Campbell McInnes

Peptide inhibitors of CDK2-cyclin A that target the cyclin recruitment-site: structural variants of the C-terminal Phe.

Peptidomimetic design of CDK inhibitors targeting the recruitment site of the cyclin subunit.

Discovery of a novel family of CDK inhibitors with the program LIDAEUS: structural basis for ligand-induced disordering of the activation loop.

Insights into cyclin groove recognition: complex crystal structures and inhibitor design through ligand exchange.

2-Anilino-4-(thiazol-5-yl)pyrimidine CDK inhibitors: synthesis, SAR analysis, X-ray crystallography, and biological activity.

Structural determinants of CDK4 inhibition and design of selective ATP competitive inhibitors.

Cambridge Healthtech Institute fourth annual conference in structure-based drug design.

Synthesis and biological activity of 2-anilino-4-(1H-pyrrol-3-yl) pyrimidine CDK inhibitors.

Design, synthesis, biological activity and structural analysis of cyclic peptide inhibitors targeting the substrate recruitment site of cyclin-dependent kinase complexes.

Structural and biochemical studies of human proliferating cell nuclear antigen complexes provide a rationale for cyclin association and inhibitor design.

Progress in the discovery of polo-like kinase inhibitors.

Strategies for the design of potent and selective kinase inhibitors.

Structure of free MDM2 N-terminal domain reveals conformational adjustments that accompany p53-binding.

PharmaDiscovery 2005. Kinases in drug discovery.

Protein structures in virtual screening: a case study with CDK2.

Differential binding of inhibitors to active and inactive CDK2 provides insights for drug design.

Structure-based discovery and optimization of potential cancer therapeutics targeting the cell cycle.

Improved lead-finding for kinase targets using high-throughput docking.

Catch the kinase conformer.

Inhibitors of Polo-like kinase reveal roles in spindle-pole maintenance.

REPLACE: a strategy for iterative design of cyclin-binding groove inhibitors.

Virtual screening strategies in drug discovery.

Progress in the evaluation of CDK inhibitors as anti-tumor agents.

Functional characterization of the RAD51D E233G genetic variant.

Synthesis and evaluation of novel inhibitors of Pim-1 and Pim-2 protein kinases.

Non-ATP competitive protein kinase inhibitors as anti-tumor therapeutics.

Functional characterization and identification of mouse Rad51d splice variants.

Truncation and optimisation of peptide inhibitors of cyclin-dependent kinase 2-cyclin a through structure-guided design.

Design, synthesis, and evaluation of 2-methyl- and 2-amino-N-aryl-4,5-dihydrothiazolo[4,5-h]quinazolin-8-amines as ring-constrained 2-anilino-4-(thiazol-5-yl)pyrimidine cyclin-dependent kinase inhibitors.

Discovery of N-phenyl-4-(thiazol-5-yl)pyrimidin-2-amine aurora kinase inhibitors.

Structural and functional analysis of cyclin D1 reveals p27 and substrate inhibitor binding requirements.

Discovery and characterization of 2-anilino-4- (thiazol-5-yl)pyrimidine transcriptional CDK inhibitors as anticancer agents.

PLK1 as an oncology target: current status and future potential.

Calpain 10 homology modeling with CYGAK and increased lipophilicity leads to greater potency and efficacy in cells.

Targeting subcellular localization through the polo-box domain: non-ATP competitive inhibitors recapitulate a PLK1 phenotype.

Optimization of non-ATP competitive CDK/cyclin groove inhibitors through REPLACE-mediated fragment assembly.

Structural characterization of the binding interactions of various endogenous estrogen metabolites with human estrogen receptor α and β subtypes: a molecular modeling study.

Fragment based discovery of arginine isosteres through REPLACE: towards non-ATP competitive CDK inhibitors.

Current assessment of polo-like kinases as anti-tumor drug targets.

Quantification of the effects of ionic strength, viscosity, and hydrophobicity on protein-ligand binding affinity.

Iterative conversion of cyclin binding groove peptides into druglike CDK inhibitors with antitumor activity.

Efficient soluble expression of active recombinant human cyclin A2 mediated by E. coli molecular chaperones.