Complexes of a Zn-metalloenzyme binding site with hydroxamate-containing ligands. A case for detailed benchmarkings of polarizable molecular mechanics/dynamics potentials when the experimental binding structure is unknown

Autor: Laurent Salmon, Jean-Philip Piquemal, Céline Roux, Johanna Foret, Lea El-Khoury, Benoit de Courcy, Nohad Gresh, David Perahia

Publikováno v: Journal of Computational Chemistry. 37:2770-2782

Zn-metalloproteins are a major class of targets for drug design. They constitute a demanding testing ground for polarizable molecular mechanics/dynamics aimed at extending the realm of quantum chemistry (QC) to very long-duration molecular dynamics (

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f411a6f471fd7e181393409b0f0f7176
https://doi.org/10.1002/jcc.24503

The reaction mechanism of type I phosphomannose isomerases: New information from inhibition and polarizable molecular mechanics studies

Autor: Forum Bhatt, Johanna Foret, Benoit de Courcy, Laurent Salmon, Céline Roux, Constance J. Jeffery, Jean-Philip Piquemal, Nohad Gresh

Publikováno v: Proteins: Structure, Function, and Bioinformatics. 79:203-220

Type I phosphomannose isomerases (PMIs) are zinc-dependent metalloenzymes involved in the reversible isomerization of D-mannose 6-phosphate (M6P) and D-fructose 6-phosphate (F6P). 5-Phospho-D-arabinonohydroxamic acid (5PAH), an inhibitor endowed with

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::29f81098ebd3f4f21d4ce36cdac7314e
https://doi.org/10.1002/prot.22873

Synthesis and evaluation of non-hydrolyzable d-mannose 6-phosphate surrogates reveal 6-deoxy-6-dicarboxymethyl-d-mannose as a new strong inhibitor of phosphomannose isomerases

Autor: Nohad Gresh, Laurent Salmon, Jean-Philip Piquemal, Benoit de Courcy, Johanna Foret

Publikováno v: Bioorganic and Medicinal Chemistry
Bioorganic and Medicinal Chemistry, 2009, 17 (20), pp.7100-7107. ⟨10.1016/j.bmc.2009.09.005⟩
Bioorganic and Medicinal Chemistry, Elsevier, 2009, 17 (20), pp.7100-7107. ⟨10.1016/j.bmc.2009.09.005⟩

Non-hydrolyzable d-mannose 6-phosphate analogues in which the phosphate group was replaced by a phosphonomethyl, a dicarboxymethyl, or a carboxymethyl group were synthesized and kinetically evaluated as substrate analogues acting as potential inhibit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8681850b4e0794e1e1c289bc42a9cc92
https://hal.science/hal-02126828