C
C. Tiraidis
Researcher at Novo Nordisk
Publications - 11
Citations - 388
C. Tiraidis is an academic researcher from Novo Nordisk. The author has contributed to research in topics: Glycogen phosphorylase & Ligand (biochemistry). The author has an hindex of 9, co-authored 11 publications receiving 374 citations.
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Journal ArticleDOI
New Inhibitors of Glycogen Phosphorylase as Potential Antidiabetic Agents
László Somsák,Katalin Czifrák,Marietta Tóth,Éva Bokor,Evangelia D. Chrysina,K.-M. Alexacou,Joseph Hayes,C. Tiraidis,E. Lazoura,Demetres D. Leonidas,Spyros E. Zographos,Nikos G. Oikonomakos +11 more
TL;DR: The synthesis, structure determination and computational studies of the most recent inhibitors of glycogen phosphorylase at the different binding sites are presented and analyzed and have the potential to facilitate structure-based drug design.
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Glucose-based spiro-isoxazolines: a new family of potent glycogen phosphorylase inhibitors.
Mahmoud Benltifa,Joseph Hayes,Sébastien Vidal,David Gueyrard,Peter G. Goekjian,Jean-Pierre Praly,Gregory Kizilis,C. Tiraidis,K.-M. Alexacou,Evangelia D. Chrysina,Spyros E. Zographos,Demetres D. Leonidas,Georgios Archontis,Nikos G. Oikonomakos +13 more
TL;DR: Docking calculations with GLIDE in extra-precision (XP) mode yielded excellent agreement with experiment, as judged by comparison of the predicted binding modes of the five ligands with the crystallographic conformations and the good correlation between the docking scores and the experimental free binding energies.
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Iminosugars as Potential Inhibitors of Glycogenolysis: Structural Insights into the Molecular Basis of Glycogen Phosphorylase Inhibition
Nikos G. Oikonomakos,C. Tiraidis,Demetres D. Leonidas,Spyros E. Zographos,Marit Kristiansen,Claus U. Jessen,Leif Nørskov-Lauritsen,Loranne Agius +7 more
TL;DR: X-ray structures of 5, 9, and its N-3-phenylpropyl analogue 8 in complex with rabbit muscle glycogen phosphorylase (GPb) shows that iminosugars bind tightly at the catalytic site in the presence of the substrate phosphate and induce conformational changes that characterize the R-state conformation of the enzyme.
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Crystallographic and computational studies on 4‐phenyl‐N‐(β‐D‐glucopyranosyl)‐1H‐1,2,3‐triazole‐1‐acetamide, an inhibitor of glycogen phosphorylase: Comparison with α‐D‐glucose, N‐acetyl‐β‐D‐glucopyranosylamine and N‐benzoyl‐N′‐β‐D‐glucopyranosyl urea binding
K.-M. Alexacou,Joseph Hayes,C. Tiraidis,Spyros E. Zographos,Demetres D. Leonidas,Evangelia D. Chrysina,Georgios Archontis,Nikos G. Oikonomakos,Jashuva V. Paul,Babu Varghese,Duraikkannu Loganathan +10 more
TL;DR: In this article, the structure of GPb in complex with glucosyltriazolylacetamide at 100 K to 188 A resolution was determined, with and without the crystallographic ordered cavity waters using the GoldScore scoring function.
Journal ArticleDOI
Bioactivity of glycogen phosphorylase inhibitors that bind to the purine nucleoside site.
Laura J. Hampson,Catherine Arden,Loranne Agius,Minas Ganotidis,Magda Kosmopoulou,C. Tiraidis,Yiannis Elemes,Constantinos Sakarellos,Demetres D. Leonidas,Nikos G. Oikonomakos +9 more
TL;DR: Results show key differences between purine site and indole carboxamide site inhibitors in terms of relative roles of dephosphorylation of phosphorylase-a as compared with allosteric inhibition, counteraction of the efficacy of the inhibitors on glycogenolysis by dibutyryl-cAMP and stimulation of glycogen synthesis.