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Rites of Passage: Moving Biotech Proteins Through the ER

Bio/Technology volume 10, pages 1413–1420 (1992)Cite this article

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References

  1. Hwang, C., Sinskey, A. and Lodish, H. 1992. The oxidized redox potential in the endoplasmic reticulum: Glutathione as the principal redox buffer. science 257.

  2. Lodish, H., Kong, N. and Wikstrom, L. 1992. Calcium is required for folding of newly made subunits of the asialoglycoprotein receptor within the endoplasmic reticulum. J. Biol. Chem. 267: 12753–12760.

    CAS  PubMed  Google Scholar 

  3. Braakmam, I., Helenius, J. and Helenius, A. 1992. Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum. Nature 356: 260–262.

    Article  Google Scholar 

  4. Braakman, I., Helenius, J. and Helenius, A. 1992. Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum. EMBO. 11: 1717–1722.

    Article  CAS  Google Scholar 

  5. Gething, M.-J. and Sambrook, J. 1992. Protein folding in the cell. Nature 355: 33–45.

    Article  CAS  PubMed  Google Scholar 

  6. Puig, A. and Gilbert, H. 1992. Heavy chain binding protein (BiP) and protein disulfide isomerase (PDI): cooperation or competition in protein folding. 1992. ASBMBSymposia Abstract.

  7. Dorner, A., Krane, M. and Kaufman, R. 1988. Reduction of endogenous GRP78 levels improves secretion of a heterologous protein in CHO cells. Mol. Cell. Bio. 8: 4063–4070.

    Article  CAS  Google Scholar 

  8. Dorner, A., Wasley, L. and Kaufman, R. 1989. Increased synthesis of secreted proteins induces expression of glucose-regulated proteinsin butyrate-treated chinese hamster ovary cells. J. Biol. Chem. 264: 20602–20607.

    CAS  PubMed  Google Scholar 

  9. Dorner, A., Wasley, L. and Kaufman, R. 1992. Overexpression of GRP78 mitigates stress induction of glucose regulated proteins and blocks secretion of selective proteinsin chinese hamster ovary cells. EMBO. 11: 1563–1571.

    Article  CAS  Google Scholar 

  10. Dorner, A., Wasley, L. and Kaufman, R. 1990. Protein dissociation from GRP78 and secretion are blocked by depletion of cellular ATP levels. Proc. Natl. Acad. Sci. U. S. A. 87: 7429–7432.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  11. Robinson, A. and Wittrup, K.A. 1992. The role of the protein folding chaperone BiP in secretion of foreign proteins in eucaryotic cells. ACS Symposium Series, Protein Folding: In Vitro and In Vivo.

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  1. senior editor of Bio/Technology,

    Stephen M. Edgington

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Edgington, S. Rites of Passage: Moving Biotech Proteins Through the ER. Nat Biotechnol 10, 1413–1420 (1992). https://doi.org/10.1038/nbt1192-1413

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