Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Pascale Coric"'
Autor:
Bernard P. Roques, Catherine Llorens-Cortes, M. C. Fournie-Zaluski, Nicolas Inguimbert, Pascale Coric, Hélène Dhotel
Publikováno v:
Journal of Labelled Compounds and Radiopharmaceuticals. 47:997-1005
With the aim of studying the bioavailability of two related aminopeptidase A (APA) inhibitors, we have synthesized tritiated disulfide prodrugs. These molecules, 4,4′-dithiobis-(3,3′-amino)-1,1′-butanesulfonic acid (RB 150) and its 2,2-dimethyl
Autor:
Bernard P. Roques, Evelyne Lucas, Florence Noble, Pascale Coric, Serge Turcaud, Luce Bruetschy, Marie Claude Fournie-Zaluski
Publikováno v:
Journal of Medicinal Chemistry
Journal of Medicinal Chemistry, American Chemical Society, 1992, 35 (7), pp.1259-1266. ⟨10.1021/jm00085a013⟩
Journal of Medicinal Chemistry, American Chemical Society, 1992, 35 (7), pp.1259-1266. ⟨10.1021/jm00085a013⟩
Derivatives of amino acids bearing various zinc-coordinating moieties (SH, COOH, CONHOH, and PO3H2) were synthesized and tested for their ability to inhibit aminopeptidase N (APN). Among them, beta-amino thiols were found to be the most efficient wit
Autor:
Hervé Meudal, Marie-Claude Fournie-Zaluski, Franck Teffot, Bernard P. Roques, Nicolas Inguimbert, Hervé Poras, Pascale Coric
Publikováno v:
Journal of Medicinal Chemistry
Journal of Medicinal Chemistry, American Chemical Society, 2002, 45 (7), pp.1477-86
Journal of Medicinal Chemistry, 2002, 45 (7), pp.1477-86
HAL
Journal of Medicinal Chemistry, American Chemical Society, 2002, 45 (7), pp.1477-86
Journal of Medicinal Chemistry, 2002, 45 (7), pp.1477-86
HAL
International audience; The formation of vasoconstrictors (e.g., angiotensin II and endothelin) and the inactivation of vasodilators (e.g., bradykinin and atrial natriuretic) by membrane-bound zinc metallopeptidases are key mechanisms in the control
Autor:
Pascal George, Aurélie Mothé, Sophie Danascimento, Huixiong Chen, Marie-Claude Fournie-Zaluski, Florence Noble, Hervé Meudal, Pascale Coric, Bernard P. Roques
Publikováno v:
Journal of Medicinal Chemistry
Journal of Medicinal Chemistry, American Chemical Society, 2000, 43 (7), pp.1398-408
Journal of Medicinal Chemistry, American Chemical Society, 2000, 43 (7), pp.1398-1408. ⟨10.1021/jm990483l⟩
HAL
Journal of Medicinal Chemistry, American Chemical Society, 2000, 43 (7), pp.1398-408
Journal of Medicinal Chemistry, American Chemical Society, 2000, 43 (7), pp.1398-1408. ⟨10.1021/jm990483l⟩
HAL
International audience; The development of dual inhibitors of the two zinc metallopeptidases, neprilysin (neutral endopeptidase) and aminopeptidase N involved in the inactivation of the opioid peptides, enkephalins, represents an attractive physiolog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d955abead22b714e8d98f04de2a9de9
https://hal.archives-ouvertes.fr/hal-02122153
https://hal.archives-ouvertes.fr/hal-02122153
Autor:
Marie-Claude Fournie-Zaluski, Loïc Martin, Bernard P. Roques, Fabrice Cornille, Pascale Coric
Publikováno v:
Journal of Medicinal Chemistry
Journal of Medicinal Chemistry, American Chemical Society, 1998, 41 (18), pp.3450-3460. ⟨10.1021/jm981015z⟩
Journal of Medicinal Chemistry, 1998, 41 (18), pp.3450-3460. ⟨10.1021/jm981015z⟩
Journal of Medicinal Chemistry, American Chemical Society, 1998, 41 (18), pp.3450-3460. ⟨10.1021/jm981015z⟩
Journal of Medicinal Chemistry, 1998, 41 (18), pp.3450-3460. ⟨10.1021/jm981015z⟩
Tetanus neurotoxin is a 150-kDa protein produced by Clostridium tetani, which causes the lethal spastic paralytic syndromes of tetanus by blocking inhibitory neurotransmitter release at central synapses. The toxin light chain (50 kDa) has a zinc endo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::574bd7f53bd2b63e9ce6253c62d4e302
https://hal.archives-ouvertes.fr/hal-02461413
https://hal.archives-ouvertes.fr/hal-02461413
Autor:
Pascale Coric, Claire Smadja, Rafael Maldonado, Olga Valverde, Marie-Claude Fournie-Zaluski, Serge Turcaud, Florence Noble, Bernard P. Roques
Publikováno v:
PAIN
PAIN, Elsevier, 1997, 73 (3), pp.383-391. ⟨10.1016/S0304-3959(97)00125-5⟩
Pain
Pain, 1997, 73 (3), pp.383-391. ⟨10.1016/S0304-3959(97)00125-5⟩
PAIN, Elsevier, 1997, 73 (3), pp.383-391. ⟨10.1016/S0304-3959(97)00125-5⟩
Pain
Pain, 1997, 73 (3), pp.383-391. ⟨10.1016/S0304-3959(97)00125-5⟩
RB 101 (N-((R,S)-2-benzyl-3[(S)(2-amino-4-methylthio)butyldithio]-1-oxopr opyl)-L-phenylalanine benzyl ester) is a full inhibitor of the enkephalin-catabolizing enzymes, which induces strong naloxone-reversible antinociceptive responses after i.v. or
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2d5feb7191881569d831fdffcd917bd
https://hal.archives-ouvertes.fr/hal-02461424
https://hal.archives-ouvertes.fr/hal-02461424
Publikováno v:
Journal of Medicinal Chemistry
Journal of Medicinal Chemistry, American Chemical Society, 1996, 39 (6), pp.1210-1219. ⟨10.1021/jm950590p⟩
Journal of Medicinal Chemistry, 1996, 39 (6), pp.1210-1219. ⟨10.1021/jm950590p⟩
Journal of Medicinal Chemistry, American Chemical Society, 1996, 39 (6), pp.1210-1219. ⟨10.1021/jm950590p⟩
Journal of Medicinal Chemistry, 1996, 39 (6), pp.1210-1219. ⟨10.1021/jm950590p⟩
International audience; An interesting approach for the treatment of congestive heart failure and chronic hypertension could be to avoid the formation of angiotensin II by inhibiting angiotensin converting enzyme (ACE) and to protect atrial natriuret
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a5c7c6e193d15baa4cb398b560ef7d0
https://hal.archives-ouvertes.fr/hal-02122055
https://hal.archives-ouvertes.fr/hal-02122055
Autor:
Walter Gonzalez, Vincent Thery, Bernard P. Roques, Jean-Baptiste Michel, Marie-Claude Fournie-Zaluski, Hervé Meudal, Pascale Coric, Serge Turcaud
Publikováno v:
Journal of Medicinal Chemistry
Journal of Medicinal Chemistry, 1996, 39 (13), pp.2594-2608. ⟨10.1021/jm950783c⟩
Journal of Medicinal Chemistry, American Chemical Society, 1996, 39 (13), pp.2594-2608. ⟨10.1021/jm950783c⟩
Journal of Medicinal Chemistry, 1996, 39 (13), pp.2594-2608. ⟨10.1021/jm950783c⟩
Journal of Medicinal Chemistry, American Chemical Society, 1996, 39 (13), pp.2594-2608. ⟨10.1021/jm950783c⟩
International audience; Mercaptoacyl dipeptides, containing a glycine linked to a C-terminal 5-phenylproline, have been synthesized in order to obtain new highly efficient dual inhibitors of the two zinc metallopeptidases, neutral endopeptidase (NEP)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6845a5103c7d44a4522001abb6ba9396
https://doi.org/10.1021/jm950783c
https://doi.org/10.1021/jm950783c
Autor:
Eric N. Chauvel, Catherine Llorens-Cortes, Bernard P. Roques, Pascale Coric, Sherwin Wilk, Marie-Claude Fournie-Zaluski
Publikováno v:
Journal of Medicinal Chemistry
Journal of Medicinal Chemistry, American Chemical Society, 1994, 37 (18), pp.2950-2957. ⟨10.1021/jm00044a016⟩
Journal of Medicinal Chemistry, 1994, 37 (18), pp.2950-2957. ⟨10.1021/jm00044a016⟩
Journal of Medicinal Chemistry, American Chemical Society, 1994, 37 (18), pp.2950-2957. ⟨10.1021/jm00044a016⟩
Journal of Medicinal Chemistry, 1994, 37 (18), pp.2950-2957. ⟨10.1021/jm00044a016⟩
Aminopeptidase A (APA) is a highly selective peptidase, which cleaves the N-terminal Glu or Asp residues of biologically active peptides, and has therefore been proposed to be involved in angiotensin II and CCK8 metabolism. Highly potent and selectiv
Autor:
Catherine Llorens-Cortes, Sherwin Wilk, Pascale Coric, Bernard P. Roques, Marie-Claude Fournie-Zaluski, Eric N. Chauvel
Publikováno v:
Journal of Medicinal Chemistry
Journal of Medicinal Chemistry, American Chemical Society, 1994, 37 (9), pp.1339-1346. ⟨10.1021/jm00035a014⟩
Journal of Medicinal Chemistry, 1994, 37 (9), pp.1339-1346. ⟨10.1021/jm00035a014⟩
Journal of Medicinal Chemistry, American Chemical Society, 1994, 37 (9), pp.1339-1346. ⟨10.1021/jm00035a014⟩
Journal of Medicinal Chemistry, 1994, 37 (9), pp.1339-1346. ⟨10.1021/jm00035a014⟩
Aminopeptidase A (APA) and aminopeptidase N (APN) are two metallopeptidases which have been suggested to be involved in the enzymatic cascade of the renin-angiotensin system. APA liberates angotensin III from angiotensin II by releasing the N-termina