Kb, Kd, and Ld molecules share common tapasin dependencies as determined using a novel epitope tag.

@article{Myers2000KbKA,
  title={Kb, Kd, and Ld molecules share common tapasin dependencies as determined using a novel epitope tag.},
  author={Nancy B. Myers and Michael R. Harris and Janet M. Connolly and Lonnie P Lybarger and Yik Yeung Lawrence Yu and Ted H. Hansen},
  journal={Journal of immunology},
  year={2000},
  volume={165 10},
  pages={5656-63}
}
The endoplasmic reticulum protein tapasin is considered to be a class I-dedicated chaperone because it facilitates peptide loading by proposed mechanisms such as peptide editing, endoplasmic reticulum retention of nonpeptide-bound molecules, and/or localizing class I near the peptide source. Nonetheless, the primary functions of tapasin remain controversial as do the relative dependencies of different class I molecules on tapasin for optimal peptide loading and surface expression. Tapasin… CONTINUE READING

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