Výsledky vyhledávání - "Sophie Sasso"

Circular dichroism and molecular modeling of theE. coli TolA periplasmic domains

Autor: Henri Bouteille, Roland Lloubès, Sophie Sasso, Rahmona Derouiche, Claude Lazdunski, Erwann Loret, R. Oughideni

Publikováno v: Biospectroscopy. 5:189-198

Colicins are killer proteins that use envelope proteins from the outer and the inner membranes to reach their cellular target in susceptible cells of Escherichia coli. Each group A colicin uses a combination of Tol proteins to cross the outer membran

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d240d40a9e3d46a8027308122b2f1b66
https://doi.org/10.1002/(sici)1520-6343(1999)5:3<189::aid-bspy8>3.0.co

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Thermal denaturation of bacterial and bovine dihydrofolate reductases and their complexes with NADPH, trimethoprim and methotrexate

Autor: Alexander A. Makarov, Robert Gilli, Sophie Sasso, I.I. Protasevich, Claudette Briand

Publikováno v: Journal of biomolecular structuredynamics. 12(5)

Scanning microcalorimetry was used for the study of thermal denaturation of E.coli and bovine liver dihydrofolate reductases (cDHFR and bDHFR, respectively) and their complexes with NADPH, trimethoprim (TMP) and methotrexate (MTX) at pH 6.8. It was s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::849e598dcc455d38bf55960fd4ba23e5
https://pubmed.ncbi.nlm.nih.gov/7626237

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Thermodynamic study of dihydrofolate reductase inhibitor selectivity

Autor: Jean Claude Sari, Odile S. Rimet, Claudette Briand, Robert Gilli, Sophie Sasso

Publikováno v: Biochimica et biophysica acta. 1207(1)

The thermodynamic parameters of the binding of some folate analogues (methotrexate, trimetrexate and trimethoprim) to dihydrofolate reductases from different species have been measured with a flow microcalorimetric method at 37°C. In the absence of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7085768ab4b0722d193d6f9860a065b
https://pubmed.ncbi.nlm.nih.gov/8043612

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Thermodynamic Study of Folate Analogue Binding to Dihydrofolate Reductases from Different Species

Autor: Jean Claude Sari, Robert Gilli, Claudette Briand, Colette Lopez, Sophie Sasso

Publikováno v: Advances in Experimental Medicine and Biology ISBN: 9781461362876

Dihydrofolate reductase (DHFR) is the target of numerous folate analogues including the antibacterial agent Trimethoprim (TMP), the anticancer agent Methotrexate (MTX), and a second generation antifolate compound, Trimetrexate (TMQ).

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d80913359fa2316a6a33f3d9e3b0506d
https://doi.org/10.1007/978-1-4615-2960-6_105

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