“Autophosphorylation: a salient feature of protein kinases”. Molecular and Cellular Biochemistry127–128: 51–70. (Nov 1993). doi:10.1007/BF01076757. PMID7935362.
“Structure of a c-kit product complex reveals the basis for kinase transactivation”. The Journal of Biological Chemistry278 (34): 31461–4. (Aug 2003). doi:10.1074/jbc.C300186200. PMID12824176.
“Structure-based drug design enables conversion of a DFG-in binding CSF-1R kinase inhibitor to a DFG-out binding mode”. Bioorganic & Medicinal Chemistry Letters20 (5): 1543–7. (Mar 2010). doi:10.1016/j.bmcl.2010.01.078. PMID20137931.
“Classifying protein kinase structures guides use of ligand-selectivity profiles to predict inactive conformations: structure of lck/imatinib complex”. Proteins70 (4): 1451–60. (Mar 2008). doi:10.1002/prot.21633. PMID17910071.
“Structural insights into the autoactivation mechanism of p21-activated protein kinase”. Structure19 (12): 1752–61. (Dec 2011). doi:10.1016/j.str.2011.10.013. PMID22153498.
“Back pocket flexibility provides group II p21-activated kinase (PAK) selectivity for type I 1/2 kinase inhibitors”. Journal of Medicinal Chemistry57 (3): 1033–45. (Feb 2014). doi:10.1021/jm401768t. PMID24432870.
“Structure-Guided Design of Group I Selective p21-Activated Kinase Inhibitors”. Journal of Medicinal Chemistry58 (12): 5121–36. (Jun 2015). doi:10.1021/acs.jmedchem.5b00572. PMID26030457.
“Asymmetric tyrosine kinase arrangements in activation or autophosphorylation of receptor tyrosine kinases”. Molecules and Cells29 (5): 443–8. (May 2010). doi:10.1007/s10059-010-0080-5. PMID20432069.
“Src in cancer: deregulation and consequences for cell behaviour”. Biochimica et Biophysica Acta (BBA) - Reviews on Cancer1602 (2): 114–30. (Jun 2002). doi:10.1016/s0304-419x(02)00040-9. PMID12020799.
“Autophosphorylation: a salient feature of protein kinases”. Molecular and Cellular Biochemistry127–128: 51–70. (Nov 1993). doi:10.1007/BF01076757. PMID7935362.
“Structure of a c-kit product complex reveals the basis for kinase transactivation”. The Journal of Biological Chemistry278 (34): 31461–4. (Aug 2003). doi:10.1074/jbc.C300186200. PMID12824176.
“Structure-based drug design enables conversion of a DFG-in binding CSF-1R kinase inhibitor to a DFG-out binding mode”. Bioorganic & Medicinal Chemistry Letters20 (5): 1543–7. (Mar 2010). doi:10.1016/j.bmcl.2010.01.078. PMID20137931.
“Classifying protein kinase structures guides use of ligand-selectivity profiles to predict inactive conformations: structure of lck/imatinib complex”. Proteins70 (4): 1451–60. (Mar 2008). doi:10.1002/prot.21633. PMID17910071.
“Structural insights into the autoactivation mechanism of p21-activated protein kinase”. Structure19 (12): 1752–61. (Dec 2011). doi:10.1016/j.str.2011.10.013. PMID22153498.
“Back pocket flexibility provides group II p21-activated kinase (PAK) selectivity for type I 1/2 kinase inhibitors”. Journal of Medicinal Chemistry57 (3): 1033–45. (Feb 2014). doi:10.1021/jm401768t. PMID24432870.
“Structure-Guided Design of Group I Selective p21-Activated Kinase Inhibitors”. Journal of Medicinal Chemistry58 (12): 5121–36. (Jun 2015). doi:10.1021/acs.jmedchem.5b00572. PMID26030457.
“Asymmetric tyrosine kinase arrangements in activation or autophosphorylation of receptor tyrosine kinases”. Molecules and Cells29 (5): 443–8. (May 2010). doi:10.1007/s10059-010-0080-5. PMID20432069.
“Src in cancer: deregulation and consequences for cell behaviour”. Biochimica et Biophysica Acta (BBA) - Reviews on Cancer1602 (2): 114–30. (Jun 2002). doi:10.1016/s0304-419x(02)00040-9. PMID12020799.