ArticleCell2009
Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms.
Article in Cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 242 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
242 citing papers in PubMed, 402 citations in OpenAlex.
- The SLC-ome of membrane transport: from molecular discovery to physiology and clinical applications.Physiological reviews · 2026Review
- N-linked glycosylation sites with low occupancy support sustained circulation of the A(H3N2) influenza A virus in the human population.Journal of virology · 2026Article
- Micro- and Macro-Heterogeneity of N-Glycoproteome Remodeling in Endoplasmic Reticulum Stress.Molecular & cellular proteomics : MCP · 2026Article
- Expanding roles of N-glycosylation in the endoplasmic reticulum.Trends in cell biology · 2026Review
- A homozygous nonsense variant in the oligosaccharyltransferase complex gene, RPN1, causes a congenital disorder of glycosylation.HGG advances · 2026Article
- Taxonomic context and genomic architecture jointly shape expression divergence across animals.Evolution; international journal of organic evolution · 2026Article
- Article
- Membrane Protein Glycosylation Revisited: Functional Dynamics and Emerging Clinical Insights.International journal of molecular sciences · 2026Review
- The Oligosaccharyltransferase Catalytic Subunit PsSTT3B Is Required for Asexual Development and Pathogenicity inJournal of fungi (Basel, Switzerland) · 2026Article
- Calsyntenin-3 suppresses inflammation via inhibition of TLR N-glycosylation and membrane localization.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Differential contributions of human oligosaccharyltransferase complexes OST-A and OST-B to HIV-1 envelope glycoprotein glycosylation.Journal of virology · 2026Article
- Mannose metabolic pathway senses glucose supply and regulates cell fate decisions.The Journal of biological chemistry · 2026Article
- Posttranslational modifications of heterologous proteins expressed in Nicotiana benthamiana.Plant biotechnology journal · 2026Review
- Article
- Chemical inhibition of α-mannosidase inFrontiers in parasitology · 2026Article
- Oligosaccharyltransferase (OST) complex inhibition effectively treats rodent and human prions.PLoS pathogens · 2026Article
- O-mannosylation of misfolded ER proteins promotes ERAD.The EMBO journal · 2026Article
- Functional inactivation of oligosaccharyltransferase a isoform suppresses tumor metastasis.Glycobiology · 2025Article
- Taxonomic context and genomic architecture jointly shape expression divergence across animals.bioRxiv : the preprint server for biology · 2025Article
- Global analysis of translocon remodeling during protein synthesis at the ER.Nature structural & molecular biology · 2025Article
182 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Asparagine-linked glycosylation of polypeptides in the lumen of the endoplasmic reticulum is catalyzed by the hetero-oligomeric oligosaccharyltransferase (OST). OST isoforms with different catalytic subunits (STT3A versus STT3B) and distinct enzymatic properties are coexpressed in mammalian cells. Using siRNA to achieve isoform-specific knockdowns, we show that the OST isoforms cooperate and act sequentially to mediate protein N-glycosylation. The STT3A OST isoform is primarily responsible for cotranslational glycosylation of the nascent polypeptide as it enters the lumen of the endoplasmic reticulum. The STT3B isoform is required for efficient cotranslational glycosylation of an acceptor site adjacent to the N-terminal signal sequence of a secreted protein. Unlike STT3A, STT3B efficiently mediates posttranslational glycosylation of a carboxyl-terminal glycosylation site in an unfolded protein. These distinct and complementary roles for the OST isoforms allow sequential scanning of polypeptides for acceptor sites to insure the maximal efficiency of N-glycosylation.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.