Differential regulation and properties of MAPKs

Mitogen-Activated Protein Kinase Pathways Mediated by ERK, JNK, and p38 Protein Kinases

Johnson, G. L., & Lapadat, R. (2002) · Science · doi:10.1126/science.1072682 · Cited by 4,295 · see citing works

Mammalian Mitogen-Activated Protein Kinase Signal Transduction Pathways Activated by Stress and Inflammation

Kyriakis, J. M., & Avruch, J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.807 · Cited by 3,369 · see citing works

A central role for JNK in obesity and insulin resistance

Hirosumi, J., Tuncman, G., Chang, L., Görgün, C. Z., Uysal, K. T., Maeda, K., Karin, M., & Hotamisligil, G. S. (2002) · Nature · doi:10.1038/nature01137 · Cited by 3,359 · see citing works

A protein kinase involved in the regulation of inflammatory cytokine biosynthesis

Lee, J. C., Laydon, J. T., McDonnell, P., Gallagher, T. F., Kumar, S., Green, D., McNulty, D. E., Blumenthal, M. J., Keys, J., vatter, S. W. L., et al. (1994) · Nature · doi:10.1038/372739a0 · Cited by 3,266 · see citing works

Protein Tyrosine Phosphatases in the Human Genome

Alonso, A., Sasin, J., Bottini, N., Friedberg, I., Friedberg, I., Osterman, A., Godzik, A., Hunter, T., Dixon, J., & Mustelin, T. (2004) · Cell · doi:10.1016/j.cell.2004.05.018 · Cited by 1,886 · see citing works

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 · see citing works

Signal Transduction through MAP Kinase Cascades

Lewis, T. S., Shapiro, P. S., & Ahn, N. G. (1998) · Advances in cancer research · doi:10.1016/s0065-230x(08)60765-4 · Cited by 1,746 · see citing works

The c-Jun NH2-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser307

Aguirre, V., Uchida, T., Yenush, L., Davis, R., & White, M. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.9047 · Cited by 1,487 · see citing works

The extracellular signal-regulated kinase: Multiple substrates regulate diverse cellular functions

Yoon, S., & Seger, R. (2006) · Growth Factors · doi:10.1080/02699050500284218 · Cited by 1,278 · see citing works

Coordinating ERK/MAPK signalling through scaffolds and inhibitors

Kölch, W. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1743 · Cited by 1,070 · see citing works

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 1,060 · see citing works

Activation and targeting of extracellular signal-regulated kinases by β-arrestin scaffolds

Luttrell, L. M., Roudabush, F. L., Choy, E. W., Miller, W. E., Field, M. E., Pierce, K. L., & Lefkowitz, R. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.041604898 · Cited by 832 · see citing works

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 · see citing works

TNF-α Induction by LPS Is Regulated Posttranscriptionally via a Tpl2/ERK-Dependent Pathway

Dumitru, C. D., Ceci, J. D., Tsatsanis, C., Kontoyiannis, D. L., Stamatakis, K., Lin, J., Patriotis, C., Jenkins, N. A., Copeland, N. G., Kollias, G. A., et al. (2000) · Cell · doi:10.1016/s0092-8674(00)00210-5 · Cited by 801 · see citing works

MAP Kinases

Chen, Z., Gibson, T. B., Robinson, F. L., Silvestro, L., Pearson, G. W., Xu, B.-E., Wright, A., Vanderbilt, C. A., & Cobb, M. H. (2001) · Chemical Reviews · doi:10.1021/cr000241p · Cited by 789 · see citing works

Regulation of MAP Kinase Signaling Modules by Scaffold Proteins in Mammals

Morrison, D. K., & Davis, R. J. (2003) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.19.111401.091942 · Cited by 787 · see citing works

Regulation of Raf-1 by direct feedback phosphorylation.

Dougherty, M., Müller, J., Ritt, D. A., Zhou, M., Zhou, X.-Z., Copeland, T., Conrads, T., Veenstra, T., Lu, K., & Morrison, D. (2005) · Molecules and Cells · doi:10.1016/j.molcel.2004.11.055 · Cited by 663 · see citing works

A Mammalian Scaffold Complex That Selectively Mediates MAP Kinase Activation

Whitmarsh, A. J., Cavanagh, J., Tournier, C., Yasuda, J., & Davis, R. J. (1998) · Science · doi:10.1126/science.281.5383.1671 · Cited by 652 · see citing works

Yersinia YopJ Acetylates and Inhibits Kinase Activation by Blocking Phosphorylation

Mukherjee, S., Keitany, G. J., Li, Y., Wang, Y., Ball, H. L., Goldsmith, E. J., & Orth, K. (2006) · Science · doi:10.1126/science.1126867 · Cited by 615 · see citing works

Dynamic regulation of pro- and anti-inflammatory cytokines by MAPK phosphatase 1 (MKP-1) in innate immune responses

Chi, H., Barry, S. P., Flach, R. J. R., Wu, J. J., Jones, E. A., Bennett, A. M., & Flavell, R. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510965103 · Cited by 568 · see citing works

Selective Activation of p38 Mitogen-activated Protein (MAP) Kinase Isoforms by the MAP Kinase Kinases MKK3 and MKK6

Enslen, H., Raingeaud, J., & Davis, R. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.3.1741 · Cited by 534 · see citing works

Initiation of a G2/M checkpoint after ultraviolet radiation requires p38 kinase

Bulavin, D. V., Higashimoto, Y., Popoff, I., Gaarde, W. A., Basrur, V., Potapova, O., Appella, E., & Fornace, A. J. (2001) · Nature · doi:10.1038/35075107 · Cited by 531 · see citing works

Mechanism of p38 MAP kinase activation in vivoPreprint

Brancho, D., Tanaka, N., Jaeschke, A., Ventura, J., Kelkar, N., Tanaka, Y., Kyuuma, M., Takeshita, T., Flavell, R. A., & Davis, R. J. (2003) · Genes & Development · doi:10.1101/gad.1107303 · Cited by 490 · see citing works

Docking domains and substrate-specificity determination for MAP kinases

Sharrocks, A. D., Yang, S.-H., & Galanis, A. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01627-3 · Cited by 442 · see citing works

Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase

Jacobs, D., Glossip, D., Xing, H., Muslin, A. J., & Kornfeld, K. (1999) · Genes & Development · doi:10.1101/gad.13.2.163 · Cited by 439 · see citing works

MAPKAP Kinase-2 Is a Cell Cycle Checkpoint Kinase that Regulates the G2/M Transition and S Phase Progression in Response to UV Irradiation

Manke, I. A., Nguyen, A., Lim, D., Stewart, M. Q., Elia, A. E. H., & Yaffe, M. B. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.11.021 · Cited by 416 · see citing works

Inhibition of the Mitogen-Activated Protein Kinase Kinase Superfamily by a Yersinia Effector

Orth, K., Palmer, L. E., Bao, Z., Stewart, S., Rudolph, A. E., Bliska, J. B., & Dixon, J. E. (1999) · Science · doi:10.1126/science.285.5435.1920 · Cited by 402 · see citing works

Distinct Roles for JNK1 and JNK2 in Regulating JNK Activity and c-Jun-Dependent Cell Proliferation

Sabapathy, K., Hochedlinger, K., Nam, S. Y., Bauer, A., Karin, M., & Wagner, E. F. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.08.028 · Cited by 397 · see citing works

Rac–MEKK3–MKK3 scaffolding for p38 MAPK activation during hyperosmotic shock

Uhlik, M. T., Abell, A. N., Johnson, N. L., Sun, W., Cuevas, B. D., Lobel-Rice, K. E., Horne, E. A., Dell’Acqua, M. L., & Johnson, G. L. (2003) · Nature Cell Biology · doi:10.1038/ncb1071 · Cited by 378 · see citing works

Cholesterol Depletion of Caveolae Causes Hyperactivation of Extracellular Signal-related Kinase (ERK)

Furuchi, T., & Anderson, R. G. W. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.33.21099 · Cited by 374 · see citing works

Localization of the MP1-MAPK Scaffold Complex to Endosomes Is Mediated by p14 and Required for Signal Transduction

Teis, D., Wunderlich, W., & Huber, L. A. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00364-7 · Cited by 371 · see citing works

Association of mitogen-activated protein kinase with the microtubule cytoskeleton.

Reszka, A. A., Seger, R., Diltz, C. D., Krebs, E. G., & Fischer, E. H. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.19.8881 · Cited by 357 · see citing works

Cyclic AMP activates B-Raf and ERK in cyst epithelial cells from autosomal-dominant polycystic kidneys

Yamaguchi, T., Nagao, S., Wallace, D. P., Belibi, F. A., Cowley, B. D., Pelling, J. C., & Grantham, J. J. (2003) · Kidney International · doi:10.1046/j.1523-1755.2003.00023.x · Cited by 346 · see citing works

Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2

Ben-Levy, R., Hooper, S., Wilson, R., Paterson, H. F., & Marshall, C. J. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70442-7 · Cited by 338 · see citing works

Essential Role of MAPK Phosphatase-1 in the Negative Control of Innate Immune Responses

Salojin, K. V., Owusu, I. B., Millerchip, K. A., Potter, M. D., Platt, K. A., & Oravecz, T. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.3.1899 · Cited by 333 · see citing works

The PHD Domain of MEKK1 Acts as an E3 Ubiquitin Ligase and Mediates Ubiquitination and Degradation of ERK1/2

Lu, Z., Xu, S., Joazeiro, C. A. P., Cobb, M. H., & Hunter, T. R. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00519-1 · Cited by 323 · see citing works

NMDA-mediated activation of the tyrosine phosphatase STEP regulates the duration of ERK signaling

Paul, S., Nairn, A. C., Wang, P., & Lombroso, P. J. (2002) · Nature Neuroscience · doi:10.1038/nn989 · Cited by 314 · see citing works

PEA-15 Mediates Cytoplasmic Sequestration of ERK MAP Kinase

Formstecher, É., Ramos, J. W., Fauquet, M., Calderwood, D., Hsieh, J.-C., Canton, B., Nguyen, X.-T., Barnier, J., Camonis, J., Ginsberg, M. H., et al. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00035-1 · Cited by 313 · see citing works

Crystal Structures of MAP Kinase p38 Complexed to the Docking Sites on Its Nuclear Substrate MEF2A and Activator MKK3b

Chang, C.-I., Xu, B.-E., Akella, R., Cobb, M. H., & Goldsmith, E. J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00525-7 · Cited by 302 · see citing works

Activation of MEK‐1 and SEK‐1 by Tpl‐2 proto‐oncoprotein, a novel MAP kinase kinase kinase.

Salmerón, A., Ahmad, T. B., Carlile, G. W., Pappin, D., Narsimhan, R. P., & Ley, S. C. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00417.x · Cited by 300 · see citing works

Sef is a spatial regulator for Ras/MAP kinase signaling.

Torii, S., Kusakabe, M., Yamamoto, T., Maekawa, M., & Nishida, E. (2004) · Developmental Cell · doi:10.1016/j.devcel.2004.05.019 · Cited by 292 · see citing works

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 · see citing works

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 · cited 4× · see citing works

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 · see citing works

Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125

Heo, Y., Kim, S., Seo, C. I., Kim, Y. K., Sung, B., Lee, H. S., Lee, J. I., Park, S., Kim, J. H., Hwang, K. Y., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600212 · Cited by 275 · cited 1× · see citing works

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 · see citing works

Crystal Structure of p38 Mitogen-activated Protein Kinase

Wilson, K. P., Fitzgibbon, M. J., Caron, P. R., Griffith, J. P., Chen, W., McCaffrey, P. G., Chambers, S. P., & Su, M. S. S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.44.27696 · Cited by 262 · see citing works

Involvement of the MKK6-p38γ Cascade in γ-Radiation-Induced Cell Cycle Arrest

Wang, X., McGowan, C. H., Zhao, M. F., He, L., Downey, J. S., Fearns, C., Wang, Y., Huang, S., & Han, J. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.13.4543-4552.2000 · Cited by 247 · see citing works

Paxillin Serves as an ERK-Regulated Scaffold for Coordinating FAK and Rac Activation in Epithelial Morphogenesis

Ishibe, S., Joly, D., Liu, Z., & Cantley, L. G. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.006 · Cited by 241 · see citing works

The Ste5p scaffold

Elion, E. A. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.22.3967 · Cited by 226 · see citing works

B56‐containing PP2A dephosphorylate ERK and their activity is controlled by the early gene IEX‐1 and ERK

Letourneux, C., Rocher, G., & Porteu, F. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7600980 · Cited by 224 · see citing works

Nuclear Export of Map Kinase (ERK) Involves a Map Kinase Kinase (Mek-Dependent) Active Transport Mechanism

Adachi, M., Fukuda, M., & Nishida, E. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.5.849 · Cited by 218 · see citing works

IQGAP1 Binds Rap1 and Modulates Its Activity

Jeong, H., Li, Z., Brown, M. P., & Sacks, D. B. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700487200 · Cited by 218 · see citing works

Mice lacking MAP kinase phosphatase-1 have enhanced MAP kinase activity and resistance to diet-induced obesity

Wu, J., Flach, R. J. R., Anderson, E. J., Hong, E., Lee, M., Choi, C. S., Neufer, P. D., Shulman, G. I., Kim, J. K., & Bennett, A. M. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.05.010 · Cited by 212 · see citing works

A new Rac target POSH is an SH3‐containing scaffold protein involved in the JNK and NF‐κB signalling pathways

Tapon, N., Nagata, K., Lamarche, N., & Hall, A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.5.1395 · Cited by 207 · see citing works

IQGAP1 Binds ERK2 and Modulates Its Activity

Roy, M., Li, Z., & Sacks, D. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308405200 · Cited by 206 · see citing works

JNKK1 organizes a MAP kinase module through specific and sequential interactions with upstream and downstream components mediated by its amino-terminal extensionPreprint

Xia, Y., Wu, Z., Su, B., Murray, B. W., & Karin, M. (1998) · Genes & Development · doi:10.1101/gad.12.21.3369 · Cited by 203 · see citing works

Synergistic activation of SAPK1/JNK1 by two MAP kinase kinases in vitro

Lawler, S. E., Fleming, Y., Goedert, M., & Cohen, P. (1998) · Current Biology · doi:10.1016/s0960-9822(98)00019-0 · Cited by 202 · see citing works

The Activation State of p38 Mitogen-Activated Protein Kinase Determines the Efficiency of ATP Competition for Pyridinylimidazole Inhibitor Binding

Frantz, B., Klatt, T., Pang, M., Parsons, J. N., Rolando, A. M., Williams, H. R., Tocci, M. J., O'Keef, S. J., & O’Neill, E. A. (1998) · Biochemistry · doi:10.1021/bi980832y · Cited by 200 · see citing works

Interaction of Rac exchange factors Tiam1 and Ras-GRF1 with a scaffold for the p38 mitogen-activated protein kinase cascade

Buchsbaum, R. J., Connolly, B. A., & Feig, L. A. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.12.4073-4085.2002 · Cited by 198 · see citing works

Multiple Mitogen-Activated Protein Kinase Signaling Pathways Connect the Cot Oncoprotein to the c- jun Promoter and to Cellular Transformation

Chiariello, M., Marinissen, M. J., & Gutkind, J. S. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.5.1747-1758.2000 · Cited by 195 · see citing works

SEK1 deficiency reveals mitogen-activated protein kinase cascade crossregulation and leads to abnormal hepatogenesis

Ganiatsas, S., Kwee, L., Fujiwara, Y., Perkins, A. C., Ikeda, T., Labow, M., & Zon, L. I. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.12.6881 · Cited by 193 · see citing works

POSH acts as a scaffold for a multiprotein complex that mediates JNK activation in apoptosis

Xu, Z., Kukekov, N. V., & Greene, L. A. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg021 · Cited by 190 · see citing works

EPAS1 trans-activation during hypoxia requires p42/p44 MAPK

Conrad, P. W., Freeman, T. L., Beitner-Johnson, D., & Millhorn, D. E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.47.33709 · Cited by 178 · see citing works

The MKK7 Gene Encodes a Group of c-Jun NH 2 -Terminal Kinase Kinases

Tournier, C., Whitmarsh, A. J., Cavanagh, J., Barrett, T., & Davis, R. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.2.1569 · Cited by 173 · see citing works

Role of the JIP4 Scaffold Protein in the Regulation of Mitogen-Activated Protein Kinase Signaling Pathways

Kelkar, N., Standen, C. L., & Davis, R. J. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.7.2733-2743.2005 · Cited by 171 · see citing works

Regulation of gene expression by the small GTPase Rho through the ERK6 (p38γ) MAP kinase pathwayPreprint

Marinissen, M. J., Chiariello, M., & Gutkind, J. S. (2001) · Genes & Development · doi:10.1101/gad.855801 · Cited by 167 · see citing works

Stress-induced Inhibition of ERK1 and ERK2 by Direct Interaction with p38 MAP Kinase

Zhang, H., Shi, X., Hampong, M., Blanis, L., & Pelech, S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c000917200 · Cited by 166 · see citing works

Docking Interactions Induce Exposure of Activation Loop in the MAP Kinase ERK2

Zhou, T., Sun, L., Humphreys, J., & Goldsmith, E. J. (2006) · Structure · doi:10.1016/j.str.2006.04.006 · Cited by 164 · see citing works

Conserved Docking Site Is Essential for Activation of Mammalian MAP Kinase Kinases by Specific MAP Kinase Kinase Kinases

Takekawa, M., Tatebayashi, K., & Saito, H. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.001 · Cited by 155 · see citing works

Protein phosphatase 5 in signal transduction

Chinkers, M. (2001) · Trends in Endocrinology and Metabolism · doi:10.1016/s1043-2760(00)00335-0 · Cited by 151 · see citing works

Mxi2, a mitogen-activated protein kinase that recognizes and phosphorylates Max protein.

Zervos, A. S., Faccio, L., Gatto, J., Kyriakis, J. M., & Brent, R. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.23.10531 · Cited by 150 · see citing works

Identification of a Cytoplasmic-Retention Sequence in ERK2

Rubinfeld, H., Hanoch, T., & Seger, R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.43.30349 · Cited by 147 · see citing works

Evidence for Existence of a Nuclear Pore Complex-mediated, Cytosol-independent Pathway of Nuclear Translocation of ERK MAP Kinase in Permeabilized Cells

Matsubayashi, Y., Fukuda, M., & Nishida, E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106012200 · Cited by 144 · see citing works

APLIP1, a Kinesin Binding JIP-1/JNK Scaffold Protein, Influences the Axonal Transport of Both Vesicles and Mitochondria in Drosophila

Horiuchi, D., Barkus, R. V., Pilling, A. D., Gassman, A., & Saxton, W. M. (2005) · Current Biology · doi:10.1016/j.cub.2005.10.047 · Cited by 141 · see citing works

JLP: A scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors

Lee, C. M., Onésime, D., Reddy, C. D., Dhanasekaran, N., & Reddy, E. P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.232310199 · Cited by 139 · see citing works

IB1, a JIP-1-related Nuclear Protein Present in Insulin-secreting Cells

Bonny, C., NICOD, P. H., & Waeber, G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.4.1843 · Cited by 139 · see citing works

ERK2 enters the nucleus by a carrier-independent mechanism

Whitehurst, A. W., Wilsbacher, J. L., You, Y., Luby‐Phelps, K., Moore, M. S., & Cobb, M. H. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.112495999 · Cited by 139 · see citing works

Tpl2/Cot Signals Activate ERK, JNK, and NF-κB in a Cell-type and Stimulus-specific Manner

Das, S., Cho, J., Lambertz, I., Kelliher, M. A., Eliopoulos, A. G., Du, K., & Tsichlis, P. N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412837200 · Cited by 138 · see citing works

Axin Forms a Complex with MEKK1 and Activates c-Jun NH2-terminal Kinase/Stress-activated Protein Kinase through Domains Distinct from Wnt Signaling

Zhang, Y., Neo, S. Y., Wang, X., Han, J., & Lin, S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.49.35247 · Cited by 132 · see citing works

Extracellular signals and scores of phosphatases: All roads lead to MAP kinase

Saxena, M., & Mustelin, T. (2000) · Seminars in Immunology · doi:10.1006/smim.2000.0219 · Cited by 128 · see citing works

Regulation of ERK1 and ERK2 by Glucose and Peptide Hormones in Pancreatic β Cells

Arnette, D., Gibson, T. B., Lawrence, M. C., January, B., Khoo, S., McGlynn, K., Vanderbilt, C. A., & Cobb, M. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301174200 · Cited by 126 · see citing works

Mitotic Phosphorylation of Golgi Reassembly Stacking Protein 55 by Mitogen-activated Protein Kinase ERK2

Jesch, S. A., Lewis, T. S., Ahn, N. G., & Linstedt, A. D. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.6.1811 · Cited by 115 · see citing works

MEKK1 Binds Directly to the c-Jun N-terminal Kinases/Stress-activated Protein Kinases

Xu, S., & Cobb, M. H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.51.32056 · Cited by 112 · see citing works

Fibroblast Growth Factor Homologous Factors and the Islet Brain-2 Scaffold Protein Regulate Activation of a Stress-activated Protein Kinase*

Schoorlemmer, J., & Goldfarb, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205520200 · Cited by 108 · see citing works

Murine p38-δ Mitogen-activated Protein Kinase, a Developmentally Regulated Protein Kinase That Is Activated by Stress and Proinflammatory Cytokines

Hu, M. C. ‐., Wang, Y., Mikhail, A. A., Qiu, W. R., & Tan, T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.11.7095 · Cited by 99 · see citing works

Identification of Novel Point Mutations in ERK2 That Selectively Disrupt Binding to MEK1

Robinson, F. L., Whitehurst, A. W., Raman, M., & Cobb, M. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107776200 · Cited by 99 · see citing works

Ubiquitylation of MEKK1 Inhibits Its Phosphorylation of MKK1 and MKK4 and Activation of the ERK1/2 and JNK Pathways

Witowsky, J. A., & Johnson, G. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200616200 · Cited by 95 · see citing works

ERK1c regulates Golgi fragmentation during mitosis

Shaul, Y. D., & Seger, R. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200509063 · Cited by 95 · see citing works

A Bipartite Mechanism for ERK2 Recognition by Its Cognate Regulators and Substrates

Zhang, J., Zhou, B., Zheng, C.-F., & Zhang, Z. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303909200 · Cited by 92 · see citing works

Novel Protein Kinase C Isoforms Regulate Human Keratinocyte Differentiation by Activating a p38δ Mitogen-activated Protein Kinase Cascade That Targets CCAAT/Enhancer-binding Protein α

Efimova, T., Deucher, A., Kuroki, T., Ohba, M., & Eckert, R. L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205098200 · Cited by 88 · see citing works

TAB-1 Modulates Intracellular Localization of p38 MAP Kinase and Downstream Signaling

Lü, G., Kang, Y. J., Han, J., Herschman, H. R., Stefani, E., & Wang, Y. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507610200 · Cited by 83 · see citing works

The Death Effector Domain Protein PEA-15 Prevents Nuclear Entry of ERK2 by Inhibiting Required Interactions

Whitehurst, A. W., Robinson, F. L., Moore, M. S., & Cobb, M. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310031200 · Cited by 81 · see citing works

Feedback control of MKP-1 expression by p38

Hu, J., Chen, T., Zhuang, Z., Kong, L., Yu, M., Liu, Y., Zang, J., & Ge, B. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.07.010 · Cited by 81 · see citing works

Both Binding and Activation of p38 Mitogen-Activated Protein Kinase (MAPK) Play Essential Roles in Regulation of the Nucleocytoplasmic Distribution of MAPK-Activated Protein Kinase 5 by Cellular Stress

Seternes, O. M., Johansen, B., Hegge, B., Johannessen, M., Keyse, S. M., & Moens, U. L. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.20.6931-6945.2002 · Cited by 78 · see citing works

Specificity Determinants in MAPK Signaling to Transcription Factors

Baršytė-Lovejoy, D., Galanis, Α., & Sharrocks, A. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108145200 · Cited by 77 · see citing works

Axin Utilizes Distinct Regions for Competitive MEKK1 and MEKK4 Binding and JNK Activation

Luo, W., Ng, W. W., Jin, L., Ye, Z., Han, J., & Lin, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305277200 · Cited by 75 · see citing works

Identification of Stathmin as a Novel Substrate for p38 Delta

Parker, C. G., Hunt, J. B., Diener, K., McGinley, M., Soriano, B., Keesler, G. A., Bray, J., Yao, Z., Wang, X. S., Kohno, T., et al. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9250 · Cited by 70 · see citing works

Phosphorylation at Thr-290 regulates Tpl2 binding to NF-κB1/p105 and Tpl2 activation and degradation by lipopolysaccharide

Cho, J., & Tsichlis, P. N. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409856102 · Cited by 63 · see citing works

Cell adhesion differentially regulates the nucleocytoplasmic distribution of active MAP kinases

Aplin, A. E., Hogan, B. P., Tomeu, J., & Juliano, R. L. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.13.2781 · Cited by 61 · see citing works

c-Jun-NH2 Kinase (JNK) Contributes to the Regulation of c-Myc Protein Stability

Alarcon-Vargas, D., & Ronai, Z. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312054200 · Cited by 59 · see citing works

Cardiac Expression and Subcellular Localization of the p38 Mitogen-activated Protein Kinase Member, Stress-activated Protein Kinase-3 (SAPK3)

Court, N. W., dos Remedios, C. G., Cordell, J., & Bogoyevitch, M. A. (2002) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.2001.1523 · Cited by 59 · see citing works

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 · see citing works

BuCy RAFs drive cells into MEK addiction

Rapp, U. R., Götz, R., & Albert, S. (2006) · Cancer Cell · doi:10.1016/j.ccr.2005.12.022 · Cited by 52 · see citing works

Protein Phosphatase 4 Is a Positive Regulator of Hematopoietic Progenitor Kinase 1

Zhou, G., Boomer, J. S., & Tan, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410317200 · Cited by 46 · see citing works

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 · see citing works

POSH, a scaffold protein for JNK signaling, binds to ALG‐2 and ALIX in Drosophila

Tsuda, M., Seong, K., & Aigaki, T. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.05.005 · Cited by 43 · see citing works

The Nuclear Localization of ERK2 Occurs by Mechanisms Both Independent of and Dependent on Energy

Ranganathan, A., Yazicioglu, M. N., & Cobb, M. H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513866200 · Cited by 43 · see citing works

Cyclic AMP Selectively Uncouples Mitogen-Activated Protein Kinase Cascades from Activating Signals

Pearson, G. W., Earnest, S. A., & Cobb, M. H. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.8.3039-3047.2006 · Cited by 41 · see citing works

Hypoxia Differentially Regulates the Mitogen- and Stress-Activated Protein Kinases

Conrad, P., Millhorn, D. E., & Beitner‐Johnson, D. (2002) · Advances in experimental medicine and biology · doi:10.1007/0-306-46825-5_28 · Cited by 40 · see citing works

MEKK1 regulates the AP-1 dimer repertoire via control of JunB transcription and Fra-2 protein stability

Cuevas, B. D., Uhlik, M. T., Garrington, T. P., & Johnson, G. L. (2004) · Oncogene · doi:10.1038/sj.onc.1208239 · Cited by 40 · see citing works

Phosphorylation of NF-κB1/p105 by oncoprotein kinase Tpl2: Implications for a novel mechanism of Tpl2 regulation

Babu, G. R., Jin, W., Norman, L. P., Waterfield, M. R., Chang, M., Wu, X., Zhang, M., & Sun, S. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2005.12.010 · Cited by 32 · see citing works

JNK-Interacting Leucine Zipper Protein Is a Novel Scaffolding Protein in the Gα13 Signaling Pathway

Kashef, K., Lee, C. M., Ha, J. H., Reddy, E. P., & Dhanasekaran, D. N. (2005) · Biochemistry · doi:10.1021/bi050604l · Cited by 31 · see citing works

Mxi2, a splice variant of p38 stress-activated kinase, is a distal nephron protein regulated with kidney ischemia

Faccio, L., Chen, A., Fusco, C., Martinotti, S., Bonventre, J. V., & Zervos, A. S. (2000) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2000.278.4.c781 · Cited by 28 · see citing works

Exip, a New Alternative Splicing Variant of p38α, Can Induce an Earlier Onset of Apoptosis in HeLa Cells

SUDO, T., Yagasaki, Y., Hama, H., Watanabe, N., & Osada, H. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2002.6529 · Cited by 27 · see citing works

Distinct carboxy‐termini confer divergent characteristics to the mitogen‐activated protein kinase p38α and its splice isoform Mxi2

Sanz, V., Arozarena, I., & Crespo, P. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01598-2 · Cited by 26 · see citing works

Paxillin Regulates Steroid-triggered Meiotic Resumption in Oocytes by Enhancing an All-or-None Positive Feedback Kinase Loop

Rasar, M., DeFranco, D. B., & Hammes, S. R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608959200 · Cited by 21 · see citing works

Exip, a splicing variant of p38α, participates in interleukin‐1 receptor proximal complex and downregulates NF‐κB pathway

Yagasaki, Y., SUDO, T., & Osada, H. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.08.050 · Cited by 19 · see citing works

Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling

Ray, P. D., Huang, B.-W., & Tsuji, Y. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.01.008 · Cited by 4,373 · see citing works

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 · see citing works

ERK1/2 MAP kinases: Structure, function, and regulation

Roskoski, R. J. (2012) · Pharmacological Research · doi:10.1016/j.phrs.2012.04.005 · Cited by 1,642 · see citing works

Oxidative stress: the mitochondria-dependent and mitochondria-independent pathways of apoptosis

Sinha, K., Das, J., Pal, P. B., & Sil, P. C. (2013) · Archives of Toxicology · doi:10.1007/s00204-013-1034-4 · Cited by 1,622 · see citing works

JNK signaling in apoptosis

Dhanasekaran, D. N., & Reddy, E. P. (2008) · Oncogene · doi:10.1038/onc.2008.301 · Cited by 1,529 · see citing works

Mammalian MAPK Signal Transduction Pathways Activated by Stress and Inflammation: A 10-Year Update

Kyriakis, J. M., & Avruch, J. (2012) · Physiological Reviews · doi:10.1152/physrev.00028.2011 · Cited by 1,476 · see citing works

Multiple functions of p21 in cell cycle, apoptosis and transcriptional regulation after DNA damage.

Karimian, A., Ahmadi, Y., & Yousefi, B. (2016) · DNA Repair · doi:10.1016/j.dnarep.2016.04.008 · Cited by 1,110 · see citing works

Molecular mechanisms of opioid receptor-dependent signaling and behavior

Al-Hasani, R., & Bruchas, M. R. (2011) · Anesthesiology · doi:10.1097/aln.0b013e318238bba6 · Cited by 1,067 · see citing works

The MAPK cascades: Signaling components, nuclear roles and mechanisms of nuclear translocation

Plotnikov, A. N., Zehorai, E., Procaccia, S., & Seger, R. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.12.012 · Cited by 990 · see citing works

Targeting the RAS/RAF/MAPK pathway for cancer therapy: from mechanism to clinical studies

Bahar, M. E., Kim, H. J., & Kim, D. R. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01705-z · Cited by 888 · see citing works

MAP Kinase PathwaysPreprint

Morrison, D. K. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011254 · Cited by 846 · see citing works

Phosphatase‐mediated crosstalk between MAPK signaling pathways in the regulation of cell survival

Junttila, M. R., Li, S., & Westermarck, J. (2008) · The FASEB Journal · doi:10.1096/fj.06-7859rev · Cited by 826 · see citing works

Mitogen-Activated Protein Kinase Signaling in the Heart: Angels Versus Demons in a Heart-Breaking Tale

Rose, B. A., Force, T. L., & Wang, Y. (2010) · Physiological Reviews · doi:10.1152/physrev.00054.2009 · Cited by 720 · see citing works

p38MAPK: stress responses from molecular mechanisms to therapeutics

Coulthard, L. R., White, D. E., Jones, D. L., McDermott, M. F., & Burchill, S. A. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.06.005 · Cited by 691 · see citing works

Cutaneous melanoma: From pathogenesis to therapy (Review)

Leonardi, G. C., Falzone, L., Salemi, R., Zanghì, A., Spandidos, D. A., McCubrey, J. A., Candido, S., & Libra, M. (2018) · International Journal of Oncology · doi:10.3892/ijo.2018.4287 · Cited by 594 · see citing works

Dual‐specificity MAP kinase phosphatases (MKPs): Shaping the outcome of MAP kinase signalling

Caunt, C. J., & Keyse, S. M. (2013) · The FEBS Journal · doi:10.1111/j.1742-4658.2012.08716.x · Cited by 535 · see citing works

Mitogen-Activated Protein (MAP) Kinase/MAP Kinase Phosphatase Regulation: Roles in Cell Growth, Death, and Cancer

Boutros, T., Chevet, É., & Metrakos, P. P. (2008) · Pharmacological Reviews · doi:10.1124/pr.107.00106 · Cited by 545 · see citing works

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 · see citing works

Endogenous and Exogenous Opioids in Pain

Corder, G. F., Castro, D. C., Bruchas, M. R., & Scherrer, G. (2018) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-080317-061522 · Cited by 511 · see citing works

The ERK Cascade: Distinct Functions within Various Subcellular Organelles

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

Atrial fibrillation

Brundel, B. J. J. M., Ai, X., Hills, M. T., Kuipers, M. F., Lip, G. Y. H., & de Groot, N. M. S. (2022) · Nature Reviews Disease Primers · doi:10.1038/s41572-022-00347-9 · Cited by 528 · see citing works

MAPK signalling in cardiovascular health and disease: molecular mechanisms and therapeutic targets

Muslin, A. J. (2008) · Clinical Science · doi:10.1042/cs20070430 · Cited by 496 · see citing works

Gene regulation in the immediate-early response process

Bahrami, S., & Drabløs, F. (2016) · Advances in Biological Regulation · doi:10.1016/j.jbior.2016.05.001 · Cited by 465 · see citing works

MAPKs and their relevance to arthritis and inflammation

Thalhamer, T., McGrath, M., & Harnett, M. M. (2007) · Lara D. Veeken · doi:10.1093/rheumatology/kem297 · Cited by 460 · see citing works

Signaling effectors underlying pathologic growth and remodeling of the heart

van Berlo, J. H., Maillet, M., & Molkentin, J. D. (2013) · Journal of Clinical Investigation · doi:10.1172/jci62839 · Cited by 446 · see citing works

Non-Classical P38 Map Kinase Functions: Cell Cycle Checkpoints and Survival

Thornton, T. M., & Rincón, M. (2009) · International Journal of Biological Sciences · doi:10.7150/ijbs.5.44 · Cited by 442 · see citing works

The clinical development of MEK inhibitors

Zhao, Y., & Adjei, A. A. (2014) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2014.83 · Cited by 403 · see citing works

The role of MAPK signalling pathways in the response to endoplasmic reticulum stress

Darling, N. J., & Cook, S. J. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.01.009 · Cited by 401 · see citing works

SMYD3 links lysine methylation of MAP3K2 to Ras-driven cancer

Mazur, P., Reynoird, N., Khatri, P., Jansen, P., Wilkinson, A. W., Liu, S.-C., Barbash, O., Aller, G. V. V., Huddleston, M. J., Dhanak, D., et al. (2014) · Nature · doi:10.1038/nature13320 · Cited by 370 · see citing works

The ERK and JNK pathways in the regulation of metabolic reprogramming

Papa, S., Choy, P. M., & Bubici, C. (2018) · Oncogene · doi:10.1038/s41388-018-0582-8 · Cited by 381 · see citing works

Phosphorylation of Nrf2 at Multiple Sites by MAP Kinases Has a Limited Contribution in Modulating the Nrf2-Dependent Antioxidant Response

Sun, Z., Huang, Z., & Zhang, D. D. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006588 · Cited by 362 · see citing works

Discovery of Potent and Selective Covalent Inhibitors of JNK

Zhang, T., Iñesta-Vaquera, F., Niepel, M., Zhang, J., Ficarro, S. B., Machleidt, T., Xie, T., Marto, J. A., Kim, N., Sim, T., et al. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.11.010 · Cited by 348 · see citing works

Rab GTPases-Dependent Endocytic Pathways Regulate Neuronal Migration and Maturation through N-Cadherin Trafficking

Kawauchi, T., Sekine, K., Shikanai, M., Chihama, K., Tomita, K., Kubo, K., Nakajima, K., Nabeshima, Y.-I., & Hoshino, M. (2010) · Neuron · doi:10.1016/j.neuron.2010.07.007 · Cited by 328 · see citing works

Kinase cascades and ligand-directed signaling at the kappa opioid receptor

Bruchas, M. R., & Chavkin, C. (2010) · Psychopharmacology · doi:10.1007/s00213-010-1806-y · Cited by 318 · see citing works

Calcium-Dependent Signaling and Kinases in Apicomplexan Parasites

Billker, O., Lourido, S., & Sibley, L. D. (2009) · Cell Host & Microbe · doi:10.1016/j.chom.2009.05.017 · Cited by 315 · see citing works

Potential use of the DREB/ERF, MYB, NAC and WRKY transcription factors to improve abiotic and biotic stress in transgenic plants

Erpen, L., Devi, H. S., Grosser, J. W., & Dutt, M. (2017) · Plant Cell Tissue and Organ Culture (PCTOC) · doi:10.1007/s11240-017-1320-6 · Cited by 310 · see citing works

Targeting ERK1/2 protein-serine/threonine kinases in human cancers

Roskoski, R. J. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.01.039 · Cited by 309 · see citing works

Nociceptin/Orphanin FQ Receptor Structure, Signaling, Ligands, Functions, and Interactions with Opioid Systems

Toll, L., Bruchas, M. R., Calò, G., Cox, B. M., & Zaveri, N. T. (2016) · Pharmacological Reviews · doi:10.1124/pr.114.009209 · Cited by 301 · see citing works

Molecular Targets Underlying the Anticancer Effects of Quercetin: An Update

Khan, F., Niaz, K., Maqbool, F., Hassan, F. I., Abdollahi, M. R., Venkata, K. C. N., Nabavi, S. M., & Bishayee, A. (2016) · Nutrients · doi:10.3390/nu8090529 · Cited by 287 · see citing works

Selective p38α MAPK Deletion in Serotonergic Neurons Produces Stress Resilience in Models of Depression and Addiction

Bruchas, M. R., Schindler, A. G., Shankar, H., Messinger, D. I., Miyatake, M., Land, B. B., Lemos, J. C., Hagan, C. E., Neumaier, J. F., Quintana, A., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.06.011 · Cited by 266 · see citing works

The UV response of the skin: a review of the MAPK, NFκB and TNFα signal transduction pathways

Muthusamy, V., & Piva, T. J. (2010) · Archives of Dermatological Research · doi:10.1007/s00403-009-0994-y · Cited by 265 · see citing works

MAPK signaling pathways in the regulation of hematopoiesis

Geest, C. R., & Coffer, P. J. (2009) · Journal of Leukocyte Biology · doi:10.1189/jlb.0209097 · Cited by 261 · see citing works

Neutrophil diversity and function in health and disease

Zhang, F., Xia, Y., Su, J., Quan, F., Zhou, H., Li, Q., Feng, Q., Lin, C., Wang, D., & Jiang, Z. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02049-y · Cited by 284 · see citing works

Roles of Mitogen-Activated Protein Kinases in Osteoclast Biology

Lee, K., Seo, I., Choi, M. H., & Jeong, D. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103004 · Cited by 251 · see citing works

The Mammalian MAPK/ERK Pathway Exhibits Properties of a Negative Feedback Amplifier

Sturm, O. E., Orton, R. J., Grindlay, J., Birtwistle, M. R., Vyshemirsky, V., Gilbert, D., Muffy Calder, A., Pitt, A. R., Kholodenko, B. Ν., & Kölch, W. (2010) · Science Signaling · doi:10.1126/scisignal.2001212 · Cited by 248 · see citing works

Toxicity of Deoxynivalenol and Its Acetylated Derivatives on the Intestine: Differential Effects on Morphology, Barrier Function, Tight Junction Proteins, and Mitogen-Activated Protein Kinases

Pinton, P., Tsybulskyy, D., Lucioli, J., Laffitte, J., Callu, P., Lyazhri, F., Grosjean, F., Bracarense, A. P. F. R. L., Kolf‐Clauw, M., & Oswald, I. P. (2012) · Toxicological Sciences · doi:10.1093/toxsci/kfs239 · Cited by 247 · see citing works

Dietary phytochemicals and cancer prevention: Nrf2 signaling, epigenetics, and cell death mechanisms in blocking cancer initiation and progression

Lee, J. H., Khor, T. O., Shu, L., Su, Z., Fuentes, F., & Kong, A. T. (2012) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2012.09.008 · Cited by 248 · see citing works

Dynamics and Variability of ERK2 Response to EGF in Individual Living Cells

Cohen‐Saidon, C., Cohen, A. A., Sigal, A., Liron, Y., & Alon, U. S. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.11.025 · Cited by 246 · see citing works

From basic research to clinical development of MEK1/2 inhibitors for cancer therapy

Frémin, C., & Meloche, S. (2010) · Journal of Hematology & Oncology · doi:10.1186/1756-8722-3-8 · Cited by 243 · see citing works

The extracellular signal-regulated kinase 1/2 pathway in neurological diseases: A potential therapeutic target (Review)

Sun, J., & Nan, G. (2017) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2017.2962 · Cited by 241 · see citing works

Regulation of Primary Response Genes

Fowler, T., Sen, R., & Roy, A. L. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.09.014 · Cited by 246 · see citing works

How DNA lesions are turned into powerful killing structures: Insights from UV-induced apoptosis

Batista, L. F. Z., Kaina, B., Meneghini, R., & Menck, C. F. M. (2009) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2008.09.001 · Cited by 234 · see citing works

Vascular endothelial cell Toll-like receptor pathways in sepsis

Khakpour, S., Wilhelmsen, K., & Hellman, J. (2015) · Innate Immunity · doi:10.1177/1753425915606525 · Cited by 232 · see citing works

The roles of MAPKs in disease

Lawrence, M. C., Jivan, A., Shao, C., Duan, L., Goad, D. L., Zaganjor, E., Osborne, J. K., McGlynn, K., Stippec, S., Earnest, S. A., et al. (2008) · Cell Research · doi:10.1038/cr.2008.37 · Cited by 233 · see citing works

The Mitogen-Activated Protein Kinase (MAPK) Pathway: Role in Immune Evasion by Trypanosomatids

Soares-Silva, M., Diniz, F. F., Gomes, G. N., & Bahia, D. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.00183 · Cited by 233 · see citing works

Nuclear ERK: Mechanism of Translocation, Substrates, and Role in Cancer

Maik-Rachline, G., Hacohen-Lev-Ran, A., & Seger, R. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20051194 · Cited by 225 · see citing works

Adenosine receptors and cancer

Gessi, S., Merighi, S., Sacchetto, V., Simioni, C., & Borea, P. A. (2010) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.09.020 · Cited by 224 · see citing works

ERK5: Structure, regulation and function

Nithianandarajah-Jones, G. N., Wilm, B., Goldring, C. E., Müller, J., & Cross, M. J. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.07.007 · Cited by 221 · see citing works

Molecular Markers and Targets in Melanoma

Teixidó, C., Castillo, P., Martínez-Vila, C., Arance, A. M., & Alós, L. (2021) · Cells · doi:10.3390/cells10092320 · Cited by 246 · see citing works

m6A Reader YTHDF2 Regulates LPS-Induced Inflammatory Response

Yu, R., Li, Q., Feng, Z., Cai, L., & Xu, Q. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20061323 · Cited by 217 · see citing works

Specific Functions for ERK/MAPK Signaling during PNS Development

Newbern, J. M., Li, X., Shoemaker, S. E., Zhou, J., Zhong, J., Wu, Y., Bonder, D. E., Hollenback, S. M., Coppola, G., Geschwind, D. H., et al. (2011) · Neuron · doi:10.1016/j.neuron.2010.12.003 · Cited by 216 · see citing works

Membrane Localization of LRRK2 Is Associated with Increased Formation of the Highly Active LRRK2 Dimer and Changes in Its Phosphorylation

Berger, Z., Smith, K. A., & LaVoie, M. J. (2010) · Biochemistry · doi:10.1021/bi100157u · Cited by 215 · see citing works

Intracellular signaling pathway regulation of myelination and remyelination in the CNS

Gaesser, J. M., & Fyffe-Maricich, S. L. (2016) · Experimental Neurology · doi:10.1016/j.expneurol.2016.03.008 · Cited by 208 · see citing works

Protein kinases: mechanisms and downstream targets in inflammation-mediated obesity and insulin resistance

Nandipati, K. C., Subramanian, S., & Agrawal, D. K. (2016) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-016-2878-8 · Cited by 210 · see citing works

MKP-1 mRNA Stabilization and Translational Control by RNA-Binding Proteins HuR and NF90

Kuwano, Y., Kim, H. H., Abdelmohsen, K., Pullmann, R., Martindale, J. L., Yang, X., & Gorospe, M. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00165-08 · Cited by 209 · see citing works

Cysteine sulfenylation directs IRE-1 to activate the SKN-1/Nrf2 antioxidant response

Hourihan, J. M., Mazzeo, L. E. M., Fernández-Cárdenas, L. P., & Blackwell, T. (2016) · Molecules and Cells · doi:10.1016/j.molcel.2016.07.019 · Cited by 195 · see citing works

Regulation of Dual-Specificity Phosphatase (DUSP) Ubiquitination and Protein Stability

Chen, H., Chuang, H., & Tan, T. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20112668 · Cited by 205 · see citing works

A Comprehensive Analysis and Anti-Cancer Activities of Quercetin in ROS-Mediated Cancer and Cancer Stem Cells

Biswas, P., Dey, D., Biswas, P. K., Rahaman, T. I., Saha, S., Parvez, A., Khan, D. A., Lily, N. J., Saha, K., Sohel, M., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911746 · Cited by 204 · see citing works

Muscle Wasting and Impaired Myogenesis in Tumor Bearing Mice Are Prevented by ERK Inhibition

Penna, F., Costamagna, D., Fanzani, A., Bonelli, G., Baccino, F. M., & Costelli, P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013604 · Cited by 191 · see citing works

Salp15 Binding to DC-SIGN Inhibits Cytokine Expression by Impairing both Nucleosome Remodeling and mRNA Stabilization

Hovius, J. W., de Jong, M. A. W. P., den Dunnen, J., Litjens, M., Fikrig, E., van der Poll, T., Gringhuis, S. I., & Geijtenbeek, T. B. H. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.0040031 · Cited by 190 · see citing works

Pharmacological Inhibition of BMK1 Suppresses Tumor Growth through Promyelocytic Leukemia Protein

Yang, Q., Deng, X., Lu, B., Cameron, M. D., Fearns, C., Patricelli, M. P., Yates, J. R., Gray, N. S., & Lee, J. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.08.008 · Cited by 189 · see citing works

Ras Stabilization Through Aberrant Activation of Wnt/β-Catenin Signaling Promotes Intestinal Tumorigenesis

Jeong, W.-J., Yoon, J., Park, J., Lee, S.-H., Lee, S., Kaduwal, S., Kim, H., Yoon, J., & Choi, K. (2012) · Science Signaling · doi:10.1126/scisignal.2002242 · Cited by 189 · see citing works

GLP-1 Mediates Antiapoptotic Effect by Phosphorylating Bad through a β-Arrestin 1-mediated ERK1/2 Activation in Pancreatic β-Cells

Quoyer, J., Longuet, C., Broca, C., Linck, N., Costes, S., Varin, E. M., Bockaert, J., Bertrand, G., & Dalle, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.067207 · Cited by 187 · see citing works

Quercetin: A functional dietary flavonoid with potential chemo‐preventive properties in colorectal cancer

Darband, S. G., Kaviani, M., Yousefi, B., Sadighparvar, S., Pakdel, F. G., Aghazadeh-Attari, J., Mohebbi, I., Naderi, S., & Majidinia, M. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26595 · Cited by 189 · see citing works

Relations between the mitogen-activated protein kinase and the cAMP-dependent protein kinase pathways: Comradeship and hostility

Gerits, N., Kostenko, S., Shiryaev, A., Johannessen, M., & Moens, U. L. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2008.02.022 · Cited by 183 · see citing works

Luteolin, quercetin and ursolic acid are potent inhibitors of proliferation and inducers of apoptosis in both KRAS and BRAF mutated human colorectal cancer cells

Xavier, C. P. R., Lima, C. F., Preto, A., Seruca, R., Fernandes‐Ferreira, M., & Pereira‐Wilson, C. (2009) · Cancer Letters · doi:10.1016/j.canlet.2009.02.041 · Cited by 176 · see citing works

Doxorubicin induces an extensive transcriptional and metabolic rewiring in yeast cells

Taymaz‐Nikerel, H., Karabekmez, M. E., Eraslan, S., & Kırdar, B. (2018) · Scientific Reports · doi:10.1038/s41598-018-31939-9 · Cited by 175 · see citing works

The retinal pigment epithelium: An important player of retinal disorders and regeneration

Chiba, C. (2013) · Experimental Eye Research · doi:10.1016/j.exer.2013.07.009 · Cited by 172 · see citing works

MSK activation and physiological roles

J. Simon, C. A. (2008) · Frontiers in bioscience · doi:10.2741/3122 · Cited by 165 · see citing works

Receptor tyrosine kinases: Characterisation, mechanism of action and therapeutic interests for bone cancers

Ségaliny, A. I., Tellez-Gabriel, M., Heymann, M.-F., & Heymann, D. (2015) · Journal of Bone Oncology · doi:10.1016/j.jbo.2015.01.001 · Cited by 164 · see citing works

Role of p38 MAPK in Atherosclerosis and Aortic Valve Sclerosis

Reustle, A., & Torzewski, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123761 · Cited by 162 · see citing works

Role of protein phosphorylation in cell signaling, disease, and the intervention therapy

Pang, K., Wang, W., Qin, J., Shi, Z., Hao, L., Ma, Y., Xu, H., Wu, Z., Pan, D., Chen, Z., et al. (2022) · MedComm · doi:10.1002/mco2.175 · Cited by 163 · see citing works

Hypoxia-Inducible Factors (HIFs) and Phosphorylation: Impact on Stability, Localization, and Transactivity

Kietzmann, T., Mennerich, D., & Dimova, E. Y. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2016.00011 · Cited by 176 · see citing works

The ghost in the machine: small GTPases as spatial regulators of exocytosis

Wu, H., Rossi, G., & Brennwald, P. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.06.007 · Cited by 159 · see citing works

Integrin Signaling, Cell Survival, and Anoikis: Distinctions, Differences, and Differentiation

Vachon, P. H. (2011) · Journal of Signal Transduction · doi:10.1155/2011/738137 · Cited by 154 · see citing works

Crosstalk between mitogen-activated protein kinases and mitochondria in cardiac diseases: Therapeutic perspectives

Javadov, S. A., Jang, S., & Agostini, B. (2014) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2014.05.013 · Cited by 157 · see citing works

Inflammatory mediators promote production of shed LRP1/CD91, which regulates cell signaling and cytokine expression by macrophages

Gorovoy, M. S., Gaultier, A., Campana, W. M., Firestein, G. S., & Gonias, S. L. (2010) · Journal of Leukocyte Biology · doi:10.1189/jlb.0410220 · Cited by 157 · see citing works

Role of MAPK/MNK1 signaling in virus replication

Kumar, R., Khandelwal, N., Thachamvally, R., Tripathi, B. N., Barua, S., Kashyap, S. K., Maherchandani, S., & Kumar, N. (2018) · Virus Research · doi:10.1016/j.virusres.2018.05.028 · Cited by 153 · see citing works

Essential Role of ERK Dimers in the Activation of Cytoplasmic but Not Nuclear Substrates by ERK-Scaffold Complexes

Casar, B., Pinto, A., & Crespo, P. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.07.024 · Cited by 152 · see citing works

Effects of nitrite exposure on haematological parameters, oxidative stress and apoptosis in juvenile turbot (Scophthalmus maximus)

Jia, R., Han, C., Lei, J., Liu, B., Huang, B., Huo, H., & Yin, S.-T. (2015) · Aquatic Toxicology · doi:10.1016/j.aquatox.2015.09.016 · Cited by 149 · see citing works

Adenosine and adenosine receptors in the immunopathogenesis and treatment of cancer

Kazemi, M., Mohseni, S. R., Hojjat-Farsangi, M., Anvari, E., Ghalamfarsa, G., Mohammadi, H., & Jadidi-Niaragh, F. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.25873 · Cited by 139 · see citing works

Adenosine Receptors and Cancer

Fishman, P., Bar‐Yehuda, S., Synowitz, M., Powell, J. D., Klotz, K., Gessi, S., & Borea, P. A. (2009) · Handbook of experimental pharmacology · doi:10.1007/978-3-540-89615-9_14 · Cited by 149 · see citing works

The bottleneck of JNK signaling: Molecular and functional characteristics of MKK4 and MKK7

Haeusgen, W., Herdegen, T., & Waetzig, V. (2011) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2010.11.008 · Cited by 149 · see citing works

New Insights into Toxicity and Drug Testing

Gowder, S. J. (2013) · InTech eBooks · doi:10.5772/55886 · Cited by 149 · see citing works

Resveratrol Protects against TNF-α-Induced Injury in Human Umbilical Endothelial Cells through Promoting Sirtuin-1-Induced Repression of NF-KB and p38 MAPK

Pan, W. X., Yu, H., Huang, S., & Zhu, P. (2016) · PLoS ONE · doi:10.1371/journal.pone.0147034 · Cited by 147 · see citing works

Substrate Discrimination among Mitogen-activated Protein Kinases through Distinct Docking Sequence Motifs

Sheridan, D. L., Kong, Y., Parker, S. A., Dalby, K. N., & Turk, B. E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801074200 · Cited by 147 · see citing works

The emerging role of redox-sensitive Nrf2–Keap1 pathway in diabetes

Bhakkiyalakshmi, E., Sireesh, D., Rajaguru, P., Paulmurugan, R., & Ramkumar, K. M. (2014) · Pharmacological Research · doi:10.1016/j.phrs.2014.10.004 · Cited by 148 · see citing works

Role of Caspases in Cytokine-Induced Barrier Breakdown in Human Brain Endothelial Cells

Lopez‐Ramirez, M. A., Fischer, R., Torres-Badillo, C. C., Davies, H. A., Logan, K. E., Pfizenmaier, K., Male, D. K., Sharrack, B., & Romero, I. A. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1103460 · Cited by 140 · see citing works

The redox biology network in cancer pathophysiology and therapeutics

Manda, G., Isvoranu, G., Comănescu, M., Manea, A., Butuner, B. D., & Korkmaz, K. (2015) · Redox Biology · doi:10.1016/j.redox.2015.06.014 · Cited by 130 · see citing works

From the cellular perspective: exploring differences in the cellular baseline in macroscale and microfluidic cultures

Paguirigan, A. L., & Beebe, D. J. (2009) · Integrative Biology · doi:10.1039/b814565b · Cited by 136 · see citing works

The MAPK Signaling Cascades

Maik-Rachline, G., Wexler, S., & Seger, R. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-821618-7.00130-9 · Cited by 2 · see citing works

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 · see citing works

MAP Kinase PathwaysPreprint

Morrison, D. K. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011254 · Cited by 846 · see citing works

Mitogen‐activated Protein Kinases ( MAPKs ): ERKs , JNKs , and p 38 s

Chen, W., Juang, Y.-C. A., & Cobb, M. H. (2008) · Wiley Encyclopedia of Chemical Biology · doi:10.1002/9780470048672.wecb348

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 · see citing works