Výsledky vyhledávání - "J C, Boulain"

Artificial Evolution of an Enzyme Active Site: Structural Studies of Three Highly Active Mutants of Escherichia coli Alkaline Phosphatase

Autor: André Ménez, O.V. Bulgakov, M.H. Le Du, J.-C. Boulain, E. Lajeunesse, Bruno H. Muller, C. Lamoure

Publikováno v: Journal of Molecular Biology. 316:941-953

The crystal structure of three mutants of Escherichia coli alkaline phosphatase with catalytic activity (k(cat)) enhancement as compare to the wild-type enzyme is described in different states. The biological aspects of this study have been reported

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae68457df83e578959a6706e3b467c0d
https://doi.org/10.1006/jmbi.2001.5384

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Stability of a structural scaffold upon activity transfer: X-ray structure of a three fingers chimeric protein 1 1Edited by R. Huber

Autor: Renée Ménez, M.H. Le Du, J.-C. Boulain, M. Khayati, André Ménez, A. Ricciardi, Frédéric Ducancel

Publikováno v: Journal of Molecular Biology. 296:1017-1026

Fasciculin 2 and toxin alpha proteins belong to the same structural family of three-fingered snake toxins. They act on different targets, but in each case the binding region involves residues from loops I and II. The superimposition of the two struct

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::15e4aee65af18214d53db6d5d63df669
https://doi.org/10.1006/jmbi.2000.3510

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A Recombinant Insect-Specific alpha-Toxin of Buthus occitanus tunetanus Scorpion Confers Protection Against Homologous Mammal Toxins

Autor: Habib Karoui, Mohamed El Ayeb, Balkiss Bouhaouala-Zahar, Lamia Borchani, I. Zenouaki, M. Pelhate, André Ménez, Frédérique Ducancel, Rym Ben Khalifa, J.-C. Boulain

Publikováno v: European Journal of Biochemistry
European Journal of Biochemistry, 1996, 238 (3), pp.653-660. ⟨10.1111/j.1432-1033.1996.0653w.x⟩

International audience; We have constructed a cDNA library from venom glands of the scorpion Buthus occitanus tunetanus and cloned a DNA sequence that encodes an alpha-toxin. This clone was efficiently expressed in Escherichia coli as a fusion protei

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abcd192c1d72c331a1c943d538e20b44
https://doi.org/10.1111/j.1432-1033.1996.0653w.x

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The low molecular weight protein which co-purifies with alpha-latrotoxin is structurally related to crustacean hyperglycemic hormones

Autor: E Forest, E Grishin, Pierre Ripoche, J.-C. Boulain, N Kiyatkin, Pascal Drevet, André Ménez, Sylvaine Gasparini, F Tacnet

Publikováno v: Journal of Biological Chemistry. 269:19803-19809

LMWP is the low molecular weight protein which copurifies with alpha-latrotoxin, the main neurotoxin from the black widow venom. It contains 70 residues and three disulfides. We found that its primary structure, including its 6 half-cystines, can be

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9953cc1890b41a93c1e0b7cf8daa15e5
https://doi.org/10.1016/s0021-9258(17)32091-4

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Precursors of vertebrate peptide antibiotics dermaseptin b and adenoregulin have extensive sequence identities with precursors of opioid peptides dermorphin, dermenkephalin, and deltorphins

Autor: J.-C. Boulain, Mohamed Amiche, A. Menez, F. Ducancel, Amram Mor, Pierre Nicolas

Publikováno v: Journal of Biological Chemistry. 269:17847-17852

The dermaseptins are a family of broad spectrum antimicrobial peptides, 27-34 amino acids long, involved in the defense of the naked skin of frogs against microbial invasion. They are the first vertebrate peptides to show lethal effects against the f

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ca922a576818e6f7805d3bd232a5ede
https://doi.org/10.1016/s0021-9258(17)32386-4

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Recombinant technology in the preparation of immunogen and enzymatic tracer. Application to the development of an enzyme immunoassay for rat prolactin

Autor: Pascal Drevet, André Ménez, J.-C. Boulain, Eric Ezan, Jean-Marc Grognet, Daniel Gillet, Frédéric Ducancel

Publikováno v: Journal of Immunological Methods. 169:205-211

A competitive enzyme immunoassay for rat prolactin using an immunogen and a tracer obtained by recombinant DNA technology is described. Polyclonal antibodies were raised in rabbits immunized with a purified chimeric protein consisting of rat prolacti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea5dff93030e7c6629ea425a1ebb060f
https://doi.org/10.1016/0022-1759(94)90264-x

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Molecular Cloning of a cDNA Encoding the Precursor of Adenoregulin from Frog Skin: Relationships with the Vertebrate Defensive Peptides, Dermaseptins

Autor: J.-C. Boulain, F. Ducancel, E. Lajeunesse, Mohamed Amiche, A. Menez, Pierre Nicolas

Publikováno v: Biochemical and Biophysical Research Communications. 191:983-990

Adenoregulin has recently been isolated from Phyllomedusa skin as a 33 amino acid residues peptide which enhanced binding of agonists to the A1 adenosine receptor. In order to study the structure of the precursor of adenoregulin we constructed a cDNA

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7635ff75ec9d2dead5bbdee0962fa171
https://doi.org/10.1006/bbrc.1993.1314

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Cloning and sequence analysis of cDNAs encoding precursors of sarafotoxins. Evidence for an unusual 'rosary-type' organization

Autor: Zvi Wollberg, J.-C. Boulain, Frédéric Ducancel, C Dupont, Elazar Kochva, André Ménez, V Matre, Avner Bdolah, E. Lajeunesse

Publikováno v: Journal of Biological Chemistry. 268:3052-3055

Sarafotoxins (SRTXs) are 21-amino acid peptides structurally and functionally similar to endothelins (ETs). To understand how SRTXs are overproduced in venom glands of the snakes Atractaspis engaddensis and hence used as toxins, we cloned cDNAs encod

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ec55361100671f0b04717f50631be0be
https://doi.org/10.1016/s0021-9258(18)53658-9

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Genetic engineering of snake toxins. Role of invariant residues in the structural and functional properties of a curaremimetic toxin, as probed by site-directed mutagenesis

Autor: Pascal Drevet, J.-C. Boulain, Frédéric Ducancel, Odile Trémeau, Suzanne Pinkasfeld, Laurence Pillet, Sophie Zinn-Justin, André Ménez

Publikováno v: Journal of Biological Chemistry. 268:909-916

To study the site by which erabutoxin a (Ea) from Laticauda semifasciata binds to the nicotinic acetylcholine receptor, we mutated most residues that are shared with other curaremimetic toxins and studied the structural and biological consequences of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::444dd6b24868ef624dd3f0994d63eb95
https://doi.org/10.1016/s0021-9258(18)54020-5

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Structure-based secondary structure-independent approach to design protein ligands: Application to the design of Kv1.2 potassium channel blockers

Autor: M. Lefranc, Michel Masella, J.-C. Boulain, M.H. Le Du, L. Pardo, Enrico A. Stura, Jean-Baptiste Charbonnier, Philippe Cuniasse, Gilles Mourier, Alain Lecoq, and A. Menez, D. Gasparini, A. Joly, A. Caruana, C. Magis

Publikováno v: Journal of the American Chemical Society. 128(50)

We have developed a structure-based approach to the design of protein ligands. This approach is based on the transfer of a functional binding motif of amino acids, often referred as to the "hot spot", on a host protein able to reproduce the functiona

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::caf9eeb4620cc292313c9a9c22b453bd
https://pubmed.ncbi.nlm.nih.gov/17165772

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