Výsledky vyhledávání - "Gilles Tiraboschi"

Rational design of potent GSK3β inhibitors with selectivity for Cdk1 and Cdk2

Autor: Gilles Dutruc-Rosset, Sébastien Maignan, Alain Chevalier, Frank Halley, Thomas Rooney, Matthias K. Dreyer, Dominique Lesuisse, Gilles Tiraboschi, Dominique Quarteronet, Philippe Bertrand, Marie-Claude Burgevin

Publikováno v: Bioorganic & Medicinal Chemistry Letters. 20:1985-1989

From an HTS hit, a series of potent and selective inhibitors of GSK3β have been designed based on a Cdk2-homology model and with the help of several crystal structures of the compounds within Cdk2.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52fd7bd1858589017041fe68fdcfe9e7
https://doi.org/10.1016/j.bmcl.2010.01.114

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Intramolecular chelation of Zn2+by α- and β-mercaptocarboxamides. A parallelab initioand polarizable molecular mechanics investigation. Assessment of the role of multipole transferability

Autor: Bernard-Pierre Roques, Gilles Tiraboschi, Marie-Claude Fournie-Zaluski, Nohad Gresh

Publikováno v: Journal of Computational Chemistry. 22:1038-1047

α- and β-mercaptocarboxamides constitute the Zn2+-ligating entity of several highly potent metalloenzyme inhibitors. We have studied their interaction energies with Zn2+ using the polarizable molecular mechanics procedure SIBFA, and compared them t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1bb264fb37f748136bcf59ad4e64d2b8
https://doi.org/10.1002/jcc.1064

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Exploration of theS?1 subsite of neprilysin: A joined molecular modeling and site-directed mutagenesis study

Autor: Marie-Claude Fournie-Zaluski, Nicolas Inguimbert, Cynthia Marie-Claire, Bernard P. Roques, Gilles Tiraboschi, Emmanuel Ruffet

Publikováno v: Proteins: Structure, Function, and Genetics. 39:365-371

Based on the recently described three-dimensional model of the 507–749 region of neprilysin, which contains the catalytic site of the enzyme, experiments were performed to improve the proposed topology of its large and hydrophobic S subsite. Dockin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::08a2760421c8bcee0c7a6292246097cd
https://doi.org/10.1002/(sici)1097-0134(20000601)39:4<365::aid-prot90>3.0.co

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Joint quantum chemical and polarizable molecular mechanics investigation of formate complexes with penta- and hexahydrated Zn2+: Comparison between energetics of model bidentate, monodentate, and through-water Zn2+ binding modes and evaluation of nonadditivity effects

Autor: Nohad Gresh, Bernard-Pierre Roques, Gilles Tiraboschi

Publikováno v: Journal of Computational Chemistry. 20:1379-1390

In order to gain an understanding of the energetics of polycoordinated Zn2+ binding to the formate anion (the end side chain of the Asp and Glu residues of proteins), we compare three competing binding modes in the presence of five and six water mole

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::39a50b97ef0238dd5bd7195b692acf33
https://doi.org/10.1002/(sici)1096-987x(199910)20:13<1379::aid-jcc5>3.0.co

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Crystal Structures of α-Mercaptoacyldipeptides in the Thermolysin Active Site: Structural Parameters for a Zn Monodentation or Bidentation in Metalloendopeptidases

Autor: Bernard-Pierre Roques, Thierry Prangé, Gilles Tiraboschi, A. Tomas, Marie-Claude Fournie-Zaluski, J.-F. Gaucher, M. Selkti

Publikováno v: Biochemistry. 38:12569-12576

Three alpha-mercaptoacyldipeptides differing essentially in the size of their C-terminal residues have been crystallized in the thermolysin active site. A new mode of binding was observed for 3 [HS-CH(CH(2)Ph)CO-Phe-Tyr] and 4 [HS-CH((CH(2))(4)CH(3))

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38b92eb4c2dabc67816854b6fab5aaae
https://doi.org/10.1021/bi991043z

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A three-dimensional construction of the active site (region 507–749) of human neutral endopeptidase (EC.3.4.24.11)

Autor: Marie-Claude Fournie-Zaluski, Gilles Tiraboschi, Vincent Thery, Serge Antonczak, Bernard P. Roques, Nathalie Jullian

Publikováno v: Protein Engineering, Design and Selection. 12:141-149

A three-dimensional model of the 507-749 region of neutral endopeptidase-24.11 (NEP; E.C.3.4.24.11) was constructed integrating the results of secondary structure predictions and sequence homologies with the bacterial endopeptidase thermolysin. Addit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a5f8da5f265ab9a2ba1573e639181eb
https://doi.org/10.1093/protein/12.2.141

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Conformational properties of a model alanyl dipeptide and of alanine-derived oligopeptides: Effects of solvation in water and in organic solvents—A combined SIBFA/continuum reaction field, ab initio self-consistent field, and density functional theory investigation

Autor: Nohad Gresh, Dennis R. Salahub, Gilles Tiraboschi

Publikováno v: Biopolymers. 45:405-425

A ϕ/ψ conformational energy map of a model alanyl dipeptide is first drawn using the SIBFA (Sum of Interactions Between Fragments Ab initio computed) procedure [N. Gresh, P. Claverie and A. Pullman (1979) International Journal of Quantum Chemistry

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6b8dfd6a84b20b221d5c17c150babe03
https://doi.org/10.1002/(sici)1097-0282(199805)45:6<405::aid-bip1>3.0.co

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Design of potent and selective GSK3beta inhibitors with acceptable safety profile and pharmacokinetics

Autor: Frank Halley, Céline Amara, Fabienne Châtreau, Gilles Tiraboschi, Pierre-Yves Abecassis, Philippe Bertrand, Sylvette Lachaud, Didier Babin, Gilles Dutruc-Rosset, Alain Chevalier, Alain Krick, Marie-Claude Burgevin, Dominique Lesuisse, Dominique Quarteronet, Thomas Rooney

Publikováno v: Bioorganicmedicinal chemistry letters. 20(7)

From potent and selective inhibitors of GSK3β displaying CYP1A2 inhibition and poor PK properties, mostly linked to metabolic instability and in vivo hydrolysis of the amide bond, we were able to obtain safe and orally available inhibitors with good

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::420b1e33556a3010c280ed66eb261378
https://pubmed.ncbi.nlm.nih.gov/20189807

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A Sos-derived peptidimer blocks the Ras signaling pathway by binding both Grb2 SH3 domains and displays antiproliferative activity

Autor: Michel Vidal, Didier Cussac, Christiane Garbay, Corinne Leprince, Gilles Tiraboschi, Bernard P. Roques, Fabrice Cornille, Wang-Qing Liu

Publikováno v: FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 13(1)

With the aim of interrupting the growth factor-stimulated Ras signaling pathway at the level of the Grb2-Sos interaction, a peptidimer, made of two identical proline-rich sequences from Sos linked by a lysine spacer, was designed using structural dat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abc2498841f3ee96f7212ba22aaa7ace
https://pubmed.ncbi.nlm.nih.gov/9872927

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