Published in J Biol Chem on April 05, 1991
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Evidence that the v-sis gene product transforms by interaction with the receptor for platelet-derived growth factor. Science (1985) 1.39
A novel mechanism regulating growth factor association with the cell surface: identification of a PDGF retention domain. Genes Dev (1991) 1.36
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Cloning and characterization of cbl-b: a SH3 binding protein with homology to the c-cbl proto-oncogene. Oncogene (1995) 1.35
Tyrosine phosphorylation of the vav proto-oncogene product links FcepsilonRI to the Rac1-JNK pathway. J Biol Chem (1997) 1.32
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Isolation and chromosomal localization of the human fgr protooncogene, a distinct member of the tyrosine kinase gene family. Proc Natl Acad Sci U S A (1985) 1.22
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The role of individual cysteine residues in the structure and function of the v-sis gene product. Science (1987) 1.12
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High-affinity IgE receptor-mediated stimulation of rat basophilic leukemia (RBL-2H3) cells induces early and late protein-tyrosine phosphorylations. J Biol Chem (1992) 1.11
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Nucleotide sequence of the transforming gene of simian sarcoma virus. Proc Natl Acad Sci U S A (1982) 1.10
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In vitro mutagenesis of the v-sis transforming gene defines functional domains of its growth factor-related product. Proc Natl Acad Sci U S A (1985) 1.07
Expression of the fgr protooncogene product as a function of myelomonocytic cell maturation. J Cell Biol (1989) 1.06
Identification of the major tyrosine kinase substrate in signaling complexes formed after engagement of Fc gamma receptors. J Biol Chem (1995) 1.06
Detection of PDGF-2 homodimers in human tumor cells. Oncogene (1987) 1.05
Molecular localization of the transforming and secretory properties of PDGF A and PDGF B. Science (1990) 1.05
Functional identification of regulatory elements within the promoter region of platelet-derived growth factor 2. Mol Cell Biol (1989) 1.05
Molecular cloning of integrated Gardner-Rasheed feline sarcoma virus: genetic structure of its cell-derived sequence differs from that of other tyrosine kinase-coding onc genes. J Virol (1983) 1.05
The interaction of streptokinase with human, cat, dog, and rabbit plasminogens. The fragmentation of streptokinase in the equimolar plasminogen-streptokinase complexes. J Biol Chem (1974) 1.03
The isolation and characterization of the S-carboxymethyl beta (light) chain derivative of human plasmin. The localization of the active site on the beta (light) chain. J Biol Chem (1967) 1.03
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Molecular weight studies on human plasminogen and plasmin at the microgram level. J Biol Chem (1969) 1.00
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Isolation of a human plasmin-derived, functionally active, light (B) chain capable of forming with streptokinase an equimolar light (B) chain-streptokinase complex with plasminogen activator activity. J Biol Chem (1976) 0.94
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Physical and chemical properties of the NH2-terminal glutamic acid and lysine forms of human plasminogen and their derived plasmins with an NH2-terminal lysine heavy (A) chain. J Biol Chem (1975) 0.90
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Steady state kinetics of activation of human and bovine plasminogens by streptokinase and its equimolar complexes with various activated forms of human plasminogen. J Biol Chem (1978) 0.89
NH2-terminal sequences of mammalian plasminogens and plasmin S-carboxymethyl heavy (A) and light (B) chain derivatives. A re-evaluation of the mechanism of activation of plasminogen. J Biol Chem (1973) 0.89
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