Discovery of Thioazepinone Ligands for Src SH2: From Non-specific to Specific Binding

Autor: Eliane Mandine, Pierre Broto, Gudrun Lange, Tran Thien Duc, Pierre Deprez, Dominique Gofflo, Bernard Schoot, Eva Albert, Edoardo Sarubbi, Véronique Jean-Baptiste, Dominique Lesuisse, Jean-Pierre Marquette, Benoit Sortais

Publikováno v: Bioorganic & Medicinal Chemistry Letters. 11:2127-2131

The structure-based design and synthesis of new thioazepinones as ligands for Src SH2 protein is presented. From benzothioazepinones, ligands with somewhat unspecific binding properties, simpler thioazepinones were designed, the best ones demonstrate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60270c2b32c45e9ce59ba104204305c2
https://doi.org/10.1016/s0960-894x(01)00386-9

Novel Mechanism of β-Lactam Resistance Due to Bypass of DD-Transpeptidation in Enterococcus faecium

Autor: Jean-Luc Mainardi, Raymond Legrand, Michel Arthur, Jean van Heijenoort, Bernard Schoot, Laurent Gutmann

Publikováno v: Journal of Biological Chemistry. 275:16490-16496

The peptidoglycan structure of in vitro selected ampicillin-resistant mutant Enterococcus faecium D344M512 and of the susceptible parental strain D344S was determined by reverse phase high performance liquid chromatography and mass spectrometry. The

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68af7cb50e352fa671ee5f94f0bb01ce
https://doi.org/10.1074/jbc.m909877199

Acquisition of Five High- M r Penicillin-Binding Protein Variants during Transfer of High-Level β-Lactam Resistance from Streptococcus mitis to Streptococcus pneumoniae

Autor: Mark van der Linden, Andrea König, Regine Hakenbeck, Raymond Legrand, Izabella Kern, Wolfgang Keck, Bernard Schoot, Danielle Billot-Klein, Laurent Gutmann

Publikováno v: Journal of Bacteriology. 180:1831-1840

Penicillin-resistant isolates of Streptococcus pneumoniae generally contain mosaic genes encoding the low-affinity penicillin-binding proteins (PBPs) PBP2x, PBP2b, and PBP1a. We now present evidence that PBP2a and PBP1b also appear to be low-affinity

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9c1f16e29dc596be50ec4e7c9350739c
https://doi.org/10.1128/jb.180.7.1831-1840.1998

Requirements for specific binding of low affinity inhibitor fragments to the SH2 domain of (pp60)Src are identical to those for high affinity binding of full length inhibitors

Autor: Gudrun Lange, Dominique Lesuisse, Pierre Deprez, Edoardo Sarubbi, Jean-Pierre Marquette, Didier Benard, Pierre Broto, Petra Loenze, Bernard Schoot, Eliane Mandine

Publikováno v: Journal of medicinal chemistry. 46(24)

Results from a novel approach which uses protein crystallography for the screening of a low affinity inhibitor fragment library are analyzed by comparing the X-ray structures with bound fragments to the structures with the corresponding full length i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff1ac5d09d00fc948c8820149de09145
https://pubmed.ncbi.nlm.nih.gov/14613321

Crystallization of a recombinant form of the complete sequence of human $\gamma$-interferon: characterization by small-angle X-ray scattering, mass spectrometry and preliminary X-ray diffraction studies

Autor: Jean-Pierre Astier, Monika Budayova-Spano, Stéphane Veesler, William Shepard, Bernard Schoot

Publikováno v: Acta Crystallographica Section D: Biological Crystallography
Acta Crystallographica Section D: Biological Crystallography, International Union of Crystallography, 2001, 57, pp.900-905. ⟨10.1107/S0907444901005820⟩
Acta crystallographica Section D : Structural biology [1993-...]
Acta crystallographica Section D : Structural biology [1993-..], 2001, 57, pp.900-905. ⟨10.1107/S0907444901005820⟩

International audience; The crystallization conditions of a recombinant form of the complete sequence of human $\gamma$-interferon, designated r-hu IFN-$\gamma$ (RU 42369), have been determined after studying the behaviour of this protein in solution

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f285efd5d38bb0b959f08fbbcbac954
https://hal.archives-ouvertes.fr/hal-01745687