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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

Proteins, structure, function, and bioinformatics, 2011-03, Vol.79 (3), p.703-719

2011

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

The EMBO journal, 2005-02, Vol.24 (3), p.452-463

2005

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

Bioorganic & medicinal chemistry, 2010-05, Vol.18 (10), p.3413-3425

2010

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

Cell cycle (Georgetown, Tex.), 2007-06, Vol.6 (11), p.1350-1359

2007

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

The Journal of biological chemistry, 2006-08, Vol.281 (32), p.23167-23179

2006

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

Structure (London), 2000-06, Vol.8 (6), p.575-584

2000

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Flavopiridol Inhibits Glycogen Phosphorylase by Binding at the Inhibitor Site

The Journal of biological chemistry, 2000-11, Vol.275 (44), p.34566-34573

2000

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Kinetic and Crystallographic Studies of Glucopyranosylidene Spirothiohydantoin Binding to Glycogen Phosphorylase b

Bioorganic & medicinal chemistry, 2002-02, Vol.10 (2), p.261-268

2002

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

Bioorganic & medicinal chemistry, 2002-05, Vol.10 (5), p.1313-1319

2002

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

Chemical biology & drug design, 2012-05, Vol.79 (5), p.663-673

2012

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Effects of commonly used cryoprotectants on glycogen phosphorylase activity and structure

Protein science, 1999-04, Vol.8 (4), p.741-749

1999

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Kinetic characterization of the double mutant R148A/E182S of glycogen phosphorylase kinase catalytic subunit: the role of the activation loop

Journal of Protein Chemistry, 2000-08, Vol.19 (6), p.499-505

2000

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3′‐Axial CH 2 OH Substitution on Glucopyranose does not Increase Glycogen Phosphorylase Inhibitory Potency. QM/MM‐PBSA Calculations Suggest Why

Chemical biology & drug design, 2012-05, Vol.79 (5), p.663-673

2012

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Structural Basis of the Synergistic Inhibition of Glycogen Phosphorylase a by Caffeine and a Potential Antidiabetic Drug

Archives of biochemistry and biophysics, 2000-12, Vol.384 (2), p.245-254

2000

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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

Protein science, 1999-10, Vol.8 (10), p.1930-1945

1999

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3'-axial CH2 OH substitution on glucopyranose does not increase glycogen phosphorylase inhibitory potency. QM/MM-PBSA calculations suggest why

Chemical biology & drug design, 2012-05, Vol.79 (5), p.663-673

2012

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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

Helvetica chimica acta, 1998, Vol.81 (5-8), p.853-864

1998

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

Structure (London), 1997-11, Vol.5 (11), p.1413-1425

1997

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The ammonium sulfate inhibition of human angiogenin

FEBS letters, 2016-09, Vol.590 (17), p.3005-3018

2016

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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

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

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

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

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

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

Flavopiridol Inhibits Glycogen Phosphorylase by Binding at the Inhibitor Site

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

Kinetic and Crystallographic Studies of Glucopyranosylidene Spirothiohydantoin Binding to Glycogen Phosphorylase b

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

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

Effects of commonly used cryoprotectants on glycogen phosphorylase activity and structure

Kinetic characterization of the double mutant R148A/E182S of glycogen phosphorylase kinase catalytic subunit: the role of the activation loop

The [sigma]-Hole Phenomenon of Halogen Atoms Forms the Structural Basis of the Strong Inhibitory Potency of C5 Halogen Substituted Glucopyranosyl Nucleosides towards Glycogen Phosphorylaseb

3′‐Axial CH 2 OH Substitution on Glucopyranose does not Increase Glycogen Phosphorylase Inhibitory Potency. QM/MM‐PBSA Calculations Suggest Why

Structural Basis of the Synergistic Inhibition of Glycogen Phosphorylase a by Caffeine and a Potential Antidiabetic Drug

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

3'-axial CH2 OH substitution on glucopyranose does not increase glycogen phosphorylase inhibitory potency. QM/MM-PBSA calculations suggest why

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

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

The ammonium sulfate inhibition of human angiogenin

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