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A protein kinase involved in the regulation of inflammatory cytokine biosynthesis
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Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669
Atomic structure of the MAP kinase ERK2 at 2.3 A resolution
Zhang, F., Strand, A., Robbins, D., Cobb, M. H., & Goldsmith, E. J. (1994) · Nature · doi:10.1038/367704a0 · Cited by 592
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Johnson, G. L., & Lapadat, R. (2002) · Science · doi:10.1126/science.1072682 · Cited by 4,295
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
SP600125, an anthrapyrazolone inhibitor of Jun N-terminal kinase
Bennett, B. L., Sasaki, D. T., Murray, B. W., O'Leary, E. C., Sakata, S. T., Xu, W., Leisten, J. C., Motiwala, A., Pierce, S., Satoh, Y., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251194298 · Cited by 2,558
Whitmarsh, A. J., & Davis, R. J. (1996) · Journal of Molecular Medicine · doi:10.1007/s001090050063 · Cited by 1,543
Differential regulation and properties of MAPKs
Raman, M., Chen, W., & Cobb, M. H. (2007) · Oncogene · doi:10.1038/sj.onc.1210392 · Cited by 1,430
Kaminska, B. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.08.017 · Cited by 1,285
Cholinergic agonists inhibit HMGB1 release and improve survival in experimental sepsis
Wang, H., Liao, H., Ochani, M., Justiniani, M., Lin, X., Yang, L., Al-Abed, Y., Wang, H., Metz, C., Miller, E. J., et al. (2004) · Nature Medicine · doi:10.1038/nm1124 · Cited by 1,170
Excitotoxicity and stroke: Identifying novel targets for neuroprotection
Lai, T. W., Zhang, S., & Wang, Y. T. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.11.006 · Cited by 1,106
Identification of two distinct mechanisms of phagocytosis controlled by different Rho GTPases
Caron, E., & Hall, A. (1998) · Science · doi:10.1126/science.282.5394.1717 · Cited by 1,019
Carbon Monoxide Generated by Heme Oxygenase 1 Suppresses Endothelial Cell Apoptosis
Brouard, S., Otterbein, L. E., Anrather, J., Tobiasch, E., Bach, F. H., Choi, A. M. K., & Soares, M. P. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.7.1015 · Cited by 984
Tikka, T., Fiebich, B. L., Goldsteins, G., Keinänen, R., & Koistinaho, J. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-08-02580.2001 · Cited by 958
Comprehensive assay of kinase catalytic activity reveals features of kinase inhibitor selectivity
Anastassiadis, T., Deacon, S. W., Devarajan, K., Ma, H., & Peterson, J. R. (2011) · Nature Biotechnology · doi:10.1038/nbt.2017 · Cited by 919
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
Mitogen-activated protein kinase cascades and regulation of gene expression
Su, B., & Karin, M. (1996) · Current Opinion in Immunology · doi:10.1016/s0952-7915(96)80131-2 · Cited by 747
Regulation of Tau Pathology by the Microglial Fractalkine Receptor
Bhaskar, K., Konerth, M., Kokiko-Cochran, O. N., Cardona, A., Ransohoff, R. M., & Lamb, B. T. (2010) · Neuron · doi:10.1016/j.neuron.2010.08.023 · Cited by 639
“, 1993), p38 MAPK phosphorylated at thr180/tyr182 (Goedert et al., 1997; Lee et al., 1994), and protein phosphatase 2A (PP2A) were measured in hippocampal extracts from 6-monthold hTau-Cx3cr1 / mice and hTau controls.”
Diversity and versatility of p38 kinase signalling in health and disease
Canovas, B., & Nebreda, A. R. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00322-w · Cited by 657
Keshet, Y., & Seger, R. (2010) · Methods in Molecular Biology · doi:10.1007/978-1-60761-795-2_1 · Cited by 642
Zhang, S., Han, J., Sells, M. A., Chernoff, J., Knaus, U. G., Ulevitch, R. J., & Bokoch, G. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.41.23934 · Cited by 614
Maphis, N., Xu, G., Kokiko-Cochran, O. N., Jiang, S., Cardona, A., Ransohoff, R. M., Lamb, B. T., & Bhaskar, K. (2015) · Brain · doi:10.1093/brain/awv081 · Cited by 595
The ERK Cascade: Distinct Functions within Various Subcellular Organelles
Wortzel, I., & Seger, R. (2011) · Genes & Cancer · doi:10.1177/1947601911407328 · Cited by 563
Targeting dual-specificity phosphatases: Manipulating MAP kinase signalling and immune responses
Jeffrey, K. L., Camps, M., Rommel, C., & Mackay, C. R. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2289 · Cited by 533
Hsu, H.-Y., & Wen, M.-H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111883200 · Cited by 519
The p38 MAPK inhibitors for the treatment of inflammatory diseases and cancer
Yong, H.-Y., Koh, M.-S., & Moon, A. (2009) · Expert Opinion on Investigational Drugs · doi:10.1517/13543780903321490 · Cited by 422
Wang, Q., Walsh, D. M., Rowan, M. J., Selkoe, D. J., & Anwyl, R. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.1633-03.2004 · Cited by 437
Translocation of SAPK/JNK to Mitochondria and Interaction with Bcl-xL in Response to DNA Damage
Kharbanda, S., Saxena, S., Yoshida, K., Pandey, P., Kaneki, M., Wang, Q., Cheng, K., Chen, Y.-N., Campbell, A., Sudha, T., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.1.322 · Cited by 429
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
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
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Igarashi, M., Wakasaki, H., Takahara, N., Ishii, H., Jiang, Z.-Y., Yamauchi, T., Kuboki, K., Meier, M., Rhodes, C. J., & King, G. L. (1999) · Journal of Clinical Investigation · doi:10.1172/jci3326 · Cited by 386
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Zhao, Q., Wang, X., Nelin, L. D., Yao, Y., Matta, R., Manson, M. E., Baliga, R. S., Meng, X., Smith, C. V., Bauer, J. A., et al. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20051794 · Cited by 370
Fitzgerald, M. L., Wang, Z., Park, P. W., Murphy, G., & Bernfield, M. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.4.811 · Cited by 367
Adolfsson, O., Pihlgren, M., Toni, N., Varisco, Y., Buccarello, A. L., Antoniello, K., Lohmann, S., Piorkowska, K., Gafner, V., Atwal, J. K., et al. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.4742-11.2012 · Cited by 317
Ito, M., Yoshioka, K., Akechi, M., Yamashita, S., Takamatsu, N., Sugiyama, K., Hibi, M., Nakabeppu, Y., Shiba, T., & Yamamoto, K.-I. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.11.7539 · Cited by 279
The structure of mitogen-activated protein kinase p38 at 2.1-Å resolution
Wang, Z., Harkins, P. C., Ulevitch, R. J., Han, J., Cobb, M. H., & Goldsmith, E. J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.6.2327 · Cited by 275
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Cheng, J.-K., & Ji, R.-R. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9711-z · Cited by 266
Malaquin, N., Martinez, A., & Rodier, F. (2016) · Experimental Gerontology · doi:10.1016/j.exger.2016.05.010 · Cited by 247
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Anti-inflammatory effects of fluoxetine in lipopolysaccharide(LPS)-stimulated microglial cells
Liu, D., Wang, Z., Liu, S., Wang, F., Zhao, S., & Hao, A. (2011) · Neuropharmacology · doi:10.1016/j.neuropharm.2011.04.033 · Cited by 221
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Identification of the Critical Features of a Small Peptide Inhibitor of JNK Activity
Barr, R. K., Kendrick, T. S., & Bogoyevitch, M. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107565200 · Cited by 211
Role of p38/MAPKs in Alzheimer's Disease: Implications for Amyloid Beta Toxicity Targeted Therapy
Kheiri, G., Dolatshahi, M., Rahmani, F., & Rezaei, N. (2018) · Reviews in the Neurosciences · doi:10.1515/revneuro-2018-0008 · Cited by 211
Crystal structure of JNK3: a kinase implicated in neuronal apoptosis
Xie, X., Gu, Y., Fox, T., Coll, J. T., Fleming, M. A., Markland, W., Caron, P. R., Wilson, K. P., & Su, M. S.-S. (1998) · Structure · doi:10.1016/s0969-2126(98)00100-2 · Cited by 198
Kikuchi, M., Tenneti, L., & Lipton, S. A. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-13-05037.2000 · Cited by 197
LPS and TNFα induce SOCS3 mRNA and inhibit IL‐6‐induced activation of STAT3 in macrophages
Bode, J. G., Nimmesgern, A., Schmitz, J., Schaper, F., Schmitt, M., Frisch, W., Häussinger, D., Heinrich, P. C., & Graeve, L. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01662-2 · Cited by 196
Giovannini, M. G., Scali, C., Prosperi, C., Bellucci, A., Vannucchi, M. G., Rosi, S., Pepeu, G., & Casamenti, F. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0538 · Cited by 190
Cellular and molecular mechanisms of immunomodulation in the brain through environmental enrichment
Singhal, G., Jaehne, E. J., Corrigan, F., & Baune, B. T. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00097 · Cited by 186
Mitogen activated protein kinases: a role in inflammatory bowel disease?
Broom, O. J., Widjaya, B., Troelsen, J., Olsen, J., & Nielsen, O. H. (2009) · Clinical and Experimental Immunology · doi:10.1111/j.1365-2249.2009.04033.x · Cited by 177
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Chung, S., Jiang, L., Cheng, S., & Furneaux, H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.19.11518 · Cited by 168
Alsayed, Y., Uddin, S., Mahmud, N., Lekmine, F., Kalvakolanu, D. V., Minucci, S., Bokoch, G., & Platanias, L. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007431200 · Cited by 161
Hashimoto, S., Gon, Y., Takeshita, I., Maruoka, S., & Horie, T. (2001) · Journal of Allergy and Clinical Immunology · doi:10.1067/mai.2001.114702 · Cited by 151
Complement pathway amplifies caspase-11–dependent cell death and endotoxin-induced sepsis severity
Napier, B. A., Brubaker, S. W., Sweeney, T. E., Monette, P., Rothmeier, G. H., Gertsvolf, N. A., Puschnik, A., Carette, J. E., Khatri, P., & Monack, D. M. (2016) · Journal of Experimental Medicine · doi:10.1084/jem.20160027 · Cited by 149
Dynamics and regulation of lipid droplet formation in lipopolysaccharide (LPS)-stimulated microglia
Khatchadourian, A., Bourque, S. D., Richard, V. R., Titorenko, V. I., & Maysinger, D. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2012.01.007 · Cited by 143
Kurgan, S., & Kantarci, A. (2018) · Periodontology 2000 · doi:10.1111/prd.12146 · Cited by 141
Lee, S. J., Drabik, K., Van Wagoner, N. J., Lee, S., Choi, C., Dong, Y., & Benveniste, E. N. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.8.4658 · Cited by 137
Molecular mechanisms linking amyloid β toxicity and Tau hyperphosphorylation in Alzheimer׳s disease
Lloret, A., Fuchsberger, T., Giraldo, E., & Viña, J. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.02.028 · Cited by 135
Chemoproteomics and Chemical Probes for Target Discovery
Drewes, G., & Knapp, S. (2018) · Trends in Biotechnology · doi:10.1016/j.tibtech.2018.06.008 · Cited by 132
Wang, X., Wu, H., & Miller, A. H. (2004) · Molecular Psychiatry · doi:10.1038/sj.mp.4001339 · Cited by 128
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Mercer, B. A., & D'Armiento, J. M. (2006) · International Journal of COPD · doi:10.2147/copd.2006.1.2.137 · Cited by 118
De Cesaris, P., Starace, D., Riccioli, A., Padula, F., Filippini, A., & Ziparo, E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.13.7566 · Cited by 116
Back to the future: oral targeted therapy for RA and other autoimmune diseases
O'Shea, J. J., Laurence, A., & McInnes, I. B. (2013) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2013.7 · Cited by 115
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Akella, R., Moon, T. M., & Goldsmith, E. J. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2007.09.016 · Cited by 108
Zheng, C., Xiang, J., Hunter, T., & Lin, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.41.28966 · Cited by 110
IL-1 and TNF-induced bone resorption is mediated by p38 mitogen activated protein kinase.
Kumar, S., Votta, B. J., Rieman, D. J., Badger, A. M., Gowen, M., & Lee, J. C. (2001) · Journal of Cellular Physiology · doi:10.1002/jcp.1082 · Cited by 107
Self-citationABCA1 influences neuroinflammation and neuronal death
Karasinska, J. M., de Haan, W., Franciosi, S., Ruddle, P., Fan, J., Kruit, J. K., Stukas, S., Lütjohann, D., Gutmann, D. H., Wellington, C. L., et al. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.01.018 · Cited by 104
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Haar, E. T., Prabakhar, P., Liu, X., & Lepre, C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611165200 · Cited by 100
Vukmanovic-Stejic, M., Chambers, E. S., Suárez-Fariñas, M., Sandhu, D., Fuentes-Duculan, J., Patel, N., Agius, E., Lacy, K. E., Turner, C. T., Larbi, A., et al. (2018) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2017.10.032 · Cited by 103
Wu, X., Yang, Z., Zou, J., Gao, H., Shao, Z., Li, C., & Lei, P. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02179-x · Cited by 88
Zhang, L., Li, H.-Z., Gong, X., Luo, F.-L., Wang, B., Hu, N., Wang, C.-D., Zhang, Z., & Wan, J.-Y. (2010) · Phytomedicine · doi:10.1016/j.phymed.2010.01.008 · Cited by 79
Shimizu, T., Kato, T., Tachibana, A., & Sasaki, M. S. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4582 · Cited by 73
Yang, C., Cao, P., Gao, Y., Wu, M., Lin, Y., Tian, Y., & Yuan, W. (2016) · Scientific Reports · doi:10.1038/srep22182 · Cited by 69
Underwood, K. W., Parris, K. D., Federico, E., Mosyak, L., Czerwinski, R. M., Shane, T., Taylor, M., Svenson, K., Liu, Y., Hsiao, C.-L., et al. (2003) · Structure · doi:10.1016/s0969-2126(03)00092-3 · Cited by 62
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Paunovic, V., & Harnett, M. M. (2013) · Drugs · doi:10.1007/s40265-013-0014-6 · Cited by 61
Bae, M.-A., Pie, J.-E., & Song, B. J. (2001) · Molecular Pharmacology · doi:10.1016/s0026-895x(24)12313-9 · Cited by 60
Amyloid precursor protein mediates proinflammatory activation of monocytic lineage cells
Sondag, C. M., & Combs, C. K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313747200 · Cited by 56
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Kasuya, Y., Umezawa, H., & Hatano, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030867 · Cited by 54
Wang, W., Wu, L., Li, Q., Zhang, Z., Xu, L., Lin, C., Gao, L., Zhao, K., Liang, F., Zhang, Q., et al. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.04.162 · Cited by 51
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
Hayes, A. L., Smith, C., Foxwell, B. M. J., & Brennan, F. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.47.33455 · Cited by 44
Sano, Y., Akimaru, H., Okamura, T., Nagao, T., Okada, M., & Ishii, S. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-11-1008 · Cited by 42
NMR backbone assignment of the mitogen-activated protein (MAP) kinase p38
Vogtherr, M., Saxena, K., Grimme, S., Betz, M., Schieborr, U., Pescatore, B., Langer, T., & Schwalbe, H. (2005) · Journal of Biomolecular NMR · doi:10.1007/s10858-005-2449-x · Cited by 30
Rouget, R., Auclair, Y., Loignon, M., Affar, E. B., & Drobetsky, E. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706257200 · Cited by 30
Hecquet, C., Lefevre, G., Valtink, M., Engelmann, K., & Mascarelli, F. (2003) · Investigative Opthalmology & Visual Science · doi:10.1167/iovs.02-0519 · Cited by 29
Callaway, K., Rainey, M. A., & Dalby, K. N. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.11.002 · Cited by 26
Dynamics in the p38α MAP Kinase–SB203580 Complex Observed by Liquid‐State NMR Spectroscopy
Honndorf, V. S., Coudevylle, N., Laufer, S., Becker, S., & Griesinger, C. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200705614 · Cited by 22
Scotter, E. L., Cao, M. C., Jansson, D., Rustenhoven, J., Smyth, L. C. D., Aalderink, M. C., Siemens, A., Fan, V., Wu, J., Mee, E. W., et al. (2022) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2022.103768 · Cited by 13
Metadata
- Authors
- Lee, J. C., Laydon, J. T., McDonnell, P. C., Gallagher, T. F., Kumar, S., Green, D., McNulty, D., Blumenthal, M. J., Keys, J. R., Land vatter, S. W., Strickler, J. E., McLaughlin, M. M., Siemens, I. R., Fisher, S. M., Livi, G. P., White, J. R., Adams, J. L., & Young, P. R.
- Venue
- Nature
- Published
- 1994-12
- Volume
- 372
- Issue
- 6508
- Pages
- 739-746
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2032731042
- Cited by
- 3,288
- References
- 2
- FWCI
- 30.27
- Type
- journal article
- Language
- en
- Open access
- closed
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