PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15835887-1 2005 Oligosaccharyltransferase (OST) catalyzes the cotranslational transfer of high-mannose sugars to nascent polypeptides during N-linked glycosylation in the rough endoplasmic reticulum lumen. Nitrogen 125-126 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 0-25 18607003-4 2008 In the mammalian OST complex one such subunit, ribophorin I, is proposed to facilitate the N-glycosylation of certain precursors during their biogenesis at the endoplasmic reticulum. Nitrogen 91-92 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 17-20 17264154-1 2007 The mammalian oligosaccharyltransferase (OST) complex is composed of about eight subunits and mediates the N-glycosylation of nascent polypeptide chains entering the endoplasmic reticulum (ER). Nitrogen 107-108 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 14-39 17264154-1 2007 The mammalian oligosaccharyltransferase (OST) complex is composed of about eight subunits and mediates the N-glycosylation of nascent polypeptide chains entering the endoplasmic reticulum (ER). Nitrogen 107-108 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 41-44 17264154-6 2007 We propose a new model for OST function where ribophorin I acts as a chaperone or escort to promote the N-glycosylation of selected substrates by the catalytic STT3 subunits. Nitrogen 104-105 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 27-30 16126345-7 2005 Genetic and biochemical characterization of oligosaccharide transferase (OST) complex in yeast and mammalian cells have demonstrated the importance of specific OST subunits in protein N-glycosylation. Nitrogen 184-185 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 73-76 16126345-7 2005 Genetic and biochemical characterization of oligosaccharide transferase (OST) complex in yeast and mammalian cells have demonstrated the importance of specific OST subunits in protein N-glycosylation. Nitrogen 184-185 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 160-163 15835887-1 2005 Oligosaccharyltransferase (OST) catalyzes the cotranslational transfer of high-mannose sugars to nascent polypeptides during N-linked glycosylation in the rough endoplasmic reticulum lumen. Nitrogen 125-126 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 27-30 9144178-10 1997 The demonstration that DAD1 is a subunit of the OST suggests that induction of a cell death pathway upon loss of DAD1 in the tsBN7 cell line reflects the essential nature of N-linked glycosylation in eukaryotes. Nitrogen 128-129 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 48-51 11580295-1 2001 The oligosaccharyltransferase (OST) preferentially utilizes the fully assembled dolichol-linked oligosaccharide Glc(3)Man(9)GlcNAc(2)-PP-Dol as the donor for N-linked glycosylation of asparagine residues in N-X-T/S consensus sites in newly synthesized proteins. Nitrogen 127-128 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 4-29 11580295-1 2001 The oligosaccharyltransferase (OST) preferentially utilizes the fully assembled dolichol-linked oligosaccharide Glc(3)Man(9)GlcNAc(2)-PP-Dol as the donor for N-linked glycosylation of asparagine residues in N-X-T/S consensus sites in newly synthesized proteins. Nitrogen 127-128 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 31-34 12887896-1 2003 Oligosaccharyltransferase (OST) is an integral membrane protein that catalyzes N-linked glycosylation of nascent proteins in the lumen of the endoplasmic reticulum. Nitrogen 79-80 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 0-25 12887896-1 2003 Oligosaccharyltransferase (OST) is an integral membrane protein that catalyzes N-linked glycosylation of nascent proteins in the lumen of the endoplasmic reticulum. Nitrogen 79-80 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 27-30 10826490-4 2000 The mammalian oligosaccharyltransferase (OST) is a protein complex that effects the cotranslational N-glycosylation of newly synthesized polypeptides, and is composed of at least four rough ER-specific membrane proteins: ribophorins I and II (RI and RII), OST48, and Dadl. Nitrogen 100-101 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 14-39 10826490-4 2000 The mammalian oligosaccharyltransferase (OST) is a protein complex that effects the cotranslational N-glycosylation of newly synthesized polypeptides, and is composed of at least four rough ER-specific membrane proteins: ribophorins I and II (RI and RII), OST48, and Dadl. Nitrogen 100-101 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 41-44 34778038-1 2021 Ribophorin 1 (RPN1) is a major part of Oligosaccharyltransferase (OST) complex, which is vital for the N-linked glycosylation. Nitrogen 103-104 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 39-64 34778038-1 2021 Ribophorin 1 (RPN1) is a major part of Oligosaccharyltransferase (OST) complex, which is vital for the N-linked glycosylation. Nitrogen 103-104 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 66-69 34354228-0 2021 The structure of an archaeal oligosaccharyltransferase provides insight into the strict exclusion of proline from the N-glycosylation sequon. Nitrogen 118-119 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 29-54 34354228-1 2021 Oligosaccharyltransferase (OST) catalyzes oligosaccharide transfer to the Asn residue in the N-glycosylation sequon, Asn-X-Ser/Thr, where Pro is strictly excluded at position X. Nitrogen 93-94 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 0-25 34354228-1 2021 Oligosaccharyltransferase (OST) catalyzes oligosaccharide transfer to the Asn residue in the N-glycosylation sequon, Asn-X-Ser/Thr, where Pro is strictly excluded at position X. Nitrogen 93-94 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 27-30 31511384-14 2019 The two specific thioredoxin subunits of STT3B-OST MAGT1 and TUSC3 were found to be essential for the N-glycosylation of viral GP. Nitrogen 102-103 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 47-50 32316603-4 2020 N-linked glycosylation occurs in the endoplasmic reticulum (ER) lumen by a membrane associated enzyme complex called the oligosaccharyltransferase (OST). Nitrogen 0-1 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 148-151 32316603-9 2020 This review explains the most recent high-resolution structures of OST determined thus far and the mechanistic implication of N-linked glycosylation throughout all domains of life. Nitrogen 126-127 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 67-70 32316603-12 2020 Both human OST complexes, OST-A (with STT3A) and OST-B (containing STT3B), are involved in the N-linked glycosylation of proteins in the ER. Nitrogen 95-96 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 11-14 32316603-15 2020 However, we still lack an understanding of the independent role of each eukaryotic OST subunit in N-linked glycosylation or in the stabilization of the enzyme complex. Nitrogen 98-99 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 83-86 30811219-3 2019 NGI-1 is a small-molecule inhibitor of oligosaccharyltransferase (OST) complexes STT3A-OST and STT3B-OST, which catalyze cotranslational and post-translational N-glycosylation, respectively. Nitrogen 0-1 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 66-69 30811219-3 2019 NGI-1 is a small-molecule inhibitor of oligosaccharyltransferase (OST) complexes STT3A-OST and STT3B-OST, which catalyze cotranslational and post-translational N-glycosylation, respectively. Nitrogen 0-1 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 87-90 30811219-3 2019 NGI-1 is a small-molecule inhibitor of oligosaccharyltransferase (OST) complexes STT3A-OST and STT3B-OST, which catalyze cotranslational and post-translational N-glycosylation, respectively. Nitrogen 0-1 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 87-90 30811219-6 2019 N-glycosylation of 2 representative envelope proteins (gC and gD) was primarily dependent upon STT3A-OST, but to a large extent replaceable by STT3B-OST. Nitrogen 0-1 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 101-104 30811219-6 2019 N-glycosylation of 2 representative envelope proteins (gC and gD) was primarily dependent upon STT3A-OST, but to a large extent replaceable by STT3B-OST. Nitrogen 0-1 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 149-152 30811219-8 2019 However, with cells lacking STT3B-OST activity (missing the catalytic subunit STT3B or the oxidoreductase subunits magnesium transporter 1/tumor suppressor candidate 3) and thus solely dependent upon STT3A-OST for N-glycosylation, NGI-1 treatment resulted in HSV-1 having cell type-dependent dysfunction (affecting infectivity with Vero cells much more than with the 293 lines). Nitrogen 214-215 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 206-209 30026325-3 2018 Here, we perform sensitivity screening of 94 lung cancer cell lines using NGI-1, a small-molecule inhibitor of the oligosaccharyltransferase (OST) that partially disrupts N-linked glycosylation, and demonstrate a selective loss of tumor cell viability. Nitrogen 74-75 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 115-140 30078634-1 2018 The oligosaccharyltransferase (OST) is a multisubunit enzyme complex that N-glycosylates proteins in the secretory pathway and is considered to be constitutive and unregulated. Nitrogen 74-75 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 4-29 30078634-1 2018 The oligosaccharyltransferase (OST) is a multisubunit enzyme complex that N-glycosylates proteins in the secretory pathway and is considered to be constitutive and unregulated. Nitrogen 74-75 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 31-34 30078634-2 2018 However, small-molecule OST inhibitors such as NGI-1 provide a pharmacological approach for regulating N-linked glycosylation. Nitrogen 47-48 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 24-27 30026325-3 2018 Here, we perform sensitivity screening of 94 lung cancer cell lines using NGI-1, a small-molecule inhibitor of the oligosaccharyltransferase (OST) that partially disrupts N-linked glycosylation, and demonstrate a selective loss of tumor cell viability. Nitrogen 74-75 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 142-145 30026325-7 2018 OST inhibition invariably disrupted EGFR N-linked glycosylation and reduced activation of receptors either with or without the T790M TKI resistance mutation. Nitrogen 41-42 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 0-3 29519914-1 2018 Protein synthesis, transport, and N-glycosylation are coupled at the mammalian endoplasmic reticulum by complex formation of a ribosome, the Sec61 protein-conducting channel, and oligosaccharyltransferase (OST). Nitrogen 34-35 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 179-204 29519914-1 2018 Protein synthesis, transport, and N-glycosylation are coupled at the mammalian endoplasmic reticulum by complex formation of a ribosome, the Sec61 protein-conducting channel, and oligosaccharyltransferase (OST). Nitrogen 34-35 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 206-209 28935112-2 2017 The central enzyme in N-linked glycosylation is the oligosaccharyltransferase (OST), which catalyzes the covalent attachment of preassembled glycans to specific asparagine residues in target proteins. Nitrogen 22-23 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 52-77 29156678-4 2017 TUSC3 is a subunit of the oligosaccharyltransferase (OST) complex at the endoplasmic reticulum (ER) which catalyzes bulk N-glycosylation of membrane and secretory proteins. Nitrogen 121-122 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 26-51 29156678-4 2017 TUSC3 is a subunit of the oligosaccharyltransferase (OST) complex at the endoplasmic reticulum (ER) which catalyzes bulk N-glycosylation of membrane and secretory proteins. Nitrogen 121-122 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 53-56 29301962-0 2018 Structure of the yeast oligosaccharyltransferase complex gives insight into eukaryotic N-glycosylation. Nitrogen 87-88 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 23-48 27997792-0 2017 Tethering an N-Glycosylation Sequon-Containing Peptide Creates a Catalytically Competent Oligosaccharyltransferase Complex. Nitrogen 13-14 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 89-114 28935112-2 2017 The central enzyme in N-linked glycosylation is the oligosaccharyltransferase (OST), which catalyzes the covalent attachment of preassembled glycans to specific asparagine residues in target proteins. Nitrogen 22-23 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 79-82 26206502-6 2015 Because the degradation of Glc3Man9GlcNAc2-PP-Dol is greatly inhibited in the presence of an N-glycosylation acceptor peptide that is recognized by the oligosaccharyltransferase (OST), the OST-mediated hydrolysis of DLO is the most likely mechanism responsible for the production of a large fraction of the cytosolic fOSs. Nitrogen 38-39 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 152-177 27694802-6 2016 These results identify OST inhibition as a potential therapeutic approach for treating receptor-tyrosine-kinase-dependent tumors and provides a chemical probe for reversibly regulating N-linked glycosylation in mammalian cells. Nitrogen 185-186 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 23-26 26206502-6 2015 Because the degradation of Glc3Man9GlcNAc2-PP-Dol is greatly inhibited in the presence of an N-glycosylation acceptor peptide that is recognized by the oligosaccharyltransferase (OST), the OST-mediated hydrolysis of DLO is the most likely mechanism responsible for the production of a large fraction of the cytosolic fOSs. Nitrogen 38-39 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 179-182 26206502-6 2015 Because the degradation of Glc3Man9GlcNAc2-PP-Dol is greatly inhibited in the presence of an N-glycosylation acceptor peptide that is recognized by the oligosaccharyltransferase (OST), the OST-mediated hydrolysis of DLO is the most likely mechanism responsible for the production of a large fraction of the cytosolic fOSs. Nitrogen 38-39 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 189-192 24720891-0 2014 RCAN1 increases Abeta generation by promoting N-glycosylation via oligosaccharyltransferase. Nitrogen 3-4 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 66-91 25135935-6 2014 Cotranslational N-glycosylation by the STT3A isoform of the OST, which lacks MagT1, allows efficient modification of acceptor sites in cysteine-rich protein domains before disulfide bond formation. Nitrogen 16-17 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 60-63 25029371-7 2014 A strong correlation between cotranslational N-glycosylation efficiency and the rate of post-translational N-glycosylation was determined, showing that the OST STT3A and STT3B isoforms are similarly influenced by the hydroxyl and middle X consensus site residues. Nitrogen 45-46 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 156-159 24720891-2 2014 N-glycosylation in ER is mediated by oligosaccharyltransferase (OST), an enzyme complex transferring preassembled oligosaccharide to asparagine residues of nascent polypeptide chain. Nitrogen 0-1 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 37-62 24720891-2 2014 N-glycosylation in ER is mediated by oligosaccharyltransferase (OST), an enzyme complex transferring preassembled oligosaccharide to asparagine residues of nascent polypeptide chain. Nitrogen 0-1 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 64-67 24685145-1 2014 N-linked glycosylation of proteins in the endoplasmic reticulum (ER) is essential in eukaryotes and catalyzed by oligosaccharyl transferase (OST). Nitrogen 0-1 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 141-144 24435307-4 2014 We provide evidence that TUSC3 is part of the OST complex and affects N-linked glycosylation in mammalian cells. Nitrogen 70-71 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 46-49 24062310-6 2013 Biochemical and genetic analyses using mutant strains of Saccharomyces cerevisiae revealed that the generation of fOSs is tightly correlated with the N-glycosylation activity of OST. Nitrogen 150-151 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 178-181 24062310-7 2013 Furthermore, we present evidence that the purified OST complex can generate fOSs by hydrolyzing dolichol-linked oligosaccharide, the glycan donor substrate for N-glycosylation. Nitrogen 160-161 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 51-54 24062310-8 2013 The heterologous expression of a single subunit of OST from the protozoan Leishmania major in S. cerevisiae demonstrated that this enzyme functions both in N-glycosylation and generation of fOSs. Nitrogen 156-157 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 51-54 23606741-0 2013 OST4 is a subunit of the mammalian oligosaccharyltransferase required for efficient N-glycosylation. Nitrogen 84-85 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 35-60 23606741-1 2013 The eukaryotic oligosaccharyltransferase (OST) is a membrane-embedded protein complex that catalyses the N-glycosylation of nascent polypeptides in the lumen of the endoplasmic reticulum (ER), a highly conserved biosynthetic process that enriches protein structure and function. Nitrogen 105-106 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 15-40 23606741-1 2013 The eukaryotic oligosaccharyltransferase (OST) is a membrane-embedded protein complex that catalyses the N-glycosylation of nascent polypeptides in the lumen of the endoplasmic reticulum (ER), a highly conserved biosynthetic process that enriches protein structure and function. Nitrogen 105-106 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 42-45 23606741-11 2013 We conclude that OST4 most likely promotes co-translational N-glycosylation by stabilising STT3A-containing OST isoforms. Nitrogen 60-61 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 17-20 22467853-0 2012 The oligosaccharyltransferase subunits OST48, DAD1 and KCP2 function as ubiquitous and selective modulators of mammalian N-glycosylation. Nitrogen 121-122 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 4-29 22467853-0 2012 The oligosaccharyltransferase subunits OST48, DAD1 and KCP2 function as ubiquitous and selective modulators of mammalian N-glycosylation. Nitrogen 121-122 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 39-44 22467853-1 2012 Protein N-glycosylation is an essential modification that occurs in all eukaryotes and is catalysed by the oligosaccharyltransferase (OST) in the endoplasmic reticulum. Nitrogen 8-9 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 107-132 22467853-1 2012 Protein N-glycosylation is an essential modification that occurs in all eukaryotes and is catalysed by the oligosaccharyltransferase (OST) in the endoplasmic reticulum. Nitrogen 8-9 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 134-137 22467853-7 2012 Thus, OST48 and DAD1 are global modulators of OST stability and hence N-glycosylation. Nitrogen 70-71 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 6-11 22467853-7 2012 Thus, OST48 and DAD1 are global modulators of OST stability and hence N-glycosylation. Nitrogen 70-71 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 6-9 22266900-1 2012 The oligosaccharyltransferase (OST) complex catalyses the N-glycosylation of polypeptides entering the endoplasmic reticulum, a process essential for the productive folding and trafficking of many secretory and membrane proteins. Nitrogen 58-59 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 4-29 22266900-1 2012 The oligosaccharyltransferase (OST) complex catalyses the N-glycosylation of polypeptides entering the endoplasmic reticulum, a process essential for the productive folding and trafficking of many secretory and membrane proteins. Nitrogen 58-59 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 31-34 20419423-5 2010 We use a combination of siRNA-mediated knockdown of individual proteins combined with a semi-permeabilized mammalian cell system to provide a robust read out for OST subunit function during N-glycosylation of model substrates in vitro. Nitrogen 27-28 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 162-165 19167329-0 2009 Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms. Nitrogen 38-39 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 92-95 19167329-3 2009 Using siRNA to achieve isoform-specific knockdowns, we show that the OST isoforms cooperate and act sequentially to mediate protein N-glycosylation. Nitrogen 9-10 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 69-72 19167329-7 2009 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. Nitrogen 157-158 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 47-50 24519942-2 2014 Protein translocation across the ER membrane and N-glycosylation are highly coordinated processes that take place at the translocon-oligosaccharyltransferase (OST) complex. Nitrogen 49-50 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 121-157 24519942-2 2014 Protein translocation across the ER membrane and N-glycosylation are highly coordinated processes that take place at the translocon-oligosaccharyltransferase (OST) complex. Nitrogen 49-50 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 159-162 24519942-6 2014 The coordinated interplay between PMTs and OST in vivo is further shown by a comprehensive mass spectrometry-based analysis of N-glycosylation site occupancy in pmtDelta mutants. Nitrogen 127-128 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 43-46 21852240-6 2011 The identification of an enzyme that integrates some of the features of OST in a cytoplasmic pathway defines a novel class of N-linked protein glycosylation found in pathogenic bacteria. Nitrogen 126-127 dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit Homo sapiens 72-75