Identification of a Dual Specificity Kinase That Activates the Jun Kinases and p38-Mpk2

Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain.

Hibi, M., Lin, A., Smeal, T., Minden, A., & Karin, M. (1993) · Genes & Development · doi:10.1101/gad.7.11.2135 · Cited by 1,886

Independent Human MAP-Kinase Signal Transduction Pathways Defined by MEK and MKK Isoforms

Dérijard, B., Raingeaud, J., Barrett, T., Wu, I.-H., Han, J., Ulevitch, R. J., & Davis, R. J. (1995) · Science · doi:10.1126/science.7839144 · Cited by 1,555

Oncogenic and transcriptional cooperation with Ha-Ras requires phosphorylation of c-Jun on serines 63 and 73

Smeal, T., Binetruy, B., Mercola, D. A., Birrer, M., & Karin, M. (1991) · Nature · doi:10.1038/354494a0 · Cited by 789

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

Rotation of photoreceptor clusters in the developing drosophila eye requires the nemo gene

Choi, K.-W., & Benzer, S. (1994) · Cell · doi:10.1016/0092-8674(94)90579-7 · Cited by 339

Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways

Whitmarsh, A. J., & Davis, R. J. (1996) · Journal of Molecular Medicine · doi:10.1007/s001090050063 · Cited by 1,543

Mitogen-activated protein kinase cascades and regulation of gene expression

Su, B., & Karin, M. (1996) · Current Opinion in Immunology · doi:10.1016/s0952-7915(96)80131-2 · Cited by 747

Inhibition of JNK activation through NF-κB target genes

Tang, G., Minemoto, Y., Dibling, B., Purcell, N. H., Li, Z., Karin, M., & Lin, A. (2001) · Nature · doi:10.1038/35104568 · Cited by 721

DNA Damaging Agents Induce Expression of Fas Ligand and Subsequent Apoptosis in T Lymphocytes via the Activation of NF-κB and AP-1

Kasibhatla, S., Brunner, T., Genestier, L., Echeverri, F., Mahboubi, A., & Green, D. R. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80054-4 · Cited by 721

Redox Regulation of NF-κB Activation: Distinct Redox Regulation Between the Cytoplasm and the Nucleus

Kabe, Y., Ando, K., Hirao, S., Yoshida, M., & Handa, H. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.395 · Cited by 585

Activation of the nuclear factor-kappaB by Rho, CDC42, and Rac-1 proteins

Perona, R., Montaner, S., Saniger, L., Sánchez-Pérez, I., Bravo, R., & Lacal, J. C. (1997) · Genes & Development · doi:10.1101/gad.11.4.463 · Cited by 519

Glucose or diabetes activates p38 mitogen-activated protein kinase via different pathways

Igarashi, M., Wakasaki, H., Takahara, N., Ishii, H., Jiang, Z.-Y., Yamauchi, T., Kuboki, K., Meier, M., Rhodes, C. J., & King, G. L. (1999) · Journal of Clinical Investigation · doi:10.1172/jci3326 · Cited by 386

Mitogenic signaling via G protein-coupled receptors

van BIESEN, T., LUTTRELL, L. M., HAWES, B. E., & LEFKOWITZ, R. J. (1996) · Endocrine Reviews · doi:10.1210/edrv-17-6-698 · Cited by 361

Ceramide Activates the Stress-activated Protein Kinases

Westwick, J. K., Bielawska, A. E., Dbaibo, G., Hannun, Y. A., & Brenner, D. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.39.22689 · Cited by 303

MEK and the inhibitors: from bench to bedside

Akinleye, A., Furqan, M., Mukhi, N., Ravella, P., & Liu, D. (2013) · Journal of Hematology & Oncology · doi:10.1186/1756-8722-6-27 · Cited by 291

Interaction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3

Kelkar, N., Gupta, S., Dickens, M., & Davis, R. J. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.3.1030-1043.2000 · Cited by 281

JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that functions as a Scaffold factor in the JNK signaling pathway

Ito, M., Yoshioka, K., Akechi, M., Yamashita, S., Takamatsu, N., Sugiyama, K., Hibi, M., Nakabeppu, Y., Shiba, T., & Yamamoto, K.-I. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.11.7539 · 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

MEK kinase 1 is critically required for c-Jun N-terminal kinase activation by proinflammatory stimuli and growth factor-induced cell migration

Xia, Y., Makris, C., Su, B., Li, E., Yang, J., Nemerow, G. R., & Karin, M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.10.5243 · Cited by 238

CD28: a signalling perspective

WARD, S. G. (1996) · Biochemical Journal · doi:10.1042/bj3180361 · Cited by 149

Selectivity of Docking Sites in MAPK Kinases

Bardwell, A. J., Frankson, E., & Bardwell, L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900080200 · Cited by 127

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

The JNKK2-JNK1 fusion protein acts as a constitutively active c-Jun kinase that stimulates c-Jun transcription activity

Zheng, C., Xiang, J., Hunter, T., & Lin, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.41.28966 · Cited by 110

Interaction of the Grb10 Adapter Protein with the Raf1 and MEK1 Kinases

Nantel, A., Mohammad-Ali, K., Sherk, J., Posner, B. I., & Thomas, D. Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.17.10475 · Cited by 108

Transforming Growth Factor-β-induced Osteoblast Elongation Regulates Osteoclastic Bone Resorption through a p38 Mitogen-activated Protein Kinase- and Matrix Metalloproteinase-dependent Pathway

Karsdal, M. A., Fjording, M. S., Foged, N. T., Delaissé, J.-M., & Lochter, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008738200 · Cited by 81

Coordinated Regulation of Radioadaptive Response by Protein Kinase C and p38 Mitogen-Activated Protein Kinase

Shimizu, T., Kato, T., Tachibana, A., & Sasaki, M. S. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4582 · Cited by 73

K-ras Asp12 mutant neither interacts with Raf, nor signals through Erk and is less tumorigenic than K-ras Val12

Cespedes, M. V., Sancho, F. J., Guerrero, S., Parreno, M., Casanova, I., Pavon, M. A., Marcuello, E., Trias, M., Cascante, M., Capella, G., et al. (2006) · Carcinogenesis · doi:10.1093/carcin/bgl063 · Cited by 67

c-Jun N-Terminal Kinase Contributes to Aberrant Retinoid Signaling in Lung Cancer Cells by Phosphorylating and Inducing Proteasomal Degradation of Retinoic Acid Receptor α

Srinivas, H., Juroske, D. M., Kalyankrishna, S., Cody, D. D., Price, R. E., Xu, X.-C., Narayanan, R., Weigel, N. L., & Kurie, J. M. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.3.1054-1069.2005 · Cited by 68

Phosphorylated Protein Kinases Associated with Neuronal and Glial Tau Deposits in Argyrophilic Grain Disease

Ferrer, I., Barrachina, M., Tolnay, M., Rey, M. J., Vidal, N., Carmona, M., Blanco, R., & Puig, B. (2003) · Brain Pathology · doi:10.1111/j.1750-3639.2003.tb00007.x · Cited by 60

Vasoactive intestinal peptide and pituitary adenylate cyclase-activating polypeptide inhibit the MEKK1/MEK4/JNK signaling pathway in endotoxin-activated microglia

Delgado, M. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00283-8 · Cited by 53

Crystal structures of MKK4 kinase domain reveal that substrate peptide binds to an allosteric site and induces an auto-inhibition state

Matsumoto, T., Kinoshita, T., Kirii, Y., Yokota, K., Hamada, K., & Tada, T. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.08.071 · Cited by 49

Induction of erythroid differentiation by inhibition of Ras/ERK pathway in a friend murine leukemia cell line

Matsuzaki, T., Aisaki, K.-I., Yamamura, Y., Noda, M., & Ikawa, Y. (2000) · Oncogene · doi:10.1038/sj.onc.1203461 · Cited by 40

Crystal and solution structures disclose a putative transient state of mitogen-activated protein kinase kinase 4

Matsumoto, T., Kinoshita, T., Kirii, Y., Tada, T., & Yamano, A. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.07.066 · Cited by 15

Acupressure attenuates fibromyalgia central sensitization via MAPK phosphorylation-mediated neuroinflammation regulation

Liu, K., Lin, Y., Rao, T., Huang, Y., Kan, Y., & Liao, J. (2025) · Journal of Orthopaedic Surgery and Research · doi:10.1186/s13018-025-05986-8 · Cited by 11