localization of Trypanosoma brucei monothiol glutaredoxin-1.
000E15 (2005)	Min Li [République populaire de Chine] ; Wei Huang ; Qing Yang ; Xingguo Liu ; Qingyu Wu	Expression and oxidative stress tolerance studies of glutaredoxin from cyanobacterium Synechocystis sp. PCC 6803 in Escherichia coli.
000E60 (2004)	Juan L. Rend N [Mexique] ; Irene P. Del Arenal ; Alberto Guevara-Flores ; Aida Uribe ; Agustín Plancarte ; Guillermo Mendoza-Hernández	Purification, characterization and kinetic properties of the multifunctional thioredoxin-glutathione reductase from Taenia crassiceps metacestode (cysticerci).
001124 (1998)	M. Dal Monte [Italie] ; I. Cecconi ; F. Buono ; P G Vilardo ; A. Del Corso ; U. Mura	Thioltransferase activity of bovine lens glutathione S-transferase.
001234 (1994)	F. Aslund [Suède] ; B. Ehn ; A. Miranda-Vizuete ; C. Pueyo ; A. Holmgren	Two additional glutaredoxins exist in Escherichia coli: glutaredoxin 3 is a hydrogen donor for ribonucleotide reductase in a thioredoxin/glutaredoxin 1 double mutant.
001242 (1994)	E. Maellaro [Italie] ; B. Del Bello ; L. Sugherini ; A. Santucci ; M. Comporti ; A F Casini	Purification and characterization of glutathione-dependent dehydroascorbate reductase from rat liver.
001264 (1993)	T. Terada [Japon] ; H. Maeda ; K. Okamoto ; T. Nishinaka ; T. Mizoguchi ; T. Nishihara	Modulation of glutathione S-transferase activity by a thiol/disulfide exchange reaction and involvement of thioltransferase.
001265 (1993)	T. Mizoguchi [Japon] ; T. Nishnaka ; G. Uchida ; J. Mizuta ; H. Uchida ; T. Terada ; H. Toya	Inhibition of bovine leukocyte thioltransferase by anti-inflammatory drugs and anti-histaminic drugs.
001310 (1990)	Z R Gan [États-Unis] ; M K Sardana ; J W Jacobs ; M A Polokoff	Yeast thioltransferase--the active site cysteines display differential reactivity.
001353 (1985)	K. Larson ; V. Eriksson ; B. Mannervik	Thioltransferase from human placenta.
001358 (1985)	A. Holmgren	Glutaredoxin from Escherichia coli and calf thymus.
001375 (1981)	B. Mannervik ; K. Axelsson ; K. Larson	Thioltransferase.

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