MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates

Maximal activation of transcription by statl and stat3 requires both tyrosine and serine phosphorylation

Wen, Z., Zhong, Z., & Darnell, J. E. (1995) · Cell · doi:10.1016/0092-8674(95)90311-9 · Cited by 1,974

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

How Proteolysis Drives the Cell Cycle

King, R. W., Deshaies, R. J., Peters, J.-M., & Kirschner, M. W. (1996) · Science · doi:10.1126/science.274.5293.1652 · Cited by 1,273

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

Ras-Mediated Phosphorylation of a Conserved Threonine Residue Enhances the Transactivation Activities of c-Ets1 and c-Ets2

Yang, B.-S., Hauser, C. A., Henkel, G., Colman, M. S., Beveren, C. V., Stacey, K. J., Hume, D. A., Maki, R. A., & Ostrowski, M. C. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.2.538 · Cited by 333

Activation and function of the MAPKs and their substrates, the MAPK-activated protein kinases

Cargnello, M., & Roux, P. P. (2011) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00031-10 · Cited by 3,274

Printing Proteins as Microarrays for High-Throughput Function Determination

MacBeath, G., & Schreiber, S. L. (2000) · Science · doi:10.1126/science.289.5485.1760 · Cited by 2,767

Mitogen-Activated Protein Kinases: Specific Messages from Ubiquitous Messengers

Schaeffer, H. J., & Weber, M. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.4.2435 · Cited by 1,600

The ERK1/2 mitogen-activated protein kinase pathway as a master regulator of the G1- to S-phase transition

Meloche, S., & Pouysségur, J. (2007) · Oncogene · doi:10.1038/sj.onc.1210414 · Cited by 1,091

Translational control of long-lasting synaptic plasticity and memory

Costa-Mattioli, M., Sossin, W. S., Klann, E., & Sonenberg, N. (2009) · Neuron · doi:10.1016/j.neuron.2008.10.055 · Cited by 944

Targeting the translation machinery in cancer

Bhat, M., Robichaud, N., Hulea, L., Sonenberg, N., Pelletier, J., & Topisirovic, I. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4505 · Cited by 799

A conserved docking motif in MAP kinases common to substrates, activators and regulators

Tanoue, T., Adachi, M., Moriguchi, T., & Nishida, E. (2000) · Nature Cell Biology · doi:10.1038/35000065 · Cited by 816

MAPKAP kinase 2 is essential for LPS-induced TNF-α biosynthesis

Kotlyarov, A., Neininger, A., Schubert, C., Eckert, R., Birchmeier, C., Volk, H.-D., & Gaestel, M. (1999) · Nature Cell Biology · doi:10.1038/10061 · Cited by 763

The MAP kinase signaling cascades: a system of hundreds of components regulates a diverse array of physiological functions

Keshet, Y., & Seger, R. (2010) · Methods in Molecular Biology · doi:10.1007/978-1-60761-795-2_1 · Cited by 642

mTOR, translation initiation and cancer

Mamane, Y., Petroulakis, E., LeBacquer, O., & Sonenberg, N. (2006) · Oncogene · doi:10.1038/sj.onc.1209888 · Cited by 607

The ERK Cascade: Distinct Functions within Various Subcellular Organelles

Wortzel, I., & Seger, R. (2011) · Genes & Cancer · doi:10.1177/1947601911407328 · Cited by 563

Signalling to translation: How signal transduction pathways control the protein synthetic machinery

Proud, C. G. (2007) · Biochemical Journal · doi:10.1042/bj20070024 · Cited by 520

Mnk2 and Mnk1 Are Essential for Constitutive and Inducible Phosphorylation of Eukaryotic Initiation Factor 4E but Not for Cell Growth or Development

Ueda, T., Watanabe-Fukunaga, R., Fukuyama, H., Nagata, S., & Fukunaga, R. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.15.6539-6549.2004 · Cited by 507

MAPKAP kinases — MKs — two's company, three's a crowd

Gaestel, M. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1834 · Cited by 413

Functional roles of p38 mitogen-activated protein kinase in macrophage-mediated inflammatory responses

Yang, Y., Kim, S. C., Yu, T., Yi, Y.-S., Rhee, M. H., Sung, G.-H., Yoo, B. C., & Cho, J. Y. (2014) · Mediators of Inflammation · doi:10.1155/2014/352371 · Cited by 406

Identification of eukaryotic mRNAs that are translated at reduced cap binding complex eIF4F concentrations using a cDNA microarray

Johannes, G., Carter, M. S., Eisen, M. B., Brown, P. O., & Sarnow, P. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.23.13118 · Cited by 394

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

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

Identification of an Extracellular Signal-regulated Kinase (ERK) Docking Site in Ribosomal S6 Kinase, a Sequence Critical for Activation by ERK in Vivo

Smith, J. A., Poteet-Smith, C. E., Malarkey, K., & Sturgill, T. W. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.5.2893 · Cited by 283

The inducible kinase IKKi is required for IL-17-dependent signaling associated with neutrophilia and pulmonary inflammation

Bulek, K., Liu, C., Swaidani, S., Wang, L., Page, R. C., Gulen, M. F., Herjan, T., Abbadi, A., Qian, W., Sun, D., et al. (2011) · Nature Immunology · doi:10.1038/ni.2080 · Cited by 192

A MAP kinase docking site is required for phosphorylation and activation of p90rsk/MAPKAP kinase-1

Gavin, A.-C., & Nebreda, A. R. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80120-1 · Cited by 158

Docking interactions in the mitogen-activated protein kinase cascades

Tanoue, T., & Nishida, E. (2002) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(02)00188-2 · Cited by 134

Characterization of Cyclin L2, a Novel Cyclin with an Arginine/Serine-rich Domain

de Graaf, K., Hekerman, P., Spelten, O., Herrmann, A., Packman, L. C., Büssow, K., Müller-Newen, G., & Becker, W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310794200 · Cited by 124

MSK1 and JNKs mediate phosphorylation of STAT3 in UVA-irradiated mouse epidermal JB6 cells

Zhang, Y., Liu, G., & Dong, Z. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106044200 · Cited by 81

BDNF stimulation of protein synthesis in cortical neurons requires the MAP kinase-interacting kinase MNK1

Genheden, M., Kenney, J. W., Johnston, H. E., Manousopoulou, A., Garbis, S. D., & Proud, C. G. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.2641-14.2015 · Cited by 78

The MAP kinase-interacting kinases regulate cell migration, vimentin expression and eIF4E/CYFIP1 binding

Beggs, J. E., Tian, S., Jones, G. G., Xie, J., Iadevaia, V., Jenei, V., Thomas, G., & Proud, C. G. (2015) · Biochemical Journal · doi:10.1042/bj20141066 · Cited by 65

Regulation of Drosophila p38 activation by specific MAP2 kinase and MAP3 kinase in response to different stimuli

Zhuang, Z.-H., Zhou, Y., Yu, M.-C., Silverman, N., & Ge, B.-X. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2005.05.013 · Cited by 45

Creation of a Stress-activated p90 Ribosomal S6 Kinase

Smith, J. A., Poteet-Smith, C. E., Lannigan, D. A., Freed, T. A., Zoltoski, A. J., & Sturgill, T. W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005892200 · Cited by 42