Expression of an Abelson murine leukemia virus-encoded protein in Escherichia coli causes extensive phosphorylation of tyrosine residues.
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The A-MuLV protein appears to be a tyrosine-specific protein kinase which is active in E. coli.About:
This article is published in Journal of Biological Chemistry.The article was published on 1982-11-25 and is currently open access. It has received 86 citations till now. The article focuses on the topics: Abelson murine leukemia virus & GRB10.read more
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Inhibition of the Abl Protein-Tyrosine Kinase in Vitro and in Vivo by a 2-Phenylaminopyrimidine Derivative
Elisabeth Buchdunger,Jürg Zimmermann,Helmut Mett,Thomas Meyer,Marcel Muller,Brian J. Druker,Nicholas B. Lydon +6 more
TL;DR: An inhibitor (CGP 57148) of the Abl and platelet-derived growth factor (PDGF) receptor protein-tyrosine kinases from the 2-phenylaminopyrimidine class is described, which is highly active in vitro and in vivo and may have therapeutic potential for the treatment of diseases that involve abnormal cellular proliferation induced by Abl protein-tiesine kinase deregulation or PDGF receptor activation.
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An alteration of the human c-abl protein in K562 leukemia cells unmasks associated tyrosine kinase activity
TL;DR: An altered human c-abl protein (P210) with associated tyrosine kinase activity in the K562 leukemia cell line is detected and may have important implications for a mechanism of activation of this oncogene.
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Growth factors: Mechanism of action and relation to oncogenes
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A C-terminal protein-binding domain in the retinoblastoma protein regulates nuclear c-Abl tyrosine kinase in the cell cycle.
Peter J. Welch,Jean Y. J. Wang +1 more
TL;DR: It is shown that the tyrosine kinase activity of nuclear c-Abl is regulated in the cell cycle through a specific interaction with the retinoblastoma protein (RB), and a domain in the C-terminus of RB, outside of the A/B pocket, binds to the ATP-binding lobe of the c- abl tyrosin kinase, resulting in kinase inhibition.
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Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites.
TL;DR: The association of Crk and Abl suggests that Abl could play a role in v-Crk and Crk-I transformation and that normal Abl function may be partly mediated through bound adapter molecules.
References
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Transforming gene product of Rous sarcoma virus phosphorylates tyrosine
TL;DR: It is inferred that pp60src is a novel protein kinase and that the modification of proteins via the phosphorylation of tyrosine is essential to the malignant transformation of cells by Rous sarcoma virus.
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Abelson murine leukaemia virus protein is phosphorylated in vitro to form phosphotyrosine.
TL;DR: The Abelson murine leukaemia virus protein (P120) can become phosphorylated in vitro by [γ-32P]ATP and is linked to P120 at tyrosine, a linkage not previously reported for a phosphorylation reaction.
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Structure of the Abelson murine leukemia virus genome and the homologous cellular gene: Studies with cloned viral DNA
TL;DR: Circular double-stranded DNA produced after infection of mouse cells with Abelson murine leukemia virus was isolated and cloned in the phage vector Charon 21A and showed homology to the ends of Moloney MuLV and to a 3.5 kb central region containing sequences unique to Abelson virus.
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Identification of an Abelson murine leukemia virus-encoded protein present in transformed fibroblast and lymphoid cells
TL;DR: Results suggest that the P120 product of the A-MuLV genome may be responsible for maintenance of the transformed phenotype of lymphoid and fibroblast cells transformed by the virus.
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Four different classes of retroviruses induce phosphorylation of tyrosines present in similar cellular proteins.
Jonathan A. Cooper,Tony Hunter +1 more
TL;DR: It is concluded that representatives of four apparently unrelated classes of transforming retroviruses all induce the phosphorylation of tyrosines present in the same set of cellular proteins.