Výsledky vyhledávání - "Sébastien Mesnildrey"

Autor: Joël Janin, Yingwu Xu, Sébastien Mesnildrey, Solange Moréra, Anna Karlsson, Michel Véron

Publikováno v: Journal of Biological Chemistry. 271:19928-19934

NDP kinase from Dictyostelium was mutated by site-directed mutagenesis at positions indicated by structural data to be involved in the trimer interface. The mutants were substitutions at residue Pro-100 (P100S and P100G) and deletions of 1-5 residues

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::bc66bacd2f63e6818ad7f857950d8040
https://doi.org/10.1074/jbc.271.33.19928

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A human NDP-kinase B specifically binds single-stranded poly-pyrimidine sequences

Autor: Sébastien Mesnildrey, Martin Hildebrandt, Michel Véron, Marie-Lise Lacombe

Publikováno v: Nucleic Acids Research. 23:3858-3864

Recently, a DNA binding protein 'PUF' was purified that binds to a poly-pyrimidine rich element in the human c-myc promoter. Cloning of the corresponding gene surprisingly identified this putative transcription factor as isoform B of the enzyme nucle

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b719d522a594d03b0bec543ffb7faa16
https://doi.org/10.1093/nar/23.19.3858

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Single Strand DNA Specificity Analysis of Human Nucleoside Diphosphate Kinase B

Autor: Sébastien Mesnildrey, Sharona Raveh, Fabrice Agou, Michel Véron

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1999, 274 (28), pp.19630-19638. ⟨10.1074/jbc.274.28.19630⟩
Journal of Biological Chemistry, 1999, 274 (28), pp.19630-19638. ⟨10.1074/jbc.274.28.19630⟩

International audience; Nucleoside diphosphate kinases (NDP kinases) form a family of oligomeric enzymes present in all organisms. Eukaryotic NDP kinases are hexamers composed of identical subunits (≈17 kDa). A distinctive property of human NDPK-B

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1db0dfa4886ae205b34495920e213a79
https://hal-pasteur.archives-ouvertes.fr/pasteur-03276872/document

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Coupling between Catalysis and Oligomeric Structure in Nucleoside Diphosphate Kinase

Autor: Sébastien Mesnildrey, Michel Véron, Anna Karlsson, Fabrice Agou, Dominique Deville Bonne

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1998, 273 (8), pp.4436-4442. ⟨10.1074/jbc.273.8.4436⟩
Journal of Biological Chemistry, 1998, 273 (8), pp.4436-4442. ⟨10.1074/jbc.273.8.4436⟩

International audience; A dimeric Dictyostelium nucleoside diphosphate kinase has been stabilized by the double mutation P100S-N150stop which targets residues involved in the trimer interface (Karlsson, A., Mesnildrey, S., Xu, Y., Moréra, S., Janin,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::585bda9d28cd9b6f42d04d3739be42b3
https://hal-pasteur.archives-ouvertes.fr/pasteur-03276730/file/1-s2.0-S0021925818925676-main.pdf

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The in vitro DNA binding properties of NDP kinase are related to its oligomeric state

Autor: Michel Véron, Fabrice Agou, Sébastien Mesnildrey

Publikováno v: FEBS Letters
FEBS Letters, Wiley, 1997, 418 (1-2), pp.53-57. ⟨10.1016/s0014-5793(97)01292-1⟩
FEBS Letters, 1997, 418 (1-2), pp.53-57. ⟨10.1016/s0014-5793(97)01292-1⟩

International audience; Genetic and biochemical evidences suggest that the enzymatic activity of NDP kinase is necessary but not sufficient for its biological function. While the human NDPK-B binds specifically single-strand polypyrimidines sequences

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87b5c4ddc6472b817a66d0adee0c7a4c
https://hal-pasteur.archives-ouvertes.fr/pasteur-03276726

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Nucleoside Diphosphate Kinase: Effect of the P100S Mutation on Activity and Quaternary Structure

Autor: Sébastien Mesnildrey, Michel Véron

Publikováno v: Interacting Protein Domains ISBN: 9783642645839

Nucleoside Diphosphate Kinase (NDP kinase) is an ubiquitous enzyme which catalyses the phosphate exchange between a triphospho-and a diphospho-nucleoside by a ping-pong mechanism involving the formation of a phospho-histidine intermediate [1,2]. The

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e813a55d51f858de24258bd43c97f1f8
https://doi.org/10.1007/978-3-642-60848-3_31

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Nuclear localization of nucleoside diphosphate kinase type B (nm23-H2) in cultured cells

Autor: Stine-Kathrein Kraeft, Michel Véron, Sébastien Mesnildrey, Julie Bourdais, Francois Traincart, Lan Bo Chen

Publikováno v: Experimental cell research. 227(1)

Nucleoside diphosphate (NDP) kinases are metabolic enzymes found ubiquitously in cells. Recently, two known human isoforms of NDP kinase (A and B), identical to the protein products of the genes nm23-H1 and nm23-H2, respectively, have been implicated

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::343dfbd7d78016fb06939457f00b174a
https://pubmed.ncbi.nlm.nih.gov/8806452

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