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FragLitesMinimal, Halogenated Fragments Displaying Pharmacophore Doublets. An Efficient Approach to Druggability Assessment and Hit Generation

Journal of medicinal chemistry, 2019-04, Vol.62 (7), p.3741-3752

2019

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Protein Kinase Inhibitors: Insights into Drug Design from Structure

Science (American Association for the Advancement of Science), 2004-03, Vol.303 (5665), p.1800-1805

2004

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Paradoxical activation of the protein kinase-transcription factor ERK5 by ERK5 kinase inhibitors

Nature communications, 2020-03, Vol.11 (1), p.1383-1383, Article 1383

2020

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Cryo-EM structure of SKP1-SKP2-CKS1 in complex with CDK2-cyclin A-p27KIP1

Scientific reports, 2023-07, Vol.13 (1), p.10718-10718, Article 10718

2023

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Crystallographic and electrophilic fragment screening of the SARS-CoV-2 main protease

Nature communications, 2020-10, Vol.11 (1), p.5047-5047, Article 5047

2020

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Isoindolinone Inhibitors of the Murine Double Minute 2 (MDM2)-p53 Protein−Protein Interaction: Structure−Activity Studies Leading to Improved Potency

Journal of medicinal chemistry, 2011-03, Vol.54 (5), p.1233-1243

2011

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The Structural Basis for Control of Eukaryotic Protein Kinases

Annual review of biochemistry, 2012-01, Vol.81 (1), p.587-613

2012

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CDK1 structures reveal conserved and unique features of the essential cell cycle CDK

Nature communications, 2015-04, Vol.6 (1), p.6769-6769, Article 6769

2015

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Cyclin-Dependent Kinase (CDK) Inhibitors: Structure–Activity Relationships and Insights into the CDK‑2 Selectivity of 6‑Substituted 2‑Arylaminopurines

Journal of medicinal chemistry, 2017-03, Vol.60 (5), p.1746-1767

2017

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MDM2-p53 protein–protein interaction inhibitors: A-ring substituted isoindolinones

Bioorganic & medicinal chemistry letters, 2011-10, Vol.21 (19), p.5916-5919

2011

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Structure-Based Design of Potent and Orally Active Isoindolinone Inhibitors of MDM2-p53 Protein–Protein Interaction

Journal of medicinal chemistry, 2021-04, Vol.64 (7), p.4071-4088

2021

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Fragment expansion with NUDELs - poised DNA-encoded libraries

Chemical science (Cambridge), 2023-08, Vol.14 (31), p.8288-8294

2023

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The structure of an MDM2-Nutlin-3a complex solved by the use of a validated MDM2 surface-entropy reduction mutant

Acta crystallographica. Section D, Biological crystallography., 2013-08, Vol.69 (8), p.1358-1366

2013

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How Tyrosine 15 Phosphorylation Inhibits the Activity of Cyclin-dependent Kinase 2-Cyclin A

The Journal of biological chemistry, 2007-02, Vol.282 (5), p.3173-3181

2007

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Specificity Determinants of Recruitment Peptides Bound to Phospho-CDK2/Cyclin A

Biochemistry (Easton), 2002-12, Vol.41 (52), p.15625-15634

2002

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Benzene Probes in Molecular Dynamics Simulations Reveal Novel Binding Sites for Ligand Design

The journal of physical chemistry letters, 2016-09, Vol.7 (17), p.3452-3457

2016

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Searching for Cyclin-Dependent Kinase Inhibitors Using a New Variant of the Cope Elimination

Journal of the American Chemical Society, 2006-05, Vol.128 (18), p.6012-6013

2006

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Expression, purification, characterization and structure of Pseudomonas aeruginosa arylamine N-acetyltransferase

Biochemical journal, 2005-01, Vol.385 (Pt 2), p.605-612

2005

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The CDK9 C-helix Exhibits Conformational Plasticity That May Explain the Selectivity of CAN508

ACS chemical biology, 2012-05, Vol.7 (5), p.811-816

2012

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An Inhibitor’s-Eye View of the ATP-Binding Site of CDKs in Different Regulatory States

ACS chemical biology, 2014-06, Vol.9 (6), p.1251-1256

2014

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The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases

Nature cell biology, 1999-11, Vol.1 (7), p.438-443

1999

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Exiting the tunnel of uncertainty: crystal soak to validated hit

Acta crystallographica. Section D, Biological crystallography., 2022-11, Vol.78 (11), p.1294-1302

2022

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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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Differences in the Conformational Energy Landscape of CDK1 and CDK2 Suggest a Mechanism for Achieving Selective CDK Inhibition

Cell chemical biology, 2019-01, Vol.26 (1), p.121-130.e5

2019

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FragLitesMinimal, Halogenated Fragments Displaying Pharmacophore Doublets. An Efficient Approach to Druggability Assessment and Hit Generation

Protein Kinase Inhibitors: Insights into Drug Design from Structure

Paradoxical activation of the protein kinase-transcription factor ERK5 by ERK5 kinase inhibitors

Cryo-EM structure of SKP1-SKP2-CKS1 in complex with CDK2-cyclin A-p27KIP1

Crystallographic and electrophilic fragment screening of the SARS-CoV-2 main protease

Isoindolinone Inhibitors of the Murine Double Minute 2 (MDM2)-p53 Protein−Protein Interaction: Structure−Activity Studies Leading to Improved Potency

The Structural Basis for Control of Eukaryotic Protein Kinases

CDK1 structures reveal conserved and unique features of the essential cell cycle CDK

Cyclin-Dependent Kinase (CDK) Inhibitors: Structure–Activity Relationships and Insights into the CDK‑2 Selectivity of 6‑Substituted 2‑Arylaminopurines

MDM2-p53 protein–protein interaction inhibitors: A-ring substituted isoindolinones

Structure-Based Design of Potent and Orally Active Isoindolinone Inhibitors of MDM2-p53 Protein–Protein Interaction

Fragment expansion with NUDELs - poised DNA-encoded libraries

The structure of an MDM2-Nutlin-3a complex solved by the use of a validated MDM2 surface-entropy reduction mutant

How Tyrosine 15 Phosphorylation Inhibits the Activity of Cyclin-dependent Kinase 2-Cyclin A

Specificity Determinants of Recruitment Peptides Bound to Phospho-CDK2/Cyclin A

Benzene Probes in Molecular Dynamics Simulations Reveal Novel Binding Sites for Ligand Design

An Alkynylpyrimidine-Based Covalent Inhibitor That Targets a Unique Cysteine in NF-κB-Inducing Kinase

Searching for Cyclin-Dependent Kinase Inhibitors Using a New Variant of the Cope Elimination

Expression, purification, characterization and structure of Pseudomonas aeruginosa arylamine N-acetyltransferase

The CDK9 C-helix Exhibits Conformational Plasticity That May Explain the Selectivity of CAN508

An Inhibitor’s-Eye View of the ATP-Binding Site of CDKs in Different Regulatory States

The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases

Exiting the tunnel of uncertainty: crystal soak to validated hit

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

Differences in the Conformational Energy Landscape of CDK1 and CDK2 Suggest a Mechanism for Achieving Selective CDK Inhibition

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