Other names published for OST3: YOR085W
OST3 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Cellular Location
- Function/Process
- Genetic Interactions
- Mutants/Phenotypes
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
OST3 - Function/Process (20)
| Reference | Other Genes Addressed |
|---|---|
| Hacioglu E, et al. (2010) The roles of thiol oxidoreductases in yeast replicative aging. Mech Ageing Dev 131(11-12):692-9 | |
| Schulz BL and Aebi M (2009) Analysis of glycosylation site occupancy reveals a role for Ost3p and Ost6p in site-specific N-glycosylation efficiency. Mol Cell Proteomics 8(2):357-64 | |
| Schulz BL, et al. (2009) Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency. Proc Natl Acad Sci U S A 106(27):11061-6 | |
| Krause SA, et al. (2008) The synthetic genetic network around PKC1 identifies novel modulators and components of protein kinase C signaling in Saccharomyces cerevisiae. Eukaryot Cell 7(11):1880-7 | |
| Pu S, et al. (2008) Local coherence in genetic interaction patterns reveals prevalent functional versatility. Bioinformatics 24(20):2376-83 | |
| Kelleher DJ, et al. (2007) Dolichol-linked oligosaccharide selection by the oligosaccharyltransferase in protist and fungal organisms. J Cell Biol 177(1):29-37 | |
| Chavan M, et al. (2005) Subunits of the translocon interact with components of the oligosaccharyl transferase complex. J Biol Chem 280(24):22917-24 | |
| Schuldiner M, et al. (2005) Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile. Cell 123(3):507-19 | |
| Schwarz M, et al. (2005) Yeast oligosaccharyltransferase consists of two functionally distinct sub-complexes, specified by either the Ost3p or Ost6p subunit. FEBS Lett 579(29):6564-8 | |
| Spirig U, et al. (2005) The 3.4-kDa Ost4 protein is required for the assembly of two distinct oligosaccharyltransferase complexes in yeast. Glycobiology 15(12):1396-406 | |
| Yan A, et al. (2003) New findings on interactions among the yeast oligosaccharyl transferase subunits using a chemical cross-linker. J Biol Chem 278(35):33078-87 | |
| Peluso S, et al. (2002) Neoglycopeptides as inhibitors of oligosaccharyl transferase: insight into negotiating product inhibition. Chem Biol 9(12):1323-8 | |
| Yan Q and Lennarz WJ (2002) Studies on the function of oligosaccharyl transferase subunits. Stt3p is directly involved in the glycosylation process. J Biol Chem 277(49):47692-700 | |
| Kim H, et al. (2000) Studies on the role of the hydrophobic domain of Ost4p in interactions with other subunits of yeast oligosaccharyl transferase. Proc Natl Acad Sci U S A 97(4):1516-20 | |
| Knauer R and Lehle L (1999) The oligosaccharyltransferase complex from Saccharomyces cerevisiae. Isolation of the OST6 gene, its synthetic interaction with OST3, and analysis of the native complex. J Biol Chem 274(24):17249-56 | |
| Karaoglu D, et al. (1997) The highly conserved Stt3 protein is a subunit of the yeast oligosaccharyltransferase and forms a subcomplex with Ost3p and Ost4p. J Biol Chem 272(51):32513-20 | |
| Reiss G, et al. (1997) A specific screen for oligosaccharyltransferase mutations identifies the 9 kDa OST5 protein required for optimal activity in vivo and in vitro. EMBO J 16(6):1164-72 | |
| Spirig U, et al. (1997) The STT3 protein is a component of the yeast oligosaccharyltransferase complex. Mol Gen Genet 256(6):628-37 | |
| Karaoglu D, et al. (1995) Functional characterization of Ost3p. Loss of the 34-kD subunit of the Saccharomyces cerevisiae oligosaccharyltransferase results in biased underglycosylation of acceptor substrates. J Cell Biol 130(3):567-77 | |
| Silberstein S, et al. (1995) The essential OST2 gene encodes the 16-kD subunit of the yeast oligosaccharyltransferase, a highly conserved protein expressed in diverse eukaryotic organisms. J Cell Biol 131(2):371-83 |





