Crossref journal-article
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences (341)
Abstract

Cell surface proteins of cultured cells are disulfide bonded to a greater degree than are total cellular proteins. In particular, the "large external transformation-sensitive" (LETS) protein, a major surface protein, is present almost exclusively in disulfide-bonded complexes including homodimers and also higher aggregates held together by disulfide bonds or concovalent interactions. Other cell surface proteins also appear to be involved in disulfide bonding, both intramolecular and intermolecular. In virally transformed cells, LETS protein and its disulfide complexes are absent and certain other disulfide-bonded proteins are also not observed.

Bibliography

Hynes, R. O., & Destree, A. (1977). Extensive disulfide bonding at the mammalian cell surface. Proceedings of the National Academy of Sciences, 74(7), 2855–2859.

Authors 2
  1. R O Hynes (first)
  2. A Destree (additional)
References 0 Referenced 104

None

Dates
Type When
Created 19 years, 2 months ago (May 31, 2006, 3:33 a.m.)
Deposited 3 years, 4 months ago (April 13, 2022, 11:17 a.m.)
Indexed 1 month, 4 weeks ago (July 1, 2025, 12:31 p.m.)
Issued 48 years, 1 month ago (July 1, 1977)
Published 48 years, 1 month ago (July 1, 1977)
Published Online 48 years, 1 month ago (July 1, 1977)
Published Print 48 years, 1 month ago (July 1, 1977)
Funders 0

None

@article{Hynes_1977, title={Extensive disulfide bonding at the mammalian cell surface.}, volume={74}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.74.7.2855}, DOI={10.1073/pnas.74.7.2855}, number={7}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Hynes, R O and Destree, A}, year={1977}, month=jul, pages={2855–2859} }