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Refinado por: Base de dados/Biblioteca: Oxford Journals remover
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1
Development of a nondestructive fluorescence‐based enzymatic staining of microcolonies for enumerating bacterial contamination in filterable products
Development of a nondestructive fluorescence‐based enzymatic staining of microcolonies for enumerating bacterial contamination in filterable products
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Development of a nondestructive fluorescence‐based enzymatic staining of microcolonies for enumerating bacterial contamination in filterable products

Baumstummler, A ; Chollet, R ; Meder, H ; Olivieri, F ; Rouillon, S ; Waiche, G ; Ribault, S

Journal of applied microbiology, 2011, Vol.110 (1), p.69-79 [Periódico revisado por pares]

Oxford, UK: Blackwell Publishing Ltd

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2
Detection of microbial contaminants in mammalian cell cultures using a new fluorescence‐based staining method
Detection of microbial contaminants in mammalian cell cultures using a new fluorescence‐based staining method
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Detection of microbial contaminants in mammalian cell cultures using a new fluorescence‐based staining method

Baumstummler, A ; Chollet, R ; Meder, H ; Rofel, C ; Venchiarutti, A ; Ribault, S

Letters in applied microbiology, 2010-12, Vol.51 (6), p.671-677 [Periódico revisado por pares]

Oxford, UK: Blackwell Publishing Ltd

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3
A Minimal Serine/Threonine Protein Kinase Circadianly Regulates Phosphoenolpyruvate Carboxylase Activity in Crassulacean Acid Metabolism-Induced Leaves of the Common Ice Plant
A Minimal Serine/Threonine Protein Kinase Circadianly Regulates Phosphoenolpyruvate Carboxylase Activity in Crassulacean Acid Metabolism-Induced Leaves of the Common Ice Plant
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A Minimal Serine/Threonine Protein Kinase Circadianly Regulates Phosphoenolpyruvate Carboxylase Activity in Crassulacean Acid Metabolism-Induced Leaves of the Common Ice Plant

Tahar Taybi ; Patil, Shameekumar ; Chollet, Raymond ; Cushman, John C.

Plant physiology (Bethesda), 2000-08, Vol.123 (4), p.1471-1481 [Periódico revisado por pares]

Rockville, MD: American Society of Plant Physiologists

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4
In vivo regulation of wheat-leaf phosphoenolpyruvate carboxylase by reversible phosphorylation
In vivo regulation of wheat-leaf phosphoenolpyruvate carboxylase by reversible phosphorylation
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In vivo regulation of wheat-leaf phosphoenolpyruvate carboxylase by reversible phosphorylation

Duff, S.M.G. (University of Manitoba, Winnipeg, Manitoba, Canada.) ; Chollet, R

Plant physiology (Bethesda), 1995-03, Vol.107 (3), p.775-782 [Periódico revisado por pares]

Rockville, MD: American Society of Plant Physiologists

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5
Enterobacter gergoviae and the prevalence of efflux in parabens resistance
Enterobacter gergoviae and the prevalence of efflux in parabens resistance
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Enterobacter gergoviae and the prevalence of efflux in parabens resistance

Davin-Regli, A. ; Chollet, R. ; Bredin, J. ; Chevalier, J. ; Lepine, F. ; Pagès, J. M.

Journal of antimicrobial chemotherapy, 2006-04, Vol.57 (4), p.757-760 [Periódico revisado por pares]

Oxford: Oxford University Press

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6
In vivo regulatory phosphorylation of soybean nodule phosphoenolpyruvate carboxylase
In vivo regulatory phosphorylation of soybean nodule phosphoenolpyruvate carboxylase
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In vivo regulatory phosphorylation of soybean nodule phosphoenolpyruvate carboxylase

Xiu-Qing Zhang ; Li, Bin ; Chollet, Raymond

Plant physiology (Bethesda), 1995-08, Vol.108 (4), p.1561-1568 [Periódico revisado por pares]

Rockville, MD: American Society of Plant Physiologists

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7
The light-dependent transduction pathway controlling the regulatory phosphorylation of C4 phosphoenolpyruvate carboxylase in protoplasts from Digitaria sanguinalis
The light-dependent transduction pathway controlling the regulatory phosphorylation of C4 phosphoenolpyruvate carboxylase in protoplasts from Digitaria sanguinalis
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The light-dependent transduction pathway controlling the regulatory phosphorylation of C4 phosphoenolpyruvate carboxylase in protoplasts from Digitaria sanguinalis

Nathalie Giglioli-Guivarc'h ; Pierre, Jean-Noël ; Brown, Spencer ; Chollet, Raymond ; Vidal, Jean ; Gadal, Pierre

The Plant cell, 1996-04, Vol.8 (4), p.573-586 [Periódico revisado por pares]

United States: American Society of Plant Physiologists

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8
Phosphoenolpyruvate carboxylase kinase in tobacco leaves is activated by light in a similar but not identical way as in maize
Phosphoenolpyruvate carboxylase kinase in tobacco leaves is activated by light in a similar but not identical way as in maize
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Phosphoenolpyruvate carboxylase kinase in tobacco leaves is activated by light in a similar but not identical way as in maize

Li, B. (Monsanto Company, Chesterfield, MO.) ; Zhang, X.Q ; Chollet, R

Plant physiology (Bethesda), 1996-06, Vol.111 (2), p.497-505 [Periódico revisado por pares]

Rockville, MD: American Society of Plant Physiologists

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9
Regulatory phosphorylation of C4 phosphoenolpyruvate carboxylase. A cardinal event influencing the photosynthesis rate in sorghum and maize
Regulatory phosphorylation of C4 phosphoenolpyruvate carboxylase. A cardinal event influencing the photosynthesis rate in sorghum and maize
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Regulatory phosphorylation of C4 phosphoenolpyruvate carboxylase. A cardinal event influencing the photosynthesis rate in sorghum and maize

Naïma Bakrim ; Jean-Louis Prioul ; Deleens, Eliane ; Jean-Paul Rocher ; Martine Arrio-Dupont ; Vidal, Jean ; Gadal, Pierre ; Chollet, Raymond

Plant physiology (Bethesda), 1993, Vol.101 (3), p.891-897 [Periódico revisado por pares]

Rockville, MD: American Society of Plant Physiologists

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10
An increase in apparent affinity for sucrose of mung bean [Vigna radiata] sucrose synthase is caused by in vitro phosphorylation or directed mutagenesis of Ser11
An increase in apparent affinity for sucrose of mung bean [Vigna radiata] sucrose synthase is caused by in vitro phosphorylation or directed mutagenesis of Ser11
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An increase in apparent affinity for sucrose of mung bean [Vigna radiata] sucrose synthase is caused by in vitro phosphorylation or directed mutagenesis of Ser11

Nakai, T. (Kyoto Univ., Uji (Japan). Wood Research Inst.) ; Konishi, T ; Zhang, X.Q ; Chollet, R ; Tonouchi, N ; Tsuchida, T ; Yoshinaga, F ; Mori, H ; Sakai, F ; Hayashi, T

Plant and cell physiology, 1998-12, Vol.39 (12), p.1337-1341 [Periódico revisado por pares]

Oxford: Oxford University Press

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