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October 1, 1993Molecular and Cellular BiologyOpen Access

Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fyn mediates interaction with glycosyl-phosphatidylinositol-anchored proteins.

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Authors

ASA M Shenoy-ScariaWashington University in St. LouisLGLisa K. Timson GauenWashington University in St. LouisJKJacky M. K. KwongRush University Medical Center

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Shenoy-Scaria et al. (1993) studied this question.

synapsesocial.com/papers/6a3f9f7aef8b3439f071c8f2https://doi.org/10.1128/mcb.13.10.6385
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Also Consider

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

  1. 1Short Related Sequences in the Cytoplasmic Domains of CD4 and CD8 Mediate Binding to the Amino-Terminal Domain of the p56 <i> <sup>lck</sup> </i> Tyrosine Protein Kinase1990 · 244 citations
  2. 2Role of Ly-6 in lymphocyte activation. II. Induction of T cell activation by monoclonal anti-Ly-6 antibodies.1986 · 190 citations
  3. 3Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface1992 · 2,933 citations
  4. 4p59fyn tyrosine kinase associates with multiple T-cell receptor subunits through its unique amino-terminal domain.1992 · 207 citations
  5. 5The glycosyl phosphatidylinositol anchor is critical for Ly-6A/E-mediated T cell activation.1991 · 97 citations