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The unique amino-terminal domain of p56lck regulates interactions with tyrosine protein phosphatases in T lymphocytes.

The catalytic activity of p56lck is repressed by phosphorylation of a conserved carboxy-terminal tyrosine residue (tyrosine 505). Accumulating data show that this phosphorylation is mediated by the tyrosine protein kinase p50csk and that it is reversed by the transmembrane tyrosine protein phosphata...

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Détails bibliographiques
Auteurs principaux: Gervais, F G, Veillette, A
Format: Artigo
Langue:Inglês
Publié: 1995
Sujets:
Accès en ligne:https://ncbi.nlm.nih.gov/pmc/articles/PMC230468/
https://ncbi.nlm.nih.gov/pubmed/7739523
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