Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Marie‐Christine Chanal"'
Autor:
Axel J. Ganzhorn, Jan Hoflack, Marie-Christine Chanal, Serge R. Piettre, Françoise Strasser, Patricia D. Pelton
Publikováno v:
Bioorganic & Medicinal Chemistry. 6:1865-1874
alpha-Hydroxyphosphonates are moderately potent (Ki = 6-600 microM) inhibitors of the enzyme myo-inositol monophosphatase (McLeod et al., Med. Chem. Res. 1992, 2, 96). Hydroxy-[4-(5,6,7,8-tetrahydronaphtyl-1-oxy)phenyl]methyl phosphonate (3) was resy
Autor:
Jean-Bernard Ducep, Axel J. Ganzhorn, François Piriou, Jean-Michel Rondeau, Serge R. Piettre, Charles G. Schelcher, Brigitte Lesur, Catherine André, Marie-Christine Chanal, Pierre Jean-Marie Bernard Raboisson, Pascale Zimmermann
Publikováno v:
Journal of Medicinal Chemistry. 40:4208-4221
The first successful preparation of mono- and disubstituted 3,7-dihydroxytropolone involves a four-step synthetic scheme. Thus, bromination of 3,7-dihydroxytropolone (8) followed by permethylation of the resultant products furnished gram quantities o
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 6:393-396
Several unsaturated thioacetic acids were synthesized as potential mechanism-based inhibitors of peptidyglycine α-hydroxylating monooxygenase (PHM) prepared from horse serum. Trans-styrylthioacetic acid produced potent time-dependent inhibition of P
Publikováno v:
Biochemical pharmacology. 53(11)
Peptidylglycine α-hydroxylating monooxygenase (PHM; EC 1.14.17.3) catalyses the ratelimiting step in the post-translational activation of substance P, among other neuropeptides, from its glycine-extended precursor. Comparative kinetic studies were p
Publikováno v:
Biochemistry. 29(25)
The kinetic properties of myo-inositol monophosphatase with different substrates were examined with respect to inhibition by fluoride, activation or inhibition by metal ions, pH profiles, and solvent isotope effects. F- is a competitive inhibitor ver
Publikováno v:
European Journal of Biochemistry
A DNA-stimulated ATP-gamma-phosphohydrolase of molecular weight 75000 was purified from Escherichia coli cells. The ATPase, a globular molecule (identical probably with an ATPase described previously by Richet and Kohiyama in 1976) shows specificity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0816687c1f7b94ede146654de81f6bbf
https://hdl.handle.net/21.11116/0000-0002-D980-821.11116/0000-0002-D982-6
https://hdl.handle.net/21.11116/0000-0002-D980-821.11116/0000-0002-D982-6