V. Skamnaki

发表

Effects of commonly used cryoprotectants on glycogen phosphorylase activity and structure

L. Johnson, K. Watson, S. Zographos, 1999, Protein science : a publication of the Protein Society.

The Role of the Phospho-CDK2/Cyclin A Recruitment Site in Substrate Recognition*

Martin E M Noble, Luke Kontogiannis, Giuliano Siligardi, 2006, Journal of Biological Chemistry.

The structure of cyclin E1/CDK2: implications for CDK2 activation and CDK2‐independent roles

L. Johnson, N. Brown, R. Honda, 2005, The EMBO journal.

The σ‐Hole Phenomenon of Halogen Atoms Forms the Structural Basis of the Strong Inhibitory Potency of C5 Halogen Substituted Glucopyranosyl Nucleosides towards Glycogen Phosphorylase b

S. Zographos, D. Leonidas, A. Psarra, 2012, ChemMedChem.

3′‐Axial CH2OH Substitution on Glucopyranose does not Increase Glycogen Phosphorylase Inhibitory Potency. QM/MM‐PBSA Calculations Suggest Why

D. Leonidas, P. Zoumpoulakis, V. Skamnaki, 2012, Chemical biology & drug design.

Effects of commonly used cryoprotectants on glycogen phosphorylase activity and structure

L. Johnson, K. Watson, S. Zographos, 1999, Protein science : a publication of the Protein Society.

Allosteric inhibition of glycogen phosphorylase a by the potential antidiabetic drug 3‐isopropyl 4‐(2‐chlorophenyl)‐1,4‐dihydro‐1‐ethyl‐2‐methyl‐pyridine‐3,5,6‐tricarboxylate

S. Zographos, N. Oikonomakos, K. Tsitsanou, 1999, Protein science : a publication of the Protein Society.

The binding of C5-alkynyl and alkylfurano[2,3-d]pyrimidine glucopyranonucleosides to glycogen phosphorylase b: synthesis, biochemical and biological assessment.

S. Zographos, D. Leonidas, A. Psarra, 2012, European journal of medicinal chemistry.

1-(3-Deoxy-3-fluoro-beta-d-glucopyranosyl) pyrimidine derivatives as inhibitors of glycogen phosphorylase b: Kinetic, crystallographic and modelling studies.

S. Zographos, D. Leonidas, V. G. Tsirkone, 2010, Bioorganic & medicinal chemistry.

Kinetic and crystallographic studies of glucopyranosylidene spirothiohydantoin binding to glycogen phosphorylase B.

László Szilágyi, B. Tóth, N. Oikonomakos, 2002, Bioorganic & medicinal chemistry.

Cooperative Interactions of the Catalytic Nucleophile and the Catalytic Acid in the Inhibition of β-Glycosidases. Calculations and their validation by comparative kinetic and structural studies of the inhibition of glycogen phosphorylase b

Spyros E. Zographos, Katerina E. Tsitsanou, S. Zographos, 1998 .

The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition

L. Johnson, N. Oikonomakos, D. Owen, 1997, The EMBO journal.

Flavopiridol Inhibits Glycogen Phosphorylase by Binding at the Inhibitor Site*

Spyros E. Zographos, Katerina E. Tsitsanou, L. Johnson, 2000, The Journal of Biological Chemistry.

Structural basis of the synergistic inhibition of glycogen phosphorylase a by caffeine and a potential antidiabetic drug.

N. Oikonomakos, K. Tsitsanou, V. Skamnaki, 2000, Archives of biochemistry and biophysics.

Kinetic Characterization of the Double Mutant R148A/E182S of Glycogen Phosphorylase Kinase Catalytic Subunit: The Role of the Activation Loop

N. Oikonomakos, V. Skamnaki, 2000, Journal of protein chemistry.

Cyclin B and Cyclin A Confer Different Substrate Recognition Properties on CDK2

L. Johnson, N. Brown, E. Lowe, 2007, Cell cycle.

Kinetics, in silico docking, molecular dynamics, and MM‐GBSA binding studies on prototype indirubins, KT5720, and staurosporine as phosphorylase kinase ATP‐binding site inhibitors: The role of water molecules examined

Georgios Archontis, S. Zographos, N. Oikonomakos, 2011, Proteins.

Catalytic mechanism of phosphorylase kinase probed by mutational studies.

L. Johnson, N. Oikonomakos, M. Noble, 1999, Biochemistry.

A new allosteric site in glycogen phosphorylase b as a target for drug interactions.

L. Johnson, N. Oikonomakos, K. Tsitsanou, 2000, Structure.

The structure of glycogen phosphorylase b with an alkyldihydropyridine-dicarboxylic acid compound, a novel and potent inhibitor.

L. Johnson, K. Watson, S. Zographos, 1997, Structure.

The 1.76 A resolution crystal structure of glycogen phosphorylase B complexed with glucose, and CP320626, a potential antidiabetic drug.

S. Zographos, N. Oikonomakos, G. Archontis, 2002, Bioorganic & medicinal chemistry.

3′‐Axial CH2OH Substitution on Glucopyranose does not Increase Glycogen Phosphorylase Inhibitory Potency. QM/MM‐PBSA Calculations Suggest Why

D. Leonidas, P. Zoumpoulakis, V. Skamnaki, 2012, Chemical biology & drug design.

The σ‐Hole Phenomenon of Halogen Atoms Forms the Structural Basis of the Strong Inhibitory Potency of C5 Halogen Substituted Glucopyranosyl Nucleosides towards Glycogen Phosphorylase b

S. Zographos, D. Leonidas, A. Psarra, 2012, ChemMedChem.