Bisphosphonate Inhibitors of Mammalian Glycolytic Aldolase

Autor: Marta Abellán-Flos, Laurent Salmon, Paul W. Heron, Jurgen Sygusch

Publikováno v: Journal of Medicinal Chemistry. 61:10558-10572

The glycolytic enzyme aldolase is an emerging drug target in diseases such as cancer and protozoan infections which are dependent on a hyperglycolytic phenotype to synthesize adenosine 5'-triphosphate and metabolic precursors for biomass production.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e80c3c1898ed765a4046c5ae82431ed
https://doi.org/10.1021/acs.jmedchem.8b01000

Carbohydrate-based electrochemical biosensor for detection of a cancer biomarker in human plasma

Autor: Laurent Salmon, Marion Devillers, Lama Ahmad, Hafsa Korri-Youssoufi

Publikováno v: Biosensors and Bioelectronics. 96:178-185

Autocrine motility factor (AMF) is a tumor-secreted cytokine that stimulates tumor cell motility in vitro and metastasis in vivo. AMF could be detected in serum or urine of cancer patients with worse prognosis. Reported as a cancer biomarker, AMF sec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2c08a0885fee9185efc1bad7503258e
https://doi.org/10.1016/j.bios.2017.04.031

Recent developments in nuclear heating measurement methods inside the OSIRIS reactor

Autor: Hubert Carcreff, Laurent Salmon, Fadhel Malouch

Publikováno v: Nuclear Instruments and Methods in Physics Research Section A: Accelerators, Spectrometers, Detectors and Associated Equipment
Nuclear Instruments and Methods in Physics Research Section A: Accelerators, Spectrometers, Detectors and Associated Equipment, Elsevier, 2019, 942, pp.162310. ⟨10.1016/j.nima.2019.06.051⟩
Nuclear Instruments and Methods in Physics Research Section A: Accelerators, Spectrometers, Detectors and Associated Equipment, 2019, 942, pp.162310. ⟨10.1016/j.nima.2019.06.051⟩

Nuclear heating inside a Material Testing Reactor (MTR) needs to be known in order to design and to run irradiation experiments that have to fulfill target temperature constraints. To improve the incore nuclear heating knowledge of the French OSIRIS

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a01872f0ddb9e49f7f188abf41853066
https://hal-cea.archives-ouvertes.fr/cea-02535369

Novel N-substituted 5-phosphate-d-arabinonamide derivatives as strong inhibitors of phosphoglucose isomerases: Synthesis, structure-activity relationship and crystallographic studies

Autor: Herman van Tilbeurgh, S. Plancqueel, Lama Ahmad, Laurent Salmon, Noureddine Lazar, Hafsa Korri-Youssoufi, Inès Li de la Sierra-Gallay

Publikováno v: Bioorganic Chemistry
Bioorganic Chemistry, 2020, 102, pp.104048. ⟨10.1016/j.bioorg.2020.104048⟩
Bioorganic Chemistry, Elsevier, 2020, 102, pp.104048. ⟨10.1016/j.bioorg.2020.104048⟩

International audience; Phosphoglucose isomerase (PGI) is a cytosolic enzyme that catalyzes the reversible interconversion of d-glucose 6-phosphate and d-fructose 6-phosphate in glycolysis. Outside the cell, PGI is also known as autocrine motility fa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc2b249f4c981ade729a73bdd3744080
https://doi.org/10.1016/j.bioorg.2020.104048

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

Publikováno v: Journal of computational chemistry. 37(32)

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=pmid________::cd20cd95576f96d0c8e2ecae6b046913
https://pubmed.ncbi.nlm.nih.gov/27699809