c-abl has a sequence-specific enhancer binding activity
暂无分享,去创建一个
[1] A. Levitzki,et al. Selective interactions of transforming and normal abl proteins with ATP, tyrosine-copolymer substrates, and tyrphostins. , 1992, The Journal of biological chemistry.
[2] R. Bronson,et al. Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene , 1991, Cell.
[3] S. Goff,et al. Mice homozygous for the abl m1 mutation show poor viability and depletion of selected B and T cell populations , 1991, Cell.
[4] J. Wang,et al. Activation of tyrosinase kinase and microfilament-binding functions of c-abl by bcr sequences in bcr/abl fusion proteins , 1991, Molecular and cellular biology.
[5] G. Daley,et al. Implicating the bcr/abl gene in the pathogenesis of Philadelphia chromosome-positive human leukemia. , 1991, Advances in cancer research.
[6] F. Hoffmann,et al. A novel tyrosine kinase-independent function of Drosophila abl correlates with proper subcellular localization , 1990, Cell.
[7] Y. Shaul,et al. Functional organization of the hepatitis B virus enhancer , 1990, Molecular and cellular biology.
[8] J. Wang,et al. Differential phosphorylation of c-Abl in cell cycle determined by cdc2 kinase and phosphatase activity. , 1990, Science.
[9] D. Baltimore,et al. The mouse type IV c-abl gene product is a nuclear protein, and activation of transforming ability is associated with cytoplasmic localization , 1989, Cell.
[10] P. Hearing,et al. Binding of nuclear factor EF-C to a functional domain of the hepatitis B virus enhancer region , 1989, Molecular and cellular biology.
[11] Y. Shaul,et al. Cellular factors that interact with the hepatitis B virus enhancer , 1989, Molecular and cellular biology.
[12] D. Baltimore,et al. N‐terminal mutations activate the leukemogenic potential of the myristoylated form of c‐abl. , 1989, The EMBO journal.
[13] T. Pawson,et al. Non-catalytic domains of cytoplasmic protein-tyrosine kinases: regulatory elements in signal transduction. , 1988, Oncogene.
[14] M. L. Le Beau,et al. Long-range mapping of the Philadelphia chromosome by pulsed-field gel electrophoresis. , 1988, Blood.
[15] P. Sharp,et al. Molecular cloning of an enhancer binding protein:Isolation by screening of an expression library with a recognition site DNA , 1988, Cell.
[16] O. Witte,et al. Normal cellular and transformation-associated abl proteins share common sites for protein kinase C phosphorylation. , 1987, Molecular and cellular biology.
[17] M. Greaves,et al. A novel abl protein expressed in Philadelphia chromosome positive acute lymphoblastic leukaemia positive acute lymphoblastic leukaemia , 1987, Nature.
[18] R. Kurzrock,et al. A novel c-abl protein product in Philadelphia-positive acute lymphoblastic leukaemia , 1987, Nature.
[19] O. Witte,et al. Unique forms of the abl tyrosine kinase distinguish Ph1-positive CML from Ph1-positive ALL. , 1987, Science.
[20] G. Daley,et al. Overlapping cDNA clones define the complete coding region for the P210c-abl gene product associated with chronic myelogenous leukemia cells containing the Philadelphia chromosome. , 1986, Proceedings of the National Academy of Sciences of the United States of America.
[21] Bruce A. Roe,et al. Alternative splicing of RNAs transcribed from the human abl gene and from the bcr-abl fused gene , 1986, Cell.
[22] G. Daley,et al. The chronic myelogenous leukemia-specific P210 protein is the product of the bcr/abl hybrid gene. , 1986, Science.
[23] G. Daley,et al. Alternative 5′ exons in c-abl mRNA , 1986, Cell.
[24] D. Baltimore,et al. Structural modification of c-abl in lymphoma and leukemia. , 1986, Current topics in microbiology and immunology.
[25] E. Canaani,et al. Fused transcript of abl and bcr genes in chronic myelogenous leukaemia , 1985, Nature.
[26] Susan M. Watanabe,et al. An alteration of the human c-abl protein in K562 leukemia cells unmasks associated tyrosine kinase activity , 1984, Cell.
[27] Rosalind C. Lee,et al. The mouse c-abl locus: Molecular cloning and characterization , 1984, Cell.
[28] J. Stephenson,et al. Philadelphia chromosomal breakpoints are clustered within a limited region, bcr, on chromosome 22 , 1984, Cell.
[29] D. Cleveland. Peptide mapping in one dimension by limited proteolysis of sodium dodecyl sulfate-solubilized proteins. , 1983, Methods in enzymology.