Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Karine Pereira de Jésus"'
Autor:
Line Cantin, Pierre Legrand, Karine Pereira de Jésus-Tran, Anne-Marie Roy, Pierre-Luc Côté, Van Luu-The, Fernand Labrie, Rock Breton, Jean-François Couture
Publikováno v:
Protein Science. 14:1485-1497
The aldo-keto reductase (AKR) human type 3 3alpha-hydroxysteroid dehydrogenase (h3alpha-HSD3, AKR1C2) plays a crucial role in the regulation of the intracellular concentrations of testosterone and 5alpha-dihydrotestosterone (5alpha-DHT), two steroids
Autor:
Mélanie Lemieux, Van Luu-The, Rock Breton, Karine Pereira de Jésus-Tran, Line Cantin, Fernand Labrie, F. Faucher
Publikováno v:
Journal of Molecular Biology. 369:525-540
The mouse 17alpha-hydroxysteroid dehydrogenase (m17alpha-HSD) is the unique known member of the aldo-keto reductase (AKR) superfamily able to catalyze efficiently and in a stereospecific manner the conversion of androstenedione (Delta4) into epi-test
Autor:
Fernand Labrie, Line Cantin, Jonathan Blanchet, Rock Breton, Karine Pereira de Jésus-Tran, Pierre-Luc Côté
Publikováno v:
Protein Science. 15:987-999
Androgens exert their effects by binding to the highly specific androgen receptor (AR). In addition to natural potent androgens, AR binds a variety of synthetic agonist or antagonist molecules with different affinities. To identify molecular determin
Publikováno v:
EMBO Journal
EMBO Journal, 2002, 21 (12), pp.2854-2865. ⟨10.1093/emboj/cdf304⟩
EMBO Journal, EMBO Press, 2002, 21 (12), pp.2854-2865. ⟨10.1093/emboj/cdf304⟩
EMBO Journal, 2002, 21 (12), pp.2854-2865. ⟨10.1093/emboj/cdf304⟩
EMBO Journal, EMBO Press, 2002, 21 (12), pp.2854-2865. ⟨10.1093/emboj/cdf304⟩
International audience; The formamidopyrimidine-DNA glycosylase (Fpg, MutM) is a bifunctional base excision repair enzyme (DNA glycosylase/AP lyase) that removes a wide range of oxidized purines, such as 8-oxoguanine and imidazole ring-opened purines
Autor:
Charles Zelwer, Bertrand Castaing, Karine Pereira de Jésus, Laurence Serre, Nadège Hervouet, Véronique Bouckson-Castaing
Publikováno v:
Acta Crystallographica Section D: Biological Crystallography
Acta Crystallographica Section D: Biological Crystallography, International Union of Crystallography, 2002, 58 (4), pp.679-682. ⟨10.1107/S0907444902001397⟩
Acta crystallographica Section D : Structural biology [1993-...]
Acta crystallographica Section D : Structural biology [1993-..], 2002, 58 (4), pp.679-682. ⟨10.1107/S0907444902001397⟩
Acta Crystallographica Section D: Biological Crystallography, International Union of Crystallography, 2002, 58 (4), pp.679-682. ⟨10.1107/S0907444902001397⟩
Acta crystallographica Section D : Structural biology [1993-...]
Acta crystallographica Section D : Structural biology [1993-..], 2002, 58 (4), pp.679-682. ⟨10.1107/S0907444902001397⟩
International audience; For protein-DNA complex crystallization, the choice of the DNA fragment is crucial. With the aim of crystallizing the 31 kDa Fpg DNA-repair enzyme bound to DNA, oligonucleotide duplexes varying in length, sequence, end type an
Autor:
Nicole Bureaud, Hélène Bénédetti, Charles Zelwer, Karine Pereira de Jésus, Françoise Schoentgen, Laurence Serre
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2001, 310 (3), pp.617-634. ⟨10.1006/jmbi.2001.4784⟩
Journal of Molecular Biology, Elsevier, 2001, 310 (3), pp.617-634. ⟨10.1006/jmbi.2001.4784⟩
International audience; In rat and human cells, RKIP (previously known as PEBP) was characterized as an inhibitor of the MEK phosphorylation by Raf-1. In Escherichia coli, the genes ybhb and ybcl possibly encode two RKIP homologues while in the genom
Autor:
F. Faucher, Line Cantin, Fernand Labrie, Karine Pereira de Jésus-Tran, Rock Breton, Van Luu-The
Publikováno v:
Journal of molecular biology. 364(4)
Very recently, the mouse 17alpha-hydroxysteroid dehydrogenase (m17alpha-HSD), a member of the aldo-keto reductase (AKR) superfamily, has been characterized and identified as the unique enzyme able to catalyze efficiently and in a stereospecific manne
Publikováno v:
Nucleic Acids Research
Fpg is a DNA glycosylase that recognizes and excises the mutagenic 8-oxoguanine (8-oxoG) and the potentially lethal formamidopyrimidic residues (Fapy). Fpg is also associated with an AP lyase activity which successively cleaves the abasic (AP) site a