The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Analysis of the sequence of amino acids surrounding sites of tyrosine phosphorylation.
Open accessAbstract
We have identified the single phosphorylated tyrosine in p60src, the transforming protein of Rous sarcoma virus, as part of the sequence. NH2-Arg-Leu-Ile-Glu-Asp-Asn-Glu-Tyr(P)-Thr-Ala-Arg-COOH. Therefore, this is a sequence that is recognized efficiently by a tyrosine protein kinase in vivo. Phosphorylation of tyrosine in cellular proteins appears to play a role in malignant transformation by four classes of genetically distinct RNA tumor viruses. Phosphorylated tyrosines in several other proteins resemble of the tyrosine in p60src in that they are located 7 residues to the COOH-terminal side of a basic amino acid and either 4 residues to the COOH-terminal side of, or in close proximity to, a glutamic acid residue. Therefore it is possible that these features play a role in the selection of sites of phosphorylation by some tyrosine protein kinases. However, several clear exceptions to this rule exist.
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Cites
Transforming gene product of Rous sarcoma virus phosphorylates tyrosine
Hunter, T., & Sefton, B. M. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.3.1311 · Cited by 2,332
Self-citationUshiro, H., & Cohen, S. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43497-7 · Cited by 1,169
Kemp, B. E., Graves, D. J., Benjamini, E., & Krebs, E. G. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40137-2 · Cited by 835
Staphylococcal Protease: A Proteolytic Enzyme Specific for Glutamoyl Bonds
Houmard, J., & Drapeau, G. R. (1972) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.69.12.3506 · Cited by 696
Sefton, B. M., Hunter, T., Beemon, K., & Eckhart, W. (1980) · Cell · doi:10.1016/0092-8674(80)90327-x · Cited by 546
Self-citationAbelson murine leukaemia virus protein is phosphorylated in vitro to form phosphotyrosine
Witte, O. N., Dasgupta, A., & Baltimore, D. (1980) · Nature · doi:10.1038/283826a0 · Cited by 530
Collett, M. S., Purchio, A. F., & Erikson, R. L. (1980) · Nature · doi:10.1038/285167a0 · Cited by 490
Changes in protein phosphorylation in Rous sarcoma virus-transformed chicken embryo cells.
Cooper, J. A., & Hunter, T. (1981) · Molecular and Cellular Biology · doi:10.1128/mcb.1.2.165 · Cited by 447
Self-citationSmart, J. E., Oppermann, H., Czernilofsky, A. P., Purchio, A. F., Erikson, R. L., & Bishop, J. M. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.10.6013 · Cited by 358
Characterization of Rous sarcoma virus src gene products synthesized in vitro
Beemon, K., & Hunter, T. (1978) · Journal of Virology · doi:10.1128/jvi.28.2.551-566.1978 · Cited by 338
Self-citation
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Identification and characterization of the tuberous sclerosis gene on chromosome 16
(1993) · Cell · doi:10.1016/0092-8674(93)90618-z · Cited by 1,645
Ellis, L., Clauser, E., Morgan, D. O., Edery, M., Roth, R. A., & Rutter, W. J. (1986) · Cell · doi:10.1016/0092-8674(86)90786-5 · Cited by 1,070
Molecular cloning and expression of a receptor for human tumor necrosis factor
Schall, T. J., Lewis, M., Koller, K. J., Lee, A., Rice, G. C., Wong, G. H. W., Gatanaga, T., Granger, G. A., Lentz, R., Raab, H., et al. (1990) · Cell · doi:10.1016/0092-8674(90)90816-w · Cited by 964
Autophosphorylation sites on the epidermal growth factor receptor
Downward, J., Parker, P., & Waterfield, M. D. (1984) · Nature · doi:10.1038/311483a0 · Cited by 704
Kmiecik, T. E., & Shalloway, D. (1987) · Cell · doi:10.1016/0092-8674(87)90756-2 · Cited by 623
Metadata
- Authors
- Patschinsky, T., Hunter, T., Esch, F. S., Cooper, J. A., & Sefton, B. M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1982-02
- Volume
- 79
- Issue
- 4
- Pages
- 973-977
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2111941226
- Cited by
- 313
- References
- 26
- FWCI
- 11.62
- Type
- journal article
- Language
- en
- Open access
- green
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- Patschinsky, T., Hunter, T., Esch, F. S., Cooper, J. A., & Sefton, B. M. (1982). Analysis of the sequence of amino acids surrounding sites of tyrosine phosphorylation. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.79.4.973
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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