| STT3A-mediated viral N-glycosylation underlies the tumor selectivity of oncolytic virus M1. | STT3A-mediated viral N-glycosylation underlies the tumor selectivity of oncolytic virus M1.
Song D, Jia X, Gao Y, Xiao T, Dan J, Shen R, Cai J, Liang J, Zhu W, Hu J, Yan G, Zhang Q, Lin Y. | 11/30/2023 |
| 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 |
| Active site variants in STT3A cause a dominant type I congenital disorder of glycosylation with neuromusculoskeletal findings. | Active site variants in STT3A cause a dominant type I congenital disorder of glycosylation with neuromusculoskeletal findings.
Wilson MP, Garanto A, Pinto E Vairo F, Ng BG, Ranatunga WK, Ventouratou M, Baerenfaenger M, Huijben K, Thiel C, Ashikov A, Keldermans L, Souche E, Vuillaumier-Barrot S, Dupré T, Michelakakis H, Fiumara A, Pitt J, White SM, Lim SC, Gallacher L, Peters H, Rymen D, Witters P, Ribes A, Morales-Romero B, Rodríguez-Palmero A, Ballhausen D, de Lonlay P, Barone R, Janssen MCH, Jaeken J, Freeze HH, Matthijs G, Morava E, Lefeber DJ., Free PMC Article | 11/27/2021 |
| Analysis of site occupancy data disclosed several new classes of STT3A-dependent acceptor sites including those with suboptimal flanking sequences and sites located within cysteine-rich protein domains. | 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 |
| 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 |
| DC2 and KCP2 mediate the interaction between the oligosaccharyltransferase STT3A and the endoplasmic reticulum translocon. | DC2 and KCP2 mediate the interaction between the oligosaccharyltransferase and the ER translocon.
Shrimal S, Cherepanova NA, Gilmore R., Free PMC Article | 11/25/2017 |
| This study showed that Congenital Disorder of Glycosylation Caused by Mutations in STT3A. | Phenotypic Heterogeneity in a Congenital Disorder of Glycosylation Caused by Mutations in STT3A.
Ghosh A, Urquhart J, Daly S, Ferguson A, Scotcher D, Morris AAM, Clayton-Smith J. | 07/15/2017 |
| Consensus sites containing large hydrophobic and negatively charged middle residues are frequently skipped by STT3A during protein translation. | 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 |
| DDIT3, STT3A, ARG2 and FAM129A immunohistochemistry does not appear to be useful in the diagnosis of thyroid follicular neoplasias, as they do not reliably distinguish follicular thyroid carcinoma from follicular thyroid adenoma. | The new molecular markers DDIT3, STT3A, ARG2 and FAM129A are not useful in diagnosing thyroid follicular tumors.
Sigstad E, Paus E, Bjøro T, Berner A, Grøholt KK, Jørgensen LH, Sobrinho-Simões M, Holm R, Warren DJ., Free PMC Article | 08/4/2012 |
| Gene-expression data suggest a difference in expression between STT3A, Clorf24, and TFF3 in FAs versus carcinomas that may be detected from an FNA sample. Findings must be validated from preoperative FNAs in larger numbers | STT3A, C1orf24, TFF3: putative markers for characterization of follicular thyroid neoplasms from fine-needle aspirates.
Patel MR, Stadler ME, Deal AM, Kim HS, Shores CG, Zanation AM. | 07/2/2011 |
| The STT3A OST isoform is primarily responsible for cotranslational glycosylation of the nascent polypeptide as it enters the lumen of the endoplasmic reticulum. | 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 |