Zobrazeno 1 - 10
of 151
pro vyhledávání: '"M. Defais"'
Autor:
M. Defais, Ulrike Sattler, Federica Bogani, Wiriya Rutvisuttinunt, Virneliz Fernandez, Paul E. Boehmer, Ilsa Corredeira
Publikováno v:
Journal of Biological Chemistry. 285:27664-27672
Herpes simplex virus-1 (HSV-1) is a large dsDNA virus that encodes its own DNA replication machinery and other enzymes involved in DNA transactions. We recently reported that the HSV-1 DNA polymerase catalytic subunit (UL30) exhibits apurinic/apyrimi
Publikováno v:
Journal of Biological Chemistry. 278:3545-3551
RecA protein from Escherichia coli catalyzes DNA strand exchange during homologous recombination in a reaction that requires nucleoside triphosphate cofactor. In the first step of this reaction RecA protein polymerizes on single-stranded DNA to form
Publikováno v:
Journal of Biological Chemistry. 276:9613-9619
The bacterial recombinase RecA forms a nucleoprotein filament in vitro with single-stranded DNA (ssDNA) at its primary DNA binding site, site I. This filament has a second site, site II, which binds ssDNA and double-stranded DNA. We have investigated
Autor:
Neil P. Johnson, M. Defais, Jean-Sébastien Blanchet, Giuseppe Villani, Delphine Dupuis, Christophe Cazaux
Publikováno v:
Journal of Biological Chemistry. 273:28799-28804
The L2 loop is a DNA-binding site of RecA protein, a recombinase from Eschericha coli. Two DNA-binding sites have been functionally defined in this protein. To determine whether the L2 loop of RecA protein is part of the primary or secondary binding
Autor:
Stéphane Vispé, M. Defais
Publikováno v:
Biochimie. 79:587-592
During the last years, homologues of E coli RecA have been cloned in numerous species including man. These Rad51 proteins share sequence as well as functional homologies with the bacterial protein. Human Rad51 (HsRad51) is able to catalyze strand exc
Autor:
Florence Larminat, M. Defais, Christophe Cazaux, Neil P. Johnson, Giuseppe Villani, Manfred Schnarr
Publikováno v:
Journal of Biological Chemistry. 269:8246-8254
Escherichia coli RecA protein plays a central role both in DNA repair and in recombination. We report biochemical properties of three new RecA proteins mutated at positions 199 (RecA694), 207 (RecA659), and 211 (RecA611) in the putative DNA binding s
Publikováno v:
Petit, P, Cayrol, C, Lesca, C, Kaiser, P, Thompson, C & Defais, M 1993, ' Characterisation of dinY, a new Escherichia coli DNA repair gene whose products are damage inducible even in a lexA(Def) background ', Journal of Bacteriology, vol. 175, pp. 642-646 .
Bacteriophage Mu dX(Ap lac) was used to isolate a mutation in an Escherichia coli lexA(Def) strain representing a previously undescribed gene (dinY) which does not seem to be under the direct control of LexA. The insertion created a dinY::lacZ fusion
Publikováno v:
Biochimie. 73:281-284
Escherichia coli RecA protein plays a fundamental role in genetic recombination and in regulation and expression of the SOS response. We have constructed 6 mutants in the recA gene by site-directed mutagenesis, 5 of which were located in the vicinity
Publikováno v:
Biochimie. 79:261-263
The UVU1 CHO cell line, a double mutant of the excision repair complementation group 1 UV4 cell line was characterized by a higher UV sensitivity than its parent (Busch et al (1989) Mutagenesis 4, 349–354). We show here that this mutant is not affe
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2002, 277 (7), pp.4764-9. ⟨10.1074/jbc.M108447200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2002, 277 (7), pp.4764-9. ⟨10.1074/jbc.M108447200⟩
DNA cross-linking agents such as mitomycin C (MMC) and cisplatin are used as chemotherapeutic agents in cancer treatment. However, the molecular mechanism underlying their antitumor activity is not entirely clear. Critical steps in cytotoxicity towar
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https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e60cace40c98f3e07a737ca7bb7949cf
https://hal.archives-ouvertes.fr/hal-00317396
https://hal.archives-ouvertes.fr/hal-00317396