Active and Inactive Protein Kinases: Structural Basis for Regulation

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

Phosphorylation meets ubiquitination: the control of NF-κB activity

Karin, M., & Ben-Neriah, Y. (2000) · Annual Review of Immunology · doi:10.1146/annurev.immunol.18.1.621 · Cited by 4,766

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

Interleukin-6-type cytokine signalling through the gp130/Jak/STAT pathway

HEINRICH, P. C., BEHRMANN, I., MÜLLER-NEWEN, G., SCHAPER, F., & GRAEVE, L. (1998) · Biochemical Journal · doi:10.1042/bj3340297 · Cited by 2,130

Modeling of loops in protein structures

Fiser, A., Do, R. K. G., & Šali, A. (2000) · Protein Science · doi:10.1110/ps.9.9.1753 · Cited by 2,116

The AMP‐Activated Protein Kinase: Fuel Gauge of the Mammalian Cell?

Hardie, D. G., & Carling, D. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00259.x · Cited by 1,317

The nuts and bolts of AGC protein kinases

Pearce, L. R., Komander, D., & Alessi, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2822 · Cited by 1,294

Characterization of the AMP-activated Protein Kinase Kinase from Rat Liver and Identification of Threonine 172 as the Major Site at Which It Phosphorylates AMP-activated Protein Kinase

Hawley, S. A., Davison, M., Woods, A., Davies, S. P., Beri, R. K., Carling, D., & Hardie, D. G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.44.27879 · Cited by 1,264

A renaissance for SRC

Yeatman, T. J. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1366 · Cited by 1,113

MARK, a Novel Family of Protein Kinases That Phosphorylate Microtubule-Associated Proteins and Trigger Microtubule Disruption

Drewes, G., Ebneth, A., Preuss, U., Mandelkow, E.-M., & Mandelkow, E. (1997) · Cell · doi:10.1016/s0092-8674(00)80208-1 · Cited by 878

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

AKT/PKB and Other D3 Phosphoinositide-Regulated Kinases: Kinase Activation by Phosphoinositide-Dependent Phosphorylation

Chan, T. O., Rittenhouse, S. E., & Tsichlis, P. N. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.965 · Cited by 737

Macrophage migration inhibitory factor (MIF) sustains macrophage proinflammatory function by inhibiting p53: Regulatory role in the innate immune response

Mitchell, R. A., Liao, H., Chesney, J., Fingerle-Rowson, G., Baugh, J., David, J., & Bucala, R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.012511599 · Cited by 622

Human p21-activated kinase (Pak1) regulates actin organization in mammalian cells

Sells, M. A., Knaus, U. G., Bagrodia, S., Ambrose, D. M., Bokoch, G. M., & Chernoff, J. (1997) · Current Biology · doi:10.1016/s0960-9822(97)70091-5 · Cited by 603

The Ste20-like kinase Mst2 activates the human large tumor suppressor kinase Lats1

Chan, E. H. Y., Nousiainen, M., Chalamalasetty, R. B., Schäfer, A., Nigg, E. A., & Silljé, H. H. W. (2005) · Oncogene · doi:10.1038/sj.onc.1208445 · Cited by 584

Rho-associated Kinase ROCK Activates LIM-kinase 1 by Phosphorylation at Threonine 508 within the Activation Loop

Ohashi, K., Nagata, K., Maekawa, M., Ishizaki, T., Narumiya, S., & Mizuno, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.5.3577 · Cited by 533

The transforming growth factor-β superfamily of receptors

de Caestecker, M. (2004) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2003.10.004 · Cited by 464

The Mediator complex and transcription regulation

Poss, Z. C., Ebmeier, C. C., & Taatjes, D. J. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.840259 · Cited by 364

Inhibition of Tumor Cell Growth, Invasion, and Metastasis by EXEL-2880 (XL880, GSK1363089), a Novel Inhibitor of HGF and VEGF Receptor Tyrosine Kinases

Qian, F., Engst, S., Yamaguchi, K., Yu, P., Won, K.-A., Mock, L., Lou, T., Tan, J., Li, C., Tam, D., et al. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-4889 · Cited by 350

Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions

BIONDI, R. M., & NEBREDA, A. R. (2003) · Biochemical Journal · doi:10.1042/bj20021641 · Cited by 334

Structure of the CaMKIIδ/Calmodulin Complex Reveals the Molecular Mechanism of CaMKII Kinase Activation

Rellos, P., Pike, A. C. W., Niesen, F. H., Salah, E., Lee, W. H., von Delft, F., & Knapp, S. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000426 · Cited by 279

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

MARKK, a Ste20‐like kinase, activates the polarity‐inducing kinase MARK/PAR‐1

Timm, T., Li, X., Biernat, J., Jiao, J., Mandelkow, E., Vandekerckhove, J., & Mandelkow, E. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg447 · Cited by 198

Additive Effects of PDGF Receptor β Signaling Pathways in Vascular Smooth Muscle Cell Development

Tallquist, M. D., French, W. J., & Soriano, P. (2003) · PLoS Biology · doi:10.1371/journal.pbio.0000052 · Cited by 192

The Selectivity of Receptor Tyrosine Kinase Signaling Is Controlled by a Secondary SH2 Domain Binding Site

Bae, J. H., Lew, E. D., Yuzawa, S., Tomé, F., Lax, I., & Schlessinger, J. (2009) · Cell · doi:10.1016/j.cell.2009.05.028 · Cited by 158

Structural Examination of Autoregulation of Multifunctional Calcium/Calmodulin-dependent Protein Kinase II

Yang, E., & Schulman, H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.37.26199 · Cited by 152

Current trends in biocompatibility testing

Kirkpatrick, C. J., Bittinger, F., Wagner, M., Köhler, H., van Kooten, T. G., Klein, C. L., & Otto, M. (1998) · Proceedings of the Institution of Mechanical Engineers, Part H: Journal of Engineering in Medicine · doi:10.1243/0954411981533845 · Cited by 145

Altered Development of Synapse Structure and Function in Striatum Caused by Parkinson's Disease-Linked LRRK2-G2019S Mutation

Matikainen-Ankney, B. A., Kezunovic, N., Mesias, R. E., Tian, Y., Williams, F. M., Huntley, G. W., & Benson, D. L. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3314-15.2016 · Cited by 139

Mechanistic insight into the dominant mode of the Parkinson's disease-associated G2019S LRRK2 mutation

Luzon-Toro, B., de la Torre, E. R., Delgado, A., Perez-Tur, J., & Hilfiker, S. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm151 · Cited by 122

Molecular mechanism of activation-triggered subunit exchange in Ca2+/calmodulin-dependent protein kinase II

Bhattacharyya, M., Stratton, M. M., Going, C. C., McSpadden, E. D., Huang, Y., Susa, A. C., Elleman, A., Cao, Y. M., Pappireddi, N., Burkhardt, P., et al. (2016) · eLife · doi:10.7554/elife.13405 · Cited by 112

Autophosphorylation Within the Atg1 Activation Loop Is Required for Both Kinase Activity and the Induction of Autophagy in Saccharomyces cerevisiae

Yeh, Y.-Y., Wrasman, K., & Herman, P. K. (2010) · Genetics · doi:10.1534/genetics.110.116566 · Cited by 94

Protein kinases in neurodegenerative diseases: current understandings and implications for drug discovery

Wu, X., Yang, Z., Zou, J., Gao, H., Shao, Z., Li, C., & Lei, P. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02179-x · Cited by 88

Hypothalamic AMP-Activated Protein Kinase Regulates Glucose Production

Yang, C. S., Lam, C. K. L., Chari, M., Cheung, G. W. C., Kokorovic, A., Gao, S., Leclerc, I., Rutter, G. A., & Lam, T. K. T. (2010) · Diabetes · doi:10.2337/db10-0221 · Cited by 86

Towards simple kinetic models of functional dynamics for a kinase subfamily

Sultan, M. M., Kiss, G., & Pande, V. S. (2018) · Nature Chemistry · doi:10.1038/s41557-018-0077-9 · Cited by 68

Catalytically Active MAP KAP Kinase 2 Structures in Complex with Staurosporine and ADP Reveal Differences with the Autoinhibited Enzyme

Underwood, K. W., Parris, K. D., Federico, E., Mosyak, L., Czerwinski, R. M., Shane, T., Taylor, M., Svenson, K., Liu, Y., Hsiao, C.-L., et al. (2003) · Structure · doi:10.1016/s0969-2126(03)00092-3 · Cited by 62

How does activation loop phosphorylation modulate catalytic activity in the cAMP-dependent protein kinase: a theoretical study

Cheng, Y., Zhang, Y., & McCammon, J. A. (2006) · Protein Science · doi:10.1110/ps.051852306 · Cited by 62

Flexible linkers in CaMKII control the balance between activating and inhibitory autophosphorylation

Bhattacharyya, M., Lee, Y. K., Muratcioglu, S., Qiu, B., Nyayapati, P., Schulman, H., Groves, J. T., & Kuriyan, J. (2020) · eLife · doi:10.7554/elife.53670 · Cited by 58

Disruption of Coiled-coil Domains in Fer Protein-tyrosine Kinase Abolishes Trimerization but Not Kinase Activation

Craig, A. W. B., Zirngibl, R., & Greer, P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.28.19934 · Cited by 52

Brassinosteroids Plant counterparts to animal steroid hormones?

Clouse, S. D. (2002) · Vitamins & Hormones · doi:10.1016/s0083-6729(02)65065-4 · Cited by 40

An ire1-phk1 chimera reveals a dispensable role of autokinase activity in endoplasmic reticulum stress response

Mannan, M. A.-U., Shadrick, W. R., Biener, G., Shin, B.-S., Anshu, A., Raicu, V., Frick, D. N., & Dey, M. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.02.036 · Cited by 18

Serum/glucocorticoid regulated kinase 1 (SGK1) in neurological disorders: pain or gain

Howard, P. G., Zou, P., Zhang, Y., Huang, F., Tesic, V., Wu, C. Y.-C., & Lee, R. H.-C. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.114973 · Cited by 13

Molecular requirements for PLK1 activation by T-loop phosphorylation

(2026) · doi:10.1038/s44318-025-00681-0 · Cited by 8

Markovian state models uncover casein kinase 1 dynamics that govern circadian period

Ricci, C. G., Philpott, J. M., Torgrimson, M. R., Freeberg, A. M., Narasimamurthy, R., Pécora de Barros, E., Amaro, R., Virshup, D. M., McCammon, J. A., & Partch, C. L. (2025) · Biophysical Journal · doi:10.1016/j.bpj.2025.09.022 · Cited by 3