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- W4298332913 endingPage "731" @default.
- W4298332913 startingPage "716" @default.
- W4298332913 abstract "Proteins targeted for secretion contain an amino-terminus signal peptide that facilitates their recognition by a host of protein complexes that specialize in catalyzing protein export: chaperones, translocase, and a membrane bound hydrolase (signal peptidase) that cleaves off the signal peptide. In human cells the endoplasmic reticulum signal peptidase complex (hSPC) is a heterotetramer made up of the subunits SPCS1, SPCS2, SPCS3, with a catalytic subunit that can be either SEC11A or SEC11C. The SEC11 subunits utilize a serine nucleophile and a histidine general acid-base. Besides its critical role is cellular protein secretion, SPC is recruited by several RNA viruses to help in the viral protein maturation. There is also evidence to suggest that SPC plays a role in the progression of some cancers. This article summaries the progress on the structural and functional characterization of the eukaryotic signal peptidase complex." @default.
- W4298332913 created "2022-10-02" @default.
- W4298332913 creator A5048104268 @default.
- W4298332913 date "2023-01-01" @default.
- W4298332913 modified "2023-09-23" @default.
- W4298332913 title "The Endoplasmic Reticulum Signal Peptidase Complex" @default.
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