Gondry, Muriel
![Sudoc [ABES], France](/viaf/images/flags/SUDOC.png "Sudoc [ABES], France")
Muriel Gondry
VIAF ID: 213284649 ( Personal )
Permalink: http://viaf.org/viaf/213284649
Preferred Forms
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100 1 _
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GONDRY, MURIEL.
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100 1 _
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Gondry, Muriel
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100 1 _
‡a
Gondry, Muriel
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100 0 _
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Muriel Gondry
4xx's: Alternate Name Forms (2)
Works
| Title | Sources |
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| The albonoursin gene Cluster of S noursei biosynthesis of diketopiperazine metabolites independent of nonribosomal peptide synthetases. |
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| Aminoacyl-tRNA-Utilizing Enzymes in Natural Product Biosynthesis. |
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| The carboxyl-terminal nucleoplasmic region of MAN1 exhibits a DNA binding winged helix domain |
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| The catalytic role of tyrosine 254 in flavocytochrome b2 (L-lactate dehydrogenase from baker's yeast). Comparison between the Y254F and Y254L mutant proteins. |
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| Cyclization Reaction Catalyzed by Cyclodipeptide Synthases Relies on a Conserved Tyrosine Residue. |
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| Cyclodipeptide synthases are a family of tRNA-dependent peptide bond-forming enzymes |
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| Cyclodipeptide Synthases of the NYH Subfamily Recognize tRNA Using an α-Helix Enriched with Positive Residues |
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| Les cyclodipeptides synthases, une nouvelle famille d'enzymes formant des liaisons peptidiques : mise en évidence de la famille, bases moléculaires de leur fonction, caractérisation structurale de l'AlbC, un membre de la famille |
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| Découverte et déchiffrage de nouvelles voies de biosynthèse dépendant des synthases de cyclodipeptides : les clés d'une diversité accrue de dicétopipérazines potentiellement bioactives |
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| Discovering and deciphering of new cyclodipeptide synthase-dependent biosynthetic pathways : key for a increased diversity of potential bioactive diketopiperazines. |
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| Functional properties of the histidine-aspartate ion pair of flavocytochrome b2 (L-lactate dehydrogenase): substitution of Asp282 with asparagine. |
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| High throughput screening identifies disulfide isomerase DsbC as a very efficient partner for recombinant expression of small disulfide-rich proteins in E. coli. |
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| An iterative nonribosomal peptide synthetase assembles the pyrrole-amide antibiotic congocidine in Streptomyces ambofaciens. |
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| Multidisciplinary studies of key aspects of polyketides biosynthesis by modular polyketide synthases. |
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| THE MUTANT ENZYMES Y254L AND D282N OF THE ACTIVE-SITE OF FLAVOCYTOCHROME B#2 FROM SACCHAROMYCES CEREVISIAE DIFFICULTIES OF FOLDING IN ESCHERICHIA COLI THE ROLE OF TYROSINE 254 IN LIGAND FIXATION AND CATALYSIS THE INFLUENCE OF ASPARTATE 282 ON THE PKA . |
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| Non-canonical Amino Acid Incorporation into 2,5-Diketopiperazines by Cyclodipeptide Synthases. |
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| Picosecond dynamics of a peptide from the acetylcholine receptor interacting with a neurotoxin probed by tailored tryptophan fluorescence. |
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| Polycétide synthases : étude de l'influence de l'organisation macromoléculaire sur la fonction par ingénierie génétique |
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| Polyketide synthases : probing the effect of macromolecular organization on function by genetic engineering. |
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| Remaniement du métabolisme carboné central microbien pour une conversion des sucres lignocellulosiques en acide glycolique avec une conservation optimale du carbone |
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| Structural basis of the interaction between cyclodipeptide synthases and aminoacylated tRNA substrates |
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| Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site |
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| Substrate and Reaction Specificity of Mycobacterium tuberculosis Cytochrome P450 CYP121: INSIGHTS FROM BIOCHEMICAL STUDIES AND CRYSTAL STRUCTURES |
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| A tandem of SH3-like domains participates in RNA binding in KIN17, a human protein activated in response to genotoxics |
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| The terpene mini-path : nouvel accès aux terpènes et exploration de l'espace chimique par une cascade enzymatique originale |
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| Unravelling the mechanism of non-ribosomal peptide synthesis by cyclodipeptide synthases |
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| Vers une meilleure compréhension de la reconnaissance des substrats naturels et non-naturels des synthases de cyclodipeptides. |
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| واکنش چرخه کاتالیز شده توسط Cyclodipeptide Synthases متکی بر یک مانده تیروزین محافظت شده است. |
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