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Homolya, L.,
Mathomes, R. T.,
Varga, L.,
Docsa, T.,
Juhász, L.,
Hayes, J. M.,
Somsák, L.:
Synthesis, in silico and kinetics evaluation of N-(beta-D-glucopyranosyl)-2-arylimidazole-4(5)-carboxamides and N-(beta-D-glucopyranosyl)-4(5)-arylimidazole-2-carboxamides as glycogen phosphorylase inhibitors.
Int. J. Mol. Sci. 25 (9), 1-21, (article identifier: 4591), 2024.
Kun, S.,
Mathomes, R. T.,
Docsa, T.,
Somsák, L.,
Hayes, J. M.:
Design and Synthesis of 3-(β-D-Glucopyranosyl)-4-amino/4-guanidino Pyrazole Derivatives and Analysis of Their Glycogen Phosphorylase Inhibitory Potential.
Molecules. 28 (7), 1-19, (article identifier: 3005), 2023.
Kola, J. B.,
Docsa, T.,
Uray, K.:
Mechanosensing in the Physiology and Pathology of the Gastrointestinal Tract.
Int. J. Mol. Sci. 24 (1), 1-12, (article identifier: 177), 2023.
Docsa, T.,
Sipos, Á.,
Cox, C. S.,
Uray, K.:
The Role of Inflammatory Mediators in the Development of Gastrointestinal Motility Disorders.
Int. J. Mol. Sci. 23 (13), 1-22, (article identifier: 6917), 2022.
Docsa, T.,
Bhattarai, D.,
Sipos, Á.,
Wade, C. E.,
Cox, C. S.,
Uray, K.:
CXCL1 is upregulated during the development of ileus resulting in decreased intestinal contractile activity.
Neurogastroenterol. Motil. 32 (3), 1-12, 2020.
Q1
Agricultural and Biological Sciences (miscellaneous)
Q1
Chemistry (miscellaneous)
13.
Szabó, E. K.,
Kyriakis, E.,
Psarra, A. M. G.,
Karra, A. G.,
Sipos, Á.,
Docsa, T.,
Stravodimos, G. A.,
Katsidou, E.,
Skamnaki, V. T.,
Liggri, P. G. V.,
Zographos, S. E.,
Mándi, A.,
Király, S. B.,
Kurtán, T.,
Leonidas, D. D.,
Somsák, L.:
Glucopyranosylidene-spiro-imidazolinones, a New Ring System: Synthesis and Evaluation as Glycogen Phosphorylase Inhibitors by Enzyme Kinetics and X-ray Crystallography.
J. Med. Chem. 62 (13), 6116-6136, 2019.
Barr, D.,
Szennyes, E.,
Bokor, É.,
Al-Oanzi, Z. H.,
Moffatt, C.,
Kun, S.,
Docsa, T.,
Sipos, Á.,
Davies, M. P.,
Mathomes, R. T.,
Snape, T. J.,
Agius, L.,
Somsák, L.,
Hayes, J. M.:
Identification of C-[béta]-d-Glucopyranosyl Azole-Type Inhibitors of Glycogen Phosphorylase That Reduce Glycogenolysis in Hepatocytes: in Silico Design, Synthesis, in Vitro Kinetics, and ex Vivo Studies.
ACS Chem. Biol. 14 (7), 1460-1470, 2019.
Kun, S.,
Begum, J.,
Kyriakis, E.,
Stamati, E. C. V.,
Barkas, T. A.,
Szennyes, E.,
Bokor, É.,
Szabó, E. K.,
Stravodimos, G. A.,
Sipos, Á.,
Docsa, T.,
Gergely, P.,
Moffatt, C.,
Patraskaki, M. S.,
Kokolaki, M. C.,
Gkerdi, A.,
Skamnaki, V. T.,
Leonidas, D. D.,
Somsák, L.,
Hayes, J. M.:
A multidisciplinary study of 3-(β-D-glucopyranosyl)-5-substituted-1,2,4-triazole derivatives as glycogen phosphorylase inhibitors: computation, synthesis, crystallography and kinetics reveal new potent inhibitors.
Eur. J. Med. Chem. 147, 266-278, 2018.
Kun, S.,
Bokor, É.,
Sipos, Á.,
Docsa, T.,
Somsák, L.:
Synthesis of New C- and N-beta-D-Glucopyranosyl Derivatives of Imidazole, 1,2,3-Triazole and Tetrazole, and Their Evaluation as Inhibitors of Glycogen Phosphorylase.
Molecules. 23 (3), 1-17, 2018.
Bokor, É.,
Kyriakis, E.,
Solovou, T. G. A.,
Koppány, C.,
Kantsadi, A. L.,
Szabó, E. K.,
Szakács, A.,
Stravodimos, G. A.,
Docsa, T.,
Skamnaki, V. T.,
Zographos, S. E.,
Gergely, P.,
Leonidas, D. D.,
Somsák, L.:
Nanomolar Inhibitors of Glycogen Phosphorylase Based on β-d-Glucosaminyl Heterocycles: A Combined Synthetic, Enzyme Kinetic, and Protein Crystallography Study.
J. Med. Chem. 60 (22), 9251-9262, 2017.
Goyard, D.,
Kónya, B.,
Chajistamatiou, A. S.,
Chrysina, E. D.,
Leroy, J.,
Balzarin, S.,
Tournier, M.,
Tousch, D.,
Petit, P.,
Duret, C.,
Maurel, P.,
Somsák, L.,
Docsa, T.,
Gergely, P.,
Praly, J. P.,
Azay-Milhau, J.,
Vidal, S.:
Glucose-derived spiro-isoxazolines are anti-hyperglycemic agents against type 2 diabetes through glycogen phosphorylase inhibition.
Eur. J. Med. Chem. 108, 444-454, 2016.
Kantsadi, A. L.,
Bokor, É.,
Kun, S.,
Stravodimos, G. A.,
Chatzileontiadou, D. S. M.,
Leonidas, D. D.,
Juhász-Tóth, É.,
Szakács, A.,
Batta, G.,
Docsa, T.,
Gergely, P.,
Somsák, L.:
Synthetic, enzyme kinetic, and protein crystallographic studies of C-[béta]-D-glucopyranosyl pyrroles and imidazoles reveal and explain low nanomolar inhibition of human liver glycogen phosphorylase.
Eur. J. Med. Chem. 123, 737-745, 2016.
