“Chromosomal mapping of members of the cdc2 family of protein kinases, cdk3, cdk6, PISSLRE, and PITALRE, and a cdk inhibitor, p27Kip1, to regions involved in human cancer.”. Cancer Res.55 (6): 1199–205. (1995). PMID7882308.
“Phorbol ester inhibits the phosphorylation of the retinoblastoma protein without suppressing cyclin D-associated kinase in vascular smooth muscle cells.”. J. Biol. Chem.271 (14): 8345–51. (1996). doi:10.1074/jbc.271.14.8345. PMID8626531.
“Suppression of apoptosis by dominant negative mutants of cyclin-dependent protein kinases.”. J. Biol. Chem.271 (17): 10205–9. (1996). doi:10.1074/jbc.271.17.10205. PMID8626584.
“Differential effects of cdk2 and cdk3 on the control of pRb and E2F function during G1 exit.”. Genes Dev.10 (7): 851–61. (1996). doi:10.1101/gad.10.7.851. PMID8846921.
“Investigation of the cell cycle regulation of cdk3-associated kinase activity and the role of cdk3 in proliferation and transformation.”. Oncogene17 (17): 2259–69. (1998). doi:10.1038/sj.onc.1202145. PMID9811456.
“ik3-2, a relative to ik3-1/cables, is associated with cdk3, cdk5, and c-abl.”. Biochim. Biophys. Acta1574 (2): 157–63. (2002). doi:10.1016/S0167-4781(01)00367-0. PMID11955625.
“Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules”. Mol. Cell. Proteomics4 (9): 1240–50. (2005). doi:10.1074/mcp.M500089-MCP200. PMID15951569.
“A probability-based approach for high-throughput protein phosphorylation analysis and site localization”. Nat. Biotechnol.24 (10): 1285–92. (2006). doi:10.1038/nbt1240. PMID16964243.