HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells

@article{Schaiff1992HLADRAW,
  title={HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells},
  author={W Timothy Schaiff and Keith A. Hruska and David McCourt and Martin X Green and Benjamin D. Schwartz},
  journal={The Journal of Experimental Medicine},
  year={1992},
  volume={176},
  pages={657 - 666}
}
The major histocompatibility complex class II molecules are composed of two polymorphic chains which, in cells normally expressing them, transiently associate with a third, nonpolymorphic molecule, the invariant chain (Ii). To determine differences in the biology of class II molecules synthesized in the presence or absence of Ii, a comparative study was performed of BALB/c 3T3 cells that had been transfected with human class II HLA-DR molecules with or without cotransfection with human Ii. It… CONTINUE READING

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Proteolysis of the class II-associated invariant chain generates a peptide binding site in intraceUular HLA-DR molecules

  • P. A. Roche, P. Cresswdl
  • Proc. Natl. Acad. Sci. USA
  • 1991

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