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February 1, 1984Proceedings of the National Academy of SciencesOpen Access

Transformation by polyoma virus is drastically reduced by substitution of phenylalanine for tyrosine at residue 315 of middle-sized tumor antigen.

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Authors

GCGordon CarmichaelUConn HealthBSBrian SchaffhausenTufts UniversityGMGail MandelOregon Health & Science University

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Cite This Study

Carmichael et al. (1984) studied this question.

synapsesocial.com/papers/6a72c09e3ce530166bc35f97https://doi.org/10.1073/pnas.81.3.679
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Also Consider

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

  1. 1Comparison of phosphorylation of two polyoma virus middle T antigens in vivo and in vitro1981 · 137 citations
  2. 2Carboxy terminus of polyoma middle-sized tumor antigen is required for attachment to membranes, associated protein kinase activities, and cell transformation.1982 · 141 citations
  3. 3Polyoma virus middle T antigen: relationship to cell membranes and apparent lack of ATP-binding activity.1982 · 73 citations
  4. 4Differential subcellular localization of in vivo-phosphorylated and nonphosphorylated middle-sized tumor antigen of polyoma virus and its relationship to middle-sized tumor antigen phosphorylating activity in vitro.1982 · 56 citations
  5. 5DNA sequencing with chain-terminating inhibitors1977 · 69,520 citations