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Volumn 2, Issue 9, 2000, Pages 593-600

Regulation of anchorage-dependent signal transduction by protein kinase A and p21-activated kinase

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; GROWTH FACTOR; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN P21;

EID: 0034282225     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/35023536     Document Type: Article
Times cited : (182)

References (52)
  • 2
    • 0031050451 scopus 로고    scopus 로고
    • Cell anchorage and the cytoskeleton as partners in growth factor dependent cell cycle progression
    • Assoian, R. K. & Zhu, X. Cell anchorage and the cytoskeleton as partners in growth factor dependent cell cycle progression. Curr. Opin. Cell Biol. 9, 93-98 (1997).
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 93-98
    • Assoian, R.K.1    Zhu, X.2
  • 3
    • 0030661566 scopus 로고    scopus 로고
    • Integrins, oncogenes, and anchorage independence
    • Schwartz, M. A. Integrins, oncogenes, and anchorage independence. J. Cell Biol. 139, 575-578 (1997).
    • (1997) J. Cell Biol. , vol.139 , pp. 575-578
    • Schwartz, M.A.1
  • 4
    • 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. & Johnson, G. L. Mitogen-activated protein kinase: conservation of a three-kinase module from yeast to human. Physiol. Rev. 79, 143-180 (1999).
    • (1999) Physiol. Rev. , vol.79 , pp. 143-180
    • Widmann, C.1    Gibson, S.2    Jarpe, M.B.3    Johnson, G.L.4
  • 5
    • 0030453194 scopus 로고    scopus 로고
    • Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: Roles of integrin aggregation and occupancy of receptors
    • Miyamoto, S., Teramoto, H., Gutkind, J. S. & Yamada, K. M. Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: roles of integrin aggregation and occupancy of receptors. J. Cell Biol. 135, 1633-1642 (1996).
    • (1996) J. Cell Biol. , vol.135 , pp. 1633-1642
    • Miyamoto, S.1    Teramoto, H.2    Gutkind, J.S.3    Yamada, K.M.4
  • 6
    • 0031550532 scopus 로고    scopus 로고
    • Extracellular matrix is required for MAP kinase activation and proliferation of rat glomerular epithelial cells
    • Cybulsky, A. V. & McTavish, A. J. Extracellular matrix is required for MAP kinase activation and proliferation of rat glomerular epithelial cells. Biochem. Biophys. Res. Commun. 231, 160-166 (1997).
    • (1997) Biochem. Biophys. Res. Commun. , vol.231 , pp. 160-166
    • Cybulsky, A.V.1    McTavish, A.J.2
  • 7
    • 0031003237 scopus 로고    scopus 로고
    • Cell anchorage permits efficient signal transduction between ras and its downstream kinases
    • Lin, T. H., Chen, Q., Howe, A. & Juliano, R. L. Cell anchorage permits efficient signal transduction between ras and its downstream kinases. J. Biol. Chem. 272, 8849-8852 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 8849-8852
    • Lin, T.H.1    Chen, Q.2    Howe, A.3    Juliano, R.L.4
  • 8
    • 0030766846 scopus 로고    scopus 로고
    • Growth factor activation of MAP kinase requires cell adhesion
    • Renshaw, M. W., Ren, X. D. & Schwartz, M. A. Growth factor activation of MAP kinase requires cell adhesion. EMBO J. 16, 5592-5599 (1997).
    • (1997) EMBO J. , vol.16 , pp. 5592-5599
    • Renshaw, M.W.1    Ren, X.D.2    Schwartz, M.A.3
  • 9
    • 0029883790 scopus 로고    scopus 로고
    • Insulin, growth factors, and cAMP: Antagonism in the signal transduction pathways
    • Graves, L. M. & Lawrence, J. C. Jr, Insulin, growth factors, and cAMP: antagonism in the signal transduction pathways. Trends Endocrinol. Metabol. 7, 43-50 (1996).
    • (1996) Trends Endocrinol. Metabol. , vol.7 , pp. 43-50
    • Graves, L.M.1    Lawrence J.C., Jr.2
  • 11
    • 0029187438 scopus 로고
    • Multiple facets of the modulation of growth by cAMP
    • Roger, P. P., Reuse, S., Maenhaut, C. & Dumont, J. E. Multiple facets of the modulation of growth by cAMP. Vitam. Horm. 51, 59-191 (1995).
    • (1995) Vitam. Horm. , vol.51 , pp. 59-191
    • Roger, P.P.1    Reuse, S.2    Maenhaut, C.3    Dumont, J.E.4
  • 12
    • 0032911020 scopus 로고    scopus 로고
    • Bidirectional signaling between the cytoskeleton and integrins
    • Schoenwaelder, S. M. & Burridge, K. Bidirectional signaling between the cytoskeleton and integrins. Curr. Opin. Cell Biol. 11, 274-286 (1999).
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 274-286
    • Schoenwaelder, S.M.1    Burridge, K.2
  • 13
    • 0033000286 scopus 로고    scopus 로고
    • Integrin and cytoskeletal regulation of growth factor signaling to the MAP kinase pathway
    • Aplin, A. E. & Juliano, R. L. Integrin and cytoskeletal regulation of growth factor signaling to the MAP kinase pathway. J. Cell Sci. 112, 695-706 (1999).
    • (1999) J. Cell Sci. , vol.112 , pp. 695-706
    • Aplin, A.E.1    Juliano, R.L.2
  • 14
    • 0031042493 scopus 로고    scopus 로고
    • Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton
    • Tapon, N. & Hall, A. Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr. Opin. Cell Biol. 9, 86-92 (1997).
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 86-92
    • Tapon, N.1    Hall, A.2
  • 15
    • 0032129189 scopus 로고    scopus 로고
    • The p21Rac/Cdc42-activated kinases (PAKs)
    • Knaus, U. G. & Bokoch, G. M. The p21Rac/Cdc42-activated kinases (PAKs). Int. J. Biochem. Cell Biol. 30, 857-862 (1998).
    • (1998) Int. J. Biochem. Cell Biol. , vol.30 , pp. 857-862
    • Knaus, U.G.1    Bokoch, G.M.2
  • 16
    • 0032511882 scopus 로고    scopus 로고
    • The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338
    • King, A. J. et al. The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338. Nature 396, 180-183 (1998).
    • (1998) Nature , vol.396 , pp. 180-183
    • King, A.J.1
  • 17
    • 0030830220 scopus 로고    scopus 로고
    • Cross-cascade activation of ERKs and ternary complex factors by Rho family proteins
    • Frost, J. A. et al. Cross-cascade activation of ERKs and ternary complex factors by Rho family proteins. EMBO J. 16, 6426-6438 (1997).
    • (1997) EMBO J. , vol.16 , pp. 6426-6438
    • Frost, J.A.1
  • 18
    • 0032168919 scopus 로고    scopus 로고
    • A dicistronic retroviral vector and culture model for analysis of neuron-Schwann cell interactions
    • Howe, D. G. & McCarthy, K. D. A dicistronic retroviral vector and culture model for analysis of neuron-Schwann cell interactions. J. Neurosci. Methods 83, 133-142 (1998).
    • (1998) J. Neurosci. Methods , vol.83 , pp. 133-142
    • Howe, D.G.1    McCarthy, K.D.2
  • 19
    • 0029127312 scopus 로고
    • Basal expression of the cystic fibrosis transmembrane conductance regulator gene is dependent on protein kinase A activity
    • McDonald, R. A., Matthews, R. P., Idzerda, R. L. & McKnight, G. S. Basal expression of the cystic fibrosis transmembrane conductance regulator gene is dependent on protein kinase A activity. Proc. Natl Acad. Sci. USA 92, 7560-7564 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 7560-7564
    • McDonald, R.A.1    Matthews, R.P.2    Idzerda, R.L.3    McKnight, G.S.4
  • 20
    • 0024576161 scopus 로고
    • A protein kinase inhibitor gene reduces both basal and multihormone-stimulated prolactin gene transcription
    • Day, R. N., Walder, J. A. & Maurer, R. A. A protein kinase inhibitor gene reduces both basal and multihormone-stimulated prolactin gene transcription. J. Biol. Chem. 264, 431-436 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 431-436
    • Day, R.N.1    Walder, J.A.2    Maurer, R.A.3
  • 21
    • 0029917915 scopus 로고    scopus 로고
    • Modulation of adhesion-dependent cAMP signaling by echistatin and alendronate
    • Fong, J. H. & Ingber, D. E. Modulation of adhesion-dependent cAMP signaling by echistatin and alendronate. Biochem. Biophys. Res. Commun. 221, 19-24 (1996).
    • (1996) Biochem. Biophys. Res. Commun. , vol.221 , pp. 19-24
    • Fong, J.H.1    Ingber, D.E.2
  • 22
    • 0032517857 scopus 로고    scopus 로고
    • Release of cAMP gating by the alpha6beta4 integrin stimulates lamellae formation and the chemotactic migration of invasive carcinoma cells
    • O'Connor, K. L., Shaw, L. M. & Mercurio, A. M. Release of cAMP gating by the alpha6beta4 integrin stimulates lamellae formation and the chemotactic migration of invasive carcinoma cells. J. Cell Biol. 143, 1749-1760 (1998).
    • (1998) J. Cell Biol. , vol.143 , pp. 1749-1760
    • O'Connor, K.L.1    Shaw, L.M.2    Mercurio, A.M.3
  • 23
    • 0028277783 scopus 로고
    • Stress relaxation of fibroblasts activates a cyclic AMP signaling pathway
    • He, Y. & Grinnell, F. Stress relaxation of fibroblasts activates a cyclic AMP signaling pathway. J. Cell Biol. 126, 457-464 (1994).
    • (1994) J. Cell Biol. , vol.126 , pp. 457-464
    • He, Y.1    Grinnell, F.2
  • 24
    • 0032734174 scopus 로고    scopus 로고
    • Cell adhesion molecules, signal transduction, and cell growth
    • Aplin, A. E., Howe, A. K. & Juliano, R. L. Cell adhesion molecules, signal transduction, and cell growth. Curr. Opin. Cell Biol. 11, 737-744 (1999).
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 737-744
    • Aplin, A.E.1    Howe, A.K.2    Juliano, R.L.3
  • 25
    • 0032103492 scopus 로고    scopus 로고
    • Hormonal regulation of focal adhesions in bovine adrenocortical cells: Induction of paxillin dephosphorylation by adrenocorticotropic hormone
    • Vilgrain, I., Chinn, A., Gaillard, I., Chambaz, E. M. & Feige, J. J. Hormonal regulation of focal adhesions in bovine adrenocortical cells: induction of paxillin dephosphorylation by adrenocorticotropic hormone. Biochem. J. 332, 533-540 (1998).
    • (1998) Biochem. J. , vol.332 , pp. 533-540
    • Vilgrain, I.1    Chinn, A.2    Gaillard, I.3    Chambaz, E.M.4    Feige, J.J.5
  • 26
    • 0029842723 scopus 로고    scopus 로고
    • Regulation of cytoskeleton organization and paxillin dephosphorylation by cAMP. Studies on murine Y1 adrenal cells
    • Han, J. D. & Rubin, C. S. Regulation of cytoskeleton organization and paxillin dephosphorylation by cAMP. Studies on murine Y1 adrenal cells. J. Biol Chem. 271, 29211-29215 (1996).
    • (1996) J. Biol Chem. , vol.271 , pp. 29211-29215
    • Han, J.D.1    Rubin, C.S.2
  • 27
    • 0030580349 scopus 로고    scopus 로고
    • Increasing cAMP antagonizes hypertrophic response to angiotensin II without affecting Ras and MAP kinase activation in vascular smooth muscle cells
    • Takahashi, T., Kawahara, Y., Okuda, M. & Yokoyama, M. Increasing cAMP antagonizes hypertrophic response to angiotensin II without affecting Ras and MAP kinase activation in vascular smooth muscle cells. FEBS Lett. 397, 89-92 (1996).
    • (1996) FEBS Lett. , vol.397 , pp. 89-92
    • Takahashi, T.1    Kawahara, Y.2    Okuda, M.3    Yokoyama, M.4
  • 28
    • 0033553428 scopus 로고    scopus 로고
    • Evidence for a calpeptin-sensitive protein-tyrosine phosphatase upstream of the small GTPase Rho. A novel role for the calpain inhibitor calpeptin in the inhibition of protein-tyrosine phosphatases
    • Schoenwaelder, S. M. & Burridge, K. Evidence for a calpeptin-sensitive protein-tyrosine phosphatase upstream of the small GTPase Rho. A novel role for the calpain inhibitor calpeptin in the inhibition of protein-tyrosine phosphatases. J. Biol. Chem. 274, 14359-14367 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 14359-14367
    • Schoenwaelder, S.M.1    Burridge, K.2
  • 29
    • 0033526541 scopus 로고    scopus 로고
    • Dibutyryl cyclic AMP-induced process formation in astrocytes is associated with a decrease in tyrosine phosphorylation of focal adhesion kinase and paxillin
    • Padmanabhan, J., Clayton, D. & Shelanski, M. L. Dibutyryl cyclic AMP-induced process formation in astrocytes is associated with a decrease in tyrosine phosphorylation of focal adhesion kinase and paxillin. J. Neurobiol. 39, 407-422 (1999).
    • (1999) J. Neurobiol. , vol.39 , pp. 407-422
    • Padmanabhan, J.1    Clayton, D.2    Shelanski, M.L.3
  • 30
    • 0029960996 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of focal adhesion kinase (p125FAK): Regulation by cAMP and thrombin in mesangial cells
    • Troyer, D. A., Bouton, A., Bedolla, R. & Padilla, R. Tyrosine phosphorylation of focal adhesion kinase (p125FAK): regulation by cAMP and thrombin in mesangial cells. J. Am. Soc. Nephrol. 7, 415-423 (1996).
    • (1996) J. Am. Soc. Nephrol. , vol.7 , pp. 415-423
    • Troyer, D.A.1    Bouton, A.2    Bedolla, R.3    Padilla, R.4
  • 31
    • 0031745571 scopus 로고    scopus 로고
    • Signal transduction and signal modulation by cell adhesion receptors: The role of integrins, cadherins, immunoglobulin-cell adhesion molecules, and selectins
    • Aplin, A. E., Howe, A., Alahari, S. K. & Juliano, R. L. Signal transduction and signal modulation by cell adhesion receptors: the role of integrins, cadherins, immunoglobulin-cell adhesion molecules, and selectins. Pharmacol. Rev. 50, 197-263 (1998).
    • (1998) Pharmacol. Rev. , vol.50 , pp. 197-263
    • Aplin, A.E.1    Howe, A.2    Alahari, S.K.3    Juliano, R.L.4
  • 32
    • 0033229747 scopus 로고    scopus 로고
    • Focal adhesion kinase mediates the integrin signaling requirement for growth factor activation of MAP kinase
    • Renshaw, M. W., Price, L. S. & Schwartz, M. A. Focal adhesion kinase mediates the integrin signaling requirement for growth factor activation of MAP kinase. J. Cell Biol. 147, 611-618 (1999).
    • (1999) J. Cell Biol. , vol.147 , pp. 611-618
    • Renshaw, M.W.1    Price, L.S.2    Schwartz, M.A.3
  • 33
    • 0033046010 scopus 로고    scopus 로고
    • Signals from the Ras, Rac, and Rho GTPases converge on the Pak protein kinase in rat-1 fibroblasts
    • Tang, Y., Yu, J. & Field, J. Signals from the Ras, Rac, and Rho GTPases converge on the Pak protein kinase in Rat-1 fibroblasts. Mol. Cell Biol. 19, 1881-1891 (1999).
    • (1999) Mol. Cell Biol. , vol.19 , pp. 1881-1891
    • Tang, Y.1    Yu, J.2    Field, J.3
  • 34
    • 0030811528 scopus 로고    scopus 로고
    • Kinase-deficient Pak1 mutants inhibit Ras transformation of rat-1 fibroblasts
    • Tang, Y. et al. Kinase-deficient Pak1 mutants inhibit Ras transformation of Rat-1 fibroblasts. Mol. Cell Biol. 17, 4454-4464 (1997).
    • (1997) Mol. Cell Biol. , vol.17 , pp. 4454-4464
    • Tang, Y.1
  • 35
    • 0034595381 scopus 로고    scopus 로고
    • Adhesion to the extracellular matrix regulates the coupling of the small GTPase Rac to its effector PAK
    • del Pozo, M. A., Price, L. S., Alderson, N. B., Ren, X. & Schwartz, M. A. Adhesion to the extracellular matrix regulates the coupling of the small GTPase Rac to its effector PAK. EMBO J. 19, 2008-2014 (2000).
    • (2000) EMBO J. , vol.19 , pp. 2008-2014
    • Del Pozo, M.A.1    Price, L.S.2    Alderson, N.B.3    Ren, X.4    Schwartz, M.A.5
  • 36
    • 0033524507 scopus 로고    scopus 로고
    • Control of G2/M transition in Xenopus by a member of the p21-activated kinase (PAK) family: A link between protein kinase A and PAK signaling pathways?
    • Faure, S. et al. Control of G2/M transition in Xenopus by a member of the p21-activated kinase (PAK) family: a link between protein kinase A and PAK signaling pathways? J. Biol. Chem. 274, 3573-3579 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 3573-3579
    • Faure, S.1
  • 37
    • 0033230933 scopus 로고    scopus 로고
    • PAKa, a putative PAK family member, is required for cytokinesis and the regulation of the cytoskeleton in Dictyostelium discoideum cells during chemotaxis
    • Chung, C. Y. & Firtel, R. A. PAKa, a putative PAK family member, is required for cytokinesis and the regulation of the cytoskeleton in Dictyostelium discoideum cells during chemotaxis. J. Cell Biol. 147, 559-576 (1999).
    • (1999) J. Cell Biol. , vol.147 , pp. 559-576
    • Chung, C.Y.1    Firtel, R.A.2
  • 38
    • 0034723262 scopus 로고    scopus 로고
    • Identification of a human brain-specific isoform of mammalian STE20-like kinase 3 that is regulated by cAMP-dependent protein kinase
    • Zhou, T. H. et al. Identification of a human brain-specific isoform of mammalian STE20-like kinase 3 that is regulated by cAMP-dependent protein kinase. J. Biol. Chem. 275, 2513-2519 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 2513-2519
    • Zhou, T.H.1
  • 39
    • 0032748298 scopus 로고    scopus 로고
    • Identification of a central phosphorylation site in p21-activated kinase regulating autoinhibition and kinase activity
    • Zenke, F. T., King, C. C., Bohl, B. P. & Bokoch, G. M. Identification of a central phosphorylation site in p21-activated kinase regulating autoinhibition and kinase activity. J. Biol. Chem. 274, 32565-32573 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 32565-32573
    • Zenke, F.T.1    King, C.C.2    Bohl, B.P.3    Bokoch, G.M.4
  • 40
    • 0033534615 scopus 로고    scopus 로고
    • Identification of kinase-phosphatase signaling modules composed of p70 S6 kinase-protein phosphatase 2A (PP2A) and p21-activated kinase-PP2A
    • Westphal, R. S., Coffee, R. L. Jr, Marotta, A., Pelech, S. L. & Wadzinski, B. E. Identification of kinase-phosphatase signaling modules composed of p70 S6 kinase-protein phosphatase 2A (PP2A) and p21-activated kinase-PP2A. J. Biol. Chem. 274, 687-692 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 687-692
    • Westphal, R.S.1    Coffee R.L., Jr.2    Marotta, A.3    Pelech, S.L.4    Wadzinski, B.E.5
  • 41
    • 0033577810 scopus 로고    scopus 로고
    • Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling
    • Turner, C. E. et al. Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: a role in cytoskeletal remodeling. J. Cell Biol. 145, 851-863 (1999).
    • (1999) J. Cell Biol. , vol.145 , pp. 851-863
    • Turner, C.E.1
  • 42
    • 0032213509 scopus 로고    scopus 로고
    • The Nck SH2/SH3 adaptor protein: A regulator of multiple intracellular signal transduction events
    • McCarty, J. H. The Nck SH2/SH3 adaptor protein: a regulator of multiple intracellular signal transduction events. Bioessays 20, 913-921 (1998).
    • (1998) Bioessays , vol.20 , pp. 913-921
    • McCarty, J.H.1
  • 43
    • 0032422785 scopus 로고    scopus 로고
    • Structural organization of MAP-kinase signaling modules by scaffold proteins in yeast and mammals
    • Whitmarsh, A. J. & Davis, R. J. Structural organization of MAP-kinase signaling modules by scaffold proteins in yeast and mammals. Trends Biochem. Sci. 23, 481-485 (1998).
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 481-485
    • Whitmarsh, A.J.1    Davis, R.J.2
  • 44
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • Pawson, T. & Scott, J. D. Signaling through scaffold, anchoring, and adaptor proteins. Science 278, 2075-2080 (1997).
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 46
    • 0032575667 scopus 로고    scopus 로고
    • cAMP-induced morphological changes are counteracted by the activated RhoA small GTPase and the Rho kinase ROKalpha
    • Dong, J. M., Leung, T., Manser, E. & Lim, L. cAMP-induced morphological changes are counteracted by the activated RhoA small GTPase and the Rho kinase ROKalpha, J. Biol. Chem. 273, 22554-22562 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 22554-22562
    • Dong, J.M.1    Leung, T.2    Manser, E.3    Lim, L.4
  • 47
    • 0023645738 scopus 로고
    • Protein kinase C and cAMP-dependent protein kinase induce opposite effects on actin polymerizability
    • Ohta, Y., Akiyama, T., Nishida, E. & Sakai, H. Protein kinase C and cAMP-dependent protein kinase induce opposite effects on actin polymerizability. FEBS Lett. 222, 305-310 (1987).
    • (1987) FEBS Lett. , vol.222 , pp. 305-310
    • Ohta, Y.1    Akiyama, T.2    Nishida, E.3    Sakai, H.4
  • 48
    • 0032698075 scopus 로고    scopus 로고
    • Cell survival promoted by the Ras-MAPK signaling pathway by transcription-dependent and -independent mechanisms
    • Bonni, A. et al. Cell survival promoted by the Ras-MAPK signaling pathway by transcription-dependent and -independent mechanisms. Science 286, 1358-1362 (1999).
    • (1999) Science , vol.286 , pp. 1358-1362
    • Bonni, A.1
  • 49
    • 0032538449 scopus 로고    scopus 로고
    • Distinct mechanisms mediate the initial and sustained phases of integrin-mediated activation of the Raf/MEK/mitogen-activated protein kinase cascade
    • Howe, A. K. & Juliano, R. L. Distinct mechanisms mediate the initial and sustained phases of integrin-mediated activation of the Raf/MEK/mitogen-activated protein kinase cascade. J. Biol. Chem. 273, 27268-27274 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 27268-27274
    • Howe, A.K.1    Juliano, R.L.2
  • 50
    • 0027374550 scopus 로고
    • Protein kinase A antagonizes platelet-derived growth factor-induced signaling by mitogen-activated protein kinase in human arterial smooth muscle cells
    • Graves, L. M. et al. Protein kinase A antagonizes platelet-derived growth factor-induced signaling by mitogen-activated protein kinase in human arterial smooth muscle cells. Proc. Natl Acad. Sci. USA 90, 10300-10304 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 10300-10304
    • Graves, L.M.1
  • 51
    • 0028036684 scopus 로고
    • The small GTP-bindmg protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
    • Chong, L. D., Traynor-Kaplan, A., Bokoch, G. M. & Schwartz, M. A. The small GTP-bindmg protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell 79, 507-513 (1994).
    • (1994) Cell , vol.79 , pp. 507-513
    • Chong, L.D.1    Traynor-Kaplan, A.2    Bokoch, G.M.3    Schwartz, M.A.4
  • 52
    • 0025998840 scopus 로고
    • Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates
    • Boyle, W. J., van der Geer, P. & Hunter, T. Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. Methods Enzymol. 201, 110-149 (1991).
    • (1991) Methods Enzymol. , vol.201 , pp. 110-149
    • Boyle, W.J.1    Van Der Geer, P.2    Hunter, T.3


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