Formation and transfer of disulphide bonds in living cells

By C. Sevier, C. Kaiser. Nature reviews. Molecular cell biology, 2002

781 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/e8cafbe7b7a61b894defa516f67cd3bcf72feb7e

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. F. Papa
2. C. Hetz
3. Roberto Sitia
4. I. Braakman

In Molecular Biology

1. C. Hetz
2. Roberto Sitia
3. F. Papa
4. I. Braakman

Citations in the corpus

• The Unfolded Protein Response and Cell Fate Control. (2017, positive): “These processes are catalyzed by an ER-resident proteinfolding and modification machinery comprising a network of chaperones, glycosylating enzymes, and oxido-reductases (Sevier and Kaiser, 2002).”
• The in silico human surfaceome (2018, background): “This presumably reflects the fact that disulfide cross-links are vital for folding surface proteins into their native conformation and for their structural stability (60).”
• Quality control in the endoplasmic reticulum protein factory (2003, background): “The requirement for oxidative equivalents is fulfilled by Ero1 proteins, which transfer electrons from protein disulphide isomerase (PDI) to oxygen through a series of specific interchange reaction”