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January 1, 1990Journal of Biological ChemistryOpen Access

Analysis of deletions of the carboxyl terminus of the epidermal growth factor receptor reveals self-phosphorylation at tyrosine 992 and enhanced in vivo tyrosine phosphorylation of cell substrates.

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Authors

GWGordon M. WaltonUniversity of ManchesterWCW S ChenHoward Hughes Medical InstituteMRM G RosenfeldHoward Hughes Medical Institute

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Walton et al. (1990) studied this question.

synapsesocial.com/papers/6a1708ae2fcf950e000593bchttps://doi.org/10.1016/s0021-9258(19)40080-x
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Alteration of epidermal growth factor receptor activity by mutation of its primary carboxyl-terminal site of tyrosine self-phosphorylation.1988 · 115 citations
  2. 2Self-phosphorylation enhances the protein-tyrosine kinase activity of the epidermal growth factor receptor.1985 · 232 citations
  3. 3Growth stimulation of A431 cells by epidermal growth factor: identification of high-affinity receptors for epidermal growth factor by an anti-receptor monoclonal antibody.1983 · 800 citations
  4. 4Phosphorylation sites in enolase and lactate dehydrogenase utilized by tyrosine protein kinases in vivo and in vitro.1984 · 414 citations
  5. 5PROTEIN-TYROSINE KINASES1985 · 2,142 citations