메뉴 건너뛰기




Volumn 90, Issue 5, 1997, Pages 859-869

Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE;

EID: 0030866897     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80351-7     Document Type: Article
Times cited : (646)

References (75)
  • 1
    • 0025832605 scopus 로고
    • Multiple components in an epidermal growth factor-stimulated protein kinase cascade
    • Ahn, N.G., Seger, R., Bratlien, R.L., Diltz, G.D., Tonks, N.K., and Krebs, E.G. (1991). Multiple components in an epidermal growth factor-stimulated protein kinase cascade. J. Biol. Chem. 266, 4220-4227.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4220-4227
    • Ahn, N.G.1    Seger, R.2    Bratlien, R.L.3    Diltz, G.D.4    Tonks, N.K.5    Krebs, E.G.6
  • 2
    • 0025120244 scopus 로고
    • Requirement for integration of signals from two distinct phosphory-lation pathways for activation of MAP kinase
    • Anderson, N.G., Maller, J.L., Tonks, N.K., and Sturgill, T.W. (1990). Requirement for integration of signals from two distinct phosphory-lation pathways for activation of MAP kinase. Nature 343, 651-653.
    • (1990) Nature , vol.343 , pp. 651-653
    • Anderson, N.G.1    Maller, J.L.2    Tonks, N.K.3    Sturgill, T.W.4
  • 3
    • 0000913086 scopus 로고
    • Afast algorithm for rendering space filling molecular pictures
    • Bacon, D.J., and Anderson, W.E. (1988). Afast algorithm for rendering space filling molecular pictures. J. Mol. Graphics 6, 219-220.
    • (1988) J. Mol. Graphics , vol.6 , pp. 219-220
    • Bacon, D.J.1    Anderson, W.E.2
  • 4
    • 0026165752 scopus 로고
    • Identification of multiple extra-cellular signal-regulated kinases (ERKs)with antipeptide antibodies
    • Boulton, T.G., and Cobb, M.H. (1991). Identification of multiple extra-cellular signal-regulated kinases (ERKs)with antipeptide antibodies. Cell Regulation 2, 357-371.
    • (1991) Cell Regulation , vol.2 , pp. 357-371
    • Boulton, T.G.1    Cobb, M.H.2
  • 5
    • 0025290163 scopus 로고
    • An insulin-stimulated protein kinase similar to yeast kinases involved in cell cycle control
    • Boulton, T.G., Yancopoulos, G.D., Gregory, J.S., Slaughter, C., Moomaw, C., Hsu, J., and Cobb, M.H. (1990). An insulin-stimulated protein kinase similar to yeast kinases involved in cell cycle control. Science 249, 64-67.
    • (1990) Science , vol.249 , pp. 64-67
    • Boulton, T.G.1    Yancopoulos, G.D.2    Gregory, J.S.3    Slaughter, C.4    Moomaw, C.5    Hsu, J.6    Cobb, M.H.7
  • 7
    • 0029918062 scopus 로고    scopus 로고
    • Crystal structure and mutational analysis of human CDK2 with cell-cycle regulatory protein CksHs1
    • Bourne, Y., Watson, M.H., Mickey, M.J., Holmes, W., Reed, S.I., and Tainer, J.A. (1996). Crystal structure and mutational analysis of human CDK2 with cell-cycle regulatory protein CksHs1. Cell 84, 863-874.
    • (1996) Cell , vol.84 , pp. 863-874
    • Bourne, Y.1    Watson, M.H.2    Mickey, M.J.3    Holmes, W.4    Reed, S.I.5    Tainer, J.A.6
  • 8
    • 0029893708 scopus 로고    scopus 로고
    • Identification of MAP kinase domains by redirecting stress signals into growth factor responses
    • Brunei, A., and Pouysségur, J. (1996). Identification of MAP kinase domains by redirecting stress signals into growth factor responses. Science 272, 1652-1655.
    • (1996) Science , vol.272 , pp. 1652-1655
    • Brunei, A.1    Pouysségur, J.2
  • 10
    • 0027475972 scopus 로고
    • Phosphorylation of the TAL1 oncoprotein by the extracellular-signal-regulated protein kinase ERK1
    • Cheng, J.-T., Cobb, M.H., and Baer, R. (1993). Phosphorylation of the TAL1 oncoprotein by the extracellular-signal-regulated protein kinase ERK1. Mol. Cell. Biol. 13, 801-808.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 801-808
    • Cheng, J.-T.1    Cobb, M.H.2    Baer, R.3
  • 12
    • 0029043582 scopus 로고
    • How MAP kinases are regulated
    • Cobb, M.H., and Goldsmith, E.J. (1995). How MAP kinases are regulated. J. Biol. Chem. 270, 14843-14846.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14843-14846
    • Cobb, M.H.1    Goldsmith, E.J.2
  • 13
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computing Project, Number 4 (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 14
    • 0027165150 scopus 로고
    • The mitogen-activated protein kinase signal transduction pathway
    • Davis, R.J. (1993). The mitogen-activated protein kinase signal transduction pathway. J. Biol. Chem. 265, 14553-14556.
    • (1993) J. Biol. Chem. , vol.265 , pp. 14553-14556
    • Davis, R.J.1
  • 16
    • 0026641090 scopus 로고
    • Activation of mitogen-activated protein kinase similartoyeast kinases involved in cell cycle control
    • Dent, P., Haser, W., Haystead, T.A.J., Vincent, L.A., Roberts, T.M., and Sturgill, T.W. (1992). Activation of mitogen-activated protein kinase similartoyeast kinases involved in cell cycle control. Science 257, 1404-1407.
    • (1992) Science , vol.257 , pp. 1404-1407
    • Dent, P.1    Haser, W.2    Haystead, T.A.J.3    Vincent, L.A.4    Roberts, T.M.5    Sturgill, T.W.6
  • 17
    • 0028329953 scopus 로고
    • JNK1 : A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
    • Dérijard, B., Hibi, M., Wu, I-H., Barrett, T., Su, B., Deng, T., Karin, M., and Davis, R.J. (1994). JNK1 : A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell 76, 1025-1037.
    • (1994) Cell , vol.76 , pp. 1025-1037
    • Dérijard, B.1    Hibi, M.2    Wu, I.-H.3    Barrett, T.4    Su, B.5    Deng, T.6    Karin, M.7    Davis, R.J.8
  • 18
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representations of macromolecules
    • Evans, S.V. (1993). SETOR: hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graphics 11, 134-138.
    • (1993) J. Mol. Graphics , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 20
    • 0029995804 scopus 로고    scopus 로고
    • Allosteric enzymes as models for chemomechanical energy transducing assemblies
    • Goldsmith, E.J. (1996). Allosteric enzymes as models for chemomechanical energy transducing assemblies. FASEB J. 10, 702-708.
    • (1996) FASEB J. , vol.10 , pp. 702-708
    • Goldsmith, E.J.1
  • 22
    • 0028143178 scopus 로고
    • 2-terminal activation domain of c-Myc
    • 2-terminal activation domain of c-Myc. FEBS Lett. 353, 281-285.
    • (1994) FEBS Lett. , vol.353 , pp. 281-285
    • Gupta, S.1    Davis, R.J.2
  • 23
    • 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. (1994). A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. Science 265, 808-811.
    • (1994) Science , vol.265 , pp. 808-811
    • Han, J.1    Lee, J.-D.2    Bibbs, L.3    Ulevitch, R.J.4
  • 24
    • 0029020282 scopus 로고
    • The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks, S.K., and Hunter, T. (1995). The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 9, 576-596.
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 25
    • 0026568161 scopus 로고
    • ERK1 and ERK2, two microtubule-associated protein 2 kinases, mediate the phosphorylation of tyrosine hydroxylase at serine-31 in situ
    • Haycock, J.W., Ahn, N.G., Cobb, M.H., and Krebs, E.G. (1992). ERK1 and ERK2, two microtubule-associated protein 2 kinases, mediate the phosphorylation of tyrosine hydroxylase at serine-31 in situ. Proc. Natl. Acad. Sci. USA 89, 2365-2369.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2365-2369
    • Haycock, J.W.1    Ahn, N.G.2    Cobb, M.H.3    Krebs, E.G.4
  • 26
    • 0027423418 scopus 로고
    • Identification of an oncoprotein and UV-responsive protein kinase that binds and potentiates the c-jun activation domain
    • Hibi, M., Lin, A., Smeal, T., Minden, A., and Karin, M. (1993). Identification of an oncoprotein and UV-responsive protein kinase that binds and potentiates the c-jun activation domain. Genes Dev. 7, 2135-2148.
    • (1993) Genes Dev. , vol.7 , pp. 2135-2148
    • Hibi, M.1    Lin, A.2    Smeal, T.3    Minden, A.4    Karin, M.5
  • 27
    • 0028287635 scopus 로고
    • Insights into autoregulation from the crystal structure of twitchin kinase
    • Hu, S.-H., Parker, M.W., Lei, J.Y., Wilce, M.C.J., Benian, G.M., and Kemp, B.E. (1994). Insights into autoregulation from the crystal structure of twitchin kinase. Nature 369, 581-584.
    • (1994) Nature , vol.369 , pp. 581-584
    • Hu, S.-H.1    Parker, M.W.2    Lei, J.Y.3    Wilce, M.C.J.4    Benian, G.M.5    Kemp, B.E.6
  • 28
    • 0023649678 scopus 로고
    • A tail of two src's: Mutatis mutandis
    • Hunter, T. (1987). A tail of two src's: Mutatis mutandis. Cell 49, 1-4.
    • (1987) Cell , vol.49 , pp. 1-4
    • Hunter, T.1
  • 29
    • 0026206788 scopus 로고
    • Sparse matrix sampling: A screening method for crystallization of proteins
    • Jancarik, J., and Kim, S.-H. (1991). Sparse matrix sampling: a screening method for crystallization of proteins. J. Appl. Crystallogr. 24, 409-411.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.-H.2
  • 31
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson, L.N., Noble, M.E.M., and Owen, D.J. (1996). Active and inactive protein kinases: structural basis for regulation. Cell 85, 149-158.
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.M.2    Owen, D.J.3
  • 33
    • 0028609209 scopus 로고
    • JNK2 contains a specificity-determining region responsiblefor efficient c-Jun binding and phosphorylation
    • Kallunki, T., Su, B., Tsigelny, I., Sluss, H.K., Dérijard, B., Moore, G., Davis, R., and Karin, M. (1994). JNK2 contains a specificity-determining region responsiblefor efficient c-Jun binding and phosphorylation. Genes Dev. 8, 2996-3007.
    • (1994) Genes Dev. , vol.8 , pp. 2996-3007
    • Kallunki, T.1    Su, B.2    Tsigelny, I.3    Sluss, H.K.4    Dérijard, B.5    Moore, G.6    Davis, R.7    Karin, M.8
  • 34
    • 0030966367 scopus 로고    scopus 로고
    • Reconstitution of MAP kinase phosphorylation cascades in bacteria: Efficient synthesis of active protein kinases
    • Khokhlatchev, A., Xu, S., English, J., Wu, P., Schaefer, E., and Cobb, M.H. (1997). Reconstitution of MAP kinase phosphorylation cascades in bacteria: efficient synthesis of active protein kinases. J. Biol. Chem. 272, 11057-11062.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11057-11062
    • Khokhlatchev, A.1    Xu, S.2    English, J.3    Wu, P.4    Schaefer, E.5    Cobb, M.H.6
  • 35
    • 0026342401 scopus 로고
    • Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton, D.R., Zheng, J., Ten Eyck, L.F., Ashford, V.A., Xuong, N.-H., Taylor, S.S., and Sowadski, J.M. (1991a). Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 407-413.
    • (1991) Science , vol.253 , pp. 407-413
    • Knighton, D.R.1    Zheng, J.2    Ten Eyck, L.F.3    Ashford, V.A.4    Xuong, N.-H.5    Taylor, S.S.6    Sowadski, J.M.7
  • 36
    • 0026326821 scopus 로고
    • Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton, D.R., Zheng, J., Ten Eyck, L.F., Xuong, N.-H., Taylor, S.S., and Sowadski, J.M. (1991b). Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 414-420.
    • (1991) Science , vol.253 , pp. 414-420
    • Knighton, D.R.1    Zheng, J.2    Ten Eyck, L.F.3    Xuong, N.-H.4    Taylor, S.S.5    Sowadski, J.M.6
  • 37
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 38
    • 0029744885 scopus 로고    scopus 로고
    • Sounding the alarm: Protein kinase cascades activated by stress and inflammation
    • Kyriakis, J.M., and Avruch, J. (1996). Sounding the alarm: protein kinase cascades activated by stress and inflammation. J. Biol. Chem. 271, 24313-24316.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24313-24316
    • Kyriakis, J.M.1    Avruch, J.2
  • 41
    • 0000243829 scopus 로고
    • Procheck: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. (1993). Procheck: a program to check the stereochemical quality of protein structures . J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 42
    • 0029162078 scopus 로고
    • Primary structure of BMK1 : A new mammalian map kinase
    • Lee, J.-D., Ulevitch, R.J., and Man, J. (1995). Primary structure of BMK1 : a new mammalian map kinase. Biochem. Biophys. Res. Commun. 213, 715-724.
    • (1995) Biochem. Biophys. Res. Commun. , vol.213 , pp. 715-724
    • Lee, J.-D.1    Ulevitch, R.J.2    Man, J.3
  • 43
    • 0028968949 scopus 로고
    • Tyrosine kinase inhibition: An approach to drug development
    • Levitzki, A., and Gazit, A. (1995). Tyrosine kinase inhibition: an approach to drug development. Science 267, 1782-1788.
    • (1995) Science , vol.267 , pp. 1782-1788
    • Levitzki, A.1    Gazit, A.2
  • 44
    • 0029034251 scopus 로고
    • ATF-2 contains a phosphorylation-dependent transcriptional activation domain
    • Livingstone, G., Patel, G., and Jones, N. (1995). ATF-2 contains a phosphorylation-dependent transcriptional activation domain. EMBO J. 14, 1785-1797.
    • (1995) EMBO J. , vol.14 , pp. 1785-1797
    • Livingstone, G.1    Patel, G.2    Jones, N.3
  • 45
    • 0029963896 scopus 로고    scopus 로고
    • Three dimensional structure of mammalian casein kinase I: Molecular basis for phosphate recognition
    • Longenecker, K.L., Roach, P.J., and Hurley, T.D. (1996). Three dimensional structure of mammalian casein kinase I: molecular basis for phosphate recognition. J. Mol. Biol. 257, 618-631.
    • (1996) J. Mol. Biol. , vol.257 , pp. 618-631
    • Longenecker, K.L.1    Roach, P.J.2    Hurley, T.D.3
  • 46
    • 0025890946 scopus 로고
    • Influence of praline residues on protein conformation
    • MacArthur, M.W., and Thornton, J.M. (1991). Influence of praline residues on protein conformation. J. Mol. Biol. 218, 397-412.
    • (1991) J. Mol. Biol. , vol.218 , pp. 397-412
    • MacArthur, M.W.1    Thornton, J.M.2
  • 48
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., Wyman, J., and Changeux, J.P. (1965). On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12, 88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 49
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta Crystallogr. A50, 157-163.
    • (1994) Acta Crystallogr. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 50
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A., and Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 51
    • 0028125907 scopus 로고
    • Ligand-induced activation of chimeric receptors between the erythropoietin receptor and areceptor tyrosine kinases
    • Ohashi, H., Maruyama, K., Liu, Y.-C., and Yoshimura, A. (1994). Ligand-induced activation of chimeric receptors between the erythropoietin receptor and areceptor tyrosine kinases. Proc. Natl. Acad. Sci. USA 91, 158-162.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 158-162
    • Ohashi, H.1    Maruyama, K.2    Liu, Y.-C.3    Yoshimura, A.4
  • 52
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • L. Sawyer, N. Issacs, and S.W. Bailey, eds. (Warrington, United Kingdom: Science and Engineering Council/Daresbury Laboratory)
    • Otwinowski, Z. (1993). Oscillation data reduction program. In Data Collection and Processing, L. Sawyer, N. Issacs, and S.W. Bailey, eds. (Warrington, United Kingdom: Science and Engineering Council/Daresbury Laboratory), pp. 56-62.
    • (1993) Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 53
    • 0029644732 scopus 로고
    • Two structures of the catalytic domain of phosphorylase kinase: An active protein kinase com plexed with substrate analogue and product
    • Owen, D.J., Noble, M.E.M., Garman, E.F., Papagerorgiou, A.C., and Johnson, L.N. (1995). Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase com plexed with substrate analogue and product. Structure 3, 467-482.
    • (1995) Structure , vol.3 , pp. 467-482
    • Owen, D.J.1    Noble, M.E.M.2    Garman, E.F.3    Papagerorgiou, A.C.4    Johnson, L.N.5
  • 55
    • 0027075932 scopus 로고
    • ERK2 autophosphorylates on a subset of peptides phosphorylated in intact cells in response to insulin and nerve growth factor: Analysis by peptide mapping
    • Robbins, D.J., and Cobb, M.H. (1992). ERK2 autophosphorylates on a subset of peptides phosphorylated in intact cells in response to insulin and nerve growth factor: analysis by peptide mapping. Mol. Biol. Cell 3, 299-308.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 299-308
    • Robbins, D.J.1    Cobb, M.H.2
  • 56
    • 0027532627 scopus 로고
    • Regulation and properties of extracellular signal-regulated protein kinases 1 and 2 in vitro
    • Robbins, D.J., Zhen, E., Owaki, H., Vanderbilt, C.A., Ebert, D., Geppert, T.D., and Cobb, M.H. (1993). Regulation and properties of extracellular signal-regulated protein kinases 1 and 2 in vitro. J. Biol. Chem. 268, 5097-5106.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5097-5106
    • Robbins, D.J.1    Zhen, E.2    Owaki, H.3    Vanderbilt, C.A.4    Ebert, D.5    Geppert, T.D.6    Cobb, M.H.7
  • 57
  • 58
    • 0029928988 scopus 로고    scopus 로고
    • Mutation of position 52 in ERK2 creates a nonproductive binding mode for adenosine 5′-tri phosphate
    • Robinson, M.J., Harkins, P.C., Zhang, J., Baer, R., Haycock, J.W., Cobb, M.H., and Goldsmith, E.J. (1996b). Mutation of position 52 in ERK2 creates a nonproductive binding mode for adenosine 5′-tri phosphate. Biochem. 35, 5641-5646.
    • (1996) Biochem. , vol.35 , pp. 5641-5646
    • Robinson, M.J.1    Harkins, P.C.2    Zhang, J.3    Baer, R.4    Haycock, J.W.5    Cobb, M.H.6    Goldsmith, E.J.7
  • 59
    • 0029767016 scopus 로고    scopus 로고
    • Structural basis of cyclin-dependent kinase activation by phosphorylation
    • Russo, A.A., Jeffrey, P.D., and Pavletich, N.P. (1996). Structural basis of cyclin-dependent kinase activation by phosphorylation. Nature Struct. Biol. 3, 696-700.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 696-700
    • Russo, A.A.1    Jeffrey, P.D.2    Pavletich, N.P.3
  • 60
    • 0029011218 scopus 로고
    • The MAPK signaling cascade
    • Seger, R., and Krebs, E.G. (1995). The MAPK signaling cascade. FASEB J. 9, 726-735.
    • (1995) FASEB J. , vol.9 , pp. 726-735
    • Seger, R.1    Krebs, E.G.2
  • 62
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri, F., Moarefi, I., and Kuriyan, J. (1997). Crystal structure of the Src family tyrosine kinase Hck. Nature 385, 602-609.
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 64
    • 0343177223 scopus 로고    scopus 로고
    • A structural basis for substrate specifics of protein Ser/Thr kinases: Primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmoodulin dependent kinase II, CDK5, and Erk1
    • Songyang, Z., Lu, K.P., Kwon, Y.T., Tsai, L.-H., Filhol, O., Cochet, C., Brickey, D.A., Soderling, T.R., Bartleson, C., Graves, D.J., et al. (1996). A structural basis for substrate specifics of protein Ser/Thr kinases: primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmoodulin dependent kinase II, CDK5, and Erk1. Mol. Cell. Biol. 16, 6486-6493.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6486-6493
    • Songyang, Z.1    Lu, K.P.2    Kwon, Y.T.3    Tsai, L.-H.4    Filhol, O.5    Cochet, C.6    Brickey, D.A.7    Soderling, T.R.8    Bartleson, C.9    Graves, D.J.10
  • 65
    • 0023139735 scopus 로고
    • Activation of human raf transforming genes by deletion of normal amino-terminal coding sequences
    • Stanton, V.P., and Cooper, G.M. (1987). Activation of human raf transforming genes by deletion of normal amino-terminal coding sequences. Mol. Cell. Biol. 7, 1171-1179.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 1171-1179
    • Stanton, V.P.1    Cooper, G.M.2
  • 67
    • 0027358722 scopus 로고
    • MKP-1 (3CH1-34), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo
    • Sun, H., Charles, C.H., Lau, L.F., and Tonks, N.K. (1993). MKP-1 (3CH1-34), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo. Cell 75, 487-493.
    • (1993) Cell , vol.75 , pp. 487-493
    • Sun, H.1    Charles, C.H.2    Lau, L.F.3    Tonks, N.K.4
  • 68
    • 0030911867 scopus 로고    scopus 로고
    • The structure of the mitogen-activated protein kinase P38 at 2.1 Å resolution
    • Wang, Z., Harkins, P.C., Cobb, M.H., and Goldsmith, E.J. (1997). The structure of the mitogen-activated protein kinase P38 at 2.1 Å resolution. Proc. Natl. Acad. Sci. USA 94, 2327-2332.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2327-2332
    • Wang, Z.1    Harkins, P.C.2    Cobb, M.H.3    Goldsmith, E.J.4
  • 70
    • 0028913538 scopus 로고
    • Crystal structure of casein kinase-1, a phosphate directed protein kinase
    • Xu, R.-M., Carmel, G., Sweet, R.M., Kuret, J., and Cheng, X. (1995). Crystal structure of casein kinase-1, a phosphate directed protein kinase. EMBO J. 14, 1015-1023.
    • (1995) EMBO J. , vol.14 , pp. 1015-1023
    • Xu, R.-M.1    Carmel, G.2    Sweet, R.M.3    Kuret, J.4    Cheng, X.5
  • 71
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu, W., Harrison, S.C., and Eck, M.J. (1997). Three-dimensional structure of the tyrosine kinase c-Src. Nature 365, 595-602.
    • (1997) Nature , vol.365 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 72
    • 0028157664 scopus 로고
    • Atomic structure of the MAP kinase ERK2at 2.3Å resolution
    • Zhang, F., Strand, A., Robbins, D., Cobb, M.H., and Goldsmith, E.J. (1994). Atomic structure of the MAP kinase ERK2at 2.3Å resolution. Nature 367, 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
  • 73
    • 0029644242 scopus 로고
    • Activity of the MAP kinase ERK2 is controlled by a flexible surface loop
    • Zhang, J., Zhang, F., Ebert, D., Cobb, M.H., and Goldsmith, E.J. (1995). Activity of the MAP kinase ERK2 is controlled by a flexible surface loop. Structure 3, 299-307.
    • (1995) Structure , vol.3 , pp. 299-307
    • Zhang, J.1    Zhang, F.2    Ebert, D.3    Cobb, M.H.4    Goldsmith, E.J.5
  • 74
    • 0027323844 scopus 로고
    • Dephosphorylation and inactivation of the mitogen-activated protein kinase by a mitogen-induced Thr/Tyr protein phosphatase
    • Zheng, C.-F., and Guan, K.-L. (1993). Dephosphorylation and inactivation of the mitogen-activated protein kinase by a mitogen-induced Thr/Tyr protein phosphatase. J. Biol. Chem. 268, 16116-16119.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16116-16119
    • Zheng, C.-F.1    Guan, K.-L.2
  • 75
    • 0029055761 scopus 로고
    • Components of a new human protein kinase signal transduction pathway
    • Zhou, G., Bao, Z.Q., and Dixon, J.E. (1995). Components of a new human protein kinase signal transduction pathway. J. Biol. Chem. 270, 12665-12669.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12665-12669
    • Zhou, G.1    Bao, Z.Q.2    Dixon, J.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.