| Stabilization of EREG via STT3B-mediated N-glycosylation is critical for PDL1 upregulation and immune evasion in head and neck squamous cell carcinoma. | Stabilization of EREG via STT3B-mediated N-glycosylation is critical for PDL1 upregulation and immune evasion in head and neck squamous cell carcinoma.
Xu S, Wang H, Zhu Y, Han Y, Liu L, Zhang X, Hu J, Zhang W, Duan S, Deng J, Zhang Z, Liu S., Free PMC Article | 07/5/2024 |
| Proteome and Glycoproteome Analyses Reveal the Protein N-Linked Glycosylation Specificity of STT3A and STT3B. | Proteome and Glycoproteome Analyses Reveal the Protein N-Linked Glycosylation Specificity of STT3A and STT3B.
Wen P, Chen J, Zuo C, Gao X, Fujita M, Yang G., Free PMC Article | 10/8/2022 |
| Acceptor sites located in short loops of multi-spanning membrane proteins represent a new class of STT3B-dependent site. | Quantitative glycoproteomics reveals new classes of STT3A- and STT3B-dependent N-glycosylation sites.
Cherepanova NA, Venev SV, Leszyk JD, Shaffer SA, Gilmore R., Free PMC Article | 05/23/2020 |
| The endoplasmic reticulum-localized mEGFP mutants contained an N-glycosylation sequon at their C-terminus and had increased fluorescence upon N-glycosylation. Among the mutants tested, the ER-mEGFP mutant containing the N185 -C186 -T187 sequon was the best substrate for the STT3B isoform in terms of glycosylation efficiency and fluorescence change. | Construction of green fluorescence protein mutant to monitor STT3B-dependent N-glycosylation.
Kitajima T, Xue W, Liu YS, Wang CD, Liu SS, Fujita M, Gao XD. | 01/12/2019 |
| Study reports that STT3B-oligosaccharyltransferase, but not STT3A-oligosaccharyltransferase, is a lipid-linked oligosaccharide hydrolase. | Mammalian STT3A/B oligosaccharyltransferases segregate N-glycosylation at the translocon from lipid-linked oligosaccharide hydrolysis.
Lu H, Fermaintt CS, Cherepanova NA, Gilmore R, Yan N, Lehrman MA., Free PMC Article | 10/13/2018 |
| These results reveal that the oxidoreductase activity of the STT3B-containing oligosaccharyltransferase is necessary for dengue virus infection. | Dengue Virus Hijacks a Noncanonical Oxidoreductase Function of a Cellular Oligosaccharyltransferase Complex.
Lin DL, Cherepanova NA, Bozzacco L, MacDonald MR, Gilmore R, Tai AW., Free PMC Article | 03/24/2018 |
| STT3B was significantly upregulated in hip osteoarthritis with affected versus intact cartilage, particularly in the analysis of hypertrophic and normotrophic compared with atrophic bone remodelling pattern. | Radiographic endophenotyping in hip osteoarthritis improves the precision of genetic association analysis.
Panoutsopoulou K, Thiagarajah S, Zengini E, Day-Williams AG, Ramos YF, Meessen JM, Huetink K, Nelissen RG, Southam L, Rayner NW, arcOGEN Consortium, Doherty M, Meulenbelt I, Zeggini E, Wilkinson JM., Free PMC Article | 08/26/2017 |
| Post-translational modification of cotranslationally skipped sites by STT3B is hindered by the middle X residue, resulting in hypoglycosylation of consensus sites containing large hydrophobic and negatively charged side chains. | The middle X residue influences cotranslational N-glycosylation consensus site skipping.
Malaby HL, Kobertz WR., Free PMC Article | 09/27/2014 |
| Results show homozygous mutation in STT3A and in STT3B causes congenital disorders of glycosylation. | Mutations in STT3A and STT3B cause two congenital disorders of glycosylation.
Shrimal S, Ng BG, Losfeld ME, Gilmore R, Freeze HH., Free PMC Article | 06/7/2014 |
| Extreme C-terminal sites are posttranslocationally glycosylated by the STT3B isoform of the OST. | Extreme C-terminal sites are posttranslocationally glycosylated by the STT3B isoform of the OST.
Shrimal S, Trueman SF, Gilmore R., Free PMC Article | 05/25/2013 |
| Data show that prolonged transthyretin (TTR) unfolding induces externalization of cryptic N-glycosylation site and triggers STT3B-dependent posttranslational N-glycosylation. | STT3B-dependent posttranslational N-glycosylation as a surveillance system for secretory protein.
Sato T, Sako Y, Sho M, Momohara M, Suico MA, Shuto T, Nishitoh H, Okiyoneda T, Kokame K, Kaneko M, Taura M, Miyata M, Chosa K, Koga T, Morino-Koga S, Wada I, Kai H. | 10/27/2012 |
| Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator) | Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score.
Rose JE, Behm FM, Drgon T, Johnson C, Uhl GR., Free PMC Article | 06/30/2010 |
| The STT3B isoform is required for efficient cotranslational glycosylation of an acceptor site adjacent to the N-terminal signal sequence of a secreted protein. | Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms.
Ruiz-Canada C, Kelleher DJ, Gilmore R., Free PMC Article | 01/21/2010 |
| STT3 proteins are the catalytic subunits of the oligosaccharyltransferase. Vertebrate, plant and insect genomes have an STT3A gene and a STT3B gene. SIMP is a member of the STT3B subfamily of STT3 proteins. | Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties.
Kelleher DJ, Karaoglu D, Mandon EC, Gilmore R. | 08/9/2005 |