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

Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation

Marshall, C. J. (1995) · Cell · doi:10.1016/0092-8674(95)90401-8 · Cited by 3,906

How MAP Kinases Are Regulated

Cobb, M. H., & Goldsmith, E. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.25.14843 · Cited by 1,718

Regulation of transcription by MAP kinase cascades

Treisman, R. (1996) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(96)80067-6 · Cited by 1,296

The MAP kinase cascade is essential for diverse signal transduction pathways

Nishida, E., & Gotoh, Y. (1993) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(93)90019-j · Cited by 1,087

Bmi-1 collaborates with c-Myc in tumorigenesis by inhibiting c-Myc-induced apoptosis via INK4a/ARFPreprint

Jacobs, J. J. L., Scheijen, B., Voncken, J. W., Kieboom, K., Berns, A. J. M., & van Lohuizen, M. (1999) · Genes & Development · doi:10.1101/gad.13.20.2678 · Cited by 1,069

Proteolytic Inactivation of MAP-Kinase-Kinase by Anthrax Lethal Factor

Duesbery, N. S., Webb, C. P., Leppla, S. H., Gordon, V. M., Klimpel, K. R., Copeland, T. D., Ahn, N. G., Oskarsson, M. K., Fukasawa, K., Paull, K. D., et al. (1998) · Science · doi:10.1126/science.280.5364.734 · Cited by 1,007

Mitogen‐activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2

Waskiewicz, A. J., Flynn, A., Proud, C. G., & Cooper, J. A. (1997) · The EMBO Journal · doi:10.1093/emboj/16.8.1909 · Cited by 951

MAPKs: new JNK expands the group

Davis, R. J. (1994) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(94)90132-5 · Cited by 944

Protein kinase cascades activated by stress and inflammatory cytokines

Kyriakis, J. M., & Avruch, J. (1996) · BioEssays · doi:10.1002/bies.950180708 · Cited by 709

Phosphorylation of the MAP Kinase ERK2 Promotes Its Homodimerization and Nuclear Translocation

Khokhlatchev, A. V., Canagarajah, B. J., Wilsbacher, J. L., Robinson, M. J., Atkinson, M. A., Goldsmith, E. J., & Cobb, M. H. (1998) · Cell · doi:10.1016/s0092-8674(00)81189-7 · Cited by 675

Identification, Nomenclature, and Evolutionary Relationships of Mitogen-Activated Protein Kinase (MAPK) Genes in Soybean

Neupane, A., Nepal, M., Piya, S., Subramanian, S., Rohila, J. S., Reese, R. N., & Benson, B. V. (2013) · Evolutionary Bioinformatics · doi:10.4137/ebo.s12526 · Cited by 59

Two Adjacent Docking Sites in the Yeast Hog1 Mitogen-Activated Protein (MAP) Kinase Differentially Interact with the Pbs2 MAP Kinase Kinase and the Ptp2 Protein Tyrosine Phosphatase

Murakami, Y., Tatebayashi, K., & Saito, H. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01817-07 · Cited by 59

A chromatin-bound kinase, ERK8, protects genomic integrity by inhibiting HDM2-mediated degradation of the DNA clamp PCNA

Groehler, A. L., & Lannigan, D. A. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201002124 · Cited by 60

PEA-15 Binding to ERK1/2 MAPKs Is Required for Its Modulation of Integrin Activation

Chou, F.-L., Hill, J. M., Hsieh, J.-C., Pouysségur, J., Brunet, A., Glading, A., Überall, F., Ramos, J. W., Werner, M. H., & Ginsberg, M. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309322200 · Cited by 59

The human Na+/H+ exchanger 1 is a membrane scaffold protein for extracellular signal-regulated kinase 2

Hendus-Altenburger, R., Pedraz‐Cuesta, E., Olesen, C. W., Papaleo, E., Schnell, J. A., Hopper, J. T. S., Robinson, C. V., Pedersen, S. F., & Kragelund, B. B. (2016) · BMC Biology · doi:10.1186/s12915-016-0252-7 · Cited by 59

A Novel Role for MAPKAPK2 in Morphogenesis during Zebrafish Development

Holloway, B. A., Canny, S. G. D. L. T., Ye, Y., Slusarski, D. C., Freisinger, C. M., Dosch, R., Chou, M. M., Wagner, D. S., & Mullins, M. C. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000413 · Cited by 58

Pulsatile and Sustained Gonadotropin-releasing Hormone (GnRH) Receptor Signaling

Armstrong, S. P., Caunt, C. J., Fowkes, R. C., Tsaneva-Atanasova, K. T., & McArdle, C. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.115964 · Cited by 58

The N-Terminal Domain of ERK1 Accounts for the Functional Differences with ERK2

Marchi, M., D'Antoni, A., Formentini, I., Parra, R., Brambilla, R., Ratto, G. M., & Costa, M. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003873 · Cited by 58

Biochemical and Biological Functions of the N-Terminal, Noncatalytic Domain of Extracellular Signal-Regulated Kinase 2

Eblen, S. T., Catling, A. D., Assanah, M. C., & Weber, M. J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.1.249-259.2001 · Cited by 58

Data‐driven modeling reconciles kinetics of ERK phosphorylation, localization, and activity states

Ahmed, S., Grant, K., Edwards, L. E., Rahman, A., Cirit, M., Goshe, M. B., & Haugh, J. M. (2014) · Molecular Systems Biology · doi:10.1002/msb.134708 · Cited by 59

Pulsatile and Sustained Gonadotropin-releasing Hormone (GnRH) Receptor Signaling

Armstrong, S. P., Caunt, C. J., Fowkes, R. C., Tsaneva-Atanasova, K. T., & McArdle, C. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.063917 · Cited by 57

Angiotensin II induces fibronectin expression in human peritoneal mesothelial cells via ERK1/2 and p38 MAPK

Kiribayashi, K., Masaki, T., Naito, T., Ogawa, T., Ito, T., Yorioka, N., & Kohno, N. (2005) · Kidney International · doi:10.1111/j.1523-1755.2005.00179.x · Cited by 57

A Distinct Interaction Mode Revealed by the Crystal Structure of the Kinase p38α with the MAPK Binding Domain of the Phosphatase MKP5

Zhang, Y.-Y., Wu, J.-W., & Wang, Z.-X. (2011) · Science Signaling · doi:10.1126/scisignal.2002241 · Cited by 52

Genome-Wide Survey and Expression Profile Analysis of the Mitogen-Activated Protein Kinase (MAPK) Gene Family in Brassica rapa

Lu, K., Guo, W., Lu, J., Yu, H. Q., Qu, C., Tang, Z., Li, J., Chai, Y., & Liang, Y. (2015) · PLoS ONE · doi:10.1371/journal.pone.0132051 · Cited by 56

Regulation of Two JunD Isoforms by Jun N-terminal Kinases

Yazgan, O., & Pfarr, C. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204552200 · Cited by 56

Mapping ERK2-MKP3 Binding Interfaces by Hydrogen/Deuterium Exchange Mass Spectrometry

Zhou, B., Zhang, J., Liu, S., Reddy, S., Wang, F., & Zhang, Z. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608916200 · Cited by 56

Activation of ERK Induces Phosphorylation of MAPK Phosphatase-7, a JNK Specific Phosphatase, at Ser-446

Masuda, K., Shima, H., Katagiri, C., & Kikuchi, K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213254200 · Cited by 55

The ternary complex factor Net contains two distinct elements that mediate different responses to MAP kinase signalling cascades

Ducret, C., Maira, S.-M., Lutz, Y., & Wasylyk, B. (2000) · Oncogene · doi:10.1038/sj.onc.1203892 · Cited by 55

Transient Protein-Protein Interactions and a Random-ordered Kinetic Mechanism for the Phosphorylation of a Transcription Factor by Extracellular-regulated Protein Kinase 2

Waas, W. F., & Dalby, K. N. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110523200 · Cited by 48

Modularity of MAP kinases allows deformation of their signalling pathways

Mody, A., Weiner, J., & Ramanathan, S. (2009) · Nature Cell Biology · doi:10.1038/ncb1856 · Cited by 54

Mutations in ERK2 Binding Sites Affect Nuclear Entry

Yazicioglu, M. N., Goad, D. L., Ranganathan, A., Whitehurst, A. W., Goldsmith, E. J., & Cobb, M. H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703460200 · Cited by 54

Exploitation of Latent Allostery Enables the Evolution of New Modes of MAP Kinase Regulation

Coyle, S. M., Flores, J. A., & Lim, W. A. (2013) · Cell · doi:10.1016/j.cell.2013.07.019 · Cited by 54

Computational identification and phylogenetic analysis of the MAPK gene family in Oryza sativa

Liu, Q., & Xue, Q. (2007) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2006.12.011 · Cited by 52

Binding of JNK/SAPK to MEKK1 Is Regulated by Phosphorylation

Gallagher, E. D., Xu, S., Moomaw, C. R., Slaughter, C. A., & Cobb, M. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207702200 · Cited by 54

ERK as a Model for Systems Biology of Enzyme Kinetics in Cells

Futran, A. S., Link, A. J., Seger, R., & Shvartsman, S. Y. (2013) · Current Biology · doi:10.1016/j.cub.2013.09.033 · Cited by 53

A Novel Tobacco Mitogen-activated Protein (MAP) Kinase Kinase, NtMEK1, Activates the Cell Cycle-regulated p43Ntf6 MAP Kinase

Calderini, O., Glab, N., Catherine Bergounioux, A., Heberle‐Bors, E., & Wilson, C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010621200 · Cited by 53

Inhibition of MKK7–JNK by the TOR Signaling Pathway Regulator-Like Protein Contributes to Resistance of HCC Cells to TRAIL-Induced Apoptosis

Song, I. S., Jun, S. Y., Na, H., Kim, H., Jung, S. Y., Ha, G., Park, Y., Long, L. Z., Yu, D., Kim, J., et al. (2012) · Gastroenterology · doi:10.1053/j.gastro.2012.07.103 · Cited by 52

Solution Structure of the MAPK Phosphatase PAC-1 Catalytic Domain

Farooq, A., Plotnikova, O. V., Chaturvedi, G., Yan, S. X., Zeng, L., Zhang, Q., & Zhou, M. (2003) · Structure · doi:10.1016/s0969-2126(02)00943-7 · Cited by 52

The molecular mechanisms underlying the ERα-36-mediated signaling in breast cancer

Omarjee, S., Jacquemetton, J., Poulard, C., Rochel, N., Dejaegere, A. P., Chebaro, Y., Treilleux, I., Marangoni, E., Corbo, L., & Romancer, M. L. (2016) · Oncogene · doi:10.1038/onc.2016.415 · Cited by 51

Cellular Complexity in MAPK Signaling in Plants: Questions and Emerging Tools to Answer Them

Krysan, P. J., & Colcombet, J. (2018) · Frontiers in Plant Science · doi:10.3389/fpls.2018.01674 · Cited by 51

A Novel MAP Kinase Gene in Cotton (Gossypium hirsutum L.), GhMAPK, is Involved in Response to Diverse Environmental Stresses

Wang, M., Zhang, Y., Wang, J., Wu, X., & Guo, X. (2007) · BMB Reports · doi:10.5483/bmbrep.2007.40.3.325 · Cited by 51

The β-Arrestin-2 Scaffold Protein Promotes c-Jun N-terminal Kinase-3 Activation by Binding to Its Nonconserved N Terminus

Guo, C., & Whitmarsh, A. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710006200 · Cited by 51

Xp38γ/SAPK3 promotes meiotic G2/M transition in Xenopus oocytes and activates Cdc25C

Perdiguero, E., Pillaire, M., Bodart, J., Hennersdorf, F., Frödin, M., Duesbery, N. S., Alonso, G., & Nebreda, A. R. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg559 · Cited by 51

Cloning and characterisation of p38 MAP kinase from Atlantic salmon

Hansen, T. E., & Jørgensen, J. B. (2007) · Molecular Immunology · doi:10.1016/j.molimm.2007.02.006 · Cited by 51

Allosteric enhancement of MAP kinase p38α's activity and substrate selectivity by docking interactions

Tokunaga, Y., Takeuchi, K., Takahashi, H. K., & Shimada, I. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2861 · Cited by 50

BnaMPK3 Is a Key Regulator of Defense Responses to the Devastating Plant Pathogen Sclerotinia sclerotiorum in Oilseed Rape

Wang, Z., Bao, L.-L., Zhao, F., Tang, M.-Q., Chen, T., Li, Y., Wang, B.-X., Fu, B., Fang, H., Li, G.-Y., et al. (2019) · Frontiers in Plant Science · doi:10.3389/fpls.2019.00091 · Cited by 50

PB1 Domain-Dependent Signaling Complex Is Required for Extracellular Signal-Regulated Kinase 5 Activation

Nakamura, K., Uhlik, M. T., Johnson, N. L., Hahn, K. M., & Johnson, G. L. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.6.2065-2079.2006 · Cited by 50

A New Paradigm for MAPK: Structural Interactions of hERK1 with Mitochondria in HeLa Cells

Galli, S., Jahn, O., Hitt, R., Hesse, D., Opitz, L., Plessmann, U., Urlaub, H., Poderoso, J. J., Jares-Erijman, E. A., & Jovin, T. M. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007541 · Cited by 55

Architecture of the MKK6-p38α complex defines the basis of MAPK specificity and activation

Juyoux, P., Galdadas, I., Gobbo, D., von Velsen, J., Pelosse, M., Tully, M. D., Vadas, O., Gervasio, F. L., Pellegrini, E., & Bowler, M. W. (2023) · Science · doi:10.1126/science.add7859 · Cited by 49

Analyses of the effects of Rck2p mutants on Pbs2pDD-induced toxicity in Saccharomyces cervisiae identify a MAP kinase docking motif, and unexpected functional inactivation due to acidic substitution of T379

Jiang, L., Niu, S., Clines, K. L., Burke, D. J., & Sturgill, T. W. (2004) · Molecular Genetics and Genomics · doi:10.1007/s00438-003-0972-6 · Cited by 49

Progesterone receptors act as sensors for mitogenic protein kinases in breast cancer models

Dressing, G. E., Hagan, C. R., Knutson, T. P., Daniel, A. R., & Lange, C. A. (2009) · Endocrine Related Cancer · doi:10.1677/erc-08-0281 · Cited by 53

Role and regulation of MKP-1 in airway inflammation

Moosavi, S. M. S., Prabhala, P., & Ammit, A. J. (2017) · Respiratory Research · doi:10.1186/s12931-017-0637-3 · Cited by 49

Ancient MAPK ERK7 is regulated by an unusual inhibitory scaffold required for Toxoplasma apical complex biogenesis

Back, P. S., O’Shaughnessy, W. J., Moon, A. S., Dewangan, P. S., Hu, X., Sha, J., Wohlschlegel, J. A., Bradley, P. J., & Reese, M. L. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1921245117 · Cited by 46

The dual-specific protein tyrosine phosphatase family

Alonso, A., Rojas, A. M., Godzik, A., & Mustelin, T. (2003) · Topics in current genetics · doi:10.1007/978-3-540-40035-6_16 · Cited by 49

Analysis of mitogen-activated protein kinase activation and interactions with regulators and substrates

BARDWELL, L., & SHAH, K. (2006) · Methods · doi:10.1016/j.ymeth.2006.06.008 · Cited by 46

Examining Docking Interactions on ERK2 with Modular Peptide Substrates

Lee, S., Warthaka, M., Yan, C., Kaoud, T. S., Ren, P. Y., & Dalby, K. N. (2011) · Biochemistry · doi:10.1021/bi201103b · Cited by 50

A Common Docking Domain in Progesterone Receptor-B links DUSP6 and CK2 signaling to proliferative transcriptional programs in breast cancer cells

Hagan, C. R., Knutson, T. P., & Lange, C. A. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt706 · Cited by 52

Understanding the molecular basis of MK2–p38α signaling complex assembly: insights into protein–protein interaction by molecular dynamics and free energy studies

Yang, Y., Liu, H., & Yao, X. (2012) · Molecular BioSystems · doi:10.1039/c2mb25042j · Cited by 48

p38α MAP Kinase C-Terminal Domain Binding Pocket Characterized by Crystallographic and Computational Analyses

Perry, J. J. P., Harris, R. M., Moiani, D., Olson, A. J., & Tainer, J. A. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.06.005 · Cited by 48

Characterization, expression patterns and functional analysis of the MAPK and MAPKK genes in watermelon (Citrullus lanatus)

Song, Q., Li, D., Dai, Y., Liu, S., Huang, L., Hong, Y., Zhang, H., & Song, F. (2015) · BMC Plant Biology · doi:10.1186/s12870-015-0681-4 · Cited by 48

A Novel Dual Specificity Phosphatase SKRP1 Interacts with the MAPK Kinase MKK7 and Inactivates the JNK MAPK Pathway

Zama, T., Aoki, R., Kamimoto, T., Inoue, K., Ikeda, Y., & Hagiwara, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200837200 · Cited by 48

LmxPK4, a mitogen‐activated protein kinase kinase homologue of Leishmania mexicana with a potential role in parasite differentiation

Kuhn, D., & Wiese, M. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04614.x · Cited by 48

Mapping the binding interface of ERK and transcriptional repressor Capicua using photocrosslinking

Futran, A. S., Kyin, S., Shvartsman, S. Y., & Link, A. J. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1501373112 · Cited by 47

Kinetic models of phosphorylation cycles: A systematic approach using the rapid-equilibrium approximation for protein–protein interactions

Salazar, C., & Höfer, T. (2005) · Biosystems · doi:10.1016/j.biosystems.2005.05.015 · Cited by 45

The roles of extracellular related-kinases 1 and 2 signaling in CNS myelination

Gonsalvez, D. G., Ferner, A. H., Peckham, H., Murray, S. S., & Xiao, J. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.04.024 · Cited by 52

Catalytic Activation of the Plant MAPK Phosphatase NtMKP1 by Its Physiological Substrate Salicylic Acid-induced Protein Kinase but Not by Calmodulins

Katou, S., Karita, E., Yamakawa, H., Seo, S., Mitsuhara, I., Kuchitsu, K., & Ohashi, Y. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508115200 · Cited by 47

Specific phosphorylation and activation of ERK1c by MEK1b: a unique route in the ERK cascadePreprint

Shaul, Y. D., Gibor, G., Plotnikov, A. N., & Seger, R. (2009) · Genes & Development · doi:10.1101/gad.523909 · Cited by 47

GmMKK4 ‐activated GmMPK6 stimulates GmERF113 to trigger resistance to Phytophthora sojae in soybean

Gao, H., Jiang, L., Du, B., Ning, B., Ding, X., Zhang, C., Song, B., Liu, S., Zhao, M., Zhao, Y., et al. (2022) · The Plant Journal · doi:10.1111/tpj.15809 · Cited by 46

MAP kinase phosphatase-1, a gatekeeper of the acute innate immune response

Kirk, S. G., Samavati, L., & Liu, Y. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.117157 · Cited by 47

Molecular characterization of the Salicornia brachiata SbMAPKK gene and its expression by abiotic stress

Agarwal, P. K., Gupta, K., & Jha, B. (2009) · Molecular Biology Reports · doi:10.1007/s11033-009-9774-1 · Cited by 46

Tight control of MEK-ERK activation is essential in regulating proliferation, survival, and cytokine production of CD34+-derived neutrophil progenitors

Geest, C. R., Buitenhuis, M., Koerkamp, M. J. A. G., Holstege, F. C. P., Vellenga, E., & Coffer, P. J. (2009) · Blood · doi:10.1182/blood-2008-08-175141 · Cited by 47

p38α Isoform Mxi2 Binds to Extracellular Signal-Regulated Kinase 1 and 2 Mitogen-Activated Protein Kinase and Regulates Its Nuclear Activity by Sustaining Its Phosphorylation Levels

Sanz‐Moreno, V., Casar, B., & Crespo, P. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.9.3079-3090.2003 · Cited by 45

Recent Advances in Plant MAP Kinase Signalling

Zwerger, K., & Heribert Hirt, A. (2001) · Biological Chemistry · doi:10.1515/bc.2001.142 · Cited by 46

Identification of Extracellular Signal-regulated Kinase 1 (ERK1) Direct Substrates using Stable Isotope Labeled Kinase Assay-Linked Phosphoproteomics

Xue, L., Wang, P., Cao, P., Zhu, J., & Tao, W. A. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o114.038588 · Cited by 46

Properties and Regulation of a Transiently Assembled ERK2·Ets-1 Signaling Complex

Callaway, K., Rainey, M. A., Riggs, A., Abramczyk, O., & Dalby, K. N. (2006) · Biochemistry · doi:10.1021/bi0610451 · Cited by 46

Extracellular Signal-regulated Kinase Activated by Epidermal Growth Factor and Cell Adhesion Interacts with and Phosphorylates Vinexin

Mitsushima, M., Suwa, A., Amachi, T., Ueda, K., & Kioka, N. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402304200 · Cited by 47

Mitogen-activated Protein Kinase Phosphorylates and Targets Inducible cAMP Early Repressor to Ubiquitin-mediated Destruction

Yehia, G., Schlotter, F., Razavi, R., Alessandrini, A., & Molina, C. A. F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105404200 · Cited by 45

Crystal Structure of the Catalytic Domain of Human MAP Kinase Phosphatase 5: Structural Insight into Constitutively Active Phosphatase

Jeong, D. G., Yoon, T., Kim, J., Shim, M. Y., Jung, S., Son, J. H., Ryu, S. E., & Kim, S. J. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.05.059 · Cited by 45

Phosphotyrosine-specific Phosphatase PTP-SL Regulates the ERK5 Signaling Pathway

Buschbeck, M., Eickhoff, J., Sommer, M. N., & Ullrich, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202149200 · Cited by 45

Solution NMR Insights into Docking Interactions Involving Inactive ERK2

Piserchio, A., Warthaka, M., Devkota, A. K., Kaoud, T. S., Lee, S., Abramczyk, O., Ren, P., Dalby, K. N., & Ghose, R. (2011) · Biochemistry · doi:10.1021/bi2000559 · Cited by 41

Titin: central player of hypertrophic signaling and sarcomeric protein quality control

Kötter, S., Andresen, C., & Krüger, M. (2014) · Biological Chemistry · doi:10.1515/hsz-2014-0178 · Cited by 44

Structure–activity relationship (SAR) studies of 3-(2-amino-ethyl)-5-(4-ethoxy-benzylidene)-thiazolidine-2,4-dione: Development of potential substrate-specific ERK1/2 inhibitors

Li, Q., Al‐Ayoubi, A. M., Guo, T.-L., Zheng, H., Sarkar, A., Nguyen, T., Eblen, S. T., Grant, S., Kellogg, G. E., & Zhang, S. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.09.057 · Cited by 44

Docking of PRAK/MK5 to the Atypical MAPKs ERK3 and ERK4 Defines a Novel MAPK Interaction Motif

Åberg, E., Torgersen, K. M., Johansen, B., Keyse, S. M., Perander, M., & Seternes, O. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.023283 · Cited by 43

Characterization of ERK Docking Domain Inhibitors that Induce Apoptosis by Targeting Rsk-1 and Caspase-9

Boston, S. R., Deshmukh, R. R., Strome, S. E., Priyakumar, U. D., MacKerell, A. D., & Shapiro, P. (2011) · BMC Cancer · doi:10.1186/1471-2407-11-7 · Cited by 44

Antagonistic interaction between MAP kinase and protein phosphatase 2C in stress recovery

Leung, J., Orfanidi, S., Chefdor, F., Mészáros, T., Bolte, S., Mizoguchi, T., Shinozaki, K., Giraudat, J., & Bögre, L. (2006) · Plant Science · doi:10.1016/j.plantsci.2006.06.009 · Cited by 43

Retrophosphorylation of Mkk1 and Mkk2 MAPKKs by the Slt2 MAPK in the Yeast Cell Integrity Pathway

Jiménez-Sánchez, M., Cid, V. J., & Molina, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706270200 · Cited by 43

Regulation of glycogen synthase kinase‐3β by products of lipid peroxidation in human neuroblastoma cells

Dozza, B., Smith, M. A., Perry, G. L., Tabaton, M., & Strocchi, P. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02413.x · Cited by 43

Integrating phosphoproteomics in systems biology

Liu, Y., & Chance, M. R. (2014) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2014.07.003 · Cited by 41

The D Domain of LRRC4 anchors ERK1/2 in the cytoplasm and competitively inhibits MEK/ERK activation in glioma cells

Wang, Z., Guo, Q., Wang, R., Xu, G., Li, P., Sun, Y., She, X., Liu, Q., Chen, Q., Yu, Z., et al. (2016) · Journal of Hematology & Oncology · doi:10.1186/s13045-016-0355-1 · Cited by 42

Scaffolding actions of membrane-associated progesterone receptors

Hagan, C. R., Faivre, E. J., & Lange, C. A. (2008) · Steroids · doi:10.1016/j.steroids.2008.12.004 · Cited by 42

Negative Regulation of MAPKK by Phosphorylation of a Conserved Serine Residue Equivalent to Ser212 of MEK1

Gopalbhai, K., Jansen, G., Beauregard, G., Whiteway, M. S., Dumas, F., Wu, C., & Meloche, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211870200 · Cited by 42

Phosphorylation of Mammalian eIF4E by Mnk1 and Mnk2: Tantalizing Prospects for a Role in Translation

Mahalingam, M., & Cooper, J. A. (2001) · Progress in molecular and subcellular biology · doi:10.1007/978-3-662-09889-9_5 · Cited by 41

Mitogen-activated protein kinase (MAPK)-docking sites in MAPK kinases function as tethers that are crucial for MAPK regulation in vivo

Grewal, S., Molina, D. M., & Bardwell, L. (2005) · Cellular Signalling · doi:10.1016/j.cellsig.2005.04.001 · Cited by 41

MK2-Dependent p38b Signalling Protects Drosophila Hindgut Enterocytes against JNK-Induced Apoptosis under Chronic Stress

Seisenbacher, G., Hafen, E., & Stocker, H. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002168 · Cited by 41

Up-Regulation of P-TEFb by the MEK1-Extracellular Signal-Regulated Kinase Signaling Pathway Contributes to Stimulated Transcription Elongation of Immediate Early Genes in Neuroendocrine Cells

Fujita, T., Ryser, S., Piuz, I., & Schlegel, W. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01767-07 · Cited by 41

New Insights into the Catalytic Activation of the MAPK Phosphatase PAC-1 Induced by its Substrate MAPK ERK2 Binding

Zhang, Q., Müller, M., Chen, C. H., Zeng, L., Farooq, A., & Zhou, M. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.10.006 · Cited by 40

Specificity of signaling from MAPKs to MAPKAPKs: Kinases' Tango Nuevo

Gaestel, M. (2008) · Frontiers in bioscience · doi:10.2741/3136 · Cited by 40

p38 MAP Kinase Inhibits Neutrophil Development Through Phosphorylation of C/EBPα on Serine 21

Geest, C. R., Buitenhuis, M., Laarhoven, A. G., Bierings, M., Bruin, M. C. A., Vellenga, E., & Coffer, P. J. (2009) · Stem Cells · doi:10.1002/stem.152 · Cited by 40

Novel Noncatalytic Substrate-Selective p38α-Specific MAPK Inhibitors with Endothelial-Stabilizing and Anti-Inflammatory Activity

Shah, N. G., Tulapurkar, M. E., Ramarathnam, A., Brophy, A., Martinez, R., Hom, K., Hodges, T., Samadani, R., Singh, I. S., MacKerell, A. D., et al. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1602059 · Cited by 40

Evolution of domain combinations in protein kinases and its implications for functional diversity

Deshmukh, K., Anamika, K., & Srinivasan, N. (2009) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2009.12.009 · Cited by 40

Characterization of the p90 Ribosomal S6 Kinase 2 Carboxyl-terminal Domain as a Protein Kinase

Chrestensen, C. A., & Sturgill, T. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202663200 · Cited by 40

Extracellular ATP activates MAP kinase cascades through a P2Y purinergic receptor in the human intestinal Caco-2 cell line

Buzzi, N. S., Bilbao, P., Boland, R., & de Boland, A. R. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.10.005 · Cited by 40

Parasite Mitogen-Activated Protein Kinases as Drug Discovery Targets to Treat Human Protozoan Pathogens

Brumlik, M. J., Pandeswara, S., Ludwig, S. M., Murthy, K., & Curiel, T. J. (2011) · Journal of Signal Transduction · doi:10.1155/2011/971968 · Cited by 41

Activation of AtMPK9 through autophosphorylation that makes it independent of the canonical MAPK cascades

Nagy, S. K., Darula, Z., Kállai, B. M., Bögre, L., Bánhegyi, G., Medzihradszky, K. F., Horváth, G. V., & Mészáros, T. (2015) · Biochemical Journal · doi:10.1042/bj20141176 · Cited by 39

Regulators of the RAS-ERK pathway as therapeutic targets in thyroid cancer

Zaballos, M. A., Acuña-Ruíz, A., Morante, M., Crespo, P., & Santisteban, P. (2019) · Endocrine Related Cancer · doi:10.1530/erc-19-0098 · Cited by 39

Emerging Features of Linear Motif-Binding Hub Proteins

Jespersen, N. E., & Barbar, E. J. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.01.004 · Cited by 40

Identification, evolution and expression analyses of mapk gene family in Japanese flounder (Paralichthys olivaceus) provide insight into its divergent functions on biotic and abiotic stresses response

Qiao, Y., Yan, W., He, J., Liu, X., Zhang, Q., & Wang, X. (2021) · Aquatic Toxicology · doi:10.1016/j.aquatox.2021.106005 · Cited by 39

Identification of a nuclear export signal in MKK6, an activator of the carp p38 mitogen‐activated protein kinases

Hashimoto, H., Fukuda, M., Matsuo, Y., Yokoyama, Y., Nishida, E., Toyohara, H., & Sakaguchi, M. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01479.x · Cited by 39

MAPKs trigger antiviral immunity by directly phosphorylating a rhabdovirus nucleoprotein in plants and insect vectors

Ding, Z., Gao, Q., Tong, X., Xu, W., Ma, L., Zhang, Z., Wang, Y., & Wang, X. (2022) · The Plant Cell · doi:10.1093/plcell/koac143 · Cited by 38

New Docking Motifs in MAPKs

(2000) · Science Signaling · doi:10.1126/scisignal.182000tw5

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