Augustin Y Lin

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The interaction of the T cell receptor for antigen (TCR) with its antigen-major histocompatibility complex ligand is difficult to study because both are cell surface multimers. The TCR consists of two chains (alpha and beta) that are complexed to the five or more nonpolymorphic CD3 polypeptides. A soluble form of the TCR was engineered by replacing the(More)
Immunoglobulin heavy chain binding protein (BiP, GRP 78) coprecipitates with soluble and membrane-associated variants of the T-cell antigen receptor a chain (TCR-a) which are stably retained within the ER. Chelation of Caz+ during solubilization of cells leads to the dissociation of BiP from the TCR-a variants, which is dependent upon the availability of(More)
Immunoglobulin heavy chain binding protein (BiP, GRP 78) coprecipitates with soluble and membrane-associated variants of the T-cell antigen receptor alpha chain (TCR-alpha) which are stably retained within the ER. Chelation of Ca2+ during solubilization of cells leads to the dissociation of BiP from the TCR-alpha variants, which is dependent upon the(More)
M.M. DAvaS,*t L.J. BERG,t..A.Y. Ln~,*t B. FAZEKAS DE ST. GROTH,t B. DEVAUX,*t C.G. SAGERSTROM,t P.J. BJORKMAN,r AND J .F . ELLIOTTtw *Howard Hughes Medical Institute and tThe Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, California 94305-5428; J~Biology Division, The California Institute of Technology,(More)
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