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Volumn 19, Issue 6, 1997, Pages 447-450

A crystal milestone: The structure of regulated Src

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 0031171392     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.950190602     Document Type: Article
Times cited : (25)

References (31)
  • 1
    • 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 385, 595-602.
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 2
    • 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
  • 4
    • 16144364951 scopus 로고    scopus 로고
    • Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation
    • Yamaguchi, H. and Hendrickson, W. A. (1996). Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation. Nature 384, 484-489.
    • (1996) Nature , vol.384 , pp. 484-489
    • Yamaguchi, H.1    Hendrickson, W.A.2
  • 5
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of src
    • Brown, M. T. and Cooper, J. A. (1996). Regulation, substrates and functions of src. Biochim. Biophys. Acta 1287, 121-149.
    • (1996) Biochim. Biophys. Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 6
    • 0029786988 scopus 로고    scopus 로고
    • Knockouts of Src-family kinases: Stiff bones, wimpy T cells, and bad memories
    • Lowell, C. A. and Soriano, P. (1996). Knockouts of Src-family kinases: Stiff bones, wimpy T cells, and bad memories. Genes Dev. 10, 1845-1857.
    • (1996) Genes Dev. , vol.10 , pp. 1845-1857
    • Lowell, C.A.1    Soriano, P.2
  • 7
    • 0029563574 scopus 로고
    • Structural requirements for the efficient regulation of the Src protein tyrosine kinase by Csk
    • Koegl, M., Courtneidge, S. A. and Superti-Furga, G. (1995). Structural requirements for the efficient regulation of the Src protein tyrosine kinase by Csk. Oncogene 11, 2317-2329.
    • (1995) Oncogene , vol.11 , pp. 2317-2329
    • Koegl, M.1    Courtneidge, S.A.2    Superti-Furga, G.3
  • 8
  • 9
    • 0030891301 scopus 로고    scopus 로고
    • Src regulated by C-terminal phosphorylation is monomeric
    • in press
    • Weijland, A. et al. (1997). Src regulated by C-terminal phosphorylation is monomeric. Proc. Natl Acad. Sci. USA (in press).
    • (1997) Proc. Natl Acad. Sci. USA
    • Weijland, A.1
  • 10
    • 0022081671 scopus 로고
    • c-src kinase by middle-T antigen binding or by dephosphorylation
    • c-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
  • 11
    • 0029278886 scopus 로고
    • Structure-function relationships in Src family and related protein tyrosine kinases
    • Superti-Furga, G. and Courtneidge, S. A. (1995). Structure-function relationships in Src family and related protein tyrosine kinases. BioEssays 17, 321-330.
    • (1995) BioEssays , vol.17 , pp. 321-330
    • Superti-Furga, G.1    Courtneidge, S.A.2
  • 12
    • 0028983318 scopus 로고
    • Regulation of the Src protein tyrosine kinase
    • Superti-Furga, G. (1995). Regulation of the Src protein tyrosine kinase. FEBS Lett. 369, 62-66.
    • (1995) FEBS Lett. , vol.369 , pp. 62-66
    • Superti-Furga, G.1
  • 13
    • 0343494918 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain
    • Lee, C.-H., Saksela, K., Mirza, U. A., Chait, B. T. and Kuriyan, J. (1996). Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain. Cell 85, 931-942.
    • (1996) Cell , vol.85 , pp. 931-942
    • Lee, C.-H.1    Saksela, K.2    Mirza, U.A.3    Chait, B.T.4    Kuriyan, J.5
  • 14
    • 0029881450 scopus 로고    scopus 로고
    • The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase
    • Grzesiek, S. et al. (1996). The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase. Natl. Struct. Biol. 3, 340-344.
    • (1996) Natl. Struct. Biol. , vol.3 , pp. 340-344
    • Grzesiek, S.1
  • 15
    • 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
  • 16
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the insulin receptor
    • Hubbard, S. R., Wei, L., Ellis, L. and Hendrickson, W. A. (1994). Crystal structure of the tyrosine kinase domain of the insulin receptor. Nature 372, 746-754.
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 17
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson, T. (1995). Protein modules and signalling networks. Nature 373, 573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 18
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • Cohen, G. B., Ren, R. and Baltimore, D. (1995). Modular binding domains in signal transduction proteins. Cell 80, 237-248.
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 19
    • 0023515851 scopus 로고
    • Cell transformation by the viral src oncogene
    • Jove, R. and Hanafusa, H. (1987). Cell transformation by the viral src oncogene. Ann. Rev. Cell. Biol. 3, 31-56.
    • (1987) Ann. Rev. Cell. Biol. , vol.3 , pp. 31-56
    • Jove, R.1    Hanafusa, H.2
  • 20
    • 0024821548 scopus 로고
    • Genetics of src: Structure and functional organization of a protein tyrosine kinase
    • Parsons, J. T. and Weber, M. J. (1989). Genetics of src: structure and functional organization of a protein tyrosine kinase. Curr. Top. Microbiol. Immunol. 147, 79-127.
    • (1989) Curr. Top. Microbiol. Immunol. , vol.147 , pp. 79-127
    • Parsons, J.T.1    Weber, M.J.2
  • 21
    • 0027978304 scopus 로고
    • Origin and evolution of the c-src-transducing avian sarcoma virus PR2257
    • Yatsula, B. Y. et al. (1994). Origin and evolution of the c-src-transducing avian sarcoma virus PR2257. J. Gen. Virol. 74, 2777-2781.
    • (1994) J. Gen. Virol. , vol.74 , pp. 2777-2781
    • Yatsula, B.Y.1
  • 22
    • 0027288978 scopus 로고
    • Regulation of c-Src tyrosine kinase activity by the Src SH2 domain
    • Liu, X. et al. (1993). Regulation of c-Src tyrosine kinase activity by the Src SH2 domain. Oncogene 8, 1119-1126.
    • (1993) Oncogene , vol.8 , pp. 1119-1126
    • Liu, X.1
  • 23
    • 0031017838 scopus 로고    scopus 로고
    • Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement
    • Moarefi, I. et al. (1997). Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement. Nature 385, 650-653.
    • (1997) Nature , vol.385 , pp. 650-653
    • Moarefi, I.1
  • 24
    • 0019432795 scopus 로고
    • Structural and functional domains of RSV transforming protein pp60src
    • Levinson, A., Courtneidge, S. A. and Bishop, J. M. (1981). Structural and functional domains of RSV transforming protein pp60src. Proc. Natl Acad. Sci. USA 78, 1624-1628.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 1624-1628
    • Levinson, A.1    Courtneidge, S.A.2    Bishop, J.M.3
  • 25
    • 0027182279 scopus 로고
    • Csk inhibition of 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 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
  • 26
    • 0028958025 scopus 로고
    • Src family protein kinases and cellular signal transduction pathways
    • Erpel, T. and Courtneidge, S. A. (1995). Src family protein kinases and cellular signal transduction pathways. Curr. Biol. 7, 176-182.
    • (1995) Curr. Biol. , vol.7 , pp. 176-182
    • Erpel, T.1    Courtneidge, S.A.2
  • 28
    • 0028938721 scopus 로고
    • Catalytic specificity of protein-tyrosine kinases is critical for selective signalling
    • Songyang, Z. et al. (1995). Catalytic specificity of protein-tyrosine kinases is critical for selective signalling. Nature 373, 536-539.
    • (1995) Nature , vol.373 , pp. 536-539
    • Songyang, Z.1
  • 29
    • 0027406462 scopus 로고
    • Abl tyrosine kinase in signal transduction and cell-cycle regulation
    • Wang, J. Y. J. (1993). Abl tyrosine kinase in signal transduction and cell-cycle regulation. Curr. Opin. Gen. Dev. 3, 35-43.
    • (1993) Curr. Opin. Gen. Dev. , vol.3 , pp. 35-43
    • Wang, J.Y.J.1
  • 31
    • 0030152357 scopus 로고    scopus 로고
    • Regulation of Btk function by a major autophosphorylation site within the SH3 domain
    • Park, H. et al. (1996). Regulation of Btk function by a major autophosphorylation site within the SH3 domain. Immunity 4, 515-525.
    • (1996) Immunity , vol.4 , pp. 515-525
    • Park, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.