Search Results - "Biou, V."

The Crystal Structure of Dimeric Kinesin and Implications for Microtubule-Dependent Motility by Kozielski, F, Sack, S, Marx, A, Thormählen, M, Schönbrunn, E, Biou, V, Thompson, A, Mandelkow, E.-M, Mandelkow, E

“…The dimeric form of the kinesin motor and neck domain from rat brain with bound ADP has been solved by X-ray crystallography. The two heads of the dimer are…”
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Enzymology, Structure, and Dynamics of Acetohydroxy Acid Isomeroreductase by Dumas, Renaud, Biou, Valérie, Halgand, Frédéric, Douce, Roland, Duggleby, Ronald G

“…Acetohydroxy acid isomeroreductase is a key enzyme involved in the biosynthetic pathway of the amino acids isoleucine, valine, and leucine. This enzyme is of…”
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X‐ray crystallography shows that translational initiation factor IF3 consists of two compact alpha/beta domains linked by an alpha‐helix by Biou, V., Shu, F., Ramakrishnan, V.

“…The structures of the two domains of translational initiation factor IF3 from Bacillus stearothermophilus have been solved by X‐ray crystallography using…”
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Prokaryotic Translation Initiation Factor IF3 Is an Elongated Protein Consisting of Two Crystallizable Domains by Kycia, Jadwiga H, Biou, Valerie, Shu, Fong, Gerchman, Sue Ellen, Graziano, Vito, Ramakrishnan, V

“…We show that translation initiation factor IF3 can be split into two fragments of nearly equal size by the Escherichia coli outer membrane protease omptin…”
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MAD on threonine synthase: the phasing power of oxidized selenomethionine by Thomazeau, Karine, Curien, Gilles, Thompson, Andrew, Dumas, Renaud, Biou, Valérie

“…The use of selenomethionine and anomalous dispersion has become the most widely used way of solving the phase problem for de novo protein structure…”
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The 2.9 Å Crystal Structure of T. thermophilus Seryl-tRNA Synthetase Complexed with tRNA$^{Ser} by Biou, Valérie, Yaremchuk, Anna, Tukalo, Michael, Cusack, Stephen

“…The crystal structure of Thermus thermophilus seryl-transfer RNA synthetase, a class 2 aminoacyl-tRNA synthetase, complexed with a single tRNA$^{Ser}$ molecule…”
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A new crystal form of the complex between seryl-tRNA synthetase and tRNA(Ser) from Thermus thermophilus that diffracts to 2.8 A resolution by Yaremchuk, A D, Tukalo, M A, Krikliviy, I, Malchenko, N, Biou, V, Berthet-Colominas, C, Cusack, S

“…Two distinct complexes between seryl-tRNA synthetase and tRNA(Ser) from Thermus thermophilus have been crystallized using ammonium sulphate as a precipitant…”
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A new crystal form of the complex between seryl‐tRNA synthetase and tRNASer from Thermus thermophilus that diffracts to 2.8 Å resolution by Yaremchuk, A.D., Tukalo, M.A., Krikliviy, I., Malchenko, N., Biou, V., Berthet-Colominas, C., Cusack, S.

“…Two distinct complexes between seryl‐tRNA synthetase and tRNA Ser from Thermus themophilus have been crystallized using ammonium sulphate as a precipitant…”
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The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65Aresolution by Biou, V.

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The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 Å resolution by Biou, Valérie, Dumas, Renaud, Cohen-Addad, Claudine, Douce, Roland, Job, Dominique, Pebay-Peyroula, Eva

“…Acetohydroxy acid isomeroreductase catalyzes the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic…”
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Secondary structure prediction and protein design by Garnier, J, Levin, J M, Gibrat, J F, Biou, V

“…For non-homologous proteins, and after cross-validation, the methods reviewed in this article exhibit a probability index (percentage of correctly predicted…”
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Crystal structure of threonine synthase from Arabidopsis thaliana by Thomazeau, Karine, Curien, Gilles, Dumas, Renaud, Biou, Valérie

“…Threonine synthase (TS) is a PLP‐dependent enzyme that catalyzes the last reaction in the synthesis of threonine from aspartate. In plants, the methionine…”
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Treatment of multiwavelength anomalous diffraction data as a special case of multiple isomorphous replacement by Ramakrishnan, V, Biou, V

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What makes homologous small GTPases specific? A combined X-ray, SAXS and NMR study by Cherfils, J., Biou, V., Aizel, K., Zeghouf, M., Buosi, V., Thureau, A., Jacquet, E., Guittet, E., Heijenoort, C. V., Roblin, P., Perez, J.

“…Abstract only…”
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An unfolding model for the GDP/GTP conformational switch of the GTPase Arf6 by Aizel, K., Biou, V., Roblin, P., Thureau, A., Jacquet, E., Guittet, E., Heijenoort, C. V., Zeghouf, M., Buosi, V., Perez, J., Cherfils, J.

“…Abstract only…”
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Structure of spinach acetohydroxyacid isomeroreductase complexed with its reaction product dihydroxymethylvalerate, manganese and (phospho)-ADP-ribose by Thomazeau, Karine, Dumas, Renaud, Halgand, Frédéric, Forest, Eric, Douce, Roland, Biou, Valérie

“…Acetohydroxyacid isomeroreductase catalyses a two‐step reaction composed of an alkyl migration followed by an NADPH‐dependent reduction. Both steps require a…”
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Crystal structure of plant threonine synthase complexed with S -adenosylmethionine reveals allosteric activation mechanism by Mas, C., Biou, V., Dumas, R.

“…Abstract only…”
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Structure and inhibition of Arf GTPases by Cherfils, J., Zeeh, J.-C., Zeghouf, M., Biou, V., Buosi, V., Thureau, A., van Heijenoort, C., Guittet, E.

“…Abstract only…”
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Purification and characterization of a fusion protein of plant acetohydroxy acid synthase and acetohydroxy acid isomeroreductase by Dumas, Renaud, Biou, Valérie, Douce, Roland

“…The nucleotide sequence coding for the Arabidopsis thaliana acetohydroxy acid synthase was genetically fused in frame with the nucleotide sequence coding for…”
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Kinetic and Mass Spectrometric Analyses of the Interactions between Plant Acetohydroxy Acid Isomeroreductase and Thiadiazole Derivatives by Halgand, Frédéric, Vives, Françoise, Dumas, Renaud, Biou, Valérie, Andersen, Jens, Andrieu, Jean-Pierre, Cantegril, Richard, Gagnon, Jean, Douce, Roland, Forest, Eric, Job, Dominique

“…Plant acetohydroxy acid isomeroreductase (EC 1.1.1.86), the second enzyme of the branched chain amino acid biosynthetic pathway, has been submitted to…”
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