A method to quantify binding of unlabeled peptides to class I MHC molecules and detect their allele specificity.
A general method has been developed for measuring the stabilization of class I MHC molecules in extracts of the mutant cell lines .174/T2 and RMA-S. 35S-Met-labeled class I molecules which have been stabilized by peptides in vitro are immunoprecipitated with conformation dependent monoclonal antibod...
Váldodahkkit: | Elvin, J, Potter, C, Elliott, T, Cerundolo, V, Townsend, A |
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Materiálatiipa: | Journal article |
Giella: | English |
Almmustuhtton: |
1993
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Geahča maid
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The binding affinity and dissociation rates of peptides for class I major histocompatibility complex molecules.
Dahkki: Cerundolo, V, et al.
Almmustuhtton: (1991) -
Assembly of MHC class I molecules analyzed in vitro.
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Almmustuhtton: (1990) -
Biophysical evidence for conformational change in MHC class I molecules upon peptide binding
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Almmustuhtton: (1997) -
Fast association rates suggest a conformational change in the MHC class I molecule H-2Db upon peptide binding.
Dahkki: Springer, S, et al.
Almmustuhtton: (1998) -
Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer.
Dahkki: Spies, T, et al.
Almmustuhtton: (1992)