메뉴 건너뛰기




Volumn 19, Issue 4, 2008, Pages 975-980

The cysteine-cluster motif of c-Yes, Lyn and FAK as a suppressive module for the kinases

Author keywords

c Yes; Cysteine; FAK; Kinase inactivation; Lyn; SH alkylating agent N (9 acridinyl) maleimide

Indexed keywords

ALKYLATING AGENT; CYSTEINE; FOCAL ADHESION KINASE; MALEIMIDE DERIVATIVE; PROTEIN KINASE LYN; PROTEIN KINASE YES; PROTEIN TYROSINE KINASE; LYN PROTEIN-TYROSINE KINASE; N (9 ACRIDINYL)MALEIMIDE; N-(9-ACRIDINYL)MALEIMIDE;

EID: 43849092144     PISSN: 1021335X     EISSN: None     Source Type: Journal    
DOI: 10.3892/or.19.4.975     Document Type: Article
Times cited : (5)

References (19)
  • 1
    • 0035374609 scopus 로고    scopus 로고
    • The hunting of the Src
    • Martin GS: The hunting of the Src. Nat Rev Mol Cell Biol 2: 467-475, 2001.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 467-475
    • Martin, G.S.1
  • 2
    • 0033061032 scopus 로고    scopus 로고
    • Protein tyrosine kinase inhibitors as novel therapeutic agents
    • Levitzki A: Protein tyrosine kinase inhibitors as novel therapeutic agents. Pharmacol Ther 82: 231-239, 1999.
    • (1999) Pharmacol Ther , vol.82 , pp. 231-239
    • Levitzki, A.1
  • 3
    • 0034614490 scopus 로고    scopus 로고
    • Signaling-2000 and beyond
    • Hunter T: Signaling-2000 and beyond. Cell 100: 113-127, 2000.
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 4
    • 20144376030 scopus 로고    scopus 로고
    • Cell Biology: Lessons in rational drug design for protein kinases
    • Ahn NG and Resing KA: Cell Biology: Lessons in rational drug design for protein kinases. Science 308: 1266-1267, 2005.
    • (2005) Science , vol.308 , pp. 1266-1267
    • Ahn, N.G.1    Resing, K.A.2
  • 5
    • 0037422184 scopus 로고    scopus 로고
    • Cysteine residues in the C-terminal lobe of Src: Their role in the suppression of the Src kinase
    • Oo ML, Senga T, Thant AA, Amin ARMR, Huang P, Mon NN and Hamaguchi M: Cysteine residues in the C-terminal lobe of Src: their role in the suppression of the Src kinase. Oncogene 22: 1411-1417, 2003.
    • (2003) Oncogene , vol.22 , pp. 1411-1417
    • Oo, M.L.1    Senga, T.2    Thant, A.A.3    Amin, A.R.M.R.4    Huang, P.5    Mon, N.N.6    Hamaguchi, M.7
  • 6
    • 0034642550 scopus 로고    scopus 로고
    • Clustered cysteine residues in the kinase domain of v-Src: Critical role for protein stability, cell transformation and sensitivity to herbimycin A
    • Senga T, Miyazaki K, Machida K, Iwata H, Matsuda S, Nakashima I and Hamaguchi M: Clustered cysteine residues in the kinase domain of v-Src: critical role for protein stability, cell transformation and sensitivity to herbimycin A. Oncogene 19: 273-279, 2000.
    • (2000) Oncogene , vol.19 , pp. 273-279
    • Senga, T.1    Miyazaki, K.2    Machida, K.3    Iwata, H.4    Matsuda, S.5    Nakashima, I.6    Hamaguchi, M.7
  • 7
    • 2942618768 scopus 로고    scopus 로고
    • A renaissance for Src
    • Yeatman TJ: A renaissance for Src. Nat Rev Cancer 4: 470-480, 2004.
    • (2004) Nat Rev Cancer , vol.4 , pp. 470-480
    • Yeatman, T.J.1
  • 8
    • 0027300619 scopus 로고
    • The when and how of Src regulation
    • Cooper JA and Howell B: The when and how of Src regulation. Cell 73: 1051-1054, 1993.
    • (1993) Cell , vol.73 , pp. 1051-1054
    • Cooper, J.A.1    Howell, B.2
  • 9
    • 0031452274 scopus 로고    scopus 로고
    • Structures of Src-family tyrosine kinases
    • Sicheri F and Kuriyan J: Structures of Src-family tyrosine kinases. Curr Opin Struct Biol 7: 777-785, 1997.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 777-785
    • Sicheri, F.1    Kuriyan, J.2
  • 10
    • 0031025991 scopus 로고    scopus 로고
    • Three dimensional structure of the tyrosine kinase c-Src
    • Xu W and Harrison S: Three dimensional structure of the tyrosine kinase c-Src. Nature 385: 595-601, 1997.
    • (1997) Nature , vol.385 , pp. 595-601
    • Xu, W.1    Harrison, S.2
  • 11
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of Src
    • Brown MT and Cooper JA: Regulation, substrates and functions of Src. Biochim Biophys Acta 1287: 121-149, 1996.
    • (1996) Biochim Biophys Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 12
    • 0020501846 scopus 로고
    • Isolation of monoclonal antibodies that recognize the transforming proteins of avian sarcoma viruses
    • Lipsich LA, Lewis AJ and Brugge JS: Isolation of monoclonal antibodies that recognize the transforming proteins of avian sarcoma viruses. J Virol 48: 352-360, 1983.
    • (1983) J Virol , vol.48 , pp. 352-360
    • Lipsich, L.A.1    Lewis, A.J.2    Brugge, J.S.3
  • 15
    • 0026674919 scopus 로고
    • Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin
    • Hanks SK, Calalb MB, Harper MC and Patel SK: Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc Natl Acad Sci USA 89: 8487-8491, 1992.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8487-8491
    • Hanks, S.K.1    Calalb, M.B.2    Harper, M.C.3    Patel, S.K.4
  • 16
    • 0026573580 scopus 로고
    • A general and fast method to generate multiple site directed mutations
    • Mikaelian I and Sergeant A: A general and fast method to generate multiple site directed mutations. Nucleic Acids Res 20: 376, 1992.
    • (1992) Nucleic Acids Res , vol.20 , pp. 376
    • Mikaelian, I.1    Sergeant, A.2
  • 17
    • 0023317189 scopus 로고
    • Association of p60src with Triton X-100-resistant cellular structure correlates with morphological transformation
    • Hamaguchi M and Hanafusa H: Association of p60src with Triton X-100-resistant cellular structure correlates with morphological transformation. Proc Natl Acad Sci USA 84: 2312-2316, 1987.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 2312-2316
    • Hamaguchi, M.1    Hanafusa, H.2
  • 18
    • 0027459346 scopus 로고
    • p60v-src causes tyrosine phosphorylation and inactivation of the N-cadherin-catenin cell adhesion system
    • Hamaguchi M, Matsuyoshi N, Ohnishi Y, Gotoh B, Takeichi M and Nagai Y: p60v-src causes tyrosine phosphorylation and inactivation of the N-cadherin-catenin cell adhesion system. EMBO J 12: 307-314, 1993.
    • (1993) EMBO J , vol.12 , pp. 307-314
    • Hamaguchi, M.1    Matsuyoshi, N.2    Ohnishi, Y.3    Gotoh, B.4    Takeichi, M.5    Nagai, Y.6
  • 19
    • 0027522507 scopus 로고
    • Herbimycin A inhibits the association of p60v-src with the cytoskeletal structure and with phosphatidylinositol 3′ kinase
    • Hamaguchi M, Xiao H, Uehara Y, Ohnishi Y and Nagai Y: Herbimycin A inhibits the association of p60v-src with the cytoskeletal structure and with phosphatidylinositol 3′ kinase. Oncogene 8: 559-564, 1993.
    • (1993) Oncogene , vol.8 , pp. 559-564
    • Hamaguchi, M.1    Xiao, H.2    Uehara, Y.3    Ohnishi, Y.4    Nagai, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.