The Ick tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain
Shaw A, Amrein K, Hammond C, Stern D, Sefton B, Rose J. The Ick tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain. Cell 1989, 59: 627-636. PMID: 2582490, DOI: 10.1016/0092-8674(89)90008-1.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCD4 AntigensCytoplasmHeLa CellsHumansLymphocyte Specific Protein Tyrosine Kinase p56(lck)Macromolecular SubstancesMembrane GlycoproteinsMolecular Sequence DataMutationOligonucleotide ProbesPhosphoproteinsPlasmidsProtein BindingProtein MultimerizationProtein-Tyrosine KinasesT-LymphocytesTransfectionConceptsAmino-terminal domainCytoplasmic domainTyrosine protein kinase p56lckUnique amino-terminal domainT cell-specific proteinsTyrosine protein kinaseSpecific transmembrane proteinsCell-specific proteinsIntracellular tyrosine kinaseAmino-terminal residuesCarboxy-terminal residuesTransmembrane proteinCytoplasmic tailSrc familyProtein kinaseKinase p56lckTyrosine kinaseHeLa cellsCell surfaceProteinDeleted formsSurface glycoproteinP56lckKinaseResiduesBiosynthesis of a Phosphatidylinositol-Glycan-Linked Membrane Protein: Signals for Posttranslational Processing of the Ly-6E Antigen
Su B, Bothwell A. Biosynthesis of a Phosphatidylinositol-Glycan-Linked Membrane Protein: Signals for Posttranslational Processing of the Ly-6E Antigen. Molecular And Cellular Biology 1989, 9: 3369-3376. DOI: 10.1128/mcb.9.8.3369-3376.1989.Peer-Reviewed Original ResearchPhosphatidylinositol-glycanPhosphatidylinositol-glycan tailMutant proteinsLy-6Proteolytic cleavagePhosphatidylinositol glycan moietyPrimary translation productAmino acid sitesLy-6 proteinsCarboxy-terminal residuesTransient transfection proceduresCell surface proteinsMurine cell surface proteinLy-6 antigensCytoplasmic tailTranslation productsCleavage siteAsn residuesCOS cellsMembrane proteinsCOOH terminusPosttranslational processingPlasma membraneSurface proteinsTransmembrane form
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