RECHERCHER
Résultats de la recherche ""
Evolution of abiotic cubane chemistries in a nucleic acid aptamer allows selective recognition of a malaria biomarker
Publié le 08/07/2020
... Cheung, Y.W., Röthlisberger, P., Mechaly, A.E., Weber, P., Levi-Acobas, F., Lo, Y., Wong, A.W.C., Kinghorn, A.B., Haouz, A., Savage, G.P., Hollenstein, M., Tanner, J.A. "Evolution of abiotic cubane chemistries in a nucleic acid aptamer allows selective ...
Novel N-substituted 5-phosphate-d-arabinonamide derivatives as strong inhibitors of phosphoglucose isomerases: synthesis, structure-activity relationship and crystallographic studies
Publié le 08/07/2020
... Ahmad, L., Plancqueel, S., Lazar, N., Korri-Youssoufi, H., Li de la Sierra-Gallay, I., van Tilbeurgh, H., Salmon, L. "Novel N-substituted 5-phosphate-d-arabinonamide derivatives as strong inhibitors of phosphoglucose isomerases: synthesis, structure ...
Structure and catalytic regulation of Plasmodium falciparum IMP specific nucleotidase
Publié le 04/07/2020
... Carrique, L., Ballut, L., Shukla, A., Varma, N., Ravi, R., Violot, S., Srinivasan, B., Ganeshappa, U.T., Kulkarni, S., Balaram, H., Aghajari, N. "Structure and catalytic regulation of Plasmodium falciparum IMP specific nucleotidase" Nature Communications. ...
Formation and modulation of nanotubular assemblies of oligourea foldamers in aqueous conditions using alcohol additives
Publié le 02/07/2020
... Yoo, S.H., Collie, G.W., Mauran, L., Guichard, G. "Formation and modulation of nanotubular assemblies of oligourea foldamers in aqueous conditions using alcohol additives" ChemPlusChem., 85(10): 2243-2250. (2020). ...
Structural evidence for the binding of monocarboxylates and dicarboxylates at pharmacologically relevant extracellular sites of a pentameric ligand-gated ion channel
Publié le 02/07/2020
... Fourati, Z., Sauguet, L., Delarue, M. "Structural evidence for the binding of monocarboxylates and dicarboxylates at pharmacologically relevant extracellular sites of a pentameric ligand-gated ion channel" Acta Crystallographica D., 76(7): 668-675. (2020 ...
Self-assembly of model amphiphilic peptides in non-aqueous solvents: changing driving forces, same structure?
Publié le 30/06/2020
... Del Giudice, A., Rüter, A., Pavel, N.V., Galantini, L., Olsson, U. "Self-assembly of model amphiphilic peptides in non-aqueous solvents: changing driving forces, same structure?" Langmuir., 36(29): 8451–8460. (2020). ...
Combining surface chemistry modification and in situ small-angle scattering characterization to understand and optimize the biological behavior of nanomedicines
Publié le 25/06/2020
... Le Goas, M., Roussel, T., Kalbazova, M., Carriere, D., Barruet, E., Geertsen, V., Fadda, G., Testard, F., Carrot, G., Renault, J.P. "Combining surface chemistry modification and in situ small-angle scattering characterization to understand and optimize ...
Structural insight into the formation of lipoprotein-β-barrel complexes
Publié le 24/06/2020
... Rodríguez-Alonso, R., Létoquart, J., Nguyen, V.S., Louis, G., Calabrese, A.N., Iorga, B.I., Radford, S.E., Cho, S.H., Remaut, H., Collet, J.F. "Structural insight into the formation of lipoprotein-β-barrel complexes" Nature Chemical Biology., 16(9): 1019 ...
A Transmembrane Crenarchaeal Mannosyltransferase Is Involved in N-Glycan Biosynthesis and Displays an Unexpected Minimal Cellulose-Synthase-like Fold
Publié le 23/06/2020
... Gandini, R., Reichenbach, T., Spadiut, O., Tan, T.C., Kalyani, D.C., Divne, C. "A Transmembrane Crenarchaeal Mannosyltransferase Is Involved in N-Glycan Biosynthesis and Displays an Unexpected Minimal Cellulose-Synthase-like Fold" Journal of Molecular ...
Structural and enzymatic characterisation of the Type III effector NopAA (=GunA) from Sinorhizobium fredii USDA257 reveals a Xyloglucan hydrolase activity
Publié le 20/06/2020
... Dorival, J., Philys, S., Giuntini, E., Brailly, R., de Ruyck, J., Czjzek, M., Biondi, E., Bompard, C. "Structural and enzymatic characterisation of the Type III effector NopAA (=GunA) from Sinorhizobium fredii USDA257 reveals a Xyloglucan hydrolase ...