메뉴 건너뛰기




Volumn 74, Issue 4, 1996, Pages 477-484

Activation of human pp60c-src

Author keywords

Kinase; Oncogene; Phosphorylation; Src; Tyrosine

Indexed keywords

PROTEIN KINASE P60; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE C SRC; PROTEIN-TYROSINE KINASE C-SRC;

EID: 0030346245     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o96-052     Document Type: Review
Times cited : (23)

References (88)
  • 1
    • 0028898383 scopus 로고
    • Sequence requirements for binding of Src family tyrosine kinases to activated growth factor receptors
    • Alonso, G., Koegl, M., Mazurenko, N., and Courtneidge, S.A. 1995. Sequence requirements for binding of Src family tyrosine kinases to activated growth factor receptors. J. Biol. Chem. 270: 9840-9848.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9840-9848
    • Alonso, G.1    Koegl, M.2    Mazurenko, N.3    Courtneidge, S.A.4
  • 2
    • 0022390058 scopus 로고
    • Human cellular src gene: Nucleotide sequence and derived amino acid sequence of the region coding for the carboxy-terminal two-thirds of pp60c-src
    • Anderson, S.K., Gibbs, C.P., Tanaka, A., Rung, H.J., and Fujita, D.J. 1985. Human cellular src gene: nucleotide sequence and derived amino acid sequence of the region coding for the carboxy-terminal two-thirds of pp60c-src. Mol. Cell. Biol. 5: 1122-1129.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 1122-1129
    • Anderson, S.K.1    Gibbs, C.P.2    Tanaka, A.3    Rung, H.J.4    Fujita, D.J.5
  • 3
    • 0025976997 scopus 로고
    • Altered tyrosine 527 phosphorylation and mitotic activation of p60c-src
    • Bagrodia, S., Chackalaparampil, I., Kmiecik, T.E., and Shalloway, D. 1991. Altered tyrosine 527 phosphorylation and mitotic activation of p60c-src. Nature (London), 349: 172-175.
    • (1991) Nature (London) , vol.349 , pp. 172-175
    • Bagrodia, S.1    Chackalaparampil, I.2    Kmiecik, T.E.3    Shalloway, D.4
  • 4
    • 0024786266 scopus 로고
    • p34cdc2 is located in both nucleus and cytoplasm; part is centrosomally associated at G2/M and enters vesicles at anaphase
    • Bailly, E., Doree, M., Nurse, P., and Bornens, M. 1989. p34cdc2 is located in both nucleus and cytoplasm; part is centrosomally associated at G2/M and enters vesicles at anaphase. EMBO J. 8: 3985-3995.
    • (1989) EMBO J. , vol.8 , pp. 3985-3995
    • Bailly, E.1    Doree, M.2    Nurse, P.3    Bornens, M.4
  • 5
    • 0023149698 scopus 로고
    • Expression of the c-src protooncogene in human skin tumors
    • Barnekow, A., Paul, E., and Schartl, M. 1987. Expression of the c-src protooncogene in human skin tumors. Cancer Res. 47: 235-240.
    • (1987) Cancer Res. , vol.47 , pp. 235-240
    • Barnekow, A.1    Paul, E.2    Schartl, M.3
  • 6
    • 0028879873 scopus 로고
    • Myc but not Fos rescue of PDGF signalling block caused by kinase-inactive Src
    • Barone, M.V., and Courtneidge, S.A. 1995. Myc but not Fos rescue of PDGF signalling block caused by kinase-inactive Src [see comments]. Nature (London), 378: 509-512.
    • (1995) Nature (London) , vol.378 , pp. 509-512
    • Barone, M.V.1    Courtneidge, S.A.2
  • 8
    • 0027436135 scopus 로고
    • Binding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides
    • Bibbins, K.B., Boeuf, H., and Varmus, H.E. 1993. Binding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides. Mol. Cell. Biol. 13: 7278-7287.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7278-7287
    • Bibbins, K.B.1    Boeuf, H.2    Varmus, H.E.3
  • 9
    • 0028818769 scopus 로고
    • Characterization of two activated mutants of human pp60c-src that escape c-Src kinase regulation by distinct mechanisms
    • Bjorge, J.D., Bellagamba, C., Cheng, H.C., Tanaka, A., Wang, J.H., and Fujita, D.J. 1995. Characterization of two activated mutants of human pp60c-src that escape c-Src kinase regulation by distinct mechanisms. J. Biol. Chem. 270: 24 222-24 228.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24222-24228
    • Bjorge, J.D.1    Bellagamba, C.2    Cheng, H.C.3    Tanaka, A.4    Wang, J.H.5    Fujita, D.J.6
  • 10
    • 0021745176 scopus 로고
    • Enhancement of cellular src gene product associated tyrosyl kinase activity following polyoma virus infection and transformation
    • Bolen, J.B., Thiele, C.J., Israel, M.A., Yonemoto, W., Lipsich, L.A., and Brugge, J.S. 1984. Enhancement of cellular src gene product associated tyrosyl kinase activity following polyoma virus infection and transformation. Cell, 38: 767-777.
    • (1984) Cell , vol.38 , pp. 767-777
    • Bolen, J.B.1    Thiele, C.J.2    Israel, M.A.3    Yonemoto, W.4    Lipsich, L.A.5    Brugge, J.S.6
  • 11
    • 0021894809 scopus 로고
    • Stimulation of pp60c-src tyrosyl kinase activity in polyoma virus-infected mouse cells is closely associated with polyoma middle tumor antigen synthesis
    • Bolen, J.B., Lewis, A.M., Jr., and Israel, M.A. 1985. Stimulation of pp60c-src tyrosyl kinase activity in polyoma virus-infected mouse cells is closely associated with polyoma middle tumor antigen synthesis. J. Cell. Biochem. 27: 157-167.
    • (1985) J. Cell. Biochem. , vol.27 , pp. 157-167
    • Bolen, J.B.1    Lewis Jr., A.M.2    Israel, M.A.3
  • 12
    • 0023522557 scopus 로고
    • Analysis of pp60c-src in human colon carcinoma and normal human colon mucosal cells
    • Bolen, J.B., Veillette, A., Schwartz, A.M., Deseau, V., and Rosen, N. 1987. Analysis of pp60c-src in human colon carcinoma and normal human colon mucosal cells. Oncogene Res. 1: 149-168.
    • (1987) Oncogene Res. , vol.1 , pp. 149-168
    • Bolen, J.B.1    Veillette, A.2    Schwartz, A.M.3    Deseau, V.4    Rosen, N.5
  • 13
    • 0026612467 scopus 로고
    • Requirement of pp60c-src expression for osteoclasts to form ruffled borders and resorb bone in mice
    • Boyce, B.F., Yoneda, T., Lowe, C., Soriano, P., and Mundy, G.R. 1992. Requirement of pp60c-src expression for osteoclasts to form ruffled borders and resorb bone in mice. J. Clin. Invest. 90: 1622-1627.
    • (1992) J. Clin. Invest. , vol.90 , pp. 1622-1627
    • Boyce, B.F.1    Yoneda, T.2    Lowe, C.3    Soriano, P.4    Mundy, G.R.5
  • 14
  • 15
    • 0023649625 scopus 로고
    • Cell transformation by pp60c-src mutated in the carboxy-terminal regulatory domain
    • Cartwright, C.A., Eckhart, W., Simon, S., and Kaplan, P.L. 1987. Cell transformation by pp60c-src mutated in the carboxy-terminal regulatory domain. Cell, 49: 83-91.
    • (1987) Cell , vol.49 , pp. 83-91
    • Cartwright, C.A.1    Eckhart, W.2    Simon, S.3    Kaplan, P.L.4
  • 16
    • 0025192786 scopus 로고
    • Activation of the pp60c-src protein kinase is an early event in colonic carcinogenesis
    • Cartwright, C.A., Meisler, A.I., and Eckhart, W. 1990. Activation of the pp60c-src protein kinase is an early event in colonic carcinogenesis. Proc. Natl. Acad. Sci. U.S.A. 87: 558-562.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 558-562
    • Cartwright, C.A.1    Meisler, A.I.2    Eckhart, W.3
  • 17
    • 0024296405 scopus 로고
    • Altered phosphorylation and activation of pp60c-src during fibroblast mitosis
    • Chackalaparampil, I., and Shalloway, D. 1988. Altered phosphorylation and activation of pp60c-src during fibroblast mitosis. Cell, 52: 801-810.
    • (1988) Cell , vol.52 , pp. 801-810
    • Chackalaparampil, I.1    Shalloway, D.2
  • 18
    • 0025279893 scopus 로고
    • Association of type I phosphatidylinositol kinase activity with mutationally activated forms of human pp60c-src
    • Chan, T.O., Tanaka, A., Bjorge, J.D., and Fujita, D.J. 1990. Association of type I phosphatidylinositol kinase activity with mutationally activated forms of human pp60c-src. Mol. Cell. Biol. 10: 3280-3283.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3280-3283
    • Chan, T.O.1    Tanaka, A.2    Bjorge, J.D.3    Fujita, D.J.4
  • 21
    • 0022559078 scopus 로고
    • Tyr527 is phosphorylated in pp60c-src: Implications for regulation
    • Washington, D.C.
    • Cooper, J.A., Gould, K.L., Cartwright, C.A., and Hunter, T. 1986. Tyr527 is phosphorylated in pp60c-src: implications for regulation. Science (Washington, D.C.), 231: 1431-1434.
    • (1986) Science , vol.231 , pp. 1431-1434
    • Cooper, J.A.1    Gould, K.L.2    Cartwright, C.A.3    Hunter, T.4
  • 22
    • 0022081671 scopus 로고
    • Activation of the pp60c-src kinase by middle T antigen binding or by dephosphorylation
    • Courtneidge, S.A. 1985. Activation of the pp60c-src kinase by middle T antigen binding or by dephosphorylation. EMBO J. 4: 1471-1477.
    • (1985) EMBO J. , vol.4 , pp. 1471-1477
    • Courtneidge, S.A.1
  • 23
    • 0025605786 scopus 로고
    • Immunolocalization of the cellular src protein in interphase and mitotic NIH c-src overexpresser cells
    • David-Pfeuty, T., and Nouvian-Dooghe, Y. 1990. Immunolocalization of the cellular src protein in interphase and mitotic NIH c-src overexpresser cells. J. Cell Biol. 111(2): 3097-3116.
    • (1990) J. Cell Biol. , vol.111 , Issue.2 , pp. 3097-3116
    • David-Pfeuty, T.1    Nouvian-Dooghe, Y.2
  • 24
    • 0028816436 scopus 로고
    • Highly specific antibody to Rous sarcoma virus src gene product recognizes nuclear and nucleolar antigens in human cells
    • David-Pfeuty, T., and Nouvian-Dooghe, Y. 1995. Highly specific antibody to Rous sarcoma virus src gene product recognizes nuclear and nucleolar antigens in human cells. J. Virol. 69: 1699-1713.
    • (1995) J. Virol. , vol.69 , pp. 1699-1713
    • David-Pfeuty, T.1    Nouvian-Dooghe, Y.2
  • 25
    • 0028132555 scopus 로고
    • Comparative study of three protein-tyrosine phosphatases. Chicken protein-tyrosine phosphatase lambda dephosphorylates c-Src tyrosine 527
    • Fang, K.S., Sabe, H., Saito, H., and Hanafusa, H. 1994. Comparative study of three protein-tyrosine phosphatases. Chicken protein-tyrosine phosphatase lambda dephosphorylates c-Src tyrosine 527. J. Biol. Chem. 269: 20 194-20 200.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20194-20200
    • Fang, K.S.1    Sabe, H.2    Saito, H.3    Hanafusa, H.4
  • 26
    • 0026013107 scopus 로고
    • Requirement of phosphatidylinositol-3 kinase modification for its association with p60src
    • Fukui, Y., and Hanafusa, H. 1991. Requirement of phosphatidylinositol-3 kinase modification for its association with p60src. Mol. Cell. Biol. 11: 1972-1979.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1972-1979
    • Fukui, Y.1    Hanafusa, H.2
  • 27
    • 0024382926 scopus 로고
    • Phosphatidylinositol kinase type I activity associates with various oncogene products
    • Fukui, Y., Kornbluth, S., Jong, S.M., Wang, L.H., and Hanafusa, H. 1989. Phosphatidylinositol kinase type I activity associates with various oncogene products. Oncogene Res. 4: 283-292.
    • (1989) Oncogene Res. , vol.4 , pp. 283-292
    • Fukui, Y.1    Kornbluth, S.2    Jong, S.M.3    Wang, L.H.4    Hanafusa, H.5
  • 29
    • 0024256374 scopus 로고
    • p60c-src is complexed with a cellular protein in subcellular compartments involved in exocytosis
    • Grandori, C., and Hanafusa, H. 1988. p60c-src is complexed with a cellular protein in subcellular compartments involved in exocytosis. J. Cell Biol. 107(1): 2125-2135.
    • (1988) J. Cell Biol. , vol.107 , Issue.1 , pp. 2125-2135
    • Grandori, C.1    Hanafusa, H.2
  • 30
    • 0027092647 scopus 로고
    • Impaired long-term potentiation, spatial learning, and hippocampal development in fyn mutant mice
    • Washington, D.C.
    • Grant, S.G., O'Dell, T.J., Karl, K.A., Stein, P.L., Soriano, P., and Kandel, E.R. 1992. Impaired long-term potentiation, spatial learning, and hippocampal development in fyn mutant mice [see comments]. Science (Washington, D.C.), 258: 1903-1910.
    • (1992) Science , vol.258 , pp. 1903-1910
    • Grant, S.G.1    O'Dell, T.J.2    Karl, K.A.3    Stein, P.L.4    Soriano, P.5    Kandel, E.R.6
  • 31
    • 0026640629 scopus 로고
    • MAP kinase is constitutively activated in gip2 and src transformed rat 1a fibroblasts
    • Gupta, S.K., Gallego, C., Johnson, G.L., and Heasley, L.E. 1992. MAP kinase is constitutively activated in gip2 and src transformed rat 1a fibroblasts. J. Biol. Chem. 267: 7987-7990.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7987-7990
    • Gupta, S.K.1    Gallego, C.2    Johnson, G.L.3    Heasley, L.E.4
  • 32
    • 0026574838 scopus 로고
    • CD45 phosphotyrosine phosphatase and p561ck protein tyrosine kinase: A functional complex crucial in T cell signal transduction
    • Guttinger, M., Gassmann, M., Amrein, K.E., and Burn, P. 1992. CD45 phosphotyrosine phosphatase and p561ck protein tyrosine kinase: a functional complex crucial in T cell signal transduction. Int. Immunol. 4: 1325-1330.
    • (1992) Int. Immunol. , vol.4 , pp. 1325-1330
    • Guttinger, M.1    Gassmann, M.2    Amrein, K.E.3    Burn, P.4
  • 33
    • 0025010018 scopus 로고
    • Mutations in src homology regions 2 and 3 of activated chicken c-src that result in preferential transformation of mouse or chicken cells
    • Hirai, H., and Varmus, H.E. 1990. Mutations in src homology regions 2 and 3 of activated chicken c-src that result in preferential transformation of mouse or chicken cells. Proc. Natl. Acad. Sci. U.S.A. 87: 8592-8596.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 8592-8596
    • Hirai, H.1    Varmus, H.E.2
  • 34
    • 0026488404 scopus 로고
    • Osteoclasts express high levels of pp60c-src in association with intracellular membranes
    • Home, W.C., Neff, L., Chatterjee, D., Lomri, A., Levy, J.B., and Baron, R. 1992. Osteoclasts express high levels of pp60c-src in association with intracellular membranes. J. Cell Biol. 119: 1003-1013.
    • (1992) J. Cell Biol. , vol.119 , pp. 1003-1013
    • Home, W.C.1    Neff, L.2    Chatterjee, D.3    Lomri, A.4    Levy, J.B.5    Baron, R.6
  • 35
    • 0028347820 scopus 로고
    • Impaired neurite outgrowth of src-minus cerebellar neurons on the cell adhesion molecule L1
    • Ignelzi, M.A., Jr., Miller, D.R., Soriano, P., and Maness, P.F. 1994. Impaired neurite outgrowth of src-minus cerebellar neurons on the cell adhesion molecule L1. Neuron, 12: 873-884.
    • (1994) Neuron , vol.12 , pp. 873-884
    • Ignelzi Jr., M.A.1    Miller, D.R.2    Soriano, P.3    Maness, P.F.4
  • 36
    • 0026611047 scopus 로고
    • Association of p60c-src with endosomal membranes in mammalian fibroblasts
    • Kaplan, K.B., Swedlow, J.R., Varmus, H.E., and Morgan, D.O. 1992. Association of p60c-src with endosomal membranes in mammalian fibroblasts. J. Cell Biol. 118: 321-333.
    • (1992) J. Cell Biol. , vol.118 , pp. 321-333
    • Kaplan, K.B.1    Swedlow, J.R.2    Varmus, H.E.3    Morgan, D.O.4
  • 37
    • 0023581610 scopus 로고
    • Structural features of the carboxy terminus of p60c-src that are required for the regulation of its intrinsic kinase activity
    • Kato, J., Hirota, Y., Nakamura, N., and Takeya, T. 1987. Structural features of the carboxy terminus of p60c-src that are required for the regulation of its intrinsic kinase activity. Jpn. J. Cancer Res. 78: 1354-1362.
    • (1987) Jpn. J. Cancer Res. , vol.78 , pp. 1354-1362
    • Kato, J.1    Hirota, Y.2    Nakamura, N.3    Takeya, T.4
  • 39
    • 0023649672 scopus 로고
    • Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation
    • Kmiecik, T.E., and Shalloway, D. 1987. Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation. Cell, 49: 65-73.
    • (1987) Cell , vol.49 , pp. 65-73
    • Kmiecik, T.E.1    Shalloway, D.2
  • 40
    • 0027965251 scopus 로고
    • Identification and characterization of Batk, a predominantly brain-specific non-receptor protein tyrosine kinase related to Csk
    • Kuo, S.S., Moran, P., Gripp, J., Armanini, M., Phillips, H.S., Goddard, A., and Caras, I.W. 1994. Identification and characterization of Batk, a predominantly brain-specific non-receptor protein tyrosine kinase related to Csk. J. Neurosci. Res. 38: 705-715.
    • (1994) J. Neurosci. Res. , vol.38 , pp. 705-715
    • Kuo, S.S.1    Moran, P.2    Gripp, J.3    Armanini, M.4    Phillips, H.S.5    Goddard, A.6    Caras, I.W.7
  • 41
    • 0025172811 scopus 로고
    • Association between the PDGF receptor and members of the src family of tyrosine kinases
    • Kypta, R.M., Goldberg, Y., Ulug, E.T., and Courtneidge, S. 1990. Association between the PDGF receptor and members of the src family of tyrosine kinases. Cell, 62: 481-492.
    • (1990) Cell , vol.62 , pp. 481-492
    • Kypta, R.M.1    Goldberg, Y.2    Ulug, E.T.3    Courtneidge, S.4
  • 42
    • 0022477424 scopus 로고
    • Phosphorylation of tyrosine in the carboxyl-terminal tryptic peptide of pp60c-src
    • Laudano, A.P., and Buchanan, J.M. 1986. Phosphorylation of tyrosine in the carboxyl-terminal tryptic peptide of pp60c-src. Proc. Natl. Acad. Sci. U.S.A. 83: 892-896.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 892-896
    • Laudano, A.P.1    Buchanan, J.M.2
  • 43
    • 0024338959 scopus 로고
    • Biological and biochemical properties of the c-src+ gene product overexpressed in chicken embryo fibroblasts
    • Levy, J.B., and Brugge, J.S. 1989. Biological and biochemical properties of the c-src+ gene product overexpressed in chicken embryo fibroblasts. Mol. Cell. Biol. 9: 3332-3341.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3332-3341
    • Levy, J.B.1    Brugge, J.S.2
  • 44
    • 0026777791 scopus 로고
    • Host range mutants of v-src: Alterations in kinase activity and substrate interactions
    • Liebl, E.C., England, L.J., DeClue, J.E., and Martin, G.S. 1992. Host range mutants of v-src: alterations in kinase activity and substrate interactions. J. Virol. 66: 4315-4324.
    • (1992) J. Virol. , vol.66 , pp. 4315-4324
    • Liebl, E.C.1    England, L.J.2    DeClue, J.E.3    Martin, G.S.4
  • 45
    • 0026668224 scopus 로고
    • Specific association of the proto-oncogene product pp60c-src with an intracellular organelle, the PC12 synaptic vesicle
    • Linstedt, A.D., Vetter, M.L., Bishop, J.M., and Kelly, R.B. 1992. Specific association of the proto-oncogene product pp60c-src with an intracellular organelle, the PC12 synaptic vesicle. J. Cell Biol. 117: 1077-1084.
    • (1992) J. Cell Biol. , vol.117 , pp. 1077-1084
    • Linstedt, A.D.1    Vetter, M.L.2    Bishop, J.M.3    Kelly, R.B.4
  • 47
    • 0027214258 scopus 로고
    • The v-Src SH3 domain binds phosphatidylinositol 3′-kinase
    • Liu, X., Marengere, L.E., Koch, C.A., and Pawson, T. 1993b. The v-Src SH3 domain binds phosphatidylinositol 3′-kinase. Mol. Cell. Biol. 13: 5225-5232.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5225-5232
    • Liu, X.1    Marengere, L.E.2    Koch, C.A.3    Pawson, T.4
  • 48
    • 0027328182 scopus 로고
    • Elevated expression of protein tyrosine kinase c-Yes, but not c-Src, in human malignant melanoma
    • Loganzo, F., Jr., Dosik, J.S., Zhao, Y., Vidai, M.J., Nanus, D.M., Sudol, M., and Albino, A.P. 1993. Elevated expression of protein tyrosine kinase c-Yes, but not c-Src, in human malignant melanoma. Oncogene, 8: 2637-2644.
    • (1993) Oncogene , vol.8 , pp. 2637-2644
    • Loganzo Jr., F.1    Dosik, J.S.2    Zhao, Y.3    Vidai, M.J.4    Nanus, D.M.5    Sudol, M.6    Albino, A.P.7
  • 50
    • 0026767469 scopus 로고
    • She proteins are phosphorylated and regulated by the v-Src and v-Fps protein-tyrosine kinases
    • McGlade, J., Cheng, A., Pelicci, G., Pelicci, P.G., and Pawson, T. 1992. She proteins are phosphorylated and regulated by the v-Src and v-Fps protein-tyrosine kinases. Proc. Natl. Acad. Sci. U.S.A. 89: 8869-8873.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 8869-8873
    • McGlade, J.1    Cheng, A.2    Pelicci, G.3    Pelicci, P.G.4    Pawson, T.5
  • 52
    • 0024314396 scopus 로고
    • Mitosis-specific phosphorylation of p60c-src by p34cdc2-associated protein kinase
    • Morgan, D.O., Kaplan, J.M., Bishop, J.M., and Varmus, H.E. 1989. Mitosis-specific phosphorylation of p60c-src by p34cdc2-associated protein kinase. Cell, 57: 775-786.
    • (1989) Cell , vol.57 , pp. 775-786
    • Morgan, D.O.1    Kaplan, J.M.2    Bishop, J.M.3    Varmus, H.E.4
  • 53
    • 0027261372 scopus 로고
    • Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: Analysis with Saccharomyces cerevisiae
    • Murphy, S.M., Bergman, M., and Morgan, D.O. 1993. Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae. Mol. Cell. Biol. 13: 5290-5300.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5290-5300
    • Murphy, S.M.1    Bergman, M.2    Morgan, D.O.3
  • 54
    • 0028047315 scopus 로고
    • Mammary tumors expressing the neu protooncogene possess elevated c-Src tyrosine kinase activity
    • Muthuswamy, S.K., Siegel, P.M., Dankort, D.L., Webster, M.A., and Muller, W.J. 1994. Mammary tumors expressing the neu protooncogene possess elevated c-Src tyrosine kinase activity. Mol. Cell. Biol. 14: 735-743.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 735-743
    • Muthuswamy, S.K.1    Siegel, P.M.2    Dankort, D.L.3    Webster, M.A.4    Muller, W.J.5
  • 55
    • 0026897685 scopus 로고
    • pp60c-src in human melanocytes and melanoma cells exhibits elevated specific activity and reduced tyrosine 530 phosphorylation compared to human fibroblast pp60c-src
    • O'Connor, T.J., Neufeld, E., Bechberger, J., and Fujita, D.J. 1992. pp60c-src in human melanocytes and melanoma cells exhibits elevated specific activity and reduced tyrosine 530 phosphorylation compared to human fibroblast pp60c-src. Cell Growth Differ. 3: 435-442.
    • (1992) Cell Growth Differ. , vol.3 , pp. 435-442
    • O'Connor, T.J.1    Neufeld, E.2    Bechberger, J.3    Fujita, D.J.4
  • 56
    • 0028813589 scopus 로고
    • Mechanism of c-SRC activation in human melanocytes: Elevated level of protein tyrosine phosphatase activity directed against the carboxy-terminal regulatory tyrosine
    • Published erratum appears in Cell Growth Differ. 1995. 6(4): 484
    • O'Connor, T.J., Bjorge, J.D, Cheng, H.C., Wang, J.H., and Fujita, D. 1995. Mechanism of c-SRC activation in human melanocytes: elevated level of protein tyrosine phosphatase activity directed against the carboxy-terminal regulatory tyrosine. [Published erratum appears in Cell Growth Differ. 1995. 6(4): 484]. Cell Growth Differ. 6: 123-130.
    • (1995) Cell Growth Differ. , vol.6 , pp. 123-130
    • O'Connor, T.J.1    Bjorge, J.D.2    Cheng, H.C.3    Wang, J.H.4    Fujita, D.5
  • 57
    • 0027219338 scopus 로고
    • Deletion of the SH3 domain of Src interferes with regulation by the phosphorylated carboxyl-terminal tyrosine
    • Okada, M., Howell, B.W., Broome, M.A., and Cooper, J.A. 1993. Deletion of the SH3 domain of Src interferes with regulation by the phosphorylated carboxyl-terminal tyrosine. J. Biol. Chem. 268: 18070-18075.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18070-18075
    • Okada, M.1    Howell, B.W.2    Broome, M.A.3    Cooper, J.A.4
  • 59
    • 0026674221 scopus 로고
    • Characterization of protein tyrosine kinases from human breast cancer: Involvement of the c-src oncogene product
    • Ottenhoff-Kalff, A.E., Rijksen, G., van Beurden, E.A., Hennipman, A., Michels, A.A., and Staal, G.E. 1992. Characterization of protein tyrosine kinases from human breast cancer: involvement of the c-src oncogene product. Cancer Res. 52: 4773-1778.
    • (1992) Cancer Res. , vol.52 , pp. 4773-11778
    • Ottenhoff-Kalff, A.E.1    Rijksen, G.2    Van Beurden, E.A.3    Hennipman, A.4    Michels, A.A.5    Staal, G.E.6
  • 60
    • 0022558393 scopus 로고
    • p60c-src activity detected in the chromaffin granule membrane
    • Parsons, S.J., and Creutz, C.E. 1986. p60c-src activity detected in the chromaffin granule membrane. Biochem. Biophys. Res. Commun. 134: 736-742.
    • (1986) Biochem. Biophys. Res. Commun. , vol.134 , pp. 736-742
    • Parsons, S.J.1    Creutz, C.E.2
  • 61
    • 0025940264 scopus 로고
    • cyl encodes a putative cytoplasmic tyrosine kinase lacking the conserved tyrosine autophosphorylation site (Y416src)
    • Partanen, J., Armstrong, E., Bergman, M., Makela, T.P., Hirvonen, H., Huebner, K., and Alitalo, K. 1991. cyl encodes a putative cytoplasmic tyrosine kinase lacking the conserved tyrosine autophosphorylation site (Y416src). Oncogene, 6: 2013-2018.
    • (1991) Oncogene , vol.6 , pp. 2013-2018
    • Partanen, J.1    Armstrong, E.2    Bergman, M.3    Makela, T.P.4    Hirvonen, H.5    Huebner, K.6    Alitalo, K.7
  • 62
    • 0023649622 scopus 로고
    • Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-src
    • Piwnica-Worms, H., Saunders, K.B., Roberts, T.M., Smith, A.E., and Cheng, S.H. 1987. Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-src. Cell, 49: 75-82.
    • (1987) Cell , vol.49 , pp. 75-82
    • Piwnica-Worms, H.1    Saunders, K.B.2    Roberts, T.M.3    Smith, A.E.4    Cheng, S.H.5
  • 63
    • 0025572606 scopus 로고
    • p34cdc2 kinase is localized to distinct domains within the mitotic apparatus
    • Rattner, J.B., Lew, J., and Wang, J.H. 1990. p34cdc2 kinase is localized to distinct domains within the mitotic apparatus. Cell Motil. Cytoskeleton, 17: 227-235.
    • (1990) Cell Motil. Cytoskeleton , vol.17 , pp. 227-235
    • Rattner, J.B.1    Lew, J.2    Wang, J.H.3
  • 64
    • 0022930029 scopus 로고
    • Analysis of pp60c-src protein kinase activity in human tumor cell lines and tissues
    • Rosen, N., Bolen, J.B., Schwartz, A.M., Cohen, P., Deseau, V., and Israel, M.A. 1986. Analysis of pp60c-src protein kinase activity in human tumor cell lines and tissues. J. Biol. Chem. 261: 13 754 -13 759.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13754-13759
    • Rosen, N.1    Bolen, J.B.2    Schwartz, A.M.3    Cohen, P.4    Deseau, V.5    Israel, M.A.6
  • 65
    • 0025719212 scopus 로고
    • Selective binding of activated pp60c-src by an immobilized synthetic phosphopeptide modeled on the carboxyl terminus of pp60c-src
    • Roussel, R.R., Brodeur, S.R., Shalloway, D., and Laudano, A.P. 1991. Selective binding of activated pp60c-src by an immobilized synthetic phosphopeptide modeled on the carboxyl terminus of pp60c-src. Proc. Natl. Acad. Sci. U.S.A. 88: 10 696-10700.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 10696-10700
    • Roussel, R.R.1    Brodeur, S.R.2    Shalloway, D.3    Laudano, A.P.4
  • 66
    • 0028347585 scopus 로고
    • Molecular cloning of a novel non-receptor tyrosine kinase, HYL (hematopoietic consensus tyrosine-lacking kinase)
    • Sakano, S., Iwama, A., Inazawa, J., Ariyama, T., Ohno, M., and Suda, T. 1994. Molecular cloning of a novel non-receptor tyrosine kinase, HYL (hematopoietic consensus tyrosine-lacking kinase). Oncogene, 9: 1155-1161.
    • (1994) Oncogene , vol.9 , pp. 1155-1161
    • Sakano, S.1    Iwama, A.2    Inazawa, J.3    Ariyama, T.4    Ohno, M.5    Suda, T.6
  • 67
    • 0025027872 scopus 로고
    • Production of novel polyphosphoinositides in vivo is linked to cell transformation by polyomavirus middle T antigen
    • Serunian, L.A., Auger, K.R., Roberts, T.M., and Cantley, L.C. 1990. Production of novel polyphosphoinositides in vivo is linked to cell transformation by polyomavirus middle T antigen. J. Virol. 64: 4718-1725.
    • (1990) J. Virol. , vol.64 , pp. 4718-11725
    • Serunian, L.A.1    Auger, K.R.2    Roberts, T.M.3    Cantley, L.C.4
  • 68
    • 0024400222 scopus 로고
    • Purified maturation promoting factor phosphorylates pp60c-src at the sites phosphorylated during fibroblast mitosis
    • Shenoy, S., Choi, J.K., Bagrodia, S., Copeland, T.D., Maller, J.L, and Shalloway, D. 1989. Purified maturation promoting factor phosphorylates pp60c-src at the sites phosphorylated during fibroblast mitosis. Cell, 57: 763-774.
    • (1989) Cell , vol.57 , pp. 763-774
    • Shenoy, S.1    Choi, J.K.2    Bagrodia, S.3    Copeland, T.D.4    Maller, J.L.5    Shalloway, D.6
  • 70
    • 0022472990 scopus 로고
    • Requirement for c-ras proteins during viral oncogene transformation
    • Smith, M.R., DeGudicibus, S.J., and Stacey, D.W. 1986. Requirement for c-ras proteins during viral oncogene transformation. Nature (London), 320: 540-543.
    • (1986) Nature (London) , vol.320 , pp. 540-543
    • Smith, M.R.1    DeGudicibus, S.J.2    Stacey, D.W.3
  • 71
    • 0028171074 scopus 로고
    • Cdc2-mediated modulation of pp60c-src activity
    • Stover, D.R., Liebetanz, J., and Lydon, N.B. 1994. Cdc2-mediated modulation of pp60c-src activity. J. Biol. Chem. 269: 26 885-26 889.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26885-26889
    • Stover, D.R.1    Liebetanz, J.2    Lydon, N.B.3
  • 72
    • 0027182279 scopus 로고
    • Csk inhibition of c-Src activity requires both the SH2 and SH3 domains of Src
    • Superti-Furga, G., Fumagalli, S., Koegl, M., Courtneidge, S.A., and Draetta, G. 1993. Csk inhibition of c-Src activity requires both the SH2 and SH3 domains of Src. EMBO J. 12: 2625-2634.
    • (1993) EMBO J. , vol.12 , pp. 2625-2634
    • Superti-Furga, G.1    Fumagalli, S.2    Koegl, M.3    Courtneidge, S.A.4    Draetta, G.5
  • 73
    • 0020566206 scopus 로고
    • Structure and sequence of the cellular gene homologous to the RSV src gene and the mechanism for generating the transforming virus
    • Takeya, T., and Hanafusa, H. 1983. Structure and sequence of the cellular gene homologous to the RSV src gene and the mechanism for generating the transforming virus. Cell, 32: 881-890.
    • (1983) Cell , vol.32 , pp. 881-890
    • Takeya, T.1    Hanafusa, H.2
  • 74
    • 0022820128 scopus 로고
    • Expression of a molecularly cloned human c-src oncogene by using a replication-competent retroviral vector
    • Tanaka, A., and Fujita, D.J. 1986. Expression of a molecularly cloned human c-src oncogene by using a replication-competent retroviral vector. Mol. Cell. Biol. 6: 3900-3909.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 3900-3909
    • Tanaka, A.1    Fujita, D.J.2
  • 75
    • 0023128439 scopus 로고
    • DNA sequence encoding the amino-terminal region of the human c-src protein: Implications of sequence divergence among src-type kinase oncogenes
    • Tanaka, A., Gibbs, C.P., Arthur, R.R., Anderson, S.K., Kung, H.J., and Fujita, D.J. 1987. DNA sequence encoding the amino-terminal region of the human c-src protein: implications of sequence divergence among src-type kinase oncogenes. Mol. Cell. Biol. 7: 1978-1983.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 1978-1983
    • Tanaka, A.1    Gibbs, C.P.2    Arthur, R.R.3    Anderson, S.K.4    Kung, H.J.5    Fujita, D.J.6
  • 76
    • 0024986531 scopus 로고
    • Characterization of avian retroviruses carrying activated transforming human c-src genes and of steps involved in expression of activated src-PKases in vitro
    • Tanaka, A., Salem, M., Eckroade, R.J., and Fujita, D.J. 1990. Characterization of avian retroviruses carrying activated transforming human c-src genes and of steps involved in expression of activated src-PKases in vitro. Oncogene Res. 5: 305-322.
    • (1990) Oncogene Res. , vol.5 , pp. 305-322
    • Tanaka, A.1    Salem, M.2    Eckroade, R.J.3    Fujita, D.J.4
  • 77
    • 0028329195 scopus 로고
    • An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis
    • Taylor, S.J., and Shalloway, D. 1994. An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis. Nature (London), 368: 867-871.
    • (1994) Nature (London) , vol.368 , pp. 867-871
    • Taylor, S.J.1    Shalloway, D.2
  • 78
    • 0028945960 scopus 로고
    • Functional interaction between c-Src and its mitotic target, Sam 68
    • Taylor, S.J., Anafi, M., Pawson, T., and Shalloway, D. 1995. Functional interaction between c-Src and its mitotic target, Sam 68. J. Biol. Chem. 270: 10 120-10 124.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10120-10124
    • Taylor, S.J.1    Anafi, M.2    Pawson, T.3    Shalloway, D.4
  • 79
    • 0027172209 scopus 로고
    • The Src family tyrosine kinases are required for platelet-derived growth factor-mediated signal transduction in NIH 3T3 cells
    • Twamley-Stein, G.M., Pepperkok, R., Ansorge, W., and Courtneidge, S.A. 1993. The Src family tyrosine kinases are required for platelet-derived growth factor-mediated signal transduction in NIH 3T3 cells. Proc. Natl. Acad. Sci. U.S.A. 90: 7696-7700.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 7696-7700
    • Twamley-Stein, G.M.1    Pepperkok, R.2    Ansorge, W.3    Courtneidge, S.A.4
  • 80
    • 0027333338 scopus 로고
    • The SH3 domain of p561ck is involved in binding to phosphatidylinositol 3′-kinase from T lymphocytes
    • Vogel, L.B., and Fujita, D.J. 1993. The SH3 domain of p561ck is involved in binding to phosphatidylinositol 3′-kinase from T lymphocytes. Mol. Cell. Biol. 13: 7408-7417.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7408-7417
    • Vogel, L.B.1    Fujita, D.J.2
  • 81
    • 0028984220 scopus 로고
    • p70 phosphorylation and binding to p561ck is an early event in interleukin-2-induced onset of cell cycle progression in T-lymphocytes
    • Vogel, L.B., and Fujita, D.J. 1995. p70 phosphorylation and binding to p561ck is an early event in interleukin-2-induced onset of cell cycle progression in T-lymphocytes. J. Biol. Chem. 270: 2506-2511.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2506-2511
    • Vogel, L.B.1    Fujita, D.J.2
  • 82
    • 0026612625 scopus 로고
    • Differential pp60c-src activity in well and poorly differentiated human colon carcinomas and cell lines
    • Weber, T.K., Steele, G., and Summerhayes, I.C. 1992. Differential pp60c-src activity in well and poorly differentiated human colon carcinomas and cell lines. J. Clin. Invest. 90: 815-821.
    • (1992) J. Clin. Invest. , vol.90 , pp. 815-821
    • Weber, T.K.1    Steele, G.2    Summerhayes, I.C.3
  • 83
    • 0029097471 scopus 로고
    • Induction of mammary epithelial hyperplasias and mammary tumors in transgenic mice expressing a murine mammary tumor virus-activated c-src fusion gene
    • Webster, M.A., Cardiff, R.D., and Muller, W.J. 1995. Induction of mammary epithelial hyperplasias and mammary tumors in transgenic mice expressing a murine mammary tumor virus-activated c-src fusion gene. Proc. Natl. Acad. Sci. U.S.A. 92: 7849-7853.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 7849-7853
    • Webster, M.A.1    Cardiff, R.D.2    Muller, W.J.3
  • 84
    • 0023425731 scopus 로고
    • Evidence for two distinct phosphatidylinositol kinases in fibroblasts. Implications for cellular regulation
    • Whitman, M., Kaplan, D., Roberts, T., and Cantley, L. 1987. Evidence for two distinct phosphatidylinositol kinases in fibroblasts. Implications for cellular regulation. Biochem. J. 247: 165-174.
    • (1987) Biochem. J. , vol.247 , pp. 165-174
    • Whitman, M.1    Kaplan, D.2    Roberts, T.3    Cantley, L.4
  • 85
    • 0026488321 scopus 로고
    • Platelet activation leads to increased c-src kinase activity and association of c-src with an 85-kDa tyrosine phosphoprotein
    • Wong, S., Reynolds, A.B., and Papkoff, J. 1992. Platelet activation leads to increased c-src kinase activity and association of c-src with an 85-kDa tyrosine phosphoprotein. Oncogene, 7: 2407-2415.
    • (1992) Oncogene , vol.7 , pp. 2407-2415
    • Wong, S.1    Reynolds, A.B.2    Papkoff, J.3
  • 86
    • 0024094591 scopus 로고
    • A host-dependent temperature-sensitive mutant of Rous sarcoma virus: Evidence for host factors affecting transformation
    • Young, J.C., Liebl, E., and Martin, G.S. 1988. A host-dependent temperature-sensitive mutant of Rous sarcoma virus: evidence for host factors affecting transformation. Virology, 166: 561-572.
    • (1988) Virology , vol.166 , pp. 561-572
    • Young, J.C.1    Liebl, E.2    Martin, G.S.3
  • 87
    • 0026705734 scopus 로고
    • Cell transformation and activation of pp60c-src by overexpression of a protein tyrosine phosphatase
    • Zheng, X.M., Wang, Y., and Pallen, C.J. 1992. Cell transformation and activation of pp60c-src by overexpression of a protein tyrosine phosphatase. Nature (London), 359: 336-339.
    • (1992) Nature (London) , vol.359 , pp. 336-339
    • Zheng, X.M.1    Wang, Y.2    Pallen, C.J.3
  • 88
    • 0027172833 scopus 로고
    • Increased tyrosine kinase activity in pp60c-src immunoprecipitate from platelet activating factor stimulated human platelets: In vitro phosphorylation of a synthetic peptide
    • Zhu, C.Y., and Shukla, S.D. 1993. Increased tyrosine kinase activity in pp60c-src immunoprecipitate from platelet activating factor stimulated human platelets: in vitro phosphorylation of a synthetic peptide. Life Sci. 53: 175-183.
    • (1993) Life Sci. , vol.53 , pp. 175-183
    • Zhu, C.Y.1    Shukla, S.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.