Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Gérard Loison"'
Autor:
Claudine Picard, Pierre Casellas, Annick Peleraux, Sandra Silve, Sylvaine Galiègue, Christiane Dhers, Omar Jbilo, Gérard Loison, Elisa Cinato
SR31747A is an immunosuppressive agent that arrests cell proliferation in the yeast Saccharomyces cerevisiae. In this microorganism, SR31747A was shown to inhibit the ERG2 gene product, namely the delta8-delta7 sterol isomerase, involved in the ergos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30055ce58872bd2a9d779b260f12c419
https://europepmc.org/articles/PMC5977520/
https://europepmc.org/articles/PMC5977520/
Publikováno v:
Research in Microbiology. 156:1031-1038
The recently described anaerobic moderately halophilic bacterium Halanaerobium congolense has been shown to reduce thiosulfate and sulfur—but not sulfate—into sulfide. When cultivated in the presence of thiosulfate as terminal electron acceptor,
Autor:
Gérard Loison, Pascal Leplatois, Natalio Vita, Annick Josse, Martine Febvre, Pascual Ferrara, Marie Guillemot
Publikováno v:
European Journal of Biochemistry. 268:4860-4867
Heterologous expression of the human neurotensin receptor type I (hNT1-R) has been achieved in the yeast Saccharomyces cerevisiae. Immunoanalysis of membranes prepared from cells expressing a c-myc-tagged version of hNT1-R revealed multiple c-myc cro
Publikováno v:
FEBS Letters
FEBS Letters, Wiley, 2000, 470, pp.102-106
FEBS Letters, Wiley, 2000, 470, pp.102-106
Certain exogenously-supplied sterols, like ergost-8-enol, are efficiently converted into ergosterol in yeast. We have taken advantage of this property to study the regulation of the Delta8-Delta7-sterol isomerase-encoding ERG2 gene in an ergosterol a
Autor:
Pascual Ferrara, Hubert Vidal, Jean-Pierre Maffrand, Nathalie De Nys, Gérard Le Fur, Pierre Carayon, Sandra Silve, Gérard Loison, Bernard Bourrie, Mohammed Bensaid, Omar Jbilo, Danielle Davi, Sylvaine Galiègue, Jean-Claude Guillemot, Pierre Casellas, Raymond Paul
Publikováno v:
Journal of Biological Chemistry. 272:27107-27115
SR 31747A, defined as a sigma ligand, is a novel immunosuppressive agent that blocks proliferation of human and mouse lymphocytes. Using a radiolabeled chemical probe, we here purified a target of SR 31747A and called it SR 31747A-binding protein (SR
Publikováno v:
Journal of Biological Chemistry. 272:28102-28106
The peripheral type benzodiazepine receptor (PBR) binds benzodiazepines such as RO5-4864 and isoquinoline carboxamide derivatives such as PK11195. This receptor includes an Mr 18,000 isoquinoline-binding subunit predominantly located in mitochondrial
Autor:
Daniel Caput, G Le Fur, A Rahier, Mourad Kaghad, C Lanau, P.-H. Dupuy, M Taton, Gérard Loison, Claudine Picard, A Josse, Pascal Leplatois, P. Ferrara, C Dhers, Sandra Silve
Publikováno v:
Molecular and Cellular Biology. 16:2719-2727
SR 31747 is a novel immunosuppressant agent that arrests cell proliferation in the yeast Saccharomyces cerevisiae, SR 31747-treated cells accumulate the same aberrant sterols as those found in a mutant impaired in delta 8- delta 7-sterol isomerase. S
Autor:
Mourad Kaghad, Sophie Gilbert, Pascual Ferrara, Patrick Jara, Jean-Claude Guillemot, Gérard Loison, Pascal Delmas
Publikováno v:
Molecular and General Genetics MGG. 250:97-105
Two new proteinases secreted by Cryphonectria parasitica, namely EapB and EapC, have been purified. The corresponding structural genes were isolated by screening a cosmid library, and sequenced. Comparison of genomic and cDNA sequences revealed that
Autor:
Pascal Delmas, Luellen Olsen, Alain Bayol, Vohangy Razanamparany, Patrick Jara, Joël Bégueret, Patrice Dupin, Gérard Loison
Publikováno v:
Journal of Biotechnology. 40:111-120
The filamentous ascomycete fungus Cryphonectria parasitica naturally secretes endothiapepsin, an aspartic proteinase. It is cultured on a commercial scale as a source of the milk-clotting enzyme for cheese making. Our objective was to increase enzyme
Publikováno v:
Journal of Biological Chemistry. 270:15821-15826
The gene encoding endothiapepsin (EAP), an extracellular aspartic proteinase from the filamentous ascomycete Cryphonectria parasitica, was expressed into Saccharomyces cerevisiae. Efficient secretion of an active and correctly processed enzyme was ac