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Phosphorylation of the smooth muscle master splicing regulator RBPMS regulates its splicing activity

Barnhart, M. D., Yang, Y. A., Nakagaki-Silva, E. E., Hammond, T. H., Pizzinga, M., Gooding, C., Stott, K. M., & Smith, C. W. J. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac1048 · Cited by 12

Different Domains of the Mitogen-activated Protein Kinases ERK3 and ERK2 Direct Subcellular Localization and Upstream Specificityin Vivo

Robinson, M. J., Xu, B.-E., Stippec, S. A., & Cobb, M. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110935200 · Cited by 14

Meet Me Halfway: When Genomics Meets Structural Bioinformatics

Gong, S., Worth, C. L., Cheng, T. M. K., & Blundell, T. L. (2011) · Journal of Cardiovascular Translational Research · doi:10.1007/s12265-011-9259-1 · Cited by 15

A Growing Family of Dual Specificity Phosphatases with Low Molecular Masses

Aoki, N., Aoyama, K., Nagata, M., & Matsuda, T. (2001) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a002952 · Cited by 14

A subdomain of MEKK1 that is critical for binding to MKK4

Tu, Z., Mooney, S. M., & Lee, F. S. (2003) · Cellular Signalling · doi:10.1016/s0898-6568(02)00056-6 · Cited by 14

Dual-specificity protein phosphatase 1: A potential therapeutic target in cancer

Niture, S. K., Mooers, B. H. M., Wu, D. H., Hart, M., Jaboin, J. J., & Seneviratne, D. S. (2025) · iScience · doi:10.1016/j.isci.2025.113706 · Cited by 14

p38 alpha MAP kinase

Rousseau, S. (2011) · AfCS-Nature Molecule Pages · doi:10.1038/mp.a001717.01 · Cited by 13

Identification and analysis of MAPK cascade gene families of Camellia oleifera and their roles in response to cold stress

Xing, K., Zhang, J., Xie, H., Zhang, L., Zhang, H., Feng, L., Zhou, J., Xiang, X., Zhao, Y., & Rong, J. (2024) · Molecular Biology Reports · doi:10.1007/s11033-024-09551-0 · Cited by 13

Mxi2 sustains ERK1/2 phosphorylation in the nucleus by preventing ERK1/2 binding to phosphatases

Casar, B., Rodríguez, J., Gibor, G., Seger, R., & Crespo, P. (2011) · Biochemical Journal · doi:10.1042/bj20110870 · Cited by 13

Genome-wide identification and expression pattern analysis under abiotic stress of mitogen-activated protein kinase genes in Pyropia yezoensis

Li, C., Kong, F., Sun, P., Bi, G., Li, N., Mao, Y., & Sun, M. (2018) · Journal of Applied Phycology · doi:10.1007/s10811-018-1412-7 · Cited by 13

Toll-like receptor 3-mediated inflammation by p38 is enhanced by endothelial nitric oxide synthase knockdown

Koch, S. R., Choi, H., Mace, E. H., & Stark, R. J. (2019) · Cell Communication and Signaling · doi:10.1186/s12964-019-0345-3 · Cited by 13

Variants of the yeast MAPK Mpk1 are fully functional independently of activation loop phosphorylation

Goshen‐Lago, T., Goldberg-Carp, A., Kadosh, D. M., Darlyuk‐Saadon, I., Bai, C. G., Ahn, N. G., Admon, A., & Engelberg, D. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-03-0167 · Cited by 13

Mnk1 kinase activity is required for abscission

Rannou, Y., Salaün, P., Benaud, C. M., Khan, J., Dutertre, S., Giet, R., & Prigent, C. (2012) · Journal of Cell Science · doi:10.1242/jcs.058081 · Cited by 13

The Drosophila protein kinase LK6 is regulated by ERK and phosphorylates the eukaryotic initiation factor eIF4E in vivo

Parra-Palau, J. L., Scheper, G. C., HARPER, D. E., & Proud, C. G. (2005) · Biochemical Journal · doi:10.1042/bj20040769 · Cited by 13

Isolation and characterization of an oilseed rape MAP kinase BnMPK3 involved in diverse environmental stresses

Yu, S., Zhang, L., Zuo, K., Tang, D., & Tang, K. (2005) · Plant Science · doi:10.1016/j.plantsci.2005.04.005 · Cited by 13

Functional assignment of MAPK phosphatase domains

Nordle, A. K. L., Ríos, P., Gaulton, A., Pulido, R., Attwood, T. K., & Tabernero, L. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21477 · Cited by 13

Identification, structure, and phylogenetic relationships of a mitogen-activated protein kinase homologue from the parasitic protist Entamoeba histolytica

Ray, D., Dutta, S., Banerjee, S., Banerjee, R., & Raha, S. (2005) · Gene · doi:10.1016/j.gene.2004.10.026 · Cited by 13

Using Caenorhabditis elegans as a model organism for evaluating extracellular signal-regulated kinase docking domain inhibitors

Chen, F., MacKerell, A. D., Luo, Y., & Shapiro, P. (2008) · Journal of Cell Communication and Signaling · doi:10.1007/s12079-008-0034-2 · Cited by 12

New Docking Motifs in MAPKs

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Docking sites on mitogen-activated protein kinase (MAPK) kinases, MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzymic activity

BARDWELL, A. J., ABDOLLAHI, M., & BARDWELL, L. (2003) · Biochemical Journal · doi:10.1042/bj20021806 · Cited by 97

Look who’s docking

Lawler, S. E. (1999) · Trends in Cell Biology · doi:10.1016/s0962-8924(99)01530-5

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

Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions

Tanoue, T., Maeda, R., Adachi, M., & Nishida, E. (2001) · The EMBO Journal · doi:10.1093/emboj/20.3.466 · Cited by 285