Targeting NOX2 via p47/phox-p22/phox Inhibition with Novel Triproline Mimetics

Autor: Jean-Baptiste Garsi, Balázs Komjáti, Gregorio Cullia, Imre Fejes, Melinda Sipos, Zoltán Sipos, Eszter Fördős, Piroska Markacz, Barbara Balázs, Nathalie Lancelot, Sylvie Berger, Eric Raimbaud, David Brown, Laurent-Michel Vuillard, Laure Haberkorn, Cyprian Cukier, Zoltán Szlávik, Stephen Hanessian

Publikováno v: ACS medicinal chemistry letters, vol 13, iss 6
ACS Med Chem Lett

[Image: see text] On the basis of the knowledge that the proline-rich hot spot PPPRPP region of P(151)PSNPPPRPP(160), an oligopeptide derived from the cytosolic portion of p22(phox) (p22), binds to the single functional bis-SH3 domain of the regulato

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2aa70b14a5bdfbbdfe94d8e9fe7ef2af
https://doi.org/10.1021/acsmedchemlett.2c00094

3-Bromo-Isoxazoline Derivatives Inhibit GAPDH Enzyme in PDAC Cells Triggering Autophagy and Apoptotic Cell Death

Autor: Raffaella Pacchiana, Nidula Mullappilly, Andrea Pinto, Stefania Bova, Stefania Forciniti, Gregorio Cullia, Elisa Dalla Pozza, Emanuela Bottani, Ilaria Decimo, Ilaria Dando, Stefano Bruno, Paola Conti, Massimo Donadelli

Publikováno v: Cancers; Volume 14; Issue 13; Pages: 3153

A growing interest in the study of aerobic glycolysis as a key pathway for cancer-cell energetic metabolism, favouring tumour progression and invasion, has led to consider GAPDH as an effective drug target to specifically hit cancer cells. In this st

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0266e2ab9a6ed549d34455191f12834
https://doi.org/10.3390/cancers14133153

Control by Metals of Staphylopine Dehydrogenase Activity during Metallophore Biosynthesis

Autor: Christine Hajjar, Roberto Fanelli, Clémentine Laffont, Catherine Brutesco, Gregorio Cullia, Mathilde Tribout, Didier Nurizzo, Elise Borezée-Durant, Romé Voulhoux, David Pignol, Jérôme Lavergne, Florine Cavelier, Pascal Arnoux

Publikováno v: Journal of the American Chemical Society
Journal of the American Chemical Society, American Chemical Society, 2019, 141 (3), pp.5555-5562. ⟨10.1021/jacs.9b01676⟩
Journal of the American Chemical Society, 2019, 141 (3), pp.5555-5562. ⟨10.1021/jacs.9b01676⟩

International audience; Enzymatic regulations are central processes for the adaptation to changing environments. In the particular case of metallophore-dependent metal uptake, there is a need to quickly adjust the production of these metallophores to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed2532d0511fbee693989ba388a7bedf
https://hal-cea.archives-ouvertes.fr/cea-02078121

Synthesis and pharmacological evaluation of conformationally constrained glutamic acid higher homologues

Autor: Andrea Pinto, Paola Conti, Lucia Tamborini, Gregorio Cullia, Carlo De Micheli, Birgitte Nielsen

Publikováno v: Bioorganic & Medicinal Chemistry. 24:5741-5747

Homologation of glutamic acid chain together with conformational constraint is a commonly used strategy to achieve selectivity towards different types of glutamate receptors. In the present work, starting from two potent and selective unnatural amino

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a51b77663d85ce8c94a5d5b6e1b63b28
https://doi.org/10.1016/j.bmc.2016.09.029

Selectivity of 3-bromo-isoxazoline inhibitors between human and Plasmodium falciparum glyceraldehyde-3-phosphate dehydrogenases

Autor: Andrea Mozzarelli, Andrea Pinto, Paola Conti, Marilena Margiotta, Carlo De Micheli, Stefano Bruno, Gregorio Cullia

Publikováno v: Bioorganic & medicinal chemistry
24 (2016): 2654–2659. doi:10.1016/j.bmc.2016.04.033
info:cnr-pdr/source/autori:Bruno S, Margiotta M, Pinto A, Cullia G, Conti P, De Micheli C, Mozzarelli A/titolo:Selectivity of 3-bromo-isoxazoline inhibitors between human and Plasmodium falciparum glyceraldehyde-3-phosphate dehydrogenases/doi:10.1016%2Fj.bmc.2016.04.033/rivista:Bioorganic & medicinal chemistry (Print)/anno:2016/pagina_da:2654/pagina_a:2659/intervallo_pagine:2654–2659/volume:24

Compounds based on the 3-Br-isoxazoline scaffold fully inhibit glyceraldehyde 3-phosphate dehydrogenase from Plasmodium falciparum by selectively alkylating all four catalytic cysteines of the tetramer. Here, we show that, under the same experimental

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::adec988d28143935984bc93d6451d0f4
https://doi.org/10.1016/j.bmc.2016.04.033