The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Independent Human MAP-Kinase Signal Transduction Pathways Defined by MEK and MKK Isoforms
Abstract
Mammalian mitogen-activated protein (MAP) kinases include extracellular signal-regulated protein kinase (ERK), c-Jun amino-terminal kinase (JNK), and p38 subgroups. These MAP kinase isoforms are activated by dual phosphorylation on threonine and tyrosine. Two human MAP kinase kinases (MKK3 and MKK4) were cloned that phosphorylate and activate p38 MAP kinase. These MKK isoforms did not activate the ERK subgroup of MAP kinases, but MKK4 did activate JNK. These data demonstrate that the activators of p38 (MKK3 and MKK4), JNK (MKK4), and ERK (MEK1 and MEK2) define independent MAP kinase signal transduction pathways.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“a peptide derived from MKK4 (pepMKK4) bound to JNK1 and p38α with similar affinities, as expected.”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [23]
Citations
Cites
Site-directed mutagenesis by overlap extension using the polymerase chain reaction
Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., & Pease, L. R. (1989) · Gene · doi:10.1016/0378-1119(89)90358-2 · Cited by 7,414
Smith, D. B., & Johnson, K. S. (1988) · Gene · doi:10.1016/0378-1119(88)90005-4 · Cited by 5,844
Dérijard, B., Hibi, M., Wu, I.-H., Barrett, T., Su, B., Deng, T., Karin, M., & Davis, R. J. (1994) · Cell · doi:10.1016/0092-8674(94)90380-8 · Cited by 3,188
Self-citationA MAP Kinase Targeted by Endotoxin and Hyperosmolarity in Mammalian Cells
Han, J., Lee, J. D., Bibbs, L., & Ulevitch, R. J. (1994) · Science · doi:10.1126/science.7914033 · Cited by 2,647
Self-citationThe stress-activated protein kinase subfamily of c-Jun kinases
Kyriakis, J. M., Banerjee, P. T., Nikolakaki, E., Dai, T., Rubie, E. A., Ahmad, M. F., Avruch, J., & Woodgett, J. R. (1994) · Nature · doi:10.1038/369156a0 · Cited by 2,601
The mitogen-activated protein kinase signal transduction pathway
Davis, R. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82362-6 · Cited by 2,112
Self-citationRouse, J. W., Cohen, P., Trigon, S., Morange, M., Alonso‐Llamazares, A., Zamanillo, D., Hunt, T., & Nebreda, Á. R. (1994) · Cell · doi:10.1016/0092-8674(94)90277-1 · Cited by 1,671
Transcription Factor ATF2 Regulation by the JNK Signal Transduction Pathway
Gupta, S., Campbell, D., Dérijard, B., & Davis, R. J. (1995) · Science · doi:10.1126/science.7824938 · Cited by 1,433
Self-citationAn Osmosensing Signal Transduction Pathway in Yeast
Brewster, J. L., de Valoir, T., Dwyer, N. D., Winter, E., & Gustin, M. C. (1993) · Science · doi:10.1126/science.7681220 · Cited by 1,248
Andersson, S., Davis, D. L., Dahlbäck, H., Jörnvall, H., & Russell, D. W. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83172-6 · Cited by 1,229
Flagged first, then by citations
Research works printed but not linked: 1
- DRESSLER, H, BIOTECHNIQUES 13: 866 (1992).
Cited by
Sorted by citations
Items 401–500 of 999
Tournier, C., Thomas, G., Pierre, J., Jacquemin, C., Pierre, M., & Saunier, B. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00587.x · Cited by 149
Chan, W., Wu, C., & Yu, J. (2003) · Journal of Cellular Biochemistry · doi:10.1002/jcb.10638 · Cited by 148
“The components in the JNK/ SAPK regulation pathway are identified as being MAPK kinase kinase 1 (MEKK1), SAPK/ extracellular-signal-regulated kinase kinase 1 (SEK1), JNK/SAPK, and c-Jun [Sanchez et al., 1994; Yan et al., 1994; Derijard et al., 1995; Lin et al., 1995].”
MethodImportance of MEK in Neutrophil Microbicidal Responsiveness
Downey, G. P., Butler, J. R., Tapper, H., Fialkow, L., Saltiel, A. R., Rubin, B. B., & Grinstein, S. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.160.1.434 · Cited by 148
Srivastava, R. K., Sollott, S. J., Khan, L., Hansford, R. G., Lakatta, E. G., & Longo, D. L. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.8.5659 · Cited by 148
“As mentioned previously, the JNK/SAPK pathway involves an orderly activation of proteins, MEKK1, SEK1, JNK, and c-Jun (11, 12, 25).”
BackgroundInfluentialc-Jun NH2-Terminal Kinase (JNK)1 and JNK2 Have Distinct Roles in CD8+ T Cell Activation
Conze, D. B., Krahl, T., Kennedy, N. J., Weiss, L., Lumsden, J. M., Hess, P., Flavell, R. A., Gros, G. S. L., Davis, R. J., & Rincón, M. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20011508 · Cited by 145
“While MKK7 specifically regulates JNK, MKK4 has been shown to also activate p38 MAP kinase (12, 18).”
Self-citationButterfield, L., Storey, B., Maas, L., & Heasley, L. E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.15.10110 · Cited by 146
Bost, F., McKay, R. A., Bost, M., Potapova, O., Dean, N. M., & Mercola, D. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.3.1938 · Cited by 146
“The JNK pathway consists of several kinases, including mitogen-activated/extracellular response kinase kinase (MEK) kinase 1 (MEKK1) and mitogen-activated protein kinase (MAPK) kinases 7 and 4 (MKK7 and MKK4), which form a kinase cascade (22, 28, 29, 55, 61, 95, 96).”
BackgroundThe true face of JNK activation in apoptosis
Lin, A., & Dibling, B. C. (2002) · Aging Cell · doi:10.1046/j.1474-9728.2002.00014.x · Cited by 144
Akt (Protein Kinase B) Negatively Regulates SEK1 by Means of Protein Phosphorylation
Park, H.-S., Kim, M.-S., Huh, S.-H., Park, J., Chung, J., Kang, S. S., & Choi, E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110299200 · Cited by 145
Balasubramanian, S., Efimova, T., & Eckert, R. L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110376200 · Cited by 144
Basak, C., Pathak, S. K., Bhattacharyya, A., Mandal, D., Pathak, S., & Kundu, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m412820200 · Cited by 144
Miwatashi, S., Arikawa, Y., Kotani, E., Miyamoto, M., Naruo, K., Kimura, H., Tanaka, T., Asahi, S., & Ohkawa, S. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm050165o · Cited by 144
MAP2K1 ( MEK1 ) Mutations Define a Distinct Subset of Lung Adenocarcinoma Associated with Smoking
Arcila, M. E., Drilon, A. E. D. C., Sylvester, B. E., Lovly, C. M., Borsu, L. A., Reva, B. A., Kris, M. G., Solit, D. B., & Ladanyi, M. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-2124 · Cited by 144
“This kinase family also includes five additional members but only MEK1 and MEK2 are known to participate in the MAPK/ERK cascade with pivotal roles in signal integration (5).”
BackgroundSignaling by the G Class of G Proteins
Dhanasekaran, N., & Dermott, J. M. (1996) · Cellular Signalling · doi:10.1016/0898-6568(96)00048-4 · Cited by 143
Zhao, Y., Bjørbæk, C., Weremowicz, S., Morton, C. C., & Moller, D. E. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.8.4353 · Cited by 145
“It is also apparent that MAP kinase kinase and MAP kinase signaling ‘‘modules’’ in mammals consist of different isoforms that participate in growth factorversus stress-activated pathways (17, 19, 42, 48).”
BackgroundProtective Mechanisms of Flavonoids in Parkinson’s Disease
Magalingam, K. B., Radhakrishnan, A. K., & Haleagrahara, N. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/314560 · Cited by 144
Activation of Mitogen-Activated Protein Kinase Regulates Eotaxin-Induced Eosinophil Migration
Boehme, S. A., Sullivan, S., Crowe, P. D., Santos, M. A., Conlon, P. J., Sriramarao, P., & Bacon, K. B. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.3.1611 · Cited by 140
“Three families of MAPKs have been identified, the ERKs (which include p44 (ERK1) and p42 (ERK2)), c-Jun amino-terminal kinase, and the p38 subgroup of kinases, and can be distinguished by their tripeptide dual phosphorylation motif required for activation ( 22 ).”
BackgroundAkt as a therapeutic target in cancer
Steelman, L. S., Stadelman, K. M., Chappell, W. H., Horn, S., Bäsecke, J., Cervello, M., Nicoletti, F., Libra, M., Stivala, F., Martelli, A. M., et al. (2008) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.12.9.1139 · Cited by 145
“The 90 kDa ribosomal six kinase 1 (p90 Rsk1 ) is one such substrate [99-106] .”
Dual Leucine Zipper-bearing Kinase (DLK) Activates p46SAPK and p38 but Not ERK2
Fan, G., Merritt, S. E., Kortenjann, M., Shaw, P. E., & Holzman, L. B. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.40.24788 · Cited by 140
α-Synuclein Affects the MAPK Pathway and Accelerates Cell Death
Iwata, A., Maruyama, M., Kanazawa, I., & Nukina, N. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103736200 · Cited by 139
Chan, E. D., Winston, B. W., Uh, S., Wynes, M. W., Rose, D. M., & Riches, D. W. H. (1999) · PubMed · Cited by 139
Radiation-Induced Signal Transduction and Stress Response
Haimovitz‐Friedman, A. (1998) · Radiation Research · doi:10.2307/3579812 · Cited by 138
SAPKs regulation of ischemic preconditioning
Sato, M., Cordis, G. A., Maulik, N., & Das, D. K. (2000) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2000.279.3.h901 · Cited by 137
“Recently, two MAP kinase kinases (MKK3 and MKK4) have been discovered, the former being specific for p38 MAP kinase whereas the latter can activate both p38 and JNK MAP kinases (5).”
BackgroundGenome‐wide identification of miR‐200 targets reveals a regulatory network controlling cell invasion
Bracken, C. P., Li, X., Wright, J. A., Lawrence, D., Pillman, K. A., Salmanidis, M., Anderson, M. A., Dredge, B. K., Gregory, P. A., Tsykin, A., et al. (2014) · The EMBO Journal · doi:10.15252/embj.201488641 · Cited by 139
Tanaka‐Hino, M., Sagasti, A., Hisamoto, N., Kawasaki, M., Nakano, S., Ninomiya‐Tsuji, J., Bargmann, C. I., & Matsumoto, K. (2002) · EMBO Reports · doi:10.1093/embo-reports/kvf001 · Cited by 136
“MKK3 and MKK6 are specific activators of p38, whereas MKK4 can activate both the JNK and p38 subgroups of the MAPK superfamily (Derijard et al., 1995; Moriguchi et al., 1996; Stein et al., 1996).”
BackgroundA Regulatory Role for p38δ MAPK in Keratinocyte Differentiation
Efimova, T., Broome, A., & Eckert, R. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302759200 · Cited by 135
RetractedKinloch, R. A., Treherne, J. M., Furness, L. M., & Hajimohammadreza, I. (1999) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(98)01277-2 · Cited by 133
Signaling Angiogenesis via p42/p44 MAP Kinase Cascade
Pagès, G., Milanini, J., Richard, D. E., Berra, E., Gothié, E., Viñals, F., & Pouysségur, J. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06313.x · Cited by 133
Cuenda, A., Alonso, G., MORRICE, N. A., Jones, M. H., Meier, R., Cohen, P. T. W., & Nebreda, Á. R. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00790.x · Cited by 135
Tanaka, S., Ouchi, T., & Hanafusa, H. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.6.2356 · Cited by 134
Cadet, J. L., Jayanthi, S., & Deng, X. (2005) · Neurotoxicity Research · doi:10.1007/bf03033973 · Cited by 134
“Other upstream members of the JNK pathway including CrkII whose SH2 and SH3 domains bind to JNK (Yoshizumi et al., 2000) and MKK4 ( Derijard et al., 1995 ) or MKK7 (Moriguchi et al., 1997) which phosphorylate JNK also showed increased expression after METH treatment.”
BackgroundThe p38 Kinases MKK4 and MKK6 Suppress Metastatic Colonization in Human Ovarian Carcinoma
Hickson, J. A., Huo, D., Griend, D. J. V., Lin, A., Rinker-Schaeffer, C. W., & Yamada, S. D. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3676 · Cited by 132
Pandey, P., Avraham, S., Kumar, S., Nakazawa, A., Place, A. E., Ghanem, L. R., Rana, A., Kumar, V., Majumder, P. K., Avraham, H. K., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.15.10140 · Cited by 132
Self-citationZhang, 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
Self-citationNorris, J. L., & Baldwin, A. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.20.13841 · Cited by 132
Abbott, D. W., & Holt, J. T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.5.2732 · Cited by 131
Current Understanding of Sepsis
Wenzel, R. P., Pinsky, M. R., Ulevitch, R. J., & Young, L. D. (1996) · Clinical Infectious Diseases · doi:10.1093/clinids/22.3.407 · Cited by 130
“This protein, named p38, is activated by pathways distinct from those resulting in activation of another group of MAP kinases, the ERK family of proteins [34].”
BackgroundSelf-citationPedram, A., Razandi, M., & Levin, E. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202391200 · Cited by 129
Biphasic Regulation of Leukocyte Superoxide Generation by Nitric Oxide and Peroxynitrite
Lee, C.-I., Miura, K., Liu, X., & Zweier, J. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006341200 · Cited by 129
TAK1/JNK and p38 have opposite effects on rat hepatic stellate cells
Schnabl, B., Bradham, C. A., Bennett, B. L., Manning, A. M., Stefanovic, B., & Brenner, D. A. (2001) · Hepatology · doi:10.1053/jhep.2001.28790 · Cited by 129
“43 Whole cell extracts (25 g) were incubated with recombinant substrate protein glutathione S-transferase (GST)c-Jun (1-79).”
MethodExtracellular 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
Activation of p38 Mitogen-activated Protein Kinase by c-Abl-dependent and -independent Mechanisms
Pandey, P., Raingeaud, J., Kaneki, M., Weichselbaum, R. R., Davis, R. J., Kufe, D. W., & Kharbanda, S. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.39.23775 · Cited by 128
Self-citationSelectivity 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
Cho, M. K., Jang, Y. P., Kim, Y. C., & Kim, S. G. (2004) · International Immunopharmacology · doi:10.1016/j.intimp.2004.06.011 · Cited by 127
Du, J., Suzuki, H., Nagase, F., Akhand, A. A., Ma, X., Yokoyama, T., Miyata, T., & Nakashima, I. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00611-6 · Cited by 127
Cocolakis, E., Lemay, S., Ali, S., & Lebrun, J. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010768200 · Cited by 129
Fujishiro, M., Gotoh, Y., Katagiri, H., Sakoda, H., Ogihara, T., Anai, M., Onishi, Y., Ono, H., Funaki, M., Inukai, K., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101087200 · Cited by 126
Role of p38-Mitogen-Activated Protein Kinase in Spontaneous Apoptosis of Human Neutrophils
Aoshiba, K., Yasui, S., Hayashi, M., Tamaoki, J., & Nagai, A. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.3.1692 · Cited by 127
Caffrey, D. R., O'Neill, L. A. J., & Shields, D. C. (1999) · Journal of Molecular Evolution · doi:10.1007/pl00006578 · Cited by 124
“In contrast, it is unclear if MKK4 activates p38 isoforms, while it seems conclusive that MKK4 phosphorylatesJNK (Derijard et al. 1995; Enslen et al. 1998; Goedert et al. 1997; Guan et al. 1998; Jiang et al. 1997; Lin et al. 1995; Sanchez et al. 1994; Wang et al. 1997a).”
BackgroundRobidoux, J., Cao, W., Quan, H. Y., Daniel, K. W., Moukdar, F., Bai, X., Floering, L. M., & Collins, S. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.13.5466-5479.2005 · Cited by 122
Mitogen-Activated Protein Kinase
Adam, L. P. (1996) · Elsevier eBooks · doi:10.1016/b978-012078160-7/50016-0 · Cited by 131
Levi, N. L., Hanoch, T., Benard, O., Rozenblat, M., Harris, D., Reiss, N. A., Naor, Z., & Seger, R. (1998) · Molecular Endocrinology · doi:10.1210/mend.12.6.0120 · Cited by 126
“Interestingly, MKK4 [SEK1 (12, 13)] activates both JNK and p38RK, thus indicating the existence of some cross-talk between the cascades in mammalian cells.”
BackgroundNishina, H., Bachmann, M. F., Oliveira-dos-Santos, A., Kozieradzki, I., Fischer, K., Odermatt, B., Wakeham, A. C., Shahinian, A., Takimoto, H., Bernstein, A., et al. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.186.6.941 · Cited by 126
Malek, R. L., Toman, R. E., Edsall, L. C., Wong, S. C., Chiu, J., Letterle, C. A., Brocklyn, J. R. V., Milstien, S., Spiegel, S., & Lee, N. H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m003964200 · Cited by 125
Chan, E. D., Winston, B. W., Uh, S., Wynes, M. W., Rose, D. M., & Riches, D. W. H. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.1.415 · Cited by 125
Identification of MAP Kinase Domains by Redirecting Stress Signals into Growth Factor Responses
Brunet, A., & Pouysségur, J. (1996) · Science · doi:10.1126/science.272.5268.1652 · Cited by 125
Activation of the AP-1 transcription factor by inflammatory cytokines of the TNF family.
Kyriakis, J. M. (1999) · Europe PMC (PubMed Central) · Cited by 124
Lu, X., Bocangel, D., Nannenga, B., Yamaguchi, H., Appella, E., & Donehower, L. A. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.08.007 · Cited by 125
PKC-dependent activation of p46/p54 JNKs during ischemic preconditioning in conscious rabbits
Ping, P., Zhang, J., Huang, S., Cao, X., Tang, X., Li, R. C. X., Zheng, Y.-T., Qiu, Y., Clerk, A., Sugden, P. H., et al. (1999) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1999.277.5.h1771 · Cited by 122
Self-citationRegulation of MAP kinases by docking domains
Enslen, H., & Davis, R. J. (2001) · Biology of the Cell · doi:10.1016/s0248-4900(01)01156-x · Cited by 124
“, 1999), while MKK4 phosphorylates members of the JNK family and also p38α MAP kinase (Derijard et al., 1995; Enslen et al., 1998; Yang et al., 1997).”
BackgroundSelf-citationPiao, C. S., Kim, J., Han, P., & Lee, J. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10671 · Cited by 123
“The activation of p38 MAPK is regulated tightly by dual-specificity MAPK kinases (MKKs), MKK3 and MKK6 (Derijard et al., 1995), whose activation is controlled in turn by various upstream kinases including the MAPK/ERK kinase kinase family and mixedlineage kinase (Widmann et al., 1999).”
BackgroundQuercetin Prevents LPS-Induced High-Mobility Group Box 1 Release and Proinflammatory Function
Tang, D., Kang, R., Xiao, W., Zhang, H., Lotze, M. T., Wang, H., & Xiao, X. (2009) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2008-0119oc · Cited by 124
“, TNF-a and HMGB1] [19, 47–49, 65–67]), and nuclear translocation of NF-kB, a transcription factor that enhances the transcription of TNF-a and HMGB1 products of the activated macrophage (19, 49, 50, 68).”
BackgroundThe p38 Mitogen-Activated Protein Kinase Is Required for IL-12-Induced IFN-γ Expression
Zhang, S., & Kaplan, M. H. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.3.1374 · Cited by 128
Ishida, T., Takahashi, M., Corson, M. A., & Berk, B. C. (1997) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1997.tb51984.x · Cited by 123
Alford, K. A., Glennie, S. J., Turrell, B. R., Rawlinson, L. M., Saklatvala, J., & Dean, J. L. E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610987200 · Cited by 123
From Vanadis to Atropos: vanadium compounds as pharmacological tools in cell death signalling
Morinville, A., Maysinger, D., & Shaver, A. G. (1998) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(98)01257-7 · Cited by 121
Engelman, J. A., Berg, A. H., Lewis, R. Y., Lin, A., Lisanti, M. P., & Scherer, P. E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.50.35630 · Cited by 122
Meier, R., Rouse, J. W., Cuenda, A., Nebreda, Á. R., & Cohen, P. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.00796.x · Cited by 122
Son, Y., Jeong, Y.-T., Lee, K.-A., Choi, K.-H., Kim, S., Rhim, B.-Y., & Kim, K. (2008) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0b013e31815bd23d · Cited by 121
“Davis (University of Massachusetts Medical School, Worcester, MA).(19,20) Dominant-negative MKK1 (K97M) was from Dr.”
Backgroundp38 MAP KINASE REGULATES TNF-α PRODUCTION IN HUMAN ASTROCYTES AND MICROGLIA BY MULTIPLE MECHANISMS
Lee, Y. B., Schrader, J. W., & Kim, S. U. (2000) · Cytokine · doi:10.1006/cyto.2000.0688 · Cited by 121
Roach, S. K., & Schorey, J. S. (2002) · Infection and Immunity · doi:10.1128/iai.70.6.3040-3052.2002 · Cited by 120
“Although distinct in their activation (20), there is considerable cooperation between these kinases, and many substrates are shared between pathways (14).”
BackgroundSeko, Y., Takahashi, N., Tobe, K., Kadowaki, T., & Yazaki, Y. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7570 · Cited by 120
Ferrer, I., Fríguls, B., Dalfó, E., & Planas, A. M. (2003) · Acta Neuropathologica · doi:10.1007/s00401-002-0661-2 · Cited by 119
“The p38 kinases are activated by dual phosphorylation mediated by MKKs [ 10 , 14, 54, 71, 72, 96].”
BackgroundBinding of Zinc Finger Protein ZPR1 to the Epidermal Growth Factor Receptor
Galcheva-Gargova, Z., Konstantinov, K. N., Wu, I., Klier, F. G., Barrett, T., & Davis, R. J. (1996) · Science · doi:10.1126/science.272.5269.1797 · Cited by 119
Self-citationMitogen-Activated Protein Kinase Kinase 4 (MKK4)
Cuenda, A. (2000) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(00)00003-0 · Cited by 119
Park, H.-S., Park, E., Kim, M.-S., Ahn, K., Kim, I. Y., & Choi, E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.4.2527 · Cited by 119
p38 MAPK Autophosphorylation Drives Macrophage IL-12 Production during Intracellular Infection
Kim, L., Rı́o, L. D., Butcher, B. A., Mogensen, T. H., Paludan, S. R., Flavell, R. A., & Denkers, E. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.7.4178 · Cited by 118
Acute renal failure. III. The role of growth factors in the process of renal regeneration and repair
Nigám, S. K., & Lieberthal, W. (2000) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.2000.279.1.f3 · Cited by 118
Role of p38 MAP kinase in endothelial cell alignment induced by fluid shear stress
Azuma, N., Akasaka, N., Kito, H., Ikeda, M., Gahtan, V., Sasajima, T., & Sumpio, B. E. (2001) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2001.280.1.h189 · Cited by 118
“Plasmids, the wild-type and dominant negative mutant of p38-a (p38 AGF) (6) cloned by pCMV5, were generous gifts from Dr. Roger Davis (Howard Hughes Medical Institute, University of Massachusetts Medical Center, MA).”
MethodLu, X., Nemoto, S., & Lin, A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.40.24751 · Cited by 118
Feedback regulation of p38 activity via ATF2 is essential for survival of embryonic liver cellsPreprint
Breitwieser, W., Lyons, S., Flenniken, A. M., Ashton, G., Bruder, G., Willington, M. A., Lacaud, G., Kouskoff, V., & Jones, N. (2007) · Genes & Development · doi:10.1101/gad.430207 · Cited by 118
“Deficiency in MKK4 (SEK1), a regulatory kinase for JNK and p38 (Derijard et al. 1995; Lin et al. 1995), leads to embryonic lethality between E11.”
BackgroundInvolvement of p38 in Apoptosis-associated Membrane Blebbing and Nuclear Condensation
Deschesnes, R. G., Huot, J., Valerie, K. C., & Landry, J. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.6.1569 · Cited by 120
“Recombinant Chinese hamster HSP27 and ATF2-glutathione S-transferase (GST) were purified from Escherichia coli transformed with appropriate plasmids (Landry et al., 1992; Dérijard et al., 1995).”
BackgroundMethodInfluentialYabu, T., Shiba, H., Shibasaki, Y., Nakanishi, T., Imamura, S., Touhata, K., & Yamashita, M. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.128 · Cited by 116
Morooka, H., Bonventre, J. V., Pombo, C. M., Kyriakis, J. M., & Force, T. L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.50.30084 · Cited by 116
Hamada, K., Takuwa, N., Yokoyama, K. K., & Takuwa, Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.11.6334 · Cited by 115
Engel, K., Schultz, H. S., Martin, F., Kotlyarov, A., Plath, K., Hahn, M. G., Heinemann, U., & Gaestel, M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.27213 · Cited by 114
MEK4 Function, Genistein Treatment, and Invasion of Human Prostate Cancer Cells
Xu, L., Ding, Y., Catàlona, W. J., Yang, X. J., Anderson, W. F., Jovanovic, B. D., Wellman, K., Killmer, J., Huang, X., Scheidt, K. A., et al. (2009) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djp227 · Cited by 111
Yu, R., Mandlekar, S., Tan, T., & Kong, A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.13.9612 · Cited by 112
Ackerley, S., Grierson, A. J., Banner, S. J., Perkinton, M. S., Brownlees, J., Byers, H. L., Ward, M. A., Thornhill, P., Hussain, K., Waby, J. S., et al. (2004) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2004.02.009 · Cited by 112
Johnson, R. A., Huong, S., & Huang, E. (2000) · Journal of Virology · doi:10.1128/jvi.74.3.1158-1167.2000 · Cited by 112
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 110
Evidence for Multiple Activators for Stress-activated Protein Kinases/c-Jun Amino-terminal Kinases.
Moriguchi, T., Kawasaki, H., Matsuda, S., Gotoh, Y., & Nishida, E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.22.12969 · Cited by 112
Deacon, K., & Blank, J. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.22.14489 · Cited by 111
Savinainen, A., Garcia, E. P., Dorow, D. S., Marshall, J. J., & Liu, Y. F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100190200 · Cited by 111
Cheng, H.-L., & Feldman, E. L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.23.14560 · Cited by 111
Zheng, C., Xiang, J., Hunter, T., & Lin, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.41.28966 · Cited by 110
Mitogen-activated protein kinase phosphatase-1 in rat arterial smooth muscle cell proliferation.
Lai, K., Wang, H., Lee, W. S., Jain, M. K., Lee, M. E., & Haber, E. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118949 · Cited by 110
“Because MAP kinase activation accompanies a number of cellular functions such as proliferation and differentiation (30, 31), we investigated whether MAP kinase is activated in response to balloon injury.”
BackgroundShapiro, P. S., Evans, J. N. G., Davis, R. J., & Posada, J. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.10.5750 · Cited by 110
Self-citationInteraction of the Grb10 Adapter Protein with the Raf1 and MEK1 Kinases
Nantel, A., Mohammad-Ali, K., Sherk, J., Posner, B. I., & Thomas, D. Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.17.10475 · Cited by 108
Cloning and Characterization of a Human STE20-like Protein Kinase with Unusual Cofactor Requirements
Schinkmann, K. A., & Blenis, J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.45.28695 · Cited by 109
Metadata
- Authors
- Dérijard, B., Raingeaud, J., Barrett, T., Wu, I.-H., Han, J., Ulevitch, R. J., & Davis, R. J.
- Affiliations
- University of Massachusetts Chan Medical School (US)
- Venue
- Science
- Published
- 1995-02-03
- Volume
- 267
- Issue
- 5198
- Pages
- 682-685
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1998487776
- Cited by
- 1,555
- References
- 29
- Citations by year
- 2026: 8 · 2025: 9 · 2024: 9 · 2023: 12 · 2022: 16 · 2021: 19 · 2020: 14 · 2019: 20 · 2018: 16 · 2017: 19 · 2016: 24 · 2015: 15 · 2014: 27 · 2013: 25 · 2012: 27
- FWCI
- 53.10
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ca058396-09)
- National Cancer Institute (CA 58396)
- National Institute of General Medical Sciences (GM 37696, P01GM037696)
- National Institute of Allergy and Infectious Diseases (AI 15136, R01AI015136)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Melanoma and MAPK Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Keywords
- MAPK signaling, MKK3, MKK4, p38 MAPK, ERK, JNK, signaling pathways, dual phosphorylation
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Cell Line, Cloning, Molecular, Enzyme Activation, Humans, Molecular Sequence Data, Phosphorylation, Protein-Tyrosine Kinases, Substrate Specificity, Transfection, Signal Transduction, Protein Serine-Threonine Kinases, Calcium-Calmodulin-Dependent Protein Kinases, Mitogen-Activated Protein Kinase 1, Mitogen-Activated Protein Kinases, Mitogen-Activated Protein Kinase Kinases, JNK Mitogen-Activated Protein Kinases, p38 Mitogen-Activated Protein Kinases, MAP Kinase Kinase 3, MAP Kinase Kinase 4
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review