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Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
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Disulfide exchange in multimerization of von Willebrand factor and gel-forming mucins

Xianchi Dong1,2,3, Timothy A Springer4,5,6

  • 1State Key Laboratory of Pharmaceutical Biotechnology.

Blood
|September 22, 2020
PubMed
Abstract

No abstract available in PubMed .

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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