메뉴 건너뛰기




Volumn 7, Issue 1, 1997, Pages 67-74

MEKKs, GCKs, MLKs, PAKs, TAKs, and Tpls: Upstream regulators of the c-Jun amino-terminal kinases?

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE; GROWTH FACTOR; HORMONE; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHOTRANSFERASE; PROTEIN P21; TRANSFORMING GROWTH FACTOR BETA;

EID: 0031044561     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(97)80111-6     Document Type: Article
Times cited : (300)

References (58)
  • 1
    • 0028333768 scopus 로고
    • Sequential protein kinase reactions controlling cell growth and differentiation
    • Johnson GL, Vaillancourt RR. Sequential protein kinase reactions controlling cell growth and differentiation. Curr Opin Cell Biol. 6:1994;230-238.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 230-238
    • Johnson, G.L.1    Vaillancourt, R.R.2
  • 2
    • 0029011218 scopus 로고
    • The MAPK signaling cascade
    • Seger R, Krebs EG. The MAPK signaling cascade. FASEB J. 9:1995;726-735.
    • (1995) FASEB J , vol.9 , pp. 726-735
    • Seger, R.1    Krebs, E.G.2
  • 5
    • 0028880006 scopus 로고
    • Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis
    • of special interest. See annotation [8].
    • Xia Z, Dickens M, Raingeaud J, Davis RJ, Greenberg ME. Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. of special interest Science. 270:1995;1326-1331 See annotation [8].
    • (1995) Science , vol.270 , pp. 1326-1331
    • Xia, Z.1    Dickens, M.2    Raingeaud, J.3    Davis, R.J.4    Greenberg, M.E.5
  • 7
    • 0030298294 scopus 로고    scopus 로고
    • Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-κB activation prevents cell death
    • Liu Z, Hsu H, Goeddel DV, Karin M. Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-κB activation prevents cell death. Cell. 87:1996;565-576.
    • (1996) Cell , vol.87 , pp. 565-576
    • Liu, Z.1    Hsu, H.2    Goeddel, D.V.3    Karin, M.4
  • 8
    • 0029892754 scopus 로고    scopus 로고
    • Fibroblast growth factor-2 suppression of tumor necrosis factor α-mediated apoptosis requires ras and the activation of mitogen-activated protein kinase
    • of special interest. These two papers [5,8] provide good examples of the biological importance of MAPK pathway integration on the determination of cell fate and overall commitment to apoptosis.
    • Gardner AM, Johnson GL. Fibroblast growth factor-2 suppression of tumor necrosis factor α-mediated apoptosis requires ras and the activation of mitogen-activated protein kinase. of special interest J Biol Chem. 271:1996;14560-14566 These two papers [5,8] provide good examples of the biological importance of MAPK pathway integration on the determination of cell fate and overall commitment to apoptosis.
    • (1996) J Biol Chem , vol.271 , pp. 14560-14566
    • Gardner, A.M.1    Johnson, G.L.2
  • 9
    • 0028985079 scopus 로고
    • MAP kinase pathways in yeast: For mating and more
    • of outstanding interest. An excellent description of MAPK signaling modules in budding and fission yeast. The primary focus of this review revolves around pathways linking seven transmembrance receptors to six distinct MAPK pathways, mechanistically describing the components of each and their regulation. This review provides insight into specificity of signal transduction events in unicellular organisms which can be utilized to understand better the regulation of MAPK pathways in metazoan systems.
    • Herskowitz I. MAP kinase pathways in yeast: for mating and more. of outstanding interest Cell. 80:1995;187-197 An excellent description of MAPK signaling modules in budding and fission yeast. The primary focus of this review revolves around pathways linking seven transmembrance receptors to six distinct MAPK pathways, mechanistically describing the components of each and their regulation. This review provides insight into specificity of signal transduction events in unicellular organisms which can be utilized to understand better the regulation of MAPK pathways in metazoan systems.
    • (1995) Cell , vol.80 , pp. 187-197
    • Herskowitz, I.1
  • 10
    • 0028935974 scopus 로고
    • Independent human MAP kinase signal transduction pathways defined by MEK and MKK isoforms
    • of special interest. This report provides evidence that MKK3 and MKK4 are upstream regulators of p38/HOG1 and MKK4 regulates JNK, demonstrating that unique MKK isoforms regulate distinct MAPK pathways. In addition to illustrating the specificity of signal transduction events that is inherent to the MAPK pathways, this paper also provides a unique comparison of the primary structure of the first four MKK (MEK1, MEK2, MKK3, and MKK4) genes which were cloned.
    • Derijard B, Raingeaud J, Barrett T, Wu, Han J, Ulevitch RJ, Davis RJ. Independent human MAP kinase signal transduction pathways defined by MEK and MKK isoforms. of special interest Science. 267:1995;682-685 This report provides evidence that MKK3 and MKK4 are upstream regulators of p38/HOG1 and MKK4 regulates JNK, demonstrating that unique MKK isoforms regulate distinct MAPK pathways. In addition to illustrating the specificity of signal transduction events that is inherent to the MAPK pathways, this paper also provides a unique comparison of the primary structure of the first four MKK (MEK1, MEK2, MKK3, and MKK4) genes which were cloned.
    • (1995) Science , vol.267 , pp. 682-685
    • Derijard, B.1    Raingeaud, J.2    Barrett, T.3    Wu4    Han, J.5    Ulevitch, R.J.6    Davis, R.J.7
  • 13
    • 0029913457 scopus 로고    scopus 로고
    • Molecular cloning of mitogen-activated protein/ERK kinase kinases (MEKK) 2 and 3
    • Blank JL, Gerwins P, Elliott EM, Sather S, Johnson GL. Molecular cloning of mitogen-activated protein/ERK kinase kinases (MEKK) 2 and 3. J Biol Chem. 271:1996;5361-5368.
    • (1996) J Biol Chem , vol.271 , pp. 5361-5368
    • Blank, J.L.1    Gerwins, P.2    Elliott, E.M.3    Sather, S.4    Johnson, G.L.5
  • 14
    • 0030024707 scopus 로고    scopus 로고
    • Activation of the JNK pathway by distantly related protein kinases, MEKK and MUK
    • Hirai S, Izawa M, Osada S, Spyrou G, Ohno S. Activation of the JNK pathway by distantly related protein kinases, MEKK and MUK. Oncogene. 12:1996;641-650.
    • (1996) Oncogene , vol.12 , pp. 641-650
    • Hirai, S.1    Izawa, M.2    Osada, S.3    Spyrou, G.4    Ohno, S.5
  • 16
    • 0029760613 scopus 로고    scopus 로고
    • The mixed lineage kinase SPRK phosphorylates and activates the stress-activated protein kinase activator, SEK-1
    • Rana A, Gallo K, Godowski P, Hirai S, Ohno S, Zon L, Kyriakis JM, Avruch J. The mixed lineage kinase SPRK phosphorylates and activates the stress-activated protein kinase activator, SEK-1. J Biol Chem. 271:1996;19025-19028.
    • (1996) J Biol Chem , vol.271 , pp. 19025-19028
    • Rana, A.1    Gallo, K.2    Godowski, P.3    Hirai, S.4    Ohno, S.5    Zon, L.6    Kyriakis, J.M.7    Avruch, J.8
  • 17
    • 0029913510 scopus 로고    scopus 로고
    • Signaling from the small GTP-binding proteins Rac1 and Cdc42 to the c-Jun N-terminal kinase/stress activated protein kinase pathway
    • of special interest. In this paper, the authors question the ability of PAK to stimulate JNK activity and demonstrate a pronounced JNK activation by MLK3. Furthermore, MLK3 was shown to bind to Cdc42 and Rac in a GTP-dependent manner and lie downstream of these low molecular weight GTP-binding proteins in the JNK pathway.
    • Teramoto H, Coso OA, Miyata H, Igishi T, Miki T, Gutkind JS. Signaling from the small GTP-binding proteins Rac1 and Cdc42 to the c-Jun N-terminal kinase/stress activated protein kinase pathway. of special interest J Biol Chem. 271:1996;27225-27228 In this paper, the authors question the ability of PAK to stimulate JNK activity and demonstrate a pronounced JNK activation by MLK3. Furthermore, MLK3 was shown to bind to Cdc42 and Rac in a GTP-dependent manner and lie downstream of these low molecular weight GTP-binding proteins in the JNK pathway.
    • (1996) J Biol Chem , vol.271 , pp. 27225-27228
    • Teramoto, H.1    Coso, O.A.2    Miyata, H.3    Igishi, T.4    Miki, T.5    Gutkind, J.S.6
  • 18
    • 0028670788 scopus 로고
    • Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1
    • Yan M, Dal T, Deak JC, Kyriakis JM, Zon LI, Woodgett JR, Templeton TJ. Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1. Nature. 372:1994;798-800.
    • (1994) Nature , vol.372 , pp. 798-800
    • Yan, M.1    Dal, T.2    Deak, J.C.3    Kyriakis, J.M.4    Zon, L.I.5    Woodgett, J.R.6    Templeton, T.J.7
  • 19
    • 0028862297 scopus 로고
    • Molecular cloning of a new member of the p21-Cdc42/Rac-activated kinase (PAK) family
    • Manser E, Chong C, Zhao Z, Leung T, Michael G, Lim L. Molecular cloning of a new member of the p21-Cdc42/Rac-activated kinase (PAK) family. J Biol Chem. 270:1995;25070-25078.
    • (1995) J Biol Chem , vol.270 , pp. 25070-25078
    • Manser, E.1    Chong, C.2    Zhao, Z.3    Leung, T.4    Michael, G.5    Lim, L.6
  • 20
    • 0028078824 scopus 로고
    • A brain serine/threonine protein kinase activated by Cdc42 and Rac1
    • Manser E, Leung T, Salihuddin H, Zhao Z, Lim L. A brain serine/threonine protein kinase activated by Cdc42 and Rac1. Nature. 367:1994;40-46.
    • (1994) Nature , vol.367 , pp. 40-46
    • Manser, E.1    Leung, T.2    Salihuddin, H.3    Zhao, Z.4    Lim, L.5
  • 21
    • 0029056399 scopus 로고
    • A novel serine kinase activated by rac1/CDC42Hs-dependent autophosphorylation is related to PAK65 and STE20
    • Martin GA, Bollag G, McCormick F, Abo A. A novel serine kinase activated by rac1/CDC42Hs-dependent autophosphorylation is related to PAK65 and STE20. EMBO J. 14:1995;1970-1978.
    • (1995) EMBO J , vol.14 , pp. 1970-1978
    • Martin, G.A.1    Bollag, G.2    McCormick, F.3    Abo, A.4
  • 22
    • 0029055812 scopus 로고
    • The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway
    • of outstanding interest. This paper characterizes the low molecular weight GTP-binding proteins that control the JNK pathway, demonstrating that Cdc42 and Rac - as well as the oncogenic exchange factors for these molecules - can activate JNK. Using dominant inhibitory mutants, the authors also demonstrate that that Cdc42 and Rac were critical for the induction of JNK activity by growth factors and cytokines. This report, thus, provides a nice demonstration of diverging signal transduction events that regulate sequential MAPK signal transduction pathways.
    • Coso OA, Chiarello M, Yu J, Teramoto H, Crespo P, Xu N, Miki T, Gutkind JS. The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway. of outstanding interest Cell. 81:1995;1137-1146 This paper characterizes the low molecular weight GTP-binding proteins that control the JNK pathway, demonstrating that Cdc42 and Rac - as well as the oncogenic exchange factors for these molecules - can activate JNK. Using dominant inhibitory mutants, the authors also demonstrate that that Cdc42 and Rac were critical for the induction of JNK activity by growth factors and cytokines. This report, thus, provides a nice demonstration of diverging signal transduction events that regulate sequential MAPK signal transduction pathways.
    • (1995) Cell , vol.81 , pp. 1137-1146
    • Coso, O.A.1    Chiarello, M.2    Yu, J.3    Teramoto, H.4    Crespo, P.5    Xu, N.6    Miki, T.7    Gutkind, J.S.8
  • 23
    • 0029070887 scopus 로고
    • Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs
    • of outstanding interest. of special interest. See annotation [22].
    • of outstanding interest Minden A, Lin A, Claret F, Abo A, Karin M. Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs. of special interest Cell. 81:1995;1147-1157 See annotation [22].
    • (1995) Cell , vol.81 , pp. 1147-1157
    • Minden, A.1    Lin, A.2    Claret, F.3    Abo, A.4    Karin, M.5
  • 24
    • 0029968827 scopus 로고    scopus 로고
    • Rho family GTPases: The cytoskeleton and beyond
    • Symons M. Rho family GTPases: the cytoskeleton and beyond. Trends Biochem Sci. 21:1996;178-181.
    • (1996) Trends Biochem Sci , vol.21 , pp. 178-181
    • Symons, M.1
  • 25
    • 0029145073 scopus 로고
    • Rho family members: Activators of MAP kinase cascades
    • Vojtek AB, Cooper JA. Rho family members: activators of MAP kinase cascades. Cell. 82:1995;527-529.
    • (1995) Cell , vol.82 , pp. 527-529
    • Vojtek, A.B.1    Cooper, J.A.2
  • 26
    • 0028820587 scopus 로고
    • Rho family GTPases regulates p38 mitogen-activated protein kinase through the downstream mediator Pak1
    • Zhang S, Han J, Salls MA, Chernoff J, Knaus UG, Ulevitch RJ, Bokoch GM. Rho family GTPases regulates p38 mitogen-activated protein kinase through the downstream mediator Pak1. J Biol Chem. 270:1995;23934-23936.
    • (1995) J Biol Chem , vol.270 , pp. 23934-23936
    • Zhang, S.1    Han, J.2    Salls, M.A.3    Chernoff, J.4    Knaus, U.G.5    Ulevitch, R.J.6    Bokoch, G.M.7
  • 27
    • 0028935270 scopus 로고
    • Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine
    • Raingeaud J, Gupta S, Rogers JS, Dickens M, Han J, Ulevitch RJ, Davis RJ. Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine. J Biol Chem. 270:1995;7420-7426.
    • (1995) J Biol Chem , vol.270 , pp. 7420-7426
    • Raingeaud, J.1    Gupta, S.2    Rogers, J.S.3    Dickens, M.4    Han, J.5    Ulevitch, R.J.6    Davis, R.J.7
  • 28
    • 0029967151 scopus 로고    scopus 로고
    • Activation of a p38 mitogen-activated kinase in human neutrophils by lipopolysaccharide
    • Nick JA, Avdi NJ, Gerwins P, Johnson GL, Worthen GS. Activation of a p38 mitogen-activated kinase in human neutrophils by lipopolysaccharide. J Immunol. 156:1996;4867-4875.
    • (1996) J Immunol , vol.156 , pp. 4867-4875
    • Nick, J.A.1    Avdi, N.J.2    Gerwins, P.3    Johnson, G.L.4    Worthen, G.S.5
  • 29
    • 0029938805 scopus 로고    scopus 로고
    • Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP kinase
    • Wang X, Ron D. Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP kinase. Science. 272:1996;1347-1349.
    • (1996) Science , vol.272 , pp. 1347-1349
    • Wang, X.1    Ron, D.2
  • 30
    • 0029907265 scopus 로고    scopus 로고
    • A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation
    • Dikic I, Tokiwa G, Lev S, Courtneidge S, Schlessinger J. A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation. Nature. 383:1996;547-550.
    • (1996) Nature , vol.383 , pp. 547-550
    • Dikic, I.1    Tokiwa, G.2    Lev, S.3    Courtneidge, S.4    Schlessinger, J.5
  • 31
    • 0029770721 scopus 로고    scopus 로고
    • Activation of Pyk2 by stress signals and coupling with JNK signaling pathway
    • Tokiwa G, Dikic SL, Schlessinger J. Activation of Pyk2 by stress signals and coupling with JNK signaling pathway. Science. 273:1996;792-794.
    • (1996) Science , vol.273 , pp. 792-794
    • Tokiwa, G.1    Dikic, S.L.2    Schlessinger, J.3
  • 32
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • Cohen GB, Ren R, Baltimore D. Modular binding domains in signal transduction proteins. Cell. 80:1995;237-248.
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 34
    • 0029942952 scopus 로고    scopus 로고
    • Cloning of rat MEK kinase 1 cDNA reveals an endogenous membrane-associated 195-kDa protein with a large regulatory domain
    • Xu S, Robbins DJ, Christerson LB, English JM, Vanderbilt CA, Cobb MH. Cloning of rat MEK kinase 1 cDNA reveals an endogenous membrane-associated 195-kDa protein with a large regulatory domain. Proc Natl Acad Sci USA. 93:1996;5291-5295.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5291-5295
    • Xu, S.1    Robbins, D.J.2    Christerson, L.B.3    English, J.M.4    Vanderbilt, C.A.5    Cobb, M.H.6
  • 35
    • 0029077563 scopus 로고
    • Direct interaction between Ras and the kinase domain of mitogen-activated protein kinase kinase kinase (MEKK1)
    • Russell M, Lange-Carter CA, Johnson CL. Direct interaction between Ras and the kinase domain of mitogen-activated protein kinase kinase kinase (MEKK1). J Biol Chem. 270:1995;11757-11760.
    • (1995) J Biol Chem , vol.270 , pp. 11757-11760
    • Russell, M.1    Lange-Carter, C.A.2    Johnson, C.L.3
  • 36
    • 0028074621 scopus 로고
    • Ras-dependent growth factor regulation of MEK kinase in PC12 cells
    • Lange-Carter CA, Johnson GL. Ras-dependent growth factor regulation of MEK kinase in PC12 cells. Science. 265:1994;1458-1461.
    • (1994) Science , vol.265 , pp. 1458-1461
    • Lange-Carter, C.A.1    Johnson, G.L.2
  • 37
    • 0029666270 scopus 로고    scopus 로고
    • Aggregation of the FcεRI on mast cells stimulates c-Jun amino-terminal kinase activity
    • Ishizuka T, Oshiba A, Sakata N, Johnson GL, Gelfand EW. Aggregation of the FcεRI on mast cells stimulates c-Jun amino-terminal kinase activity. J Biol Chem. 271:1996;12762-12766.
    • (1996) J Biol Chem , vol.271 , pp. 12762-12766
    • Ishizuka, T.1    Oshiba, A.2    Sakata, N.3    Johnson, G.L.4    Gelfand, E.W.5
  • 38
    • 0029879315 scopus 로고    scopus 로고
    • Interaction between c-Rel and the mitogen activated protein kinase kinase kinase 1 signaling cascade in mediating κb enhancer activation
    • Meyer CF, Wang X, Chang C, Templeton D, Tan T. Interaction between c-Rel and the mitogen activated protein kinase kinase kinase 1 signaling cascade in mediating κB enhancer activation. J Biol Chem. 271:1996;8971-8976.
    • (1996) J Biol Chem , vol.271 , pp. 8971-8976
    • Meyer, C.F.1    Wang, X.2    Chang, C.3    Templeton, D.4    Tan, T.5
  • 41
    • 0028279796 scopus 로고
    • Differential expression of a novel protein kinase in human lymphocytes
    • Katz P, Whalen G, Kehrl JH. Differential expression of a novel protein kinase in human lymphocytes. J Biol Chem. 269:1994;16802-16809.
    • (1994) J Biol Chem , vol.269 , pp. 16802-16809
    • Katz, P.1    Whalen, G.2    Kehrl, J.H.3
  • 42
    • 0028842508 scopus 로고
    • Identification and molecular cloning of a p21cdc42/rac1 activated serine/threonine kinase that is rapidly activated by thrombin in platelets
    • Teo M, Manser E, Lim L. Identification and molecular cloning of a p21cdc42/rac1 activated serine/threonine kinase that is rapidly activated by thrombin in platelets. J Biol Chem. 270:1995;26690-26697.
    • (1995) J Biol Chem , vol.270 , pp. 26690-26697
    • Teo, M.1    Manser, E.2    Lim, L.3
  • 43
    • 0030298138 scopus 로고    scopus 로고
    • 1 cell cycle progression independently of p65PAK and the JNK/SAPK MAP kinase cascade
    • ROCK was unable to induce lamellipodia formation. This study, thus, refutes the concept that PAK is involved in cytoskeletal organization changes.
    • ROCK was unable to induce lamellipodia formation. This study, thus, refutes the concept that PAK is involved in cytoskeletal organization changes.
    • (1996) Cell , vol.87 , pp. 519-529
    • Lamarche, N.1    Tapon, N.2    Stowers, L.3    Burbelo, P.D.4    Aspenstrom, P.5    Bridges, T.6    Chant, J.7    Hall, A.8
  • 45
    • 0029558439 scopus 로고
    • Cloning and characterization of a member of the MST subfamily of Ste20-like kinases
    • Creasy CL, Chernoff J. Cloning and characterization of a member of the MST subfamily of Ste20-like kinases. Gene. 167:1995;303-306.
    • (1995) Gene , vol.167 , pp. 303-306
    • Creasy, C.L.1    Chernoff, J.2
  • 46
    • 0027312371 scopus 로고
    • Identification of new family of human epithelial protein kinases containing two leucine/isoleucine-zipper domains
    • Dorow DS, Devereux L, Dietzsh E, De Kretser T. Identification of new family of human epithelial protein kinases containing two leucine/isoleucine-zipper domains. Eur J Biochem. 213:1993;701-710.
    • (1993) Eur J Biochem , vol.213 , pp. 701-710
    • Dorow, D.S.1    Devereux, L.2    Dietzsh, E.3    De Kretser, T.4
  • 47
    • 0028140164 scopus 로고
    • PTK1, a novel protein kinase required for proliferation of human melanocytes
    • Ezoe K, Lee S, Strunk KM, Spritz RA. PTK1, a novel protein kinase required for proliferation of human melanocytes. Oncogene. 9:1994;935-938.
    • (1994) Oncogene , vol.9 , pp. 935-938
    • Ezoe, K.1    Lee, S.2    Strunk, K.M.3    Spritz, R.A.4
  • 48
    • 0028143060 scopus 로고
    • Identification, molecular cloning, and characterization of dual leucine-zipper bearing kinase
    • Holzman LB, Merritt SE, Fan G. Identification, molecular cloning, and characterization of dual leucine-zipper bearing kinase. J Biol Chem. 269:1994;30808-30817.
    • (1994) J Biol Chem , vol.269 , pp. 30808-30817
    • Holzman, L.B.1    Merritt, S.E.2    Fan, G.3
  • 49
    • 0028917384 scopus 로고
    • Cloning and characterization of MST, a novel (putative) serine/threonine kinase with SH3 domain
    • Katoh M, Hirai M, Sugimura T, Terada M. Cloning and characterization of MST, a novel (putative) serine/threonine kinase with SH3 domain. Oncogene. 10:1995;1447-1451.
    • (1995) Oncogene , vol.10 , pp. 1447-1451
    • Katoh, M.1    Hirai, M.2    Sugimura, T.3    Terada, M.4
  • 50
    • 0028037972 scopus 로고
    • Cloning of a novel putative protein kinase having a leucine zipper domain from human brain
    • Reddy UR, Pleasure D. Cloning of a novel putative protein kinase having a leucine zipper domain from human brain. Biochem Biophys Res Commun. 202:1994;613-620.
    • (1994) Biochem Biophys Res Commun , vol.202 , pp. 613-620
    • Reddy, U.R.1    Pleasure, D.2
  • 51
    • 0029101740 scopus 로고
    • Cloning and characterization of a human protein kinase with homology to Ste20
    • Creasy CL, Chernoff J. Cloning and characterization of a human protein kinase with homology to Ste20. J Biol Chem. 270:1995;21695-21700.
    • (1995) J Biol Chem , vol.270 , pp. 21695-21700
    • Creasy, C.L.1    Chernoff, J.2
  • 52
    • 0027447467 scopus 로고
    • Tumor progression locus 2 (Tpl-2) encodes a protein kinase involved in the progression of rodent T-cell lymphomas and in T-cell activation
    • Patrios C, Makris A, Bear SE, Tschilis PN. Tumor progression locus 2 (Tpl-2) encodes a protein kinase involved in the progression of rodent T-cell lymphomas and in T-cell activation. Proc Natl Acad Sci USA. 90:1993;2251-2255.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2251-2255
    • Patrios, C.1    Makris, A.2    Bear, S.E.3    Tschilis, P.N.4
  • 53
    • 0025778893 scopus 로고
    • Structure and transforming potential of the human cot oncogene encoding a putative protein kinase
    • Miyoshi J, Higashi T, Mukia H, Ohuchi T, Kakunaga T. Structure and transforming potential of the human cot oncogene encoding a putative protein kinase. Mol Cell Biol. 11:1991;4088-4096.
    • (1991) Mol Cell Biol , vol.11 , pp. 4088-4096
    • Miyoshi, J.1    Higashi, T.2    Mukia, H.3    Ohuchi, T.4    Kakunaga, T.5
  • 54
    • 0027937795 scopus 로고
    • Tpl-2 acts in concert with Raf-1 to activate mitogen-activated protein kinase
    • Patriotis C, Makris A, Chernoff J, Tsichilis PN. Tpl-2 acts in concert with Raf-1 to activate mitogen-activated protein kinase. Proc Natl Acad Sci USA. 91:1994;9755-9759.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9755-9759
    • Patriotis, C.1    Makris, A.2    Chernoff, J.3    Tsichilis, P.N.4
  • 55
    • 0030059508 scopus 로고    scopus 로고
    • Activation of MEK-1 and SEK-1 by Tpl-2 protoncoprotein, a novel MAP kinase kinase kinase
    • Salmeron A, Ahmad TB, Carlile GW, Pappin D, Narsimhan RP, Ley SC. Activation of MEK-1 and SEK-1 by Tpl-2 protoncoprotein, a novel MAP kinase kinase kinase. EMBO J. 15:1996;817-826.
    • (1996) EMBO J , vol.15 , pp. 817-826
    • Salmeron, A.1    Ahmad, T.B.2    Carlile, G.W.3    Pappin, D.4    Narsimhan, R.P.5    Ley, S.C.6
  • 57
    • 0029954102 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel protein kinase with a catalytic domain homologous to mitogen-activated protein kinase kinase kinase
    • Wang XS, Diener K, Jannuzzi D, Trollinger D, Tan T, Lichenstein H, Zukowski M, Yao Z. Molecular cloning and characterization of a novel protein kinase with a catalytic domain homologous to mitogen-activated protein kinase kinase kinase. J Biol Chem. 271:1996;31607-31611.
    • (1996) J Biol Chem , vol.271 , pp. 31607-31611
    • Wang, X.S.1    Diener, K.2    Jannuzzi, D.3    Trollinger, D.4    Tan, T.5    Lichenstein, H.6    Zukowski, M.7    Yao, Z.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.