Crystal structure of cyclin-dependent kinase 2

Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features

Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320

Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose

Ellis, L., Clauser, E., Morgan, D. O., Edery, M., Roth, R. A., & Rutter, W. J. (1986) · Cell · doi:10.1016/0092-8674(86)90786-5 · Cited by 1,070

DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation

Bakkenist, C. J., & Kastan, M. B. (2003) · Nature · doi:10.1038/nature01368 · Cited by 3,466

An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor

Zhang, X., Gureasko, J., Shen, K., Cole, P. A., & Kuriyan, J. (2006) · Cell · doi:10.1016/j.cell.2006.05.013 · Cited by 1,650

Mechanisms of specificity in protein phosphorylation

Ubersax, J. A., & Ferrell Jr, J. E. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2203 · Cited by 1,451

Biochemical and Cellular Effects of Roscovitine, a Potent and Selective Inhibitor of the Cyclin‐Dependent Kinases cdc2, cdk2 and cdk5

Meijer, L., Borgne, A., Mulner, O., Chong, J. P. J., Blow, J. J., Inagaki, N., Inagaki, M., Delcros, J., & Moulinoux, J. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.t01-2-00527.x · Cited by 1,352

Structures of Lung Cancer-Derived EGFR Mutants and Inhibitor Complexes: Mechanism of Activation and Insights into Differential Inhibitor Sensitivity

Yun, C.-H., Boggon, T. J., Li, Y., Woo, M. S., Greulich, H., Meyerson, M., & Eck, M. J. (2007) · Cancer Cell · doi:10.1016/j.ccr.2006.12.017 · Cited by 1,192

Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

Canagarajah, B. J., Khokhlatchev, A., Cobb, M. H., & Goldsmith, E. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80351-7 · Cited by 729

A novel cyclin associates with M015/CDK7 to form the CDK-activating kinase

Fisher, R. P., & Morgan, D. O. (1994) · Cell · doi:10.1016/0092-8674(94)90535-5 · Cited by 655

JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation.

Kallunki, T., Su, B., Tsigelny, I., Sluss, H. K., Dérijard, B., Moore, G., Davis, R., & Karin, M. (1994) · Genes & Development · doi:10.1101/gad.8.24.2996 · Cited by 642

Atomic structure of the MAP kinase ERK2 at 2.3 A resolution

Zhang, F., Strand, A., Robbins, D., Cobb, M. H., & Goldsmith, E. J. (1994) · Nature · doi:10.1038/367704a0 · Cited by 592

Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a

Russo, A. A., Tong, L., Lee, J.-O., Jeffrey, P. D., & Pavletich, N. P. (1998) · Nature · doi:10.1038/26155 · Cited by 524

Chloride sensing by WNK1 involves inhibition of autophosphorylation

Piala, A. T., Moon, T. M., Akella, R., He, H., Cobb, M. H., & Goldsmith, E. J. (2014) · Science Signaling · doi:10.1126/scisignal.2005050 · Cited by 418

Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3

Jura, N., Shan, Y., Cao, X., Shaw, D. E., & Kuriyan, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912101106 · Cited by 338

Crystal Structures of MAP Kinase p38 Complexed to the Docking Sites on Its Nuclear Substrate MEF2A and Activator MKK3b

Chang, C.-I., Xu, B.-E., Akella, R., Cobb, M. H., & Goldsmith, E. J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00525-7 · Cited by 302

Catalytic Control in the EGF Receptor and Its Connection to General Kinase Regulatory Mechanisms

Jura, N., Zhang, X., Endres, N. F., Seeliger, M. A., Schindler, T., & Kuriyan, J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.004 · Cited by 310

The structure of mitogen-activated protein kinase p38 at 2.1-Å resolution

Wang, Z., Harkins, P. C., Ulevitch, R. J., Han, J., Cobb, M. H., & Goldsmith, E. J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.6.2327 · Cited by 275

Structural Basis for the Inhibition of Tyrosine Kinase Activity of ZAP-70

Deindl, S., Kadlecek, T. A., Brdicka, T., Cao, X., Weiss, A., & Kuriyan, J. (2007) · Cell · doi:10.1016/j.cell.2007.03.039 · Cited by 234

Crystal structure of the complex of the cyclin D-dependent kinase Cdk6 bound to the cell-cycle inhibitor p19INK4d

Brotherton, D. H., Dhanaraj, V., Wick, S., Brizuela, L., Domaille, P. J., Volyanik, E., Xu, X., Parisini, E., Smith, B. O., Archer, S. J., et al. (1998) · Nature · doi:10.1038/26164 · Cited by 210

Substrate and Docking Interactions in Serine/Threonine Protein Kinases

Goldsmith, E. J., Akella, R., Min, X., Zhou, T., & Humphreys, J. M. (2007) · Chemical Reviews · doi:10.1021/cr068221w · Cited by 143

The Evolution of the MAP Kinase Pathways: Coduplication of Interacting Proteins Leads to New Signaling Cascades

Caffrey, D. R., O'Neill, L. A. J., & Shields, D. C. (1999) · Journal of Molecular Evolution · doi:10.1007/pl00006578 · Cited by 124

Current perspectives on targeting PIM kinases to overcome mechanisms of drug resistance and immune evasion in cancer

Malone, T., Schäfer, L., Simon, N., Heavey, S., Cuffe, S., Finn, S., Moore, G., & Gately, K. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.107454 · Cited by 33

T160-phosphorylated CDK2 defines threshold for HGF-dependent proliferation in primary hepatocytes

Mueller, S., Huard, J., Waldow, K., Huang, X., D'Alessandro, L. A., Bohl, S., Börner, K., Grimm, D., Klamt, S., Klingmüller, U., et al. (2015) · Molecular Systems Biology · doi:10.15252/msb.20156032 · Cited by 23