The amino-terminal region of pp60c-src has a modulatory role and contains multiple sites of tyrosine phosphorylation.

No abstract is available for this paper.

• Publication year

  1990

• Venue

  Oncogene

• Publication date

  1990-03-01

• Fields of study

  Biology, Medicine

• Identifiers
  PMID 1690377
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• pp60c-src variants containing lesions that affect phosphorylation at tyrosines 416 and 527

  1989cited by this paper
• Purified maturation promoting factor phosphorylates pp60c-src at the sites phosphorylated during fibroblast mitosis.

  1989cited by this paper
• Deletions and insertions within an amino-terminal domain of pp60v-src inactivate transformation and modulate membrane stability

  1989cited by this paper
• Linker insertion-deletion mutagenesis of the v-src gene: isolation of host- and temperature-dependent mutants

  1989cited by this paper
• Deletions within the amino-terminal half of the c-src gene product that alter the functional activity of the protein

  1989cited by this paper
• A mutation in v-src that removes a single conserved residue in the SH-2 domain of pp60v-src restricts transformation in a host-dependent manner

  1989cited by this paper
• Mutation of amino acids in pp60c-src that are phosphorylated by protein kinases C and A

  1989cited by this paper
• Structural differences between repressed and derepressed forms of p60c-src

  1989cited by this paper
• Platelet-derived growth factor induces multisite phosphorylation of pp60c-src and increases its protein-tyrosine kinase activity

  1988cited by this paper
• Peptide antibodies to the human c‐fyn gene product demonstrate pp59c‐fyn is capable of complex formation with the middle‐T antigen of polyomavirus.

  1988cited by this paper
• Substitution of Ser-17 of pp60c-src: biological and biochemical characterization in chicken embryo fibroblasts

  1988cited by this paper
• A novel viral oncogene with structural similarity to phospholipase C

  1988cited by this paper
• Sequence similarity of phospholipase C with the non-catalytic region of src

  1988cited by this paper
• Non-catalytic domains of cytoplasmic protein-tyrosine kinases: regulatory elements in signal transduction.

  1988cited by this paper
• The carboxy terminus of pp60c-src is a regulatory domain and is involved in complex formation with the middle-T antigen of polyomavirus

  1988cited by this paper
• Regulation by the autophosphorylation site in overexpressed pp60c-src

  1988cited by this paper
• Activation of the oncogenic potential of the avian cellular src protein by specific structural alteration of the carboxy terminus.

  1987cited by this paper
• The structurally distinct form of pp60c-src detected in neuronal cells is encoded by a unique c-src mRNA

  1987cited by this paper
• Neuronal pp60c-src contains a six-amino acid insertion relative to its non-neuronal counterpart.

  1987cited by this paper
• Identification of an amino terminal domain required for the transforming activity of the Rous sarcoma virus src protein.

  1987cited by this paper
• Characterization of the altered form of the c-src gene product in neuronal cells.

  1987cited by this paper
• Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-src.

  1987cited by this paper
• Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation.

  1987cited by this paper
• In vivo effect of sodium orthovanadate on pp60c-src kinase

  1987cited by this paper
• Cell transformation by pp60c-src mutated in the carboxy-terminal regulatory domain.

  1987cited by this paper
• A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps

  1986cited by this paper
• Retrovirus shuttle vector for study of kinase activities of pp60c-src synthesized in vitro and overproduced in vivo

  1986cited by this paper
• Amino acid substitutions sufficient to convert the nontransforming p60c-src protein to a transforming protein

  1986cited by this paper
• Dephosphorylation or antibody binding to the carboxy terminus stimulates pp60c-src

  1986cited by this paper
• Mutations around the NG59 lesion indicate an active association of polyoma virus middle‐T antigen with pp60c‐src is required for cell transformation.

  1986cited by this paper
• Altered sites of tyrosine phosphorylation in pp60c-src associated with polyomavirus middle tumor antigen

  1986cited by this paper
• Tyr527 is phosphorylated in pp60c-src: implications for regulation.

  1986cited by this paper
• Restriction of the in vitro and in vivo tyrosine protein kinase activities of pp60c-src relative to pp60v-src

  1985cited by this paper
• Protein kinase C phosphorylates pp60src at a novel site.

  1985cited by this paper
• Low level of cellular protein phosphorylation by nontransforming overproduced p60c-src

  1985cited by this paper
• The product of the protooncogene c-src is modified during the cellular response to platelet-derived growth factor.

  1985cited by this paper
• Activation of the pp60c‐src kinase by middle T antigen binding or by dephosphorylation.

  1985cited by this paper
• Protein-tyrosine kinases.

  1985cited by this paper
• Tyrosine phosphorylation within the amino-terminal domain of pp60c-src molecules associated with polyoma virus middle-sized tumor antigen.

  1985cited by this paper
• Overexpressed pp60c-src can induce focus formation without complete transformation of NIH 3T3 cells

  1985cited by this paper
• Overexpression of the c-src protein does not induce transformation of NIH 3T3 cells.

  1984cited by this paper
• Rous sarcoma virus variants that carry the cellular src gene instead of the viral src gene cannot transform chicken embryo fibroblasts.

  1984cited by this paper
• The complex of polyoma virus middle‐T antigen and pp60c‐src.

  1984cited by this paper
• The stimulation of pp60v-src kinase activity by vanadate in intact cells accompanies a new phosphorylation state of the enzyme.

  1984cited by this paper
• Structurally and functionally modified forms of pp60v-src in Rous sarcoma virus-transformed cell lysates

  1984cited by this paper
• Monoclonal antibodies to Rous sarcoma virus pp60src react with enzymatically active cellular pp60src of avian and mammalian origin

  1984cited by this paper
• Expression of v-src and chicken c-src in rat cells demonstrates qualitative differences between pp60v-src and pp60c-src.

  1984cited by this paper
• Construction of a retrovirus packaging mutant and its use to produce helper-free defective retrovirus.

  1983cited by this paper
• Polyoma virus transforming protein associates with the product of the c-src cellular gene

  1983cited by this paper
• Characterization of sites for tyrosine phosphorylation in the transforming protein of Rous sarcoma virus (pp60v-src) and its normal cellular homologue (pp60c-src).

  1981cited by this paper
• Transforming gene product of Rous sarcoma virus phosphorylates tyrosine

  1980cited by this paper
• Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.

  1977cited by this paper

• Phosphorylation of Vanilloid Receptor 1 by Ca2+/Calmodulin-dependent Kinase II Regulates Its Vanilloid Binding*

  2004cites this paper
• Protein phosphorylation and dephosphorylation in physiologic and oncologic processes.

  1996cites this paper
• Requirement for c-Src Catalytic Activity and the SH3 Domain in Platelet-derived Growth Factor BB and Epidermal Growth Factor Mitogenic Signaling*

  1996cites this paper
• Mutations in v-Src SH3 and catalytic domains that jointly confer temperature-sensitive transformation with minimal temperature-dependent changes in cellular tyrosine phosphorylation

  1994cites this paper
• Biochemistry of the Src protein-tyrosine kinase: regulation by SH2 and SH3 domains.

  1994cites this paper
• Substrate affinity of the protein tyrosine kinase pp60c-src is increased on thrombin stimulation of human platelets.

  1993cites this paper
• Csk inhibition of c‐Src activity requires both the SH2 and SH3 domains of Src.

  1993cites this paper
• Both the SH2 and SH3 domains of human CRK protein are required for neuronal differentiation of PC12 cells

  1993cites this paper
• Biological and biochemical activity of v-Crk chimeras containing the SH2/SH3 regions of phosphatidylinositol-specific phospholipase C-gamma and Src

  1992cites this paper
• Characterization of protein tyrosine kinases from human breast cancer: involvement of the c-src oncogene product.

  1992cites this paper
• Two species of human CRK cDNA encode proteins with distinct biological activities

  1992cites this paper
• The amino-terminal half of pp59c-fyn contains sequences necessary for formation of a 75 kDa form and also repressive elements absent in pp60c-src.

  1992cites this paper
• Small deletion in v-src SH3 domain of a transformation defective mutant of Rous sarcoma virus restores wild type transforming properties.

  1992cites this paper
• Phosphorylation of the R domain by cAMP-dependent protein kinase regulates the CFTR chloride channel.

  1991cites this paper
• Structural elements that regulate pp59c-fyn catalytic activity, transforming potential, and ability to associate with polyomavirus middle-T antigen

  1991influential citation
• Oncoprotein kinases in mitosis.

  1991cites this paper
• Identification of domains of the v-crk oncogene product sufficient for association with phosphotyrosine-containing proteins

  1991cites this paper
• Stoichiometry of cellular and viral components in the polyomavirus middle-T antigen-tyrosine kinase complex

  1990cites this paper