Výsledky vyhledávání - "Olivier, Roitel"

Lipolysis Stimulated Lipoprotein Receptor

Autor: Lionel Bonnard, Erwan Magueur, Veronique Notet, Bernard Bihain, Dagmar Pratte, Olivier Roitel, Frances T. Yen, Christophe Stenger

Publikováno v: Journal of Biological Chemistry. 283:25650-25659

The lipolysis-stimulated lipoprotein receptor, LSR, is a multimeric protein complex in the liver that undergoes conformational changes upon binding of free fatty acids, thereby revealing a binding site (s) that recognizes both apoB and apoE. Complete

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d52a6cda62139112bc8b8b6b9ec4d5dc
https://doi.org/10.1074/jbc.m801027200

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Switching Pyridine Nucleotide Specificity in P450 BM3

Autor: Olivier Roitel, Andrew W. Munro, Rajasekhar Neeli, Nigel S. Scrutton

Publikováno v: Journal of Biological Chemistry. 280:17634-17644

Flavocytochrome P450 BM3 is a member of the diflavin reductase enzyme family. Members include cytochrome P450 reductase, nitric-oxide synthase, methionine synthase reductase, and novel oxidoreductase 1. These enzymes show a strong preference for NADP

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::fd918c9859737404c0123dbacf8e24e4
https://doi.org/10.1074/jbc.m413826200

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Misfolded forms of glyceraldehyde-3-phosphate dehydrogenase interact with GroEL and inhibit chaperonin-assisted folding of the wild-type enzyme

Autor: Oxana V. Polyakova, R.A. Asryants, Vladimir I. Muronetz, Olivier Roitel, Guy Branlant, Alexei Poliakov

Publikováno v: Protein Science. 14:921-928

We studied the interaction of chaperonin GroEL with different misfolded forms of tetrameric phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPDH): (1) GAPDH from rabbit muscles with all SH-groups modified by 5,5'-dithiobis(2-nitrobenzoate)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76de982369e3c17d58c619cc61ab7baa
https://doi.org/10.1110/ps.041211205

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Expression, Purification, and Characterization of Bacillus subtilis Cytochromes P450 CYP102A2 and CYP102A3: Flavocytochrome Homologues of P450 BM3 from Bacillus megaterium

Autor: Stephen K Chapman, Ker R. Marshall, Mattias C. U. Gustafsson, Claes von Wachenfeldt, Olivier Roitel, Antonio M Pessegueiro, Myles R Cheesman, Michael A. Noble, Armand J. Fulco, Andrew W. Munro

Publikováno v: Biochemistry. 43:5474-5487

The cyp102A2 and cyp102A3 genes encoding the two Bacillus subtilis homologues (CYP102A2 and CYP102A3) of flavocytochrome P450 BM3 (CYP102A1) from Bacillus megaterium have been cloned, expressed in Escherichia coli, purified, and characterized spectro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8a19c9020be225f062d9462b17a29d7
https://doi.org/10.1021/bi035904m

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Determination of the redox potentials and electron transfer properties of the FAD- and FMN-binding domains of the human oxidoreductase NR1

Autor: C. Roland Wolf, Mark J. I. Paine, Nigel S. Scrutton, Olivier Roitel, Andrew W. Munro, Robert D. Finn, Jaswir Basran

Publikováno v: European Journal of Biochemistry. 270:1164-1175

Human novel reductase 1 (NR1) is an NADPH dependent diflavin oxidoreductase related to cytochrome P450 reductase (CPR). The FAD/NADPH- and FMN-binding domains of NR1 have been expressed and purified and their redox properties studied by stopped-flow

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::074b9b040788f6eecf17900cc979a037
https://doi.org/10.1046/j.1432-1033.2003.03474.x

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P but not R-axis Interface is Involved in Cooperative Binding of NAD on Tetrameric Phosphorylating Glyceraldehyde-3-phosphate Dehydrogenase from Bacillus stearothermophilus

Autor: Saı̈d Azza, Guy Branlant, Olivier Roitel, Patrice Vachette

Publikováno v: Journal of Molecular Biology. 326:1513-1522

Homotetrameric phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Bacillus stearothermophilus can be described as a dimer of dimers with three non-equivalent P, R, and Q interfaces. In our previous study, negative cooperativity in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a64dbf6ce1bf389d333987d8f35cce64
https://doi.org/10.1016/s0022-2836(03)00049-4

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Thermal Unfolding Used As a Probe To Characterize the Intra- and Intersubunit Stabilizing Interactions in Phosphorylating d-Glyceraldehyde-3-phosphate Dehydrogenase from Bacillus stearothermophilus

Autor: Guy Branlant, Natalia K. Nagradova, Olga N. Ivinova, Vladimir I. Muronetz, Olivier Roitel

Publikováno v: Biochemistry. 41:7556-7564

Tetrameric phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Bacillus stearothermophilus can be described as a dimer of dimers with three nonequivalent interfaces. To investigate the contribution of intra- and intersubunit interac

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https://doi.org/10.1021/bi012084+

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The crystal structure of the FAD/NADPH-binding domain of flavocytochrome P450 BM3

Autor: Michael G, Joyce, Idorenyin S, Ekanem, Olivier, Roitel, Adrian J, Dunford, Rajasekhar, Neeli, Hazel M, Girvan, George J, Baker, Robin A, Curtis, Andrew W, Munro, David, Leys

Publikováno v: The FEBS journal. 279(9)

We report the crystal structure of the FAD/NADPH-binding domain (FAD domain) of the biotechnologically important Bacillus megaterium flavocytochrome P450 BM3, the last domain of the enzyme to be structurally resolved. The structure was solved in both

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::848e83b1d1c9a314344b0ddffb2d8d27
https://pubmed.ncbi.nlm.nih.gov/22356131

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Effect of surfactant pluronic F-68 on CHO cell growth, metabolism, production, and glycosylation of human recombinant IFN-γ in mild operating conditions

Autor: Emmanuel Guedon, Jean-Louis Goergen, Frances T Yen, Virginie Ogier, Olivier Roitel, Marie-Françoise Clincke

Publikováno v: Biotechnology Progress
Biotechnology Progress, Wiley, 2011, 27 ((1)), pp. 181-190. ⟨10.1002/btpr.503⟩

International audience; The control of glycosylation to satisfy regulatory requirements and quality consistency of recombinant proteins produced by different processes has become an important issue. With two N-glycosylation sites, γ-interferon (IFN-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee05f87cb289ef90773d3aeeb8150c4b
https://hal.archives-ouvertes.fr/hal-00606341

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