Regulation of Tyrosine Kinases by Tyrosine Phosphorylation
作者： Jonathan A. Cooper , Alasdair MacAuley , Andrius Kazlauskas
DOI: 10.1007/978-3-642-75142-4_34
关键词:
摘要: Protein kinases can be classified according to whether they phosphorylate phenolic (tyrosine) or aliphatic (serine and threonine) hydroxyl groups (Hunter Cooper, 1985). Although there are now a few examples of that seemingly break the rule (Howell et al., 1990), most tyrosine differ from serine/threonine in their primary amino acid sequences. Consequently, as open reading frames cDNA clones have been sequenced it has relatively easy predict might encode (Hanks 1988). This lead rapid expansion kinase family.
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sci-hub.st 参考文章(32)
Bruce E. Kemp, Peptides and Protein Phosphorylation ,(1990)
M Okada, H Nakagawa, A protein tyrosine kinase involved in regulation of pp60c-src function. Journal of Biological Chemistry. ,vol. 264, pp. 20886- 20893 ,(1989) , 10.1016/S0021-9258(19)30019-5
D K Morrison, D R Kaplan, S G Rhee, L T Williams, Platelet-derived growth factor (PDGF)-dependent association of phospholipase C-gamma with the PDGF receptor signaling complex. Molecular and Cellular Biology. ,vol. 10, pp. 2359- 2366 ,(1990) , 10.1128/MCB.10.5.2359
K L Gould, T Hunter, Platelet-derived growth factor induces multisite phosphorylation of pp60c-src and increases its protein-tyrosine kinase activity. Molecular and Cellular Biology. ,vol. 8, pp. 3345- 3356 ,(1988) , 10.1128/MCB.8.8.3345
T E Kmiecik, P J Johnson, D Shalloway, Regulation by the autophosphorylation site in overexpressed pp60c-src. Molecular and Cellular Biology. ,vol. 8, pp. 4541- 4546 ,(1988) , 10.1128/MCB.8.10.4541
K X Luo, B M Sefton, Cross-linking of T-cell surface molecules CD4 and CD8 stimulates phosphorylation of the lck tyrosine protein kinase at the autophosphorylation site Molecular and Cellular Biology. ,vol. 10, pp. 5305- 5313 ,(1990) , 10.1128/MCB.10.10.5305
C L Yu, M H Tsai, D W Stacey, Serum stimulation of NIH 3T3 cells induces the production of lipids able to inhibit GTPase-activating protein activity. Molecular and Cellular Biology. ,vol. 10, pp. 6683- 6689 ,(1990) , 10.1128/MCB.10.12.6683
A. Kazlauskas, J. A. Cooper, Phosphorylation of the PDGF receptor beta subunit creates a tight binding site for phosphatidylinositol 3 kinase. The EMBO Journal. ,vol. 9, pp. 3279- 3286 ,(1990) , 10.1002/J.1460-2075.1990.TB07527.X
N Abraham, A Veillette, Activation of p56lck through mutation of a regulatory carboxy-terminal tyrosine residue requires intact sites of autophosphorylation and myristylation. Molecular and Cellular Biology. ,vol. 10, pp. 5197- 5206 ,(1990) , 10.1128/MCB.10.10.5197
D Anderson, C. Koch, L Grey, C Ellis, M. Moran, T Pawson, Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors Science. ,vol. 250, pp. 979- 982 ,(1990) , 10.1126/SCIENCE.2173144