Zobrazeno 1 - 10 of 16 pro vyhledávání: '"David Lascoux"'
1
A ZnS4 Structural Zinc Site in the Helicobacter pylori Ferric Uptake Regulator
Autor: Isabelle Michaud-Soret, David Lascoux, Kristine Schauer, Sylvia Vitale, Christine Saint-Pierre, Caroline Fauquant
Publikováno v: Biochemistry
Biochemistry, American Chemical Society, 2009, 48 (24), pp.5582-91. ⟨10.1021/bi9004396⟩
Biochemistry, American Chemical Society, 2009, 48 (24), pp.5582-5591. ⟨10.1021/bi9004396⟩
Biochemistry, 2009, 48 (24), pp.5582-91. ⟨10.1021/bi9004396⟩
International audience; The ferric uptake regulator, Fur, is a global bacterial transcriptional regulator using iron as a cofactor to bind to specific DNA sequences. This paper describes the biochemical characterization of the native ferric uptake re
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2cfb3b874c97eae42b7faeb8a38ec71c
https://doi.org/10.1021/bi9004396
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2
Structural and functional characterization of 2-oxo-histidine in oxidized PerR protein
Autor: Jean-Marc Latour, Michel Jaquinod, Jean-Luc Ravanat, Abdelnasser El Ghazouani, David Lascoux, Franck Borel, Christelle Caux-Thang, Lilian Jacquamet, Jean Luc Ferrer, Daouda A K Traore, Geneviève Blondin, Victor Duarte
Publikováno v: Nature Chemical Biology
Nature Chemical Biology, Nature Publishing Group, 2008, 5 (1), pp.53. ⟨10.1038/nchembio.133⟩
Nature Chemical Biology, Nature Publishing Group, 2009, 5 (1), pp.53-9. ⟨10.1038/nchembio.133⟩
Nature Chemical Biology, 2009, 5 (1), pp.53-9. ⟨10.1038/nchembio.133⟩
International audience; In Bacillus subtilis, PerR is a metal-dependent sensor of hydrogen peroxide. PerR is a dimeric zinc protein with a regulatory site that coordinates either Fe(2+) (PerR-Zn-Fe) or Mn(2+) (PerR-Zn-Mn). Though most of the peroxide
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc65808a28dfb79c695cc9cab0764a75
https://doi.org/10.1038/nchembio.133
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3
CopH from Cupriavidus metallidurans CH34. A Novel Periplasmic Copper-Binding Protein
Autor: David Lascoux, Franck Fieschi, Stéphane Ménage, Dominique Cannella, Jacques Covès, Beate Bersch, Véronique Sendra
Publikováno v: Biochemistry. 45:5557-5566
The copH gene is one of the 19 open reading frames (ORFs) found in the cop cluster borne by the large plasmid pMol30 in Cupriavidus metallidurans CH34. The entire cluster is involved in detoxification of copper from the cytoplasm as well as from the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c17a4d22fac14f17d4fff427865b1a0
https://doi.org/10.1021/bi060328q
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4
Analysis of the Heteromeric CsdA-CsdE Cysteine Desulfurase, Assisting Fe-S Cluster Biogenesis in Escherichia coli
Autor: Eric Forest, Frédéric Barras, Sandrine Ollagnier de Choudens, Laurent Loiseau, Marc Fontecave, David Lascoux
Publikováno v: Journal of Biological Chemistry. 280:26760-26769
Biogenesis of iron-sulfur (Fe-S) cluster-containing proteins relies on assistance of complex machineries. To date three systems, NIF, ISC, and SUF, were reported to allow maturation of Fe-S proteins. Here we report that the csdA-csdE (formally ygdK)
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::348cca39989d26c1d42529cd32feb5ca
https://doi.org/10.1074/jbc.m504067200
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6
Mechanistic studies of the SufS-SufE cysteine desulfurase: evidence for sulfur transfer from SufS to SufE
Autor: Laurent Loiseau, Sandrine Ollagnier-de-Choudens, Frédéric Barras, Marc Fontecave, David Lascoux, Eric Forest
Publikováno v: FEBS Letters. 555:263-267
SufS is a cysteine desulfurase of the suf operon shown to be involved in iron–sulfur cluster biosynthesis under iron limitation and oxidative stress conditions. The enzyme catalyzes the conversion of L-cysteine to L-alanine and sulfide through the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::099d879f3239e1ad08f2d86c7a3c5d8f
https://doi.org/10.1016/s0014-5793(03)01244-4
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7
The Crystal Structure of the Epstein–Barr Virus Protease Shows Rearrangement of the Processed C Terminus
Autor: Marlyse Buisson, Eric Forest, Guy Schoehn, Jean-Marie Seigneurin, Rob W.H. Ruigrok, Gérard J. Arlaud, Wim P. Burmeister, Jean-François Hernandez, David Lascoux
Publikováno v: Journal of Molecular Biology. 324:89-103
Epstein-Barr virus (EBV) belongs to the gamma-herpesvirinae subfamily of the Herpesviridae. The protease domain of the assemblin protein of herpesviruses forms a monomer-dimer equilibrium in solution. The protease domain of EBV was expressed in Esche
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f24e38d8a36784e9eb57a7b7845c2c7d
https://doi.org/10.1016/s0022-2836(02)01040-9
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8
Involvement of the C-terminal end of the prostrate-specific antigen in a conformational epitope: characterization by proteolytic degradation of monoclonal antibody-bound antigen and mass spectrometry
Autor: Yves Pétillot, Sandrine Michel, Yves Courty, Eric Forest, David Lascoux, Nathalie Heuzé-Vourc'h, Gilbert Deléage, Michel Jolivet, Colette Jolivet-Reynaud
Publikováno v: Journal of Molecular Recognition. 14:406-413
Prostate-specific antigen (PSA), a 237-amino acid glycoprotein, encoded by the hKLK3 gene, is widely used as a serum marker for the diagnosis and management of prostate cancer. We report here the localization of a conformational epitope recognized by
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1bdb55f1d41fcb88c2f864a9d3461e0e
https://doi.org/10.1002/jmr.552
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9
Discrimination and Selective Enhancement of Signals in the MALDI Mass Spectrum of a Protein by Combining a Matrix-Based Label for Lysine Residues with a Neutral Matrix
Autor: Eric Forest, Gilles Subra, Michaël Heymann, David Lascoux, Christophe Geourjon, David Paramelle, Jean Martinez
Publikováno v: Angewandte Chemie International Edition
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2007, 46, pp.5594-5597. ⟨10.1002/ange.200700811⟩
Angewandte Chemie International Edition, 2007, 46, pp.5594-5597. ⟨10.1002/ange.200700811⟩
International audience
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d37d7fb7db757f48f83018b2d2f5795
https://hal.archives-ouvertes.fr/hal-00170418
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10
SufE Transfers Sulfur from SufS to SufB for Iron-Sulfur Cluster Assembly
Autor: Carla Ayala-Castro, Marc Fontecave, David Lascoux, S. Aparna Gaddam, Gunhild Layer, F. Wayne Outten, Sandrine Ollagnier de Choudens
Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2007, pp.13342-13350. ⟨10.1074/jbc.M608555200⟩
Journal of Biological Chemistry, 2007, pp.13342-13350. ⟨10.1074/jbc.M608555200⟩
Iron-sulfur (Fe-S) clusters are key metal cofactors of metabolic, regulatory, and stress response proteins in most organisms. The unique properties of these clusters make them susceptible to disruption by iron starvation or oxidative stress. Both iro
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f637273642fe370a52ea15840b256ab
https://hal.archives-ouvertes.fr/hal-00374619
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