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Volumn 405, Issue 5, 2011, Pages 1154-1169

Active mutants of the TCR-mediated p38α alternative activation site show changes in the phosphorylation lip and DEF site formation

Author keywords

alternative activation; MAP kinase; p38 ; signaling; T cells

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE 14; T LYMPHOCYTE RECEPTOR;

EID: 78751578955     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.11.023     Document Type: Article
Times cited : (15)

References (61)
  • 1
    • 0032928614 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase: Conservation of a three-kinase module from yeast to human
    • Widmann C., Gibson S., Jarpe M.B., and Johnson G.L. Mitogen-activated protein kinase: conservation of a three-kinase module from yeast to human Physiol. Rev. 79 1999 143 180
    • (1999) Physiol. Rev. , vol.79 , pp. 143-180
    • Widmann, C.1    Gibson, S.2    Jarpe, M.B.3    Johnson, G.L.4
  • 2
    • 0030828701 scopus 로고    scopus 로고
    • Characterization of the structure and function of the fourth member of p38 group mitogen-activated protein kinases, p38delta
    • Jiang Y., Gram H., Zhao M., New L., Gu J., and Feng L. Characterization of the structure and function of the fourth member of p38 group mitogen-activated protein kinases, p38delta J. Biol. Chem. 272 1997 30122 30128
    • (1997) J. Biol. Chem. , vol.272 , pp. 30122-30128
    • Jiang, Y.1    Gram, H.2    Zhao, M.3    New, L.4    Gu, J.5    Feng, L.6
  • 3
    • 0034653850 scopus 로고    scopus 로고
    • Molecular determinants that mediate selective activation of p38 MAP kinase isoforms
    • Enslen H., Brancho D.M., and Davis R.J. Molecular determinants that mediate selective activation of p38 MAP kinase isoforms EMBO J. 19 2000 1301 1311
    • (2000) EMBO J. , vol.19 , pp. 1301-1311
    • Enslen, H.1    Brancho, D.M.2    Davis, R.J.3
  • 4
    • 0030756286 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel p38 mitogen-activated protein kinase
    • Wang X.S., Diener K., Manthey C.L., Wang S., Rosenzweig B., and Bray J. Molecular cloning and characterization of a novel p38 mitogen-activated protein kinase J. Biol. Chem. 272 1997 23668 23674
    • (1997) J. Biol. Chem. , vol.272 , pp. 23668-23674
    • Wang, X.S.1    Diener, K.2    Manthey, C.L.3    Wang, S.4    Rosenzweig, B.5    Bray, J.6
  • 6
    • 0033548597 scopus 로고    scopus 로고
    • Murine p38-delta mitogen-activated protein kinase, a developmentally regulated protein kinase that is activated by stress and proinflammatory cytokines
    • Hu M.C., Wang Y.P., Mikhail A., Qiu W.R., and Tan T.H. Murine p38-delta mitogen-activated protein kinase, a developmentally regulated protein kinase that is activated by stress and proinflammatory cytokines J. Biol. Chem. 274 1999 7095 7102
    • (1999) J. Biol. Chem. , vol.274 , pp. 7095-7102
    • Hu, M.C.1    Wang, Y.P.2    Mikhail, A.3    Qiu, W.R.4    Tan, T.H.5
  • 7
    • 0036803602 scopus 로고    scopus 로고
    • In the cellular garden of forking paths: How p38 MAPKs signal for downstream assistance
    • Shi Y., and Gaestel M. In the cellular garden of forking paths: how p38 MAPKs signal for downstream assistance Biol. Chem. 383 2002 1519 1536
    • (2002) Biol. Chem. , vol.383 , pp. 1519-1536
    • Shi, Y.1    Gaestel, M.2
  • 8
    • 0028605318 scopus 로고
    • A protein kinase involved in the regulation of inflammatory cytokine biosynthesis
    • Lee J.C., Laydon J.T., McDonnell P.C., Gallagher T.F., Kumar S., and Green D. A protein kinase involved in the regulation of inflammatory cytokine biosynthesis Nature 372 1994 739 746
    • (1994) Nature , vol.372 , pp. 739-746
    • Lee, J.C.1    Laydon, J.T.2    McDonnell, P.C.3    Gallagher, T.F.4    Kumar, S.5    Green, D.6
  • 9
    • 0027936755 scopus 로고
    • A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells
    • Han J., Lee J.D., Bibbs L., and Ulevitch R.J. A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells Science 265 1994 808 811
    • (1994) Science , vol.265 , pp. 808-811
    • Han, J.1    Lee, J.D.2    Bibbs, L.3    Ulevitch, R.J.4
  • 10
    • 0031873505 scopus 로고    scopus 로고
    • Inhibition of apoptotic signaling pathways in cancer cells as a mechanism of chemotherapy resistance
    • Haq R., and Zanke B. Inhibition of apoptotic signaling pathways in cancer cells as a mechanism of chemotherapy resistance Cancer Metastasis Rev. 17 1998 233 239
    • (1998) Cancer Metastasis Rev. , vol.17 , pp. 233-239
    • Haq, R.1    Zanke, B.2
  • 11
    • 0033612303 scopus 로고    scopus 로고
    • Induction of GADD45 and JNK/SAPK-dependent apoptosis following inducible expression of BRCA1
    • Harkin D.P., Bean J.M., Miklos D., Song Y.H., Truong V.B., and Englert C. Induction of GADD45 and JNK/SAPK-dependent apoptosis following inducible expression of BRCA1 Cell 97 1999 575 586
    • (1999) Cell , vol.97 , pp. 575-586
    • Harkin, D.P.1    Bean, J.M.2    Miklos, D.3    Song, Y.H.4    Truong, V.B.5    Englert, C.6
  • 12
    • 0037034199 scopus 로고    scopus 로고
    • Hepatocyte growth factor/scatter factor activates proliferation in melanoma cells through p38 MAPK, ATF-2 and cyclin D1
    • Recio J.A., and Merlino G. Hepatocyte growth factor/scatter factor activates proliferation in melanoma cells through p38 MAPK, ATF-2 and cyclin D1 Oncogene 21 2002 1000 1008
    • (2002) Oncogene , vol.21 , pp. 1000-1008
    • Recio, J.A.1    Merlino, G.2
  • 14
    • 0036165251 scopus 로고    scopus 로고
    • Pharmacological inhibitors of MAPK pathways
    • English J.M., and Cobb M.H. Pharmacological inhibitors of MAPK pathways Trends Pharmacol. Sci. 23 2002 40 45
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 40-45
    • English, J.M.1    Cobb, M.H.2
  • 15
    • 0036715931 scopus 로고    scopus 로고
    • Pyridinylimidazole based p38 MAP kinase inhibitors
    • Jackson P.F., and Bullington J.L. Pyridinylimidazole based p38 MAP kinase inhibitors Curr. Top. Med. Chem. 2 2002 1011 1020
    • (2002) Curr. Top. Med. Chem. , vol.2 , pp. 1011-1020
    • Jackson, P.F.1    Bullington, J.L.2
  • 16
    • 0142026209 scopus 로고    scopus 로고
    • P38 MAP kinases: Key signalling molecules as therapeutic targets for inflammatory diseases
    • Kumar S., Boehm J., and Lee J.C. p38 MAP kinases: key signalling molecules as therapeutic targets for inflammatory diseases Nat. Rev., Drug Discov. 2 2003 717 726
    • (2003) Nat. Rev., Drug Discov. , vol.2 , pp. 717-726
    • Kumar, S.1    Boehm, J.2    Lee, J.C.3
  • 17
    • 0032143920 scopus 로고    scopus 로고
    • Stimulation of multiple mitogen-activated protein kinase sub-families by oxidative stress and phosphorylation of the small heat shock protein, HSP25/27, in neonatal ventricular myocytes
    • Clerk A., Michael A., and Sugden P.H. Stimulation of multiple mitogen-activated protein kinase sub-families by oxidative stress and phosphorylation of the small heat shock protein, HSP25/27, in neonatal ventricular myocytes Biochem. J. 333 1998 581 589
    • (1998) Biochem. J. , vol.333 , pp. 581-589
    • Clerk, A.1    Michael, A.2    Sugden, P.H.3
  • 18
    • 0030220456 scopus 로고    scopus 로고
    • P38/RK is essential for stress-induced nuclear responses: JNK/SAPKs and c-Jun/ATF-2 phosphorylation are insufficient
    • Hazzalin C.A., Cano E., Cuenda A., Barratt M.J., Cohen P., and Mahadevan L.C. p38/RK is essential for stress-induced nuclear responses: JNK/SAPKs and c-Jun/ATF-2 phosphorylation are insufficient Curr. Biol. 6 1996 1028 1031
    • (1996) Curr. Biol. , vol.6 , pp. 1028-1031
    • Hazzalin, C.A.1    Cano, E.2    Cuenda, A.3    Barratt, M.J.4    Cohen, P.5    Mahadevan, L.C.6
  • 19
    • 0033965158 scopus 로고    scopus 로고
    • The p38 signal transduction pathway: Activation and function
    • Ono K., and Han J. The p38 signal transduction pathway: activation and function Cell Signalling 12 2000 1 13
    • (2000) Cell Signalling , vol.12 , pp. 1-13
    • Ono, K.1    Han, J.2
  • 20
    • 0033614021 scopus 로고    scopus 로고
    • Insulin-like growth factor I-mediated activation of the transcription factor cAMP response element-binding protein in PC12 cells. Involvement of p38 mitogen-activated protein kinase-mediated pathway
    • Pugazhenthi S., Boras T., O'Connor D., Meintzer M.K., Heidenreich K.A., and Reusch J.E. Insulin-like growth factor I-mediated activation of the transcription factor cAMP response element-binding protein in PC12 cells. Involvement of p38 mitogen-activated protein kinase-mediated pathway J. Biol. Chem. 274 1999 2829 2837
    • (1999) J. Biol. Chem. , vol.274 , pp. 2829-2837
    • Pugazhenthi, S.1    Boras, T.2    O'Connor, D.3    Meintzer, M.K.4    Heidenreich, K.A.5    Reusch, J.E.6
  • 21
    • 0031594573 scopus 로고    scopus 로고
    • Nerve growth factor activates extracellular signal-regulated kinase and p38 mitogen-activated protein kinase pathways to stimulate CREB serine 133 phosphorylation
    • Xing J., Kornhauser J.M., Xia Z., Thiele E.A., and Greenberg M.E. Nerve growth factor activates extracellular signal-regulated kinase and p38 mitogen-activated protein kinase pathways to stimulate CREB serine 133 phosphorylation Mol. Cell. Biol. 18 1998 1946 1955
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1946-1955
    • Xing, J.1    Kornhauser, J.M.2    Xia, Z.3    Thiele, E.A.4    Greenberg, M.E.5
  • 22
    • 0035066383 scopus 로고    scopus 로고
    • Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation
    • Kyriakis J.M., and Avruch J. Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation Physiol. Rev. 81 2001 807 869
    • (2001) Physiol. Rev. , vol.81 , pp. 807-869
    • Kyriakis, J.M.1    Avruch, J.2
  • 24
    • 19644367000 scopus 로고    scopus 로고
    • Activation and signaling of the p38 MAP kinase pathway
    • Zarubin T., and Han J. Activation and signaling of the p38 MAP kinase pathway Cell Res. 15 2005 11 18
    • (2005) Cell Res. , vol.15 , pp. 11-18
    • Zarubin, T.1    Han, J.2
  • 25
    • 0037083375 scopus 로고    scopus 로고
    • MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha
    • Ge B., Gram H., Di Padova F., Huang B., New L., and Ulevitch R.J. MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha Science 295 2002 1291 1294
    • (2002) Science , vol.295 , pp. 1291-1294
    • Ge, B.1    Gram, H.2    Di Padova, F.3    Huang, B.4    New, L.5    Ulevitch, R.J.6
  • 26
    • 34848887761 scopus 로고    scopus 로고
    • Phosphatidylinositol ether lipid analogues that inhibit AKT also independently activate the stress kinase, p38alpha, through MKK3/6-independent and -dependent mechanisms
    • Gills J.J., Castillo S.S., Zhang C., Petukhov P.A., Memmott R.M., and Hollingshead M. Phosphatidylinositol ether lipid analogues that inhibit AKT also independently activate the stress kinase, p38alpha, through MKK3/6-independent and -dependent mechanisms J. Biol. Chem. 282 2007 27020 27029
    • (2007) J. Biol. Chem. , vol.282 , pp. 27020-27029
    • Gills, J.J.1    Castillo, S.S.2    Zhang, C.3    Petukhov, P.A.4    Memmott, R.M.5    Hollingshead, M.6
  • 28
    • 67650138623 scopus 로고    scopus 로고
    • T cell receptor-mediated activation of p38α by mono-phosphorylation of the activation loop results in altered substrate specificity
    • Mittelstadt P.R., Yamaguchi H., Appella E., and Ashwell J.D. T cell receptor-mediated activation of p38α by mono-phosphorylation of the activation loop results in altered substrate specificity J. Biol. Chem. 284 2009 15469 15474
    • (2009) J. Biol. Chem. , vol.284 , pp. 15469-15474
    • Mittelstadt, P.R.1    Yamaguchi, H.2    Appella, E.3    Ashwell, J.D.4
  • 29
    • 64049117360 scopus 로고    scopus 로고
    • Genetic disruption of p38alpha Tyr323 phosphorylation prevents T-cell receptor-mediated p38alpha activation and impairs interferon-gamma production
    • Jirmanova L., Sarma D.N., Jankovic D., Mittelstadt P.R., and Ashwell J.D. Genetic disruption of p38alpha Tyr323 phosphorylation prevents T-cell receptor-mediated p38alpha activation and impairs interferon-gamma production Blood 113 2009 2229 2237
    • (2009) Blood , vol.113 , pp. 2229-2237
    • Jirmanova, L.1    Sarma, D.N.2    Jankovic, D.3    Mittelstadt, P.R.4    Ashwell, J.D.5
  • 31
    • 0028157664 scopus 로고
    • Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution
    • Zhang F., Strand A., Robbins D., Cobb M.H., and Goldsmith E.J. Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution Nature 367 1994 704 711
    • (1994) Nature , vol.367 , pp. 704-711
    • Zhang, F.1    Strand, A.2    Robbins, D.3    Cobb, M.H.4    Goldsmith, E.J.5
  • 32
    • 1842665655 scopus 로고    scopus 로고
    • Docking motif interactions in MAP kinases revealed by hydrogen exchange mass spectrometry
    • Lee T., Hoofnagle A.N., Kabuyama Y., Stroud J., Min X., and Goldsmith E.J. Docking motif interactions in MAP kinases revealed by hydrogen exchange mass spectrometry Mol. Cell 14 2004 43 55
    • (2004) Mol. Cell , vol.14 , pp. 43-55
    • Lee, T.1    Hoofnagle, A.N.2    Kabuyama, Y.3    Stroud, J.4    Min, X.5    Goldsmith, E.J.6
  • 33
    • 0033788484 scopus 로고    scopus 로고
    • A conserved docking motif in MAP kinases common to substrates, activators and regulators
    • Tanoue T., Adachi M., Moriguchi T., and Nishida E. A conserved docking motif in MAP kinases common to substrates, activators and regulators Nat. Cell Biol. 2 2000 110 116
    • (2000) Nat. Cell Biol. , vol.2 , pp. 110-116
    • Tanoue, T.1    Adachi, M.2    Moriguchi, T.3    Nishida, E.4
  • 34
    • 0036289349 scopus 로고    scopus 로고
    • 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., and Goldsmith E.J. Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3b Mol. Cell 9 2002 1241 1249
    • (2002) Mol. Cell , vol.9 , pp. 1241-1249
    • Chang, C.I.1    Xu, B.E.2    Akella, R.3    Cobb, M.H.4    Goldsmith, E.J.5
  • 35
    • 0035847076 scopus 로고    scopus 로고
    • Selective targeting of MAPKs to the ETS domain transcription factor SAP-1
    • Galanis A., Yang S.H., and Sharrocks A.D. Selective targeting of MAPKs to the ETS domain transcription factor SAP-1 J. Biol. Chem. 276 2001 965 973
    • (2001) J. Biol. Chem. , vol.276 , pp. 965-973
    • Galanis, A.1    Yang, S.H.2    Sharrocks, A.D.3
  • 36
    • 50349093357 scopus 로고    scopus 로고
    • Substrate discrimination among mitogen-activated protein kinases through distinct docking sequence motifs
    • Sheridan D.L., Kong Y., Parker S.A., Dalby K.N., and Turk B.E. Substrate discrimination among mitogen-activated protein kinases through distinct docking sequence motifs J. Biol. Chem. 283 2008 19511 19520
    • (2008) J. Biol. Chem. , vol.283 , pp. 19511-19520
    • Sheridan, D.L.1    Kong, Y.2    Parker, S.A.3    Dalby, K.N.4    Turk, B.E.5
  • 37
    • 0030866897 scopus 로고    scopus 로고
    • Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
    • Canagarajah B.J., Khokhlatchev A., Cobb M.H., and Goldsmith E.J. Activation mechanism of the MAP kinase ERK2 by dual phosphorylation Cell 90 1997 859 869
    • (1997) Cell , vol.90 , pp. 859-869
    • Canagarajah, B.J.1    Khokhlatchev, A.2    Cobb, M.H.3    Goldsmith, E.J.4
  • 38
    • 0035816581 scopus 로고    scopus 로고
    • Isolation of hyperactive mutants of the MAPK p38/Hog1 that are independent of MAPK kinase activation
    • Bell M., Capone R., Pashtan I., Levitzki A., and Engelberg D. Isolation of hyperactive mutants of the MAPK p38/Hog1 that are independent of MAPK kinase activation J. Biol. Chem. 276 2001 25351 25358
    • (2001) J. Biol. Chem. , vol.276 , pp. 25351-25358
    • Bell, M.1    Capone, R.2    Pashtan, I.3    Levitzki, A.4    Engelberg, D.5
  • 40
    • 8744256717 scopus 로고    scopus 로고
    • Active mutants of the human p38alpha mitogen-activated protein kinase
    • Diskin R., Askari N., Capone R., Engelberg D., and Livnah O. Active mutants of the human p38alpha mitogen-activated protein kinase J. Biol. Chem. 279 2004 47040 47049
    • (2004) J. Biol. Chem. , vol.279 , pp. 47040-47049
    • Diskin, R.1    Askari, N.2    Capone, R.3    Engelberg, D.4    Livnah, O.5
  • 41
    • 33846684565 scopus 로고    scopus 로고
    • High-resolution diffracting crystals of intrinsically active p38alpha MAP kinase: A case study for low-throughput approaches
    • Diskin R., Engelberg D., and Livnah O. High-resolution diffracting crystals of intrinsically active p38alpha MAP kinase: a case study for low-throughput approaches Acta Crystallogr., Sect. D: Biol. Crystallogr. 63 2007 260 265
    • (2007) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.63 , pp. 260-265
    • Diskin, R.1    Engelberg, D.2    Livnah, O.3
  • 42
    • 64849108653 scopus 로고    scopus 로고
    • P38alpha is active in vitro and in vivo when monophosphorylated at threonine 180
    • Askari N., Beenstock J., Livnah O., and Engelberg D. p38alpha is active in vitro and in vivo when monophosphorylated at threonine 180 Biochemistry 48 2009 2497 2504
    • (2009) Biochemistry , vol.48 , pp. 2497-2504
    • Askari, N.1    Beenstock, J.2    Livnah, O.3    Engelberg, D.4
  • 43
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M., and Kuriyan J. The conformational plasticity of protein kinases Cell 109 2002 275 282
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 44
    • 0028329195 scopus 로고
    • An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis
    • Taylor S.J., and Shalloway D. An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis Nature 368 1994 867 871
    • (1994) Nature , vol.368 , pp. 867-871
    • Taylor, S.J.1    Shalloway, D.2
  • 45
    • 55549104054 scopus 로고    scopus 로고
    • Enzymatic activity and substrate specificity of mitogen-activated protein kinase p38alpha in different phosphorylation states
    • Zhang Y.Y., Mei Z.Q., Wu J.W., and Wang Z.X. Enzymatic activity and substrate specificity of mitogen-activated protein kinase p38alpha in different phosphorylation states J. Biol. Chem. 283 2008 26591 26601
    • (2008) J. Biol. Chem. , vol.283 , pp. 26591-26601
    • Zhang, Y.Y.1    Mei, Z.Q.2    Wu, J.W.3    Wang, Z.X.4
  • 46
    • 33751392926 scopus 로고    scopus 로고
    • Structures of p38alpha active mutants reveal conformational changes in L16 loop that induce autophosphorylation and activation
    • Diskin R., Lebendiker M., Engelberg D., and Livnah O. Structures of p38alpha active mutants reveal conformational changes in L16 loop that induce autophosphorylation and activation J. Mol. Biol. 365 2007 66 76
    • (2007) J. Mol. Biol. , vol.365 , pp. 66-76
    • Diskin, R.1    Lebendiker, M.2    Engelberg, D.3    Livnah, O.4
  • 47
    • 0033567706 scopus 로고    scopus 로고
    • The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation
    • Bellon S., Fitzgibbon M.J., Fox T., Hsiao H.M., and Wilson K.P. The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation Structure 7 1999 1057 1065
    • (1999) Structure , vol.7 , pp. 1057-1065
    • Bellon, S.1    Fitzgibbon, M.J.2    Fox, T.3    Hsiao, H.M.4    Wilson, K.P.5
  • 48
    • 33744798469 scopus 로고    scopus 로고
    • Docking interactions induce exposure of activation loop in the MAP kinase ERK2
    • Zhou T., Sun L., Humphreys J., and Goldsmith E.J. Docking interactions induce exposure of activation loop in the MAP kinase ERK2 Structure 14 2006 1011 1019
    • (2006) Structure , vol.14 , pp. 1011-1019
    • Zhou, T.1    Sun, L.2    Humphreys, J.3    Goldsmith, E.J.4
  • 49
    • 0033555229 scopus 로고    scopus 로고
    • 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., and Kornfeld K. Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase Genes Dev. 13 1999 163 175
    • (1999) Genes Dev. , vol.13 , pp. 163-175
    • Jacobs, D.1    Glossip, D.2    Xing, H.3    Muslin, A.J.4    Kornfeld, K.5
  • 50
    • 0036051342 scopus 로고    scopus 로고
    • Molecular interpretation of ERK signal duration by immediate early gene products
    • Murphy L.O., Smith S., Chen R.H., Fingar D.C., and Blenis J. Molecular interpretation of ERK signal duration by immediate early gene products Nat. Cell Biol. 4 2002 556 564
    • (2002) Nat. Cell Biol. , vol.4 , pp. 556-564
    • Murphy, L.O.1    Smith, S.2    Chen, R.H.3    Fingar, D.C.4    Blenis, J.5
  • 51
    • 0345732643 scopus 로고    scopus 로고
    • A network of immediate early gene products propagates subtle differences in mitogen-activated protein kinase signal amplitude and duration
    • Murphy L.O., MacKeigan J.P., and Blenis J. A network of immediate early gene products propagates subtle differences in mitogen-activated protein kinase signal amplitude and duration Mol. Cell. Biol. 24 2004 144 153
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 144-153
    • Murphy, L.O.1    MacKeigan, J.P.2    Blenis, J.3
  • 52
    • 1542364421 scopus 로고    scopus 로고
    • Differential phosphorylation of c-Jun and JunD in response to the epidermal growth factor is determined by the structure of MAPK targeting sequences
    • Vinciguerra M., Vivacqua A., Fasanella G., Gallo A., Cuozzo C., and Morano A. Differential phosphorylation of c-Jun and JunD in response to the epidermal growth factor is determined by the structure of MAPK targeting sequences J. Biol. Chem. 279 2004 9634 9641
    • (2004) J. Biol. Chem. , vol.279 , pp. 9634-9641
    • Vinciguerra, M.1    Vivacqua, A.2    Fasanella, G.3    Gallo, A.4    Cuozzo, C.5    Morano, A.6
  • 53
    • 0028228616 scopus 로고
    • Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH 3T3 cells
    • Cowley S., Paterson H., Kemp P., and Marshall C.J. Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH 3T3 cells Cell 77 1994 841 852
    • (1994) Cell , vol.77 , pp. 841-852
    • Cowley, S.1    Paterson, H.2    Kemp, P.3    Marshall, C.J.4
  • 54
    • 0024380864 scopus 로고
    • Phosphorylation inactivates Escherichia coli isocitrate dehydrogenase by preventing isocitrate binding
    • Dean A.M., Lee M.H., and Koshland D.E. Jr Phosphorylation inactivates Escherichia coli isocitrate dehydrogenase by preventing isocitrate binding J. Biol. Chem. 264 1989 20482 20486
    • (1989) J. Biol. Chem. , vol.264 , pp. 20482-20486
    • Dean, A.M.1    Lee, M.H.2    Koshland Jr., D.E.3
  • 55
    • 0026505446 scopus 로고
    • Crystallization studies of glycosylated and unglycosylated human recombinant interleukin-2
    • Stura E.A., Chen P., Wilmot C.M., Arevalo J.H., and Wilson I.A. Crystallization studies of glycosylated and unglycosylated human recombinant interleukin-2 Proteins 12 1992 24 30
    • (1992) Proteins , vol.12 , pp. 24-30
    • Stura, E.A.1    Chen, P.2    Wilmot, C.M.3    Arevalo, J.H.4    Wilson, I.A.5
  • 56
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 57
    • 0035788131 scopus 로고    scopus 로고
    • Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps
    • Vagin A.A., and Isupov M.N. Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps Acta Crystallogr., Sect. D: Biol. Crystallogr. 57 2001 1451 1456
    • (2001) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.57 , pp. 1451-1456
    • Vagin, A.A.1    Isupov, M.N.2
  • 60
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and automatic interpretation of protein electron density maps
    • Morris R.J., Perrakis A., and Lamzin V.S. ARP/wARP and automatic interpretation of protein electron density maps Methods Enzymol. 374 2003 229 244
    • (2003) Methods Enzymol. , vol.374 , pp. 229-244
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.