Mammalian glycophosphatidylinositol anchor transfer to proteins and posttransfer deacylation.

@article{Chen1998MammalianGA,
  title={Mammalian glycophosphatidylinositol anchor transfer to proteins and posttransfer deacylation.},
  author={Rui Chen and Enrico Walter and Gregory D. Parker and J P Lapurga and J. L. Mill{\'a}n and Yukio Ikehara and Sidney Udenfriend and M. Edward Medof},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1998},
  volume={95 16},
  pages={
          9512-7
        }
}
The glycophosphatidylinositol (GPI) anchors of proteins expressed on human erythrocytes and nucleated cells differ with respect to acylation of an inositol hydroxyl group, a structural feature that modulates their cleavability by PI-specific phospholipase C (PI-PLC). To determine how this GPI anchor modification is regulated, the precursor and protein-associated GPIs in two K562 cell transfectants (ATCC and .48) exhibiting alternatively PI-PLC-sensitive and resistant surface proteins were… CONTINUE READING

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