PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
32316603-14	2020	An acceptor peptide and a donor substrate (dolichylphosphate) were observed to be bound to the OST-B complex whereas only dolichylphosphate was bound to the OST-A complex suggesting disparate affinities of two OST complexes for the acceptor substrates.	dolichol monophosphate	43-60	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	95-98
5840949-0	1965	[Comparative action of different sugars on Ost"s copper-alkaline reagent].	Sugars	33-39	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	43-46
33010307-1	2020	Oligosaccharyltransferase (OST) is a membrane-bound enzyme that catalyzes the transfer of oligosaccharide chains from lipid-linked oligosaccharides (LLO) to asparagine residues in polypeptide chains.	Oligosaccharides	90-105	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
33010307-1	2020	Oligosaccharyltransferase (OST) is a membrane-bound enzyme that catalyzes the transfer of oligosaccharide chains from lipid-linked oligosaccharides (LLO) to asparagine residues in polypeptide chains.	Oligosaccharides	90-105	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
33010307-1	2020	Oligosaccharyltransferase (OST) is a membrane-bound enzyme that catalyzes the transfer of oligosaccharide chains from lipid-linked oligosaccharides (LLO) to asparagine residues in polypeptide chains.	lipid-linked oligosaccharides	118-147	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
33010307-1	2020	Oligosaccharyltransferase (OST) is a membrane-bound enzyme that catalyzes the transfer of oligosaccharide chains from lipid-linked oligosaccharides (LLO) to asparagine residues in polypeptide chains.	lipid-linked oligosaccharides	118-147	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
33010307-1	2020	Oligosaccharyltransferase (OST) is a membrane-bound enzyme that catalyzes the transfer of oligosaccharide chains from lipid-linked oligosaccharides (LLO) to asparagine residues in polypeptide chains.	lipid-linked oligosaccharides	149-152	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
33010307-1	2020	Oligosaccharyltransferase (OST) is a membrane-bound enzyme that catalyzes the transfer of oligosaccharide chains from lipid-linked oligosaccharides (LLO) to asparagine residues in polypeptide chains.	lipid-linked oligosaccharides	149-152	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
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
33010307-1	2020	Oligosaccharyltransferase (OST) is a membrane-bound enzyme that catalyzes the transfer of oligosaccharide chains from lipid-linked oligosaccharides (LLO) to asparagine residues in polypeptide chains.	Asparagine	157-167	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
33010307-1	2020	Oligosaccharyltransferase (OST) is a membrane-bound enzyme that catalyzes the transfer of oligosaccharide chains from lipid-linked oligosaccharides (LLO) to asparagine residues in polypeptide chains.	Asparagine	157-167	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
33010307-3	2020	An archaeal single-subunit OST protein was immobilized on a mica support via biotin-avidin interactions and reconstituted in a lipid bilayer.	mica	60-64	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
33010307-3	2020	An archaeal single-subunit OST protein was immobilized on a mica support via biotin-avidin interactions and reconstituted in a lipid bilayer.	Biotin	77-83	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
33010307-3	2020	An archaeal single-subunit OST protein was immobilized on a mica support via biotin-avidin interactions and reconstituted in a lipid bilayer.	Lipid Bilayers	127-140	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
32328881-11	2020	Indeed, mutation of valine23 to an aspartate impairs OST function in vivo resulting in a lethal phenotype in yeast.	valine23	20-28	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	53-56
32328881-11	2020	Indeed, mutation of valine23 to an aspartate impairs OST function in vivo resulting in a lethal phenotype in yeast.	Aspartic Acid	35-44	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	53-56
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
30439421-2	2019	In the present work, we fabricated a new antibacterial complex of l-phenylalanine-oxidized starch-coordinated zinc (II) (l-Phe-OSt Zn (II)) by successive reactions of oxidization, Maillard and coordination.	Phenylalanine	66-81	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	127-130
31511384-9	2019	NGI-1, a small-molecule OST inhibitor, can effectively reduce virus infectivity without affecting cell viability.	NGI-1	0-5	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	24-27
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
31511384-15	2019	NGI-1, a small-molecule inhibitor of OST, also showed a robust inhibitory effect on arenavirus.	NGI-1	0-5	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	37-40
31831667-1	2019	Oligosaccharyltransferase (OST) catalyzes the transfer of a high-mannose glycan onto secretory proteins in the endoplasmic reticulum.	Mannose	65-72	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
31831667-1	2019	Oligosaccharyltransferase (OST) catalyzes the transfer of a high-mannose glycan onto secretory proteins in the endoplasmic reticulum.	Mannose	65-72	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
31831667-6	2019	We observed an acceptor peptide and dolichylphosphate bound to STT3B, but only dolichylphosphate in STT3A, suggesting distinct affinities of the two OST complexes for protein substrates.	dolichylphosphate	36-53	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	149-152
31831667-6	2019	We observed an acceptor peptide and dolichylphosphate bound to STT3B, but only dolichylphosphate in STT3A, suggesting distinct affinities of the two OST complexes for protein substrates.	dolichylphosphate	79-96	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	149-152
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
33654988-2	2019	A membrane-bound enzyme, oligosaccharyltransferase, catalyzes the transfer of an oligosaccharide chain from a sugar donor (lipid-linked oligosaccharide, LLO) to an asparagine residue in the consensus sequence, Asn-X-Ser/Thr (X   Pro), in proteins.	Oligosaccharides	81-96	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	25-50
33654988-2	2019	A membrane-bound enzyme, oligosaccharyltransferase, catalyzes the transfer of an oligosaccharide chain from a sugar donor (lipid-linked oligosaccharide, LLO) to an asparagine residue in the consensus sequence, Asn-X-Ser/Thr (X   Pro), in proteins.	Sugars	110-115	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	25-50
33654988-2	2019	A membrane-bound enzyme, oligosaccharyltransferase, catalyzes the transfer of an oligosaccharide chain from a sugar donor (lipid-linked oligosaccharide, LLO) to an asparagine residue in the consensus sequence, Asn-X-Ser/Thr (X   Pro), in proteins.	lipid-linked oligosaccharides	123-151	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	25-50
33654988-2	2019	A membrane-bound enzyme, oligosaccharyltransferase, catalyzes the transfer of an oligosaccharide chain from a sugar donor (lipid-linked oligosaccharide, LLO) to an asparagine residue in the consensus sequence, Asn-X-Ser/Thr (X   Pro), in proteins.	Asparagine	164-174	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	25-50
33654988-2	2019	A membrane-bound enzyme, oligosaccharyltransferase, catalyzes the transfer of an oligosaccharide chain from a sugar donor (lipid-linked oligosaccharide, LLO) to an asparagine residue in the consensus sequence, Asn-X-Ser/Thr (X   Pro), in proteins.	asn-x-ser	210-219	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	25-50
33654988-2	2019	A membrane-bound enzyme, oligosaccharyltransferase, catalyzes the transfer of an oligosaccharide chain from a sugar donor (lipid-linked oligosaccharide, LLO) to an asparagine residue in the consensus sequence, Asn-X-Ser/Thr (X   Pro), in proteins.	Threonine	220-223	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	25-50
33654988-2	2019	A membrane-bound enzyme, oligosaccharyltransferase, catalyzes the transfer of an oligosaccharide chain from a sugar donor (lipid-linked oligosaccharide, LLO) to an asparagine residue in the consensus sequence, Asn-X-Ser/Thr (X   Pro), in proteins.	Proline	229-232	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	25-50
30439421-2	2019	In the present work, we fabricated a new antibacterial complex of l-phenylalanine-oxidized starch-coordinated zinc (II) (l-Phe-OSt Zn (II)) by successive reactions of oxidization, Maillard and coordination.	Starch	91-97	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	127-130
30439421-3	2019	Maillard reaction occurred between l-Phe and OSt to form l-Phe-OSt, which was then coordinated with Zn (II) by carboxyl groups for l-Phe-OSt Zn (II).	Phenylalanine	35-40	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	63-66
30439421-3	2019	Maillard reaction occurred between l-Phe and OSt to form l-Phe-OSt, which was then coordinated with Zn (II) by carboxyl groups for l-Phe-OSt Zn (II).	Phenylalanine	35-40	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	63-66
30439421-3	2019	Maillard reaction occurred between l-Phe and OSt to form l-Phe-OSt, which was then coordinated with Zn (II) by carboxyl groups for l-Phe-OSt Zn (II).	Zinc	100-102	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	45-48
30439421-3	2019	Maillard reaction occurred between l-Phe and OSt to form l-Phe-OSt, which was then coordinated with Zn (II) by carboxyl groups for l-Phe-OSt Zn (II).	Zinc	100-102	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	63-66
30439421-3	2019	Maillard reaction occurred between l-Phe and OSt to form l-Phe-OSt, which was then coordinated with Zn (II) by carboxyl groups for l-Phe-OSt Zn (II).	Zinc	100-102	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	63-66
30439421-3	2019	Maillard reaction occurred between l-Phe and OSt to form l-Phe-OSt, which was then coordinated with Zn (II) by carboxyl groups for l-Phe-OSt Zn (II).	Zinc	141-143	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	45-48
30439421-3	2019	Maillard reaction occurred between l-Phe and OSt to form l-Phe-OSt, which was then coordinated with Zn (II) by carboxyl groups for l-Phe-OSt Zn (II).	Zinc	141-143	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	63-66
30439421-3	2019	Maillard reaction occurred between l-Phe and OSt to form l-Phe-OSt, which was then coordinated with Zn (II) by carboxyl groups for l-Phe-OSt Zn (II).	Zinc	141-143	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	63-66
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
30513249-4	2019	OBJECTIVES: The current study is aimed at evaluation of the impact of change in buprenorphine-naloxone formulation on prescription pattern, treatment adherence, and patient satisfaction with OST.	Buprenorphine	80-93	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	191-194
30513249-4	2019	OBJECTIVES: The current study is aimed at evaluation of the impact of change in buprenorphine-naloxone formulation on prescription pattern, treatment adherence, and patient satisfaction with OST.	Naloxone	94-102	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	191-194
30384028-16	2018	CONCLUSION: Paritaprevir/ritonavir, ombitasvir, and dasabuvir with or without ribavirin for 12 weeks is effective among people with HCV genotype 1 with recent injecting drug use and/or receiving OST.	paritaprevir/ritonavir	12-34	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	195-198
30384028-16	2018	CONCLUSION: Paritaprevir/ritonavir, ombitasvir, and dasabuvir with or without ribavirin for 12 weeks is effective among people with HCV genotype 1 with recent injecting drug use and/or receiving OST.	ombitasvir	36-46	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	195-198
30384028-16	2018	CONCLUSION: Paritaprevir/ritonavir, ombitasvir, and dasabuvir with or without ribavirin for 12 weeks is effective among people with HCV genotype 1 with recent injecting drug use and/or receiving OST.	dasabuvir	52-61	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	195-198
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.	NGI-1	47-52	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	24-27
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
29252906-7	2018	As time proceeds, TBAs increase in number and size, thereby increasing the cornea area-averaged TER and decreasing OST.	tbas	18-22	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	115-118
29338205-2	2018	Coupling of a peptide chelator, hexahistidine, with hydrophobic oligostyrene allows a modular strategy to be established for the efficient synthesis and purification of these tunable amphiphiles (oSt(His)6).	His-His-His-His-His-His	32-45	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	196-199
29338205-2	2018	Coupling of a peptide chelator, hexahistidine, with hydrophobic oligostyrene allows a modular strategy to be established for the efficient synthesis and purification of these tunable amphiphiles (oSt(His)6).	oligostyrene	64-76	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	196-199
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
29519914-3	2018	A molecular model for the catalytic OST subunit STT3A (staurosporine and temperature sensitive 3A) revealed how it is integrated into the OST and how STT3-paralog specificity for translocon-associated OST is achieved.	Staurosporine	55-68	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	36-39
29519914-3	2018	A molecular model for the catalytic OST subunit STT3A (staurosporine and temperature sensitive 3A) revealed how it is integrated into the OST and how STT3-paralog specificity for translocon-associated OST is achieved.	Staurosporine	55-68	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	138-141
29519914-3	2018	A molecular model for the catalytic OST subunit STT3A (staurosporine and temperature sensitive 3A) revealed how it is integrated into the OST and how STT3-paralog specificity for translocon-associated OST is achieved.	Staurosporine	55-68	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	138-141
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
29301962-1	2018	Oligosaccharyltransferase (OST) is an essential membrane protein complex in the endoplasmic reticulum, where it transfers an oligosaccharide from a dolichol-pyrophosphate-activated donor to glycosylation sites of secretory proteins.	Oligosaccharides	125-140	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
29301962-1	2018	Oligosaccharyltransferase (OST) is an essential membrane protein complex in the endoplasmic reticulum, where it transfers an oligosaccharide from a dolichol-pyrophosphate-activated donor to glycosylation sites of secretory proteins.	Oligosaccharides	125-140	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
29301962-1	2018	Oligosaccharyltransferase (OST) is an essential membrane protein complex in the endoplasmic reticulum, where it transfers an oligosaccharide from a dolichol-pyrophosphate-activated donor to glycosylation sites of secretory proteins.	dolichol pyrophosphate	148-170	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
29301962-1	2018	Oligosaccharyltransferase (OST) is an essential membrane protein complex in the endoplasmic reticulum, where it transfers an oligosaccharide from a dolichol-pyrophosphate-activated donor to glycosylation sites of secretory proteins.	dolichol pyrophosphate	148-170	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
29042445-2	2017	The transfer of a glycan from a lipid-linked oligosaccharide (LLO) donor to the asparagine residue of a nascent polypeptide chain is catalyzed by an oligosaccharyltransferase (OST) in the lumen of the endoplasmic reticulum (ER).	Polysaccharides	18-24	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	149-174
29241533-5	2017	Viral mutants adapted to replicate in cells deficient of the OST complex showed resistance to NGI-1 treatment, reinforcing the on-target activity of NGI-1.	NGI-1	94-99	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	61-64
29241533-5	2017	Viral mutants adapted to replicate in cells deficient of the OST complex showed resistance to NGI-1 treatment, reinforcing the on-target activity of NGI-1.	2-(4-(2-carboxyethyl)phenethylamino)-5'-N-ethylcarboxamidoadenosine	94-97	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	61-64
29042445-2	2017	The transfer of a glycan from a lipid-linked oligosaccharide (LLO) donor to the asparagine residue of a nascent polypeptide chain is catalyzed by an oligosaccharyltransferase (OST) in the lumen of the endoplasmic reticulum (ER).	Polysaccharides	18-24	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	176-179
29042445-2	2017	The transfer of a glycan from a lipid-linked oligosaccharide (LLO) donor to the asparagine residue of a nascent polypeptide chain is catalyzed by an oligosaccharyltransferase (OST) in the lumen of the endoplasmic reticulum (ER).	lipid-linked oligosaccharides	32-60	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	149-174
29042445-2	2017	The transfer of a glycan from a lipid-linked oligosaccharide (LLO) donor to the asparagine residue of a nascent polypeptide chain is catalyzed by an oligosaccharyltransferase (OST) in the lumen of the endoplasmic reticulum (ER).	lipid-linked oligosaccharides	32-60	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	176-179
29042445-2	2017	The transfer of a glycan from a lipid-linked oligosaccharide (LLO) donor to the asparagine residue of a nascent polypeptide chain is catalyzed by an oligosaccharyltransferase (OST) in the lumen of the endoplasmic reticulum (ER).	lipid-linked oligosaccharides	62-65	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	149-174
29042445-2	2017	The transfer of a glycan from a lipid-linked oligosaccharide (LLO) donor to the asparagine residue of a nascent polypeptide chain is catalyzed by an oligosaccharyltransferase (OST) in the lumen of the endoplasmic reticulum (ER).	lipid-linked oligosaccharides	62-65	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	176-179
29042445-2	2017	The transfer of a glycan from a lipid-linked oligosaccharide (LLO) donor to the asparagine residue of a nascent polypeptide chain is catalyzed by an oligosaccharyltransferase (OST) in the lumen of the endoplasmic reticulum (ER).	Asparagine	80-90	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	149-174
29042445-2	2017	The transfer of a glycan from a lipid-linked oligosaccharide (LLO) donor to the asparagine residue of a nascent polypeptide chain is catalyzed by an oligosaccharyltransferase (OST) in the lumen of the endoplasmic reticulum (ER).	Asparagine	80-90	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	176-179
27997792-1	2017	Oligosaccharyltransferase (OST) transfers an oligosaccharide chain to the Asn residue in the Asn-X-Ser/Thr sequon in proteins, where X is not proline.	Proline	142-149	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
28820257-8	2017	We then introduced the optimized-enhanced aromatic sequons into other glycoproteins and observed an enhancement in N-glycan occupancy that was further supported by modeling the high-affinity interaction between the optimized sequence on hCD2ad and a human oligosaccharyltransferase (OST) subunit.	n-glycan	115-123	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	256-281
28820257-8	2017	We then introduced the optimized-enhanced aromatic sequons into other glycoproteins and observed an enhancement in N-glycan occupancy that was further supported by modeling the high-affinity interaction between the optimized sequence on hCD2ad and a human oligosaccharyltransferase (OST) subunit.	n-glycan	115-123	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	283-286
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
27997792-1	2017	Oligosaccharyltransferase (OST) transfers an oligosaccharide chain to the Asn residue in the Asn-X-Ser/Thr sequon in proteins, where X is not proline.	Oligosaccharides	45-60	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
27997792-1	2017	Oligosaccharyltransferase (OST) transfers an oligosaccharide chain to the Asn residue in the Asn-X-Ser/Thr sequon in proteins, where X is not proline.	Oligosaccharides	45-60	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
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
27997792-1	2017	Oligosaccharyltransferase (OST) transfers an oligosaccharide chain to the Asn residue in the Asn-X-Ser/Thr sequon in proteins, where X is not proline.	Threonine	103-106	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
27997792-1	2017	Oligosaccharyltransferase (OST) transfers an oligosaccharide chain to the Asn residue in the Asn-X-Ser/Thr sequon in proteins, where X is not proline.	Asparagine	74-77	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
27997792-1	2017	Oligosaccharyltransferase (OST) transfers an oligosaccharide chain to the Asn residue in the Asn-X-Ser/Thr sequon in proteins, where X is not proline.	Proline	142-149	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
27997792-1	2017	Oligosaccharyltransferase (OST) transfers an oligosaccharide chain to the Asn residue in the Asn-X-Ser/Thr sequon in proteins, where X is not proline.	Asparagine	74-77	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
27997792-1	2017	Oligosaccharyltransferase (OST) transfers an oligosaccharide chain to the Asn residue in the Asn-X-Ser/Thr sequon in proteins, where X is not proline.	asn-x-ser	93-102	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
27997792-1	2017	Oligosaccharyltransferase (OST) transfers an oligosaccharide chain to the Asn residue in the Asn-X-Ser/Thr sequon in proteins, where X is not proline.	asn-x-ser	93-102	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
27997792-1	2017	Oligosaccharyltransferase (OST) transfers an oligosaccharide chain to the Asn residue in the Asn-X-Ser/Thr sequon in proteins, where X is not proline.	Threonine	103-106	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
27997792-2	2017	A sequon was tethered to an archaeal OST enzyme via a disulfide bond.	Disulfides	54-63	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	37-40
27997792-3	2017	The positions of the cysteine residues in the OST protein and the sequon-containing acceptor peptide were selected by reference to the eubacterial OST structure in a noncovalent complex with an acceptor peptide.	Cysteine	21-29	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	46-49
27997792-3	2017	The positions of the cysteine residues in the OST protein and the sequon-containing acceptor peptide were selected by reference to the eubacterial OST structure in a noncovalent complex with an acceptor peptide.	Cysteine	21-29	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	147-150
27694802-3	2016	NGI-1 targets oligosaccharyltransferase (OST), a hetero-oligomeric enzyme that exists in multiple isoforms and transfers oligosaccharides to recipient proteins.	Oligosaccharides	121-137	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	41-44
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
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
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.	Polysaccharides	141-148	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	52-77
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.	Polysaccharides	141-148	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	79-82
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.	Asparagine	161-171	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	52-77
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.	Asparagine	161-171	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	79-82
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
25889208-9	2015	CONCLUSION: Illicit use of methadone and buprenorphine involve risks but may also have important roles to play for users who are unwilling or not given the opportunity to enter OST.	Methadone	27-36	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	177-180
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.	glc3man9glcnac2-pp-dol	27-49	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	152-177
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.	glc3man9glcnac2-pp-dol	27-49	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.	glc3man9glcnac2-pp-dol	27-49	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	189-192
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
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
26452342-5	2015	The major objective for the SABATO trial is to demonstrate that in patients with low-risk SAB a switch from intravenous to oral antimicrobial therapy (oral switch therapy, OST) is non-inferior to a conventional course of intravenous therapy (intravenous standard therapy, IST).	sabato	28-34	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	172-175
26452342-5	2015	The major objective for the SABATO trial is to demonstrate that in patients with low-risk SAB a switch from intravenous to oral antimicrobial therapy (oral switch therapy, OST) is non-inferior to a conventional course of intravenous therapy (intravenous standard therapy, IST).	sab	28-31	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	172-175
25792706-0	2015	Reduced expression of the oligosaccharyltransferase exacerbates protein hypoglycosylation in cells lacking the fully assembled oligosaccharide donor.	Oligosaccharides	127-142	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	26-51
25792706-1	2015	A defect in the assembly of the oligosaccharide donor (Dol-PP-GlcNAc(2)Man(9)Glc(3)) for N-linked glycosylation causes hypoglycosylation of proteins by the oligosaccharyltransferase (OST).	Oligosaccharides	32-47	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	156-181
25792706-1	2015	A defect in the assembly of the oligosaccharide donor (Dol-PP-GlcNAc(2)Man(9)Glc(3)) for N-linked glycosylation causes hypoglycosylation of proteins by the oligosaccharyltransferase (OST).	Oligosaccharides	32-47	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	183-186
25792706-1	2015	A defect in the assembly of the oligosaccharide donor (Dol-PP-GlcNAc(2)Man(9)Glc(3)) for N-linked glycosylation causes hypoglycosylation of proteins by the oligosaccharyltransferase (OST).	dol-pp-glcnac	55-68	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	156-181
25792706-1	2015	A defect in the assembly of the oligosaccharide donor (Dol-PP-GlcNAc(2)Man(9)Glc(3)) for N-linked glycosylation causes hypoglycosylation of proteins by the oligosaccharyltransferase (OST).	dol-pp-glcnac	55-68	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	183-186
25792706-8	2015	Thus, differences in OST subunit expression can modify the severity of hypoglycosylation displayed by cells with a primary defect in the dolichol oligosaccharide assembly pathway.	dolichol oligosaccharide	137-161	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	21-24
25889208-9	2015	CONCLUSION: Illicit use of methadone and buprenorphine involve risks but may also have important roles to play for users who are unwilling or not given the opportunity to enter OST.	Buprenorphine	41-54	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	177-180
25418169-0	2014	Lipid-linked oligosaccharides in membranes sample conformations that facilitate binding to oligosaccharyltransferase.	lipid-linked oligosaccharides	0-29	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	91-116
25418169-1	2014	Lipid-linked oligosaccharides (LLOs) are the substrates of oligosaccharyltransferase (OST), the enzyme that catalyzes the en bloc transfer of the oligosaccharide onto the acceptor asparagine of nascent proteins during the process of N-glycosylation.	lipid-linked oligosaccharides	0-29	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	59-84
25418169-1	2014	Lipid-linked oligosaccharides (LLOs) are the substrates of oligosaccharyltransferase (OST), the enzyme that catalyzes the en bloc transfer of the oligosaccharide onto the acceptor asparagine of nascent proteins during the process of N-glycosylation.	lipid-linked oligosaccharides	0-29	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	86-89
25418169-1	2014	Lipid-linked oligosaccharides (LLOs) are the substrates of oligosaccharyltransferase (OST), the enzyme that catalyzes the en bloc transfer of the oligosaccharide onto the acceptor asparagine of nascent proteins during the process of N-glycosylation.	lipid-linked oligosaccharides	31-35	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	59-84
25418169-1	2014	Lipid-linked oligosaccharides (LLOs) are the substrates of oligosaccharyltransferase (OST), the enzyme that catalyzes the en bloc transfer of the oligosaccharide onto the acceptor asparagine of nascent proteins during the process of N-glycosylation.	lipid-linked oligosaccharides	31-35	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	86-89
25418169-1	2014	Lipid-linked oligosaccharides (LLOs) are the substrates of oligosaccharyltransferase (OST), the enzyme that catalyzes the en bloc transfer of the oligosaccharide onto the acceptor asparagine of nascent proteins during the process of N-glycosylation.	Oligosaccharides	13-28	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	59-84
25418169-1	2014	Lipid-linked oligosaccharides (LLOs) are the substrates of oligosaccharyltransferase (OST), the enzyme that catalyzes the en bloc transfer of the oligosaccharide onto the acceptor asparagine of nascent proteins during the process of N-glycosylation.	Oligosaccharides	13-28	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	86-89
25418169-1	2014	Lipid-linked oligosaccharides (LLOs) are the substrates of oligosaccharyltransferase (OST), the enzyme that catalyzes the en bloc transfer of the oligosaccharide onto the acceptor asparagine of nascent proteins during the process of N-glycosylation.	Asparagine	180-190	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	59-84
25418169-1	2014	Lipid-linked oligosaccharides (LLOs) are the substrates of oligosaccharyltransferase (OST), the enzyme that catalyzes the en bloc transfer of the oligosaccharide onto the acceptor asparagine of nascent proteins during the process of N-glycosylation.	Asparagine	180-190	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	86-89
25418169-5	2014	The isoprenoid moiety shows high flexibility inside the bilayer hydrophobic core, suggesting its potential role as a tentacle to search for OST.	Terpenes	4-14	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	140-143
24614199-7	2014	We recently reported that AGEs stimulated HSC activation likely by inhibiting gene expression of AGE-R1 and inducing gene expression of RAGE in HSC, which were eliminated by the antioxidant curcumin.	Curcumin	190-198	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	97-103
25029371-2	2014	N-Glycans are attached to nascent polypeptides at consensus sites, N-X-T/S (X   P), by one of two enzymatic isoforms of the oligosaccharyltransferase (OST), STT3A or STT3B.	n-glycans	0-9	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	124-149
25029371-2	2014	N-Glycans are attached to nascent polypeptides at consensus sites, N-X-T/S (X   P), by one of two enzymatic isoforms of the oligosaccharyltransferase (OST), STT3A or STT3B.	n-glycans	0-9	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	151-154
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
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
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.	Disulfides	172-181	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	60-63
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
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
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.	Oligosaccharides	114-129	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.	Oligosaccharides	114-129	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	64-67
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.	Asparagine	133-143	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.	Asparagine	133-143	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	64-67
24614199-12	2014	In conclusions, curcumin eliminated the effects of AGEs on the divergent regulation of gene expression of RAGE and AGE-R1 in HSC by interrupting the AGE-caused activation of leptin signaling, leading to the inhibition of HSC activation.	Curcumin	16-24	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	115-121
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
24685145-4	2014	Here, we show that N33/Tusc3 possesses a membrane-anchored N-terminal thioredoxin domain located in the ER lumen that may form transient mixed disulfide complexes with OST substrates.	Disulfides	143-152	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	168-171
24271188-3	2014	OST activity assays have largely relied on the use of radioisotopic methods using [(35)S] 3"-phosphoadenosine-5"-phosphosulfate and scintillation counting.	[(35)s] 3"-phosphoadenosine-5"-phosphosulfate	82-127	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-3
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
24850608-1	2014	AIMS: Evaluation of State Opioid Substitution Treatment OST (methadone and buprenorphine/naloxone- Addnok-N) program in Georgia and optimization of the routine measurement instrument.	Methadone	61-70	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	56-59
24850608-1	2014	AIMS: Evaluation of State Opioid Substitution Treatment OST (methadone and buprenorphine/naloxone- Addnok-N) program in Georgia and optimization of the routine measurement instrument.	Buprenorphine	75-88	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	56-59
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
24149797-1	2013	The initial glycan transfer in asparagine-linked protein glycosylation is catalysed by the integral membrane enzyme oligosaccharyltransferase (OST).	Polysaccharides	12-18	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	143-146
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.	dolichol-linked oligosaccharide	96-127	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	51-54
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.	Polysaccharides	133-139	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	51-54
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
23177926-1	2013	Oligosaccharyltransferase (OST) is a membrane-bound enzyme that catalyzes the transfer of an oligosaccharide to an asparagine residue in glycoproteins.	Oligosaccharides	93-108	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
23177926-1	2013	Oligosaccharyltransferase (OST) is a membrane-bound enzyme that catalyzes the transfer of an oligosaccharide to an asparagine residue in glycoproteins.	Oligosaccharides	93-108	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
23177926-1	2013	Oligosaccharyltransferase (OST) is a membrane-bound enzyme that catalyzes the transfer of an oligosaccharide to an asparagine residue in glycoproteins.	Asparagine	115-125	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
23177926-1	2013	Oligosaccharyltransferase (OST) is a membrane-bound enzyme that catalyzes the transfer of an oligosaccharide to an asparagine residue in glycoproteins.	Asparagine	115-125	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
24105266-1	2013	Asparagine-linked glycosylation of proteins by the oligosaccharyltransferase (OST) occurs when acceptor sites or sequons (N-x P-T/S) on nascent polypeptides enter the lumen of the rough endoplasmic reticulum.	Asparagine	0-10	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	51-76
24105266-1	2013	Asparagine-linked glycosylation of proteins by the oligosaccharyltransferase (OST) occurs when acceptor sites or sequons (N-x P-T/S) on nascent polypeptides enter the lumen of the rough endoplasmic reticulum.	Asparagine	0-10	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	78-81
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
23530066-1	2013	Metazoan organisms assemble two isoforms of the oligosaccharyltransferase (OST) that have different catalytic subunits (STT3A or STT3B) and partially nonoverlapping roles in asparagine-linked glycosylation.	Asparagine	174-184	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	48-73
23530066-1	2013	Metazoan organisms assemble two isoforms of the oligosaccharyltransferase (OST) that have different catalytic subunits (STT3A or STT3B) and partially nonoverlapping roles in asparagine-linked glycosylation.	Asparagine	174-184	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	75-78
24149797-1	2013	The initial glycan transfer in asparagine-linked protein glycosylation is catalysed by the integral membrane enzyme oligosaccharyltransferase (OST).	Asparagine	31-41	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	143-146
23231241-1	2012	Oxy-s-triazine (OST) is one of the important Hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) decomposition products, while it is yet not fully clear how it is formed up to now.	oxy-s-triazine	0-14	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	16-19
23231241-1	2012	Oxy-s-triazine (OST) is one of the important Hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) decomposition products, while it is yet not fully clear how it is formed up to now.	cyclonite	45-84	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	16-19
23231241-2	2012	The study systematically investigates the reaction of s-triazine (TAZ) with nitrate radical (NO(3)) using computational chemistry methods, for which three entrance channels are devised, resulting in the formation of four isomers of OST.	Triazines	54-64	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	232-235
23231241-2	2012	The study systematically investigates the reaction of s-triazine (TAZ) with nitrate radical (NO(3)) using computational chemistry methods, for which three entrance channels are devised, resulting in the formation of four isomers of OST.	Triazines	66-69	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	232-235
23231241-2	2012	The study systematically investigates the reaction of s-triazine (TAZ) with nitrate radical (NO(3)) using computational chemistry methods, for which three entrance channels are devised, resulting in the formation of four isomers of OST.	nitrate radical	76-91	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	232-235
23231241-2	2012	The study systematically investigates the reaction of s-triazine (TAZ) with nitrate radical (NO(3)) using computational chemistry methods, for which three entrance channels are devised, resulting in the formation of four isomers of OST.	punky blue	93-98	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	232-235
23185754-9	2012	Genes correlated to carbohydrate metabolism included AGL, B3GNT1, FUT9, ST8SIA4, SULT1A4, DDOST, and PIGL, mainly involved in glucogen degradation and glycoconjugate biosynthesis.	Carbohydrates	20-32	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	90-95
23185754-9	2012	Genes correlated to carbohydrate metabolism included AGL, B3GNT1, FUT9, ST8SIA4, SULT1A4, DDOST, and PIGL, mainly involved in glucogen degradation and glycoconjugate biosynthesis.	glucogen	126-134	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	90-95
22305527-4	2012	Here, we combined biochemical analysis with whole-exome sequencing (WES) to identify the genetic defect in an untyped CDG patient, and we found a 22 bp deletion and a missense mutation in DDOST, whose product is a component of the oligosaccharyltransferase complex that transfers the glycan chain from a lipid carrier to nascent proteins in the endoplasmic reticulum lumen.	Polysaccharides	284-290	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	188-193
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
21357684-0	2011	Selective control of oligosaccharide transfer efficiency for the N-glycosylation sequon by a point mutation in oligosaccharyltransferase.	Oligosaccharides	21-36	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	111-136
23097745-8	2012	These studies suggest that the membrane sorting process of hOST is mediated by a bafilomycin A1-sensitive vesicular pathway that is associated with the actin-cytoskeleton network.	bafilomycin	81-92	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	59-63
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
21852240-2	2011	This process involves the transfer of a preassembled oligosaccharide from a lipid donor to asparagine side chains of polypeptides and is catalyzed by the membrane-bound oligosaccharyltransferase (OST).	Oligosaccharides	53-68	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	196-199
21852240-2	2011	This process involves the transfer of a preassembled oligosaccharide from a lipid donor to asparagine side chains of polypeptides and is catalyzed by the membrane-bound oligosaccharyltransferase (OST).	Asparagine	91-101	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	196-199
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
21614585-2	2011	In the central reaction of the pathway, oligosaccharyltransferase (OST), a multimeric complex located at the membrane of the endoplasmic reticulum, transfers a preassembled oligosaccharide to selected asparagine residues within the consensus sequence asparagine-X-serine/threonine.	Oligosaccharides	173-188	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	40-65
21614585-2	2011	In the central reaction of the pathway, oligosaccharyltransferase (OST), a multimeric complex located at the membrane of the endoplasmic reticulum, transfers a preassembled oligosaccharide to selected asparagine residues within the consensus sequence asparagine-X-serine/threonine.	Oligosaccharides	173-188	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	67-70
21614585-2	2011	In the central reaction of the pathway, oligosaccharyltransferase (OST), a multimeric complex located at the membrane of the endoplasmic reticulum, transfers a preassembled oligosaccharide to selected asparagine residues within the consensus sequence asparagine-X-serine/threonine.	Asparagine	201-211	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	40-65
21614585-2	2011	In the central reaction of the pathway, oligosaccharyltransferase (OST), a multimeric complex located at the membrane of the endoplasmic reticulum, transfers a preassembled oligosaccharide to selected asparagine residues within the consensus sequence asparagine-X-serine/threonine.	Asparagine	201-211	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	67-70
21614585-2	2011	In the central reaction of the pathway, oligosaccharyltransferase (OST), a multimeric complex located at the membrane of the endoplasmic reticulum, transfers a preassembled oligosaccharide to selected asparagine residues within the consensus sequence asparagine-X-serine/threonine.	asparagine-x-serine	251-270	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	40-65
21614585-2	2011	In the central reaction of the pathway, oligosaccharyltransferase (OST), a multimeric complex located at the membrane of the endoplasmic reticulum, transfers a preassembled oligosaccharide to selected asparagine residues within the consensus sequence asparagine-X-serine/threonine.	asparagine-x-serine	251-270	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	67-70
21614585-2	2011	In the central reaction of the pathway, oligosaccharyltransferase (OST), a multimeric complex located at the membrane of the endoplasmic reticulum, transfers a preassembled oligosaccharide to selected asparagine residues within the consensus sequence asparagine-X-serine/threonine.	Threonine	271-280	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	40-65
21614585-2	2011	In the central reaction of the pathway, oligosaccharyltransferase (OST), a multimeric complex located at the membrane of the endoplasmic reticulum, transfers a preassembled oligosaccharide to selected asparagine residues within the consensus sequence asparagine-X-serine/threonine.	Threonine	271-280	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	67-70
21614585-3	2011	Due to the high substrate specificity of OST, alterations in the biosynthesis of the oligosaccharide substrate result in the hypoglycosylation of many different proteins and a multitude of symptoms observed in the family of congenital disorders of glycosylation (CDG) type I.	Oligosaccharides	85-100	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	41-44
21609714-1	2011	Oligosaccharyltransferase (OST) is a membrane associated enzyme complex that mediates transfer of an oligosaccharide onto asparagine residue of a protein.	Oligosaccharides	101-116	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
21609714-1	2011	Oligosaccharyltransferase (OST) is a membrane associated enzyme complex that mediates transfer of an oligosaccharide onto asparagine residue of a protein.	Oligosaccharides	101-116	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
21609714-1	2011	Oligosaccharyltransferase (OST) is a membrane associated enzyme complex that mediates transfer of an oligosaccharide onto asparagine residue of a protein.	Asparagine	122-132	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
21609714-1	2011	Oligosaccharyltransferase (OST) is a membrane associated enzyme complex that mediates transfer of an oligosaccharide onto asparagine residue of a protein.	Asparagine	122-132	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
21768116-1	2011	The oligosaccharyltransferase complex catalyzes the transfer of oligosaccharide from a dolichol pyrophosphate donor en bloc onto a free asparagine residue of a newly synthesized nascent chain during the translocation in the endoplasmic reticulum lumen.	Oligosaccharides	64-79	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	4-29
21768116-1	2011	The oligosaccharyltransferase complex catalyzes the transfer of oligosaccharide from a dolichol pyrophosphate donor en bloc onto a free asparagine residue of a newly synthesized nascent chain during the translocation in the endoplasmic reticulum lumen.	dolichol pyrophosphate	87-109	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	4-29
21768116-1	2011	The oligosaccharyltransferase complex catalyzes the transfer of oligosaccharide from a dolichol pyrophosphate donor en bloc onto a free asparagine residue of a newly synthesized nascent chain during the translocation in the endoplasmic reticulum lumen.	Asparagine	136-146	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	4-29
21357684-2	2011	Oligosaccharyltransferase (OST) catalyzes the transfer of preassembled oligosaccharides on lipid carriers onto asparagine residues in polypeptide chains.	Oligosaccharides	71-87	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
21357684-2	2011	Oligosaccharyltransferase (OST) catalyzes the transfer of preassembled oligosaccharides on lipid carriers onto asparagine residues in polypeptide chains.	Oligosaccharides	71-87	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
21357684-2	2011	Oligosaccharyltransferase (OST) catalyzes the transfer of preassembled oligosaccharides on lipid carriers onto asparagine residues in polypeptide chains.	Asparagine	111-121	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
21357684-2	2011	Oligosaccharyltransferase (OST) catalyzes the transfer of preassembled oligosaccharides on lipid carriers onto asparagine residues in polypeptide chains.	Asparagine	111-121	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
21357684-6	2011	We performed a systematic alanine mutagenesis study of the archaeal OST to identify the essential and dispensable amino acid residues in the three catalytic motifs.	Alanine	26-33	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	68-71
21357684-10	2011	In applications, mutations at this position may facilitate the design of OST variants adapted to particular N-glycosylation sites to reduce the heterogeneity of glycan occupancy.	Polysaccharides	161-167	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	73-76
20007322-1	2010	Oligosaccharyltransferase (OST) catalyzes the transfer of an oligosaccharide from a lipid donor to an asparagine residue in nascent polypeptide chains.	Asparagine	102-112	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
19955485-1	2010	Advanced glycated end-product receptor 1 (AGER1) protects against vascular disease promoted by oxidants, such as advanced glycated end products (AGEs), via inhibition of reactive oxygen species (ROS).	Reactive Oxygen Species	170-193	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	42-47
19955485-1	2010	Advanced glycated end-product receptor 1 (AGER1) protects against vascular disease promoted by oxidants, such as advanced glycated end products (AGEs), via inhibition of reactive oxygen species (ROS).	Reactive Oxygen Species	195-198	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	42-47
19955485-5	2010	These events involved epidermal growth factor receptor-dependent PKC-delta redox-sensitive Tyr-311 and Tyr-332 phosphorylation and were suppressed in AGER1(+) ECs and enhanced in sh-mRNA-AGER1(+) ECs.	Tyrosine	91-94	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	150-155
19955485-5	2010	These events involved epidermal growth factor receptor-dependent PKC-delta redox-sensitive Tyr-311 and Tyr-332 phosphorylation and were suppressed in AGER1(+) ECs and enhanced in sh-mRNA-AGER1(+) ECs.	Tyrosine	91-94	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	187-192
19955485-5	2010	These events involved epidermal growth factor receptor-dependent PKC-delta redox-sensitive Tyr-311 and Tyr-332 phosphorylation and were suppressed in AGER1(+) ECs and enhanced in sh-mRNA-AGER1(+) ECs.	Tyrosine	103-106	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	150-155
19955485-5	2010	These events involved epidermal growth factor receptor-dependent PKC-delta redox-sensitive Tyr-311 and Tyr-332 phosphorylation and were suppressed in AGER1(+) ECs and enhanced in sh-mRNA-AGER1(+) ECs.	Tyrosine	103-106	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	187-192
19955485-8	2010	Furthermore, AGER1 provides protection against AGE-induced ROS generation via NADPH.	Reactive Oxygen Species	59-62	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	13-18
19955485-8	2010	Furthermore, AGER1 provides protection against AGE-induced ROS generation via NADPH.	NADP	78-83	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	13-18
20007322-1	2010	Oligosaccharyltransferase (OST) catalyzes the transfer of an oligosaccharide from a lipid donor to an asparagine residue in nascent polypeptide chains.	Oligosaccharides	61-76	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
20007322-1	2010	Oligosaccharyltransferase (OST) catalyzes the transfer of an oligosaccharide from a lipid donor to an asparagine residue in nascent polypeptide chains.	Asparagine	102-112	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
20007322-1	2010	Oligosaccharyltransferase (OST) catalyzes the transfer of an oligosaccharide from a lipid donor to an asparagine residue in nascent polypeptide chains.	Oligosaccharides	61-76	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
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
21318189-5	2010	Cell surface AGE-R1 expression was also decreased by high AGE diets and with diabetes in dbdb mice and in humans with RI.	dbdb	89-93	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	13-19
19835842-4	2009	We hypothesized that the hypoglycosylation observed in some of these patients could be caused by a deficiency in the transfer of the oligosaccharide precursor onto protein, a reaction catalyzed by the oligosaccharyltransferase (OST) complex.	Oligosaccharides	133-148	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	201-226
19835842-4	2009	We hypothesized that the hypoglycosylation observed in some of these patients could be caused by a deficiency in the transfer of the oligosaccharide precursor onto protein, a reaction catalyzed by the oligosaccharyltransferase (OST) complex.	Oligosaccharides	133-148	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	228-231
19835842-5	2009	For this purpose, the different subunits of the OST complex were screened in 27 CDG-Ix patients for whom structural analysis of the lipid-linked oligosaccharides revealed a normal level and intact structure of the oligosaccharide precursor.	lipid-linked oligosaccharides	132-161	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	48-51
19835842-5	2009	For this purpose, the different subunits of the OST complex were screened in 27 CDG-Ix patients for whom structural analysis of the lipid-linked oligosaccharides revealed a normal level and intact structure of the oligosaccharide precursor.	Oligosaccharides	145-160	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	48-51
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
19572687-10	2009	The high-barrier addition mechanism forms an activated hydroxy-triazinyl adduct which predominantly dissociates to 2-hydroxy-1,3,5-triazine (OST) + H(*).	hydroxy-triazinyl	55-72	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	141-144
19572687-10	2009	The high-barrier addition mechanism forms an activated hydroxy-triazinyl adduct which predominantly dissociates to 2-hydroxy-1,3,5-triazine (OST) + H(*).	2-hydroxy-1,3,5-triazine	115-139	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	141-144
19572687-12	2009	Results are also presented for isomerization of the less-stable 1,3,5-triazine-N-oxide OST species (which may form via unimolecular pathways in the liquid-phase decomposition of RDX) to 2-hydroxy-1,3,5-triazine.	2-hydroxy-1,3,5-triazine	186-210	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	87-90
19572687-13	2009	A reaction mechanism is proposed for further oxidation of the s-triazinyl radical, where an OST isomer is also a potential product.	s-triazinyl radical	62-81	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	92-95
19167329-1	2009	Asparagine-linked glycosylation of polypeptides in the lumen of the endoplasmic reticulum is catalyzed by the hetero-oligomeric oligosaccharyltransferase (OST).	Asparagine	0-10	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	155-158
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
17367717-2	2007	This process is catalyzed by a membrane-associated oligosaccharyl transferase (OST) complex that transfers a preformed oligosaccharide (Glc(3)Man(9)GlcNAc(2)-) to an asparagine (Asn) side-chain acceptor located within the sequon (-Asn-X-Ser/Thr-).	Oligosaccharides	119-134	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	79-82
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
18046457-2	2008	Oligosaccharyltransferase (OST) catalyzes the co-translational transfer of an oligosaccharide from a lipid donor to an asparagine residue in nascent polypeptide chains.	Oligosaccharides	78-93	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
18046457-2	2008	Oligosaccharyltransferase (OST) catalyzes the co-translational transfer of an oligosaccharide from a lipid donor to an asparagine residue in nascent polypeptide chains.	Oligosaccharides	78-93	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
18046457-2	2008	Oligosaccharyltransferase (OST) catalyzes the co-translational transfer of an oligosaccharide from a lipid donor to an asparagine residue in nascent polypeptide chains.	Asparagine	119-129	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
18046457-2	2008	Oligosaccharyltransferase (OST) catalyzes the co-translational transfer of an oligosaccharide from a lipid donor to an asparagine residue in nascent polypeptide chains.	Asparagine	119-129	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
18046457-3	2008	Here, we report that a thermophilic archaeon, Pyrococcus furiosus OST is composed of the STT3 protein alone, and catalyzes the transfer of a heptasaccharide, containing one hexouronate and two pentose residues, onto peptides in an Asn-X-Thr/Ser-motif-dependent manner.	Xyloglucan Heptasaccharide	141-156	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	66-69
18046457-3	2008	Here, we report that a thermophilic archaeon, Pyrococcus furiosus OST is composed of the STT3 protein alone, and catalyzes the transfer of a heptasaccharide, containing one hexouronate and two pentose residues, onto peptides in an Asn-X-Thr/Ser-motif-dependent manner.	hexouronate	173-184	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	66-69
18046457-3	2008	Here, we report that a thermophilic archaeon, Pyrococcus furiosus OST is composed of the STT3 protein alone, and catalyzes the transfer of a heptasaccharide, containing one hexouronate and two pentose residues, onto peptides in an Asn-X-Thr/Ser-motif-dependent manner.	Pentoses	193-200	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	66-69
18046457-3	2008	Here, we report that a thermophilic archaeon, Pyrococcus furiosus OST is composed of the STT3 protein alone, and catalyzes the transfer of a heptasaccharide, containing one hexouronate and two pentose residues, onto peptides in an Asn-X-Thr/Ser-motif-dependent manner.	asn-x-thr	231-240	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	66-69
18046457-3	2008	Here, we report that a thermophilic archaeon, Pyrococcus furiosus OST is composed of the STT3 protein alone, and catalyzes the transfer of a heptasaccharide, containing one hexouronate and two pentose residues, onto peptides in an Asn-X-Thr/Ser-motif-dependent manner.	Serine	241-244	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	66-69
18775604-10	2008	The issues highlighted in the study reflect the need for recommendations for physicians prescribing OST in primary care to consider buprenorphine diversion during treatment more as non-adherence behavior than an abuse.	Buprenorphine	132-145	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	100-103
18479840-10	2008	A re-assessment of the treatment efficacy through a possible dosage increase or a switch to methadone could potentially reduce diversion and assure sustained adherence to OST.	Methadone	92-101	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	171-174
18485172-22	2008	(Helse Ost) funded the purchase of estradiol tablets, the manufacturing costs of misoprostol and placebo capsules from the hospital pharmacy, as well as the costs incurred for preparing the randomisation schedule and distribution of containers containing capsules to hospital.	Estradiol	35-44	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	7-10
18032526-5	2008	We examined the effects of two defined AGEs N(epsilon)-carboxy-methyl-lysine (CML) and methyl-glyoxal derivatives (MG) on these cellular pathways and their functional relationship to AGER1 in human embryonic kidney cells (HEK293).	Magnesium	115-117	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	183-188
17403929-0	2007	Dolichol-linked oligosaccharide selection by the oligosaccharyltransferase in protist and fungal organisms.	dolichol-linked oligosaccharide	0-31	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	49-74
17403929-3	2007	We have compared donor substrate utilization by the oligosaccharyltransferase (OST) from Trypanosoma cruzi, Entamoeba histolytica, Trichomonas vaginalis, Cryptococcus neoformans, and Saccharomyces cerevisiae using structurally homogeneous dolichol-linked oligosaccharides as well as a heterogeneous dolichol-linked oligosaccharide library.	dolichol-linked oligosaccharides	239-271	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	79-82
17403929-3	2007	We have compared donor substrate utilization by the oligosaccharyltransferase (OST) from Trypanosoma cruzi, Entamoeba histolytica, Trichomonas vaginalis, Cryptococcus neoformans, and Saccharomyces cerevisiae using structurally homogeneous dolichol-linked oligosaccharides as well as a heterogeneous dolichol-linked oligosaccharide library.	dolichol-linked oligosaccharide	239-270	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	79-82
17403929-4	2007	Our results demonstrate that the OST from diverse organisms utilizes the in vivo oligo saccharide donor in preference to certain larger and/or smaller oligosaccharide donors.	Oligosaccharides	81-97	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	33-36
17403929-4	2007	Our results demonstrate that the OST from diverse organisms utilizes the in vivo oligo saccharide donor in preference to certain larger and/or smaller oligosaccharide donors.	Oligosaccharides	151-166	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	33-36
17403929-5	2007	Steady-state enzyme kinetic experiments reveal that the binding affinity of the tripeptide acceptor for the protist OST complex is influenced by the structure of the oligosaccharide donor.	tripeptide K-26	80-90	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	116-119
17403929-5	2007	Steady-state enzyme kinetic experiments reveal that the binding affinity of the tripeptide acceptor for the protist OST complex is influenced by the structure of the oligosaccharide donor.	Oligosaccharides	166-181	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	116-119
17403929-6	2007	This rudimentary donor substrate selection mechanism has been refined in fungi and vertebrate organisms by the addition of a second, regulatory dolichol-linked oligosaccharide binding site, the presence of which correlates with acquisition of the SWP1/ribophorin II subunit of the OST complex.	dolichol-linked oligosaccharide	144-175	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	281-284
17367717-2	2007	This process is catalyzed by a membrane-associated oligosaccharyl transferase (OST) complex that transfers a preformed oligosaccharide (Glc(3)Man(9)GlcNAc(2)-) to an asparagine (Asn) side-chain acceptor located within the sequon (-Asn-X-Ser/Thr-).	Asparagine	166-176	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	79-82
17367717-2	2007	This process is catalyzed by a membrane-associated oligosaccharyl transferase (OST) complex that transfers a preformed oligosaccharide (Glc(3)Man(9)GlcNAc(2)-) to an asparagine (Asn) side-chain acceptor located within the sequon (-Asn-X-Ser/Thr-).	Asparagine	178-181	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	79-82
17367717-2	2007	This process is catalyzed by a membrane-associated oligosaccharyl transferase (OST) complex that transfers a preformed oligosaccharide (Glc(3)Man(9)GlcNAc(2)-) to an asparagine (Asn) side-chain acceptor located within the sequon (-Asn-X-Ser/Thr-).	Asparagine	231-234	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	79-82
17367717-2	2007	This process is catalyzed by a membrane-associated oligosaccharyl transferase (OST) complex that transfers a preformed oligosaccharide (Glc(3)Man(9)GlcNAc(2)-) to an asparagine (Asn) side-chain acceptor located within the sequon (-Asn-X-Ser/Thr-).	Serine	237-240	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	79-82
17367717-2	2007	This process is catalyzed by a membrane-associated oligosaccharyl transferase (OST) complex that transfers a preformed oligosaccharide (Glc(3)Man(9)GlcNAc(2)-) to an asparagine (Asn) side-chain acceptor located within the sequon (-Asn-X-Ser/Thr-).	Threonine	241-244	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	79-82
17367717-2	2007	This process is catalyzed by a membrane-associated oligosaccharyl transferase (OST) complex that transfers a preformed oligosaccharide (Glc(3)Man(9)GlcNAc(2)-) to an asparagine (Asn) side-chain acceptor located within the sequon (-Asn-X-Ser/Thr-).	2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose	148-154	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	79-82
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
17137774-4	2007	We find a marked reduction in the number of proteins (e.g., those involved with calcium signaling and cellular metabolism) expressed in Ln-5 hMSC compared to hMSC, consistent with our previous finding that hOST express far fewer proteins than do their hMSC progenitors, a pattern we call "osteogenic gene focusing."	Calcium	80-87	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	206-210
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
16269519-5	2006	We show here that human OSTalpha/OSTbeta expression is induced by bile acids through ligand-dependent transactivation of both OST genes by the nuclear bile acid receptor/farnesoid X receptor (FXR).	Bile Acids and Salts	66-76	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	24-27
16269519-7	2006	Furthermore, OST mRNAs were induced in human ileal biopsies exposed to the bile acid chenodeoxycholic acid.	Bile Acids and Salts	75-84	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	13-16
16269519-7	2006	Furthermore, OST mRNAs were induced in human ileal biopsies exposed to the bile acid chenodeoxycholic acid.	Chenodeoxycholic Acid	85-106	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	13-16
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
15860005-2	2005	dgl1-1 is altered in a protein ortholog of human OST48 or yeast WBP1, an essential protein subunit of the oligosaccharyltransferase (OST) complex, which is responsible for the transfer in the ER of the N-linked glycan precursor onto Asn residues of candidate proteins.	n-linked glycan	202-217	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	49-54
15987956-2	2005	The assembly of the lipid-linked core oligosaccharide Glc3Man9GlcNAc2, the substrate for the oligosaccharyltransferase (OST), is catalyzed by different glycosyltransferases located at the membrane of the endoplasmic reticulum (ER).	Oligosaccharides	38-53	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	93-118
15987956-2	2005	The assembly of the lipid-linked core oligosaccharide Glc3Man9GlcNAc2, the substrate for the oligosaccharyltransferase (OST), is catalyzed by different glycosyltransferases located at the membrane of the endoplasmic reticulum (ER).	Oligosaccharides	38-53	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	120-123
15987956-2	2005	The assembly of the lipid-linked core oligosaccharide Glc3Man9GlcNAc2, the substrate for the oligosaccharyltransferase (OST), is catalyzed by different glycosyltransferases located at the membrane of the endoplasmic reticulum (ER).	Glc3Man9GlcNAc2	54-69	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	93-118
15987956-2	2005	The assembly of the lipid-linked core oligosaccharide Glc3Man9GlcNAc2, the substrate for the oligosaccharyltransferase (OST), is catalyzed by different glycosyltransferases located at the membrane of the endoplasmic reticulum (ER).	Glc3Man9GlcNAc2	54-69	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	120-123
15860005-2	2005	dgl1-1 is altered in a protein ortholog of human OST48 or yeast WBP1, an essential protein subunit of the oligosaccharyltransferase (OST) complex, which is responsible for the transfer in the ER of the N-linked glycan precursor onto Asn residues of candidate proteins.	Asparagine	233-236	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	49-54
15544624-4	2004	HPMC cultured with GDPs differentially modulated AGE receptors (including RAGE, AGE-R1, AGE-R2 and AGE-R3) expression in a dose-dependent manner.	gdps	19-23	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	80-86
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.	high-mannose sugars	74-93	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
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.	high-mannose sugars	74-93	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
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
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
15835887-4	2005	Using two-dimensional Blue Native polyacrylamide gel electrophoresis/sodium dodecyl sulfate-polyacrylamide gel electrophoresis and mass spectrometry, we now demonstrate that mammalian OST can be isolated from solubilized, actively engaged ribosomes as multiple distinct protein complexes that range in size from approximately 500 to 700 kDa.	polyacrylamide	34-48	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	184-187
15835887-4	2005	Using two-dimensional Blue Native polyacrylamide gel electrophoresis/sodium dodecyl sulfate-polyacrylamide gel electrophoresis and mass spectrometry, we now demonstrate that mammalian OST can be isolated from solubilized, actively engaged ribosomes as multiple distinct protein complexes that range in size from approximately 500 to 700 kDa.	Sodium Dodecyl Sulfate	69-91	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	184-187
15835887-4	2005	Using two-dimensional Blue Native polyacrylamide gel electrophoresis/sodium dodecyl sulfate-polyacrylamide gel electrophoresis and mass spectrometry, we now demonstrate that mammalian OST can be isolated from solubilized, actively engaged ribosomes as multiple distinct protein complexes that range in size from approximately 500 to 700 kDa.	polyacrylamide	92-106	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	184-187
15544624-6	2004	2-furaldehyde (FurA), methylglyoxal (M-Glx) and 3,4-dideoxy-glucosone-3-Ene (3,4-DGE) increased the expression of AGE-R1 and RAGE, the receptors that are associated with toxic effects.	Furaldehyde	0-13	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	114-120
15544624-6	2004	2-furaldehyde (FurA), methylglyoxal (M-Glx) and 3,4-dideoxy-glucosone-3-Ene (3,4-DGE) increased the expression of AGE-R1 and RAGE, the receptors that are associated with toxic effects.	Furaldehyde	15-19	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	114-120
15544624-6	2004	2-furaldehyde (FurA), methylglyoxal (M-Glx) and 3,4-dideoxy-glucosone-3-Ene (3,4-DGE) increased the expression of AGE-R1 and RAGE, the receptors that are associated with toxic effects.	Pyruvaldehyde	22-35	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	114-120
15544624-6	2004	2-furaldehyde (FurA), methylglyoxal (M-Glx) and 3,4-dideoxy-glucosone-3-Ene (3,4-DGE) increased the expression of AGE-R1 and RAGE, the receptors that are associated with toxic effects.	Pyruvaldehyde	37-42	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	114-120
15544624-6	2004	2-furaldehyde (FurA), methylglyoxal (M-Glx) and 3,4-dideoxy-glucosone-3-Ene (3,4-DGE) increased the expression of AGE-R1 and RAGE, the receptors that are associated with toxic effects.	3,4-dideoxyglucosone-3-ene	48-75	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	114-120
15544624-6	2004	2-furaldehyde (FurA), methylglyoxal (M-Glx) and 3,4-dideoxy-glucosone-3-Ene (3,4-DGE) increased the expression of AGE-R1 and RAGE, the receptors that are associated with toxic effects.	3,4-dideoxyglucosone-3-ene	77-84	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	114-120
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
14641036-9	2003	GFP-Dad1 can be used as a reporter molecule for the lateral mobility of the TCs since the OST is tightly associated with the complex.	Technetium	76-79	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	90-93
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
11866428-4	2002	Localisation of OST48 was not affected by substitution of the two lysines by histidine, indicating that a His-Xaa-His sequence, in contrast to Arg-Xaa-Arg, contains ER-specific targeting information.	Histidine	106-109	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	16-21
12123673-0	2002	A biotin capture assay for oligosaccharyltransferase.	Biotin	2-8	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-52
12123673-3	2002	Herein, we present the use of a biotinylated peptide as the acceptor substrate and dolichylpyrophosphate [3H]chitobiose as the donor substrate for the OST-catalyzed reaction.	Tritium	106-108	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	151-154
11866428-1	2002	The OST48 subunit of the oligosaccharyltransferase complex is a type I membrane protein containing three lysines in its cytosolic domain.	Lysine	105-112	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	4-9
11866428-3	2002	Substitution of these lysines by arginine resulted in cell-surface expression of OST48, whereas ER residency was maintained when either Lys-5 or Lys-3 but not both was replaced with arginine.	Lysine	22-29	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	81-86
11866428-3	2002	Substitution of these lysines by arginine resulted in cell-surface expression of OST48, whereas ER residency was maintained when either Lys-5 or Lys-3 but not both was replaced with arginine.	Arginine	33-41	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	81-86
11866428-4	2002	Localisation of OST48 was not affected by substitution of the two lysines by histidine, indicating that a His-Xaa-His sequence, in contrast to Arg-Xaa-Arg, contains ER-specific targeting information.	xanthenone-4-acetic acid	110-113	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	16-21
11866428-4	2002	Localisation of OST48 was not affected by substitution of the two lysines by histidine, indicating that a His-Xaa-His sequence, in contrast to Arg-Xaa-Arg, contains ER-specific targeting information.	Histidine	114-117	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	16-21
11580295-0	2001	Allosteric regulation provides a molecular mechanism for preferential utilization of the fully assembled dolichol-linked oligosaccharide by the yeast oligosaccharyltransferase.	dolichol-linked oligosaccharide	105-136	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	150-175
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.	dolichol-linked oligosaccharide glc	80-115	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.	dolichol-linked oligosaccharide glc	80-115	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	31-34
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.	2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose	124-130	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.	2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose	124-130	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	31-34
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.	)-pp-dol	132-140	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.	)-pp-dol	132-140	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	31-34
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
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.	Asparagine	184-194	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.	Asparagine	184-194	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	31-34
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.	n-x-t	207-212	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.	n-x-t	207-212	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	31-34
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.	Sulfur	32-33	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	4-29
11580295-4	2001	Here, the steady-state kinetic properties of the OST were reinvestigated using a proteoliposome assay system consisting of the purified yeast enzyme, near-homogeneous preparations of a dolichol-linked oligosaccharide (Glc(3)Man(9)GlcNAc(2)-PP-Dol or Man(9)GlcNAc(2)-PP-Dol) and an (125)I-labeled tripeptide as the acceptor substrate.	dolichol-linked oligosaccharide	185-216	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	49-52
11580295-4	2001	Here, the steady-state kinetic properties of the OST were reinvestigated using a proteoliposome assay system consisting of the purified yeast enzyme, near-homogeneous preparations of a dolichol-linked oligosaccharide (Glc(3)Man(9)GlcNAc(2)-PP-Dol or Man(9)GlcNAc(2)-PP-Dol) and an (125)I-labeled tripeptide as the acceptor substrate.	2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose	230-236	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	49-52
11580295-4	2001	Here, the steady-state kinetic properties of the OST were reinvestigated using a proteoliposome assay system consisting of the purified yeast enzyme, near-homogeneous preparations of a dolichol-linked oligosaccharide (Glc(3)Man(9)GlcNAc(2)-PP-Dol or Man(9)GlcNAc(2)-PP-Dol) and an (125)I-labeled tripeptide as the acceptor substrate.	)-pp-dol	238-246	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	49-52
11580295-4	2001	Here, the steady-state kinetic properties of the OST were reinvestigated using a proteoliposome assay system consisting of the purified yeast enzyme, near-homogeneous preparations of a dolichol-linked oligosaccharide (Glc(3)Man(9)GlcNAc(2)-PP-Dol or Man(9)GlcNAc(2)-PP-Dol) and an (125)I-labeled tripeptide as the acceptor substrate.	)-pp-dol	264-272	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	49-52
11580295-4	2001	Here, the steady-state kinetic properties of the OST were reinvestigated using a proteoliposome assay system consisting of the purified yeast enzyme, near-homogeneous preparations of a dolichol-linked oligosaccharide (Glc(3)Man(9)GlcNAc(2)-PP-Dol or Man(9)GlcNAc(2)-PP-Dol) and an (125)I-labeled tripeptide as the acceptor substrate.	tripeptide K-26	296-306	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	49-52
11580295-5	2001	The K(m) of the OST for the acceptor tripeptide was only slightly enhanced when Glc(3)Man(9)GlcNAc(2)-PP-Dol was the donor substrate relative to when Man(9)GlcNAc(2)-PP-Dol was the donor substrate.	tripeptide K-26	37-47	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	16-19
11580295-5	2001	The K(m) of the OST for the acceptor tripeptide was only slightly enhanced when Glc(3)Man(9)GlcNAc(2)-PP-Dol was the donor substrate relative to when Man(9)GlcNAc(2)-PP-Dol was the donor substrate.	(2)-pp-dol	98-108	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	16-19
11580295-5	2001	The K(m) of the OST for the acceptor tripeptide was only slightly enhanced when Glc(3)Man(9)GlcNAc(2)-PP-Dol was the donor substrate relative to when Man(9)GlcNAc(2)-PP-Dol was the donor substrate.	(2)-pp-dol	162-172	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	16-19
10203410-7	1999	We found significant correlations between the global skeletal uptake of 99mTc-methylendiphosphonate and serum BGP levels assayed by both N-tact Osteo SP (P < 0.01) and Elsa-Ost-Nat assay (P < 0.05).	99mtc-methylendiphosphonate	72-99	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	144-147
11470266-0	2001	Oligosaccharyltransferase is highly specific for the hydroxy amino acid in Asn-Xaa-Thr/Ser.	hydroxy amino acid	53-71	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
11470266-0	2001	Oligosaccharyltransferase is highly specific for the hydroxy amino acid in Asn-Xaa-Thr/Ser.	asn-xaa-thr	75-86	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
11470266-0	2001	Oligosaccharyltransferase is highly specific for the hydroxy amino acid in Asn-Xaa-Thr/Ser.	Serine	87-90	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
11470266-5	2001	Binding of the threonine beta-methyl group by OST is also specific, with serine, L-threo-beta-hydroxynorvaline and L-beta-hydroxynorleucine containing tripeptides all bound much less efficiently than the threonine peptide itself.	Threonine	15-24	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	46-49
11470266-5	2001	Binding of the threonine beta-methyl group by OST is also specific, with serine, L-threo-beta-hydroxynorvaline and L-beta-hydroxynorleucine containing tripeptides all bound much less efficiently than the threonine peptide itself.	Serine	73-79	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	46-49
11470266-5	2001	Binding of the threonine beta-methyl group by OST is also specific, with serine, L-threo-beta-hydroxynorvaline and L-beta-hydroxynorleucine containing tripeptides all bound much less efficiently than the threonine peptide itself.	l-threo-beta-hydroxynorvaline	81-110	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	46-49
11470266-5	2001	Binding of the threonine beta-methyl group by OST is also specific, with serine, L-threo-beta-hydroxynorvaline and L-beta-hydroxynorleucine containing tripeptides all bound much less efficiently than the threonine peptide itself.	L-3-propylserine	115-139	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	46-49
11470266-5	2001	Binding of the threonine beta-methyl group by OST is also specific, with serine, L-threo-beta-hydroxynorvaline and L-beta-hydroxynorleucine containing tripeptides all bound much less efficiently than the threonine peptide itself.	tripeptides	151-162	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	46-49
11470266-5	2001	Binding of the threonine beta-methyl group by OST is also specific, with serine, L-threo-beta-hydroxynorvaline and L-beta-hydroxynorleucine containing tripeptides all bound much less efficiently than the threonine peptide itself.	threonine peptide	204-221	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	46-49
10697522-9	1999	Furthermore, p53 induction was lost in OST/R cells after cisplatin exposure.	Cisplatin	57-66	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	39-42
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
10660554-10	2000	We also show that the dilysine motif in OST48 functions as an ER localization motif because OST48 in which the two lysine residues are replaced by serine (OST48ss) is no longer retained in the ER and is found instead also at the plasma membrane.	lysyllysine	22-30	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	40-45
10660554-10	2000	We also show that the dilysine motif in OST48 functions as an ER localization motif because OST48 in which the two lysine residues are replaced by serine (OST48ss) is no longer retained in the ER and is found instead also at the plasma membrane.	lysyllysine	22-30	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	92-97
10660554-10	2000	We also show that the dilysine motif in OST48 functions as an ER localization motif because OST48 in which the two lysine residues are replaced by serine (OST48ss) is no longer retained in the ER and is found instead also at the plasma membrane.	Lysine	24-30	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	40-45
10660554-10	2000	We also show that the dilysine motif in OST48 functions as an ER localization motif because OST48 in which the two lysine residues are replaced by serine (OST48ss) is no longer retained in the ER and is found instead also at the plasma membrane.	Lysine	24-30	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	92-97
10660554-10	2000	We also show that the dilysine motif in OST48 functions as an ER localization motif because OST48 in which the two lysine residues are replaced by serine (OST48ss) is no longer retained in the ER and is found instead also at the plasma membrane.	Serine	147-153	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	40-45
10660554-10	2000	We also show that the dilysine motif in OST48 functions as an ER localization motif because OST48 in which the two lysine residues are replaced by serine (OST48ss) is no longer retained in the ER and is found instead also at the plasma membrane.	Serine	147-153	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	92-97
9592174-1	1998	Octamer Sequencing Technology, OST, is a method of DNA sequencing using single octamer oligonucleotides to prime cycle sequencing reactions.	Oligonucleotides	87-103	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	31-34
10220030-0	1999	Dolichylpyrophosphate oligosaccharides: large-scale isolation and evaluation as oligosaccharyltransferase substrates.	dolichylpyrophosphate oligosaccharides	0-38	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	80-105
10220030-1	1999	Oligosaccharyltransferase (OST) catalyzes the transfer of a branched oligosaccharide from a dolichylpyrophosphate oligosaccharide (Dol-PP-OS) to the asparagine of a nascent polypeptide chain in vivo and peptide substrates in vitro.	branched oligosaccharide	60-84	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
10220030-1	1999	Oligosaccharyltransferase (OST) catalyzes the transfer of a branched oligosaccharide from a dolichylpyrophosphate oligosaccharide (Dol-PP-OS) to the asparagine of a nascent polypeptide chain in vivo and peptide substrates in vitro.	branched oligosaccharide	60-84	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
10220030-1	1999	Oligosaccharyltransferase (OST) catalyzes the transfer of a branched oligosaccharide from a dolichylpyrophosphate oligosaccharide (Dol-PP-OS) to the asparagine of a nascent polypeptide chain in vivo and peptide substrates in vitro.	dolichylpyrophosphate oligosaccharide	92-129	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
10220030-1	1999	Oligosaccharyltransferase (OST) catalyzes the transfer of a branched oligosaccharide from a dolichylpyrophosphate oligosaccharide (Dol-PP-OS) to the asparagine of a nascent polypeptide chain in vivo and peptide substrates in vitro.	dolichylpyrophosphate oligosaccharide	92-129	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
10220030-1	1999	Oligosaccharyltransferase (OST) catalyzes the transfer of a branched oligosaccharide from a dolichylpyrophosphate oligosaccharide (Dol-PP-OS) to the asparagine of a nascent polypeptide chain in vivo and peptide substrates in vitro.	dol-pp-os	131-140	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
10220030-1	1999	Oligosaccharyltransferase (OST) catalyzes the transfer of a branched oligosaccharide from a dolichylpyrophosphate oligosaccharide (Dol-PP-OS) to the asparagine of a nascent polypeptide chain in vivo and peptide substrates in vitro.	dol-pp-os	131-140	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
10220030-1	1999	Oligosaccharyltransferase (OST) catalyzes the transfer of a branched oligosaccharide from a dolichylpyrophosphate oligosaccharide (Dol-PP-OS) to the asparagine of a nascent polypeptide chain in vivo and peptide substrates in vitro.	Asparagine	149-159	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-25
10220030-1	1999	Oligosaccharyltransferase (OST) catalyzes the transfer of a branched oligosaccharide from a dolichylpyrophosphate oligosaccharide (Dol-PP-OS) to the asparagine of a nascent polypeptide chain in vivo and peptide substrates in vitro.	Asparagine	149-159	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
10220030-4	1999	These were determined for Dol-PP-OS, Dol-PP-DS, and the tripeptide Bz-Asn-Leu-Thr-NH2 with solubilized OST and, for the first time, saturation kinetics were observed for all substrates.	tripeptide bz-asn-leu-thr-nh2	56-85	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	103-106
9748289-2	1998	The oligosaccharyltransferase (OST), which has its active site exposed on the luminal face of the endoplasmic reticulum (ER), catalyzes the transfer of preassembled high mannose oligosaccharides onto certain asparagine residues of nascent polypeptides.	mannose oligosaccharides	170-194	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	4-29
9748289-2	1998	The oligosaccharyltransferase (OST), which has its active site exposed on the luminal face of the endoplasmic reticulum (ER), catalyzes the transfer of preassembled high mannose oligosaccharides onto certain asparagine residues of nascent polypeptides.	mannose oligosaccharides	170-194	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	31-34
9748289-2	1998	The oligosaccharyltransferase (OST), which has its active site exposed on the luminal face of the endoplasmic reticulum (ER), catalyzes the transfer of preassembled high mannose oligosaccharides onto certain asparagine residues of nascent polypeptides.	Asparagine	208-218	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	4-29
9748289-2	1998	The oligosaccharyltransferase (OST), which has its active site exposed on the luminal face of the endoplasmic reticulum (ER), catalyzes the transfer of preassembled high mannose oligosaccharides onto certain asparagine residues of nascent polypeptides.	Asparagine	208-218	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	31-34
9839012-0	1998	The design, synthesis, and initial evaluation of benzophenone-containing peptides as potential photoaffinity labels of oligosaccharyltransferase.	benzophenone	49-61	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	119-144
9839012-1	1998	The benzophenone photophore was incorporated into protected tripeptides and tetrapeptides as photoactivatable probes to study the multimeric enzyme oligosaccharyltransferase (OST).	benzophenone	4-16	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	148-173
9839012-1	1998	The benzophenone photophore was incorporated into protected tripeptides and tetrapeptides as photoactivatable probes to study the multimeric enzyme oligosaccharyltransferase (OST).	benzophenone	4-16	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	175-178
9839012-1	1998	The benzophenone photophore was incorporated into protected tripeptides and tetrapeptides as photoactivatable probes to study the multimeric enzyme oligosaccharyltransferase (OST).	tripeptides	60-71	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	175-178
9839012-3	1998	Two tripeptides, Bz-Asn-Bpa-Thr-NH2 (3b) and Bz-Asn-Lys[N epsilon-(4-Bz)Bz]-Thr-NH2 (4b), were found to be good OST substrates.	bz-asn-bpa-thr-nh2	17-35	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	112-115
9839012-3	1998	Two tripeptides, Bz-Asn-Bpa-Thr-NH2 (3b) and Bz-Asn-Lys[N epsilon-(4-Bz)Bz]-Thr-NH2 (4b), were found to be good OST substrates.	bz-asn-lys	45-55	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	112-115
9839012-3	1998	Two tripeptides, Bz-Asn-Bpa-Thr-NH2 (3b) and Bz-Asn-Lys[N epsilon-(4-Bz)Bz]-Thr-NH2 (4b), were found to be good OST substrates.	n epsilon-(4-bz)bz]	56-75	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	112-115
34354228-0	2021	The structure of an archaeal oligosaccharyltransferase provides insight into the strict exclusion of proline from the N-glycosylation sequon.	Proline	101-108	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	29-54
9368036-4	1997	Using the yeast two-hybrid system, we have shown that the luminal domains of RI and RII (RIL and RIIL, respectively) interacted with the luminal domain of OST48 (OST48L), but no direct interaction was observed between RIL and RIIL.	Cephradine	89-92	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	155-160
9368036-4	1997	Using the yeast two-hybrid system, we have shown that the luminal domains of RI and RII (RIL and RIIL, respectively) interacted with the luminal domain of OST48 (OST48L), but no direct interaction was observed between RIL and RIIL.	riil	97-101	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	155-160
8666161-2	1996	The initial stage in the biosynthesis of N-linked glycoproteins, catalyzed by the enzyme oligosaccharyltransferase (OST), involves the transfer of a preassembled high-mannose oligosaccharide from a dolichol-linked oligosaccharide donor onto asparagine acceptor sites in nascent proteins in the lumen of the rough endoplasmic reticulum.	high-mannose oligosaccharide	162-190	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	89-114
8666161-2	1996	The initial stage in the biosynthesis of N-linked glycoproteins, catalyzed by the enzyme oligosaccharyltransferase (OST), involves the transfer of a preassembled high-mannose oligosaccharide from a dolichol-linked oligosaccharide donor onto asparagine acceptor sites in nascent proteins in the lumen of the rough endoplasmic reticulum.	high-mannose oligosaccharide	162-190	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	116-119
8666161-2	1996	The initial stage in the biosynthesis of N-linked glycoproteins, catalyzed by the enzyme oligosaccharyltransferase (OST), involves the transfer of a preassembled high-mannose oligosaccharide from a dolichol-linked oligosaccharide donor onto asparagine acceptor sites in nascent proteins in the lumen of the rough endoplasmic reticulum.	dolichol-linked oligosaccharide	198-229	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	89-114
8666161-2	1996	The initial stage in the biosynthesis of N-linked glycoproteins, catalyzed by the enzyme oligosaccharyltransferase (OST), involves the transfer of a preassembled high-mannose oligosaccharide from a dolichol-linked oligosaccharide donor onto asparagine acceptor sites in nascent proteins in the lumen of the rough endoplasmic reticulum.	dolichol-linked oligosaccharide	198-229	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	116-119
8666161-2	1996	The initial stage in the biosynthesis of N-linked glycoproteins, catalyzed by the enzyme oligosaccharyltransferase (OST), involves the transfer of a preassembled high-mannose oligosaccharide from a dolichol-linked oligosaccharide donor onto asparagine acceptor sites in nascent proteins in the lumen of the rough endoplasmic reticulum.	Asparagine	241-251	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	89-114
8666161-2	1996	The initial stage in the biosynthesis of N-linked glycoproteins, catalyzed by the enzyme oligosaccharyltransferase (OST), involves the transfer of a preassembled high-mannose oligosaccharide from a dolichol-linked oligosaccharide donor onto asparagine acceptor sites in nascent proteins in the lumen of the rough endoplasmic reticulum.	Asparagine	241-251	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	116-119
8666161-7	1996	Yeast molecular genetic methods have been instrumental in the functional characterization of the OST subunits, and have proven to be powerful tools for the identification of novel gene products that influence oligosaccharide transfer in vivo.	Oligosaccharides	209-224	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	97-100
7782656-9	1995	As a result, 1 alpha hydroxyvitamin D3 was found to have significantly suppressed the relative mean tumor weight of OST and MNNG-HOS compared with a control group (p < 0.05), but did not suppress that of KHOS-NP.	alpha hydroxyvitamin d3	15-38	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	116-119
30450807-3	2019	OST transfers the oligosaccharide from a lipid-linked donor (LLO) to the Asn-Xaa-Ser/Thr sequon of nascent polypeptide, usually cotranslationally by partnering with the ribosome and the translocon.	Oligosaccharides	18-33	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-3
30450807-3	2019	OST transfers the oligosaccharide from a lipid-linked donor (LLO) to the Asn-Xaa-Ser/Thr sequon of nascent polypeptide, usually cotranslationally by partnering with the ribosome and the translocon.	asn-xaa	73-80	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-3
30450807-3	2019	OST transfers the oligosaccharide from a lipid-linked donor (LLO) to the Asn-Xaa-Ser/Thr sequon of nascent polypeptide, usually cotranslationally by partnering with the ribosome and the translocon.	Serine	81-84	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-3
30450807-3	2019	OST transfers the oligosaccharide from a lipid-linked donor (LLO) to the Asn-Xaa-Ser/Thr sequon of nascent polypeptide, usually cotranslationally by partnering with the ribosome and the translocon.	Threonine	85-88	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-3
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
9673402-1	1998	A cisplatin (CDDP)-resistant human osteosarcoma cell line (OST/R) was established by continuous exposure to CDDP.	Cisplatin	2-11	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	59-62
9673402-1	1998	A cisplatin (CDDP)-resistant human osteosarcoma cell line (OST/R) was established by continuous exposure to CDDP.	cddp	13-17	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	59-62
9673402-1	1998	A cisplatin (CDDP)-resistant human osteosarcoma cell line (OST/R) was established by continuous exposure to CDDP.	cddp	108-112	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	59-62
9673402-2	1998	OST/R cells proved to be 6.73 times more resistant to CDDP compared with parental OST cells, and showed cross-resistance to carboplatin (CBDCA).	cddp	54-58	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-3
9673402-2	1998	OST/R cells proved to be 6.73 times more resistant to CDDP compared with parental OST cells, and showed cross-resistance to carboplatin (CBDCA).	Carboplatin	124-135	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-3
9673402-2	1998	OST/R cells proved to be 6.73 times more resistant to CDDP compared with parental OST cells, and showed cross-resistance to carboplatin (CBDCA).	Carboplatin	137-142	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-3
9673402-3	1998	The mechanism of CDDP resistance was a significant decrease of intracellular platinum accumulation which was 40% of that in OST cells.	cddp	17-21	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	124-127
9673402-3	1998	The mechanism of CDDP resistance was a significant decrease of intracellular platinum accumulation which was 40% of that in OST cells.	Platinum	77-85	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	124-127
9673402-4	1998	OST/R cells were exposed to CDDP for 6 hours, the platinum was released from the cytoplasm of OST/R cells without reaching a state of equilibrium.	cddp	28-32	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-3
9673402-4	1998	OST/R cells were exposed to CDDP for 6 hours, the platinum was released from the cytoplasm of OST/R cells without reaching a state of equilibrium.	cddp	28-32	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	94-97
9673402-4	1998	OST/R cells were exposed to CDDP for 6 hours, the platinum was released from the cytoplasm of OST/R cells without reaching a state of equilibrium.	Platinum	50-58	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	0-3
9673402-4	1998	OST/R cells were exposed to CDDP for 6 hours, the platinum was released from the cytoplasm of OST/R cells without reaching a state of equilibrium.	Platinum	50-58	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	94-97
9398187-0	1997	13C- and 15N-labeled peptide substrates as mechanistic probes of oligosaccharyltransferase.	13c	0-3	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	65-90
9398187-0	1997	13C- and 15N-labeled peptide substrates as mechanistic probes of oligosaccharyltransferase.	15n	9-12	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	65-90
9398187-1	1997	The carboxamide moiety that links the carbohydrate and protein moieties in N-linked glycoproteins has been unambiguously determined to arise intact from asparagine by the use of chemically synthesized Bz-[4-13C, 15N]Asn-Leu-Thr-NH2 as an oligosaccharyltransferase (OST) substrate.	carboxamide	4-15	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	238-263
9398187-1	1997	The carboxamide moiety that links the carbohydrate and protein moieties in N-linked glycoproteins has been unambiguously determined to arise intact from asparagine by the use of chemically synthesized Bz-[4-13C, 15N]Asn-Leu-Thr-NH2 as an oligosaccharyltransferase (OST) substrate.	carboxamide	4-15	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	265-268
9398187-1	1997	The carboxamide moiety that links the carbohydrate and protein moieties in N-linked glycoproteins has been unambiguously determined to arise intact from asparagine by the use of chemically synthesized Bz-[4-13C, 15N]Asn-Leu-Thr-NH2 as an oligosaccharyltransferase (OST) substrate.	Carbohydrates	38-50	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	238-263
9398187-1	1997	The carboxamide moiety that links the carbohydrate and protein moieties in N-linked glycoproteins has been unambiguously determined to arise intact from asparagine by the use of chemically synthesized Bz-[4-13C, 15N]Asn-Leu-Thr-NH2 as an oligosaccharyltransferase (OST) substrate.	Carbohydrates	38-50	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	265-268
9398187-1	1997	The carboxamide moiety that links the carbohydrate and protein moieties in N-linked glycoproteins has been unambiguously determined to arise intact from asparagine by the use of chemically synthesized Bz-[4-13C, 15N]Asn-Leu-Thr-NH2 as an oligosaccharyltransferase (OST) substrate.	Asparagine	153-163	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	238-263
9398187-1	1997	The carboxamide moiety that links the carbohydrate and protein moieties in N-linked glycoproteins has been unambiguously determined to arise intact from asparagine by the use of chemically synthesized Bz-[4-13C, 15N]Asn-Leu-Thr-NH2 as an oligosaccharyltransferase (OST) substrate.	Asparagine	153-163	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	265-268
9398187-2	1997	Bz-[4-13C]Asn-Leu-Thr-NH2 was also synthesized and used to evaluate a proposed mechanism of OST catalysis similar to that of glutamine-dependent amidotransferases using 15NH4OAc as a potential external nucleophile.	bz-[4-13c]asn-leu-thr-nh2	0-25	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	92-95
9398187-2	1997	Bz-[4-13C]Asn-Leu-Thr-NH2 was also synthesized and used to evaluate a proposed mechanism of OST catalysis similar to that of glutamine-dependent amidotransferases using 15NH4OAc as a potential external nucleophile.	15nh4oac	169-177	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	92-95
9398187-6	1997	Together with previously published results, these data argue against nucleophilic activation of the asparagine beta-carboxamide moiety being the underlying chemical mechanism for OST-catalyzed glycosylation of peptides.	asparagine beta-carboxamide	100-127	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	179-182
9367678-2	1997	4.1.119) (DDOST) catalyzes the transfer of a high-mannose oligosaccharide (GlcNac2Man9Glc3) from a dolichol-linked oligosaccharide donor (dolichol-P-GlcNac2Man9Glc3) onto the asparagine acceptor site within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains across the membrane of the endoplasmic reticulum.	mannose oligosaccharide	50-73	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	10-15
9367678-2	1997	4.1.119) (DDOST) catalyzes the transfer of a high-mannose oligosaccharide (GlcNac2Man9Glc3) from a dolichol-linked oligosaccharide donor (dolichol-P-GlcNac2Man9Glc3) onto the asparagine acceptor site within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains across the membrane of the endoplasmic reticulum.	glcnac2man9glc3	75-90	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	10-15
9367678-2	1997	4.1.119) (DDOST) catalyzes the transfer of a high-mannose oligosaccharide (GlcNac2Man9Glc3) from a dolichol-linked oligosaccharide donor (dolichol-P-GlcNac2Man9Glc3) onto the asparagine acceptor site within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains across the membrane of the endoplasmic reticulum.	dolichol-linked oligosaccharide	99-130	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	10-15
9367678-2	1997	4.1.119) (DDOST) catalyzes the transfer of a high-mannose oligosaccharide (GlcNac2Man9Glc3) from a dolichol-linked oligosaccharide donor (dolichol-P-GlcNac2Man9Glc3) onto the asparagine acceptor site within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains across the membrane of the endoplasmic reticulum.	dolichol-p-glcnac2man9glc3	138-164	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	10-15
9367678-2	1997	4.1.119) (DDOST) catalyzes the transfer of a high-mannose oligosaccharide (GlcNac2Man9Glc3) from a dolichol-linked oligosaccharide donor (dolichol-P-GlcNac2Man9Glc3) onto the asparagine acceptor site within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains across the membrane of the endoplasmic reticulum.	Asparagine	175-185	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	10-15
9367678-2	1997	4.1.119) (DDOST) catalyzes the transfer of a high-mannose oligosaccharide (GlcNac2Man9Glc3) from a dolichol-linked oligosaccharide donor (dolichol-P-GlcNac2Man9Glc3) onto the asparagine acceptor site within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains across the membrane of the endoplasmic reticulum.	asn-x-ser	210-219	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	10-15
9367678-2	1997	4.1.119) (DDOST) catalyzes the transfer of a high-mannose oligosaccharide (GlcNac2Man9Glc3) from a dolichol-linked oligosaccharide donor (dolichol-P-GlcNac2Man9Glc3) onto the asparagine acceptor site within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains across the membrane of the endoplasmic reticulum.	Threonine	220-223	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	10-15
9367678-3	1997	We isolated mouse and human DDOST cDNAs from retinoic acid-treated mouse P19 EC cells and human NT-2 cells, respectively.	Tretinoin	45-58	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	28-33
9144178-8	1997	DAD1 can be crosslinked to OST48 in intact microsomes with dithiobis(succinimidylpropionate).	dithiobis(succinimidylpropionate)	59-91	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-32
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
9078248-1	1997	Pig liver oligosaccharyltransferase (OST) is inactivated irreversibly by a hexapeptide in which threonine has been substituted by epoxyethylglycine in the Asn-Xaa-Thr glycosylation triplet.	Threonine	96-105	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	10-35
9078248-1	1997	Pig liver oligosaccharyltransferase (OST) is inactivated irreversibly by a hexapeptide in which threonine has been substituted by epoxyethylglycine in the Asn-Xaa-Thr glycosylation triplet.	Threonine	96-105	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	37-40
9078248-1	1997	Pig liver oligosaccharyltransferase (OST) is inactivated irreversibly by a hexapeptide in which threonine has been substituted by epoxyethylglycine in the Asn-Xaa-Thr glycosylation triplet.	epoxyethylglycine	130-147	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	10-35
9078248-1	1997	Pig liver oligosaccharyltransferase (OST) is inactivated irreversibly by a hexapeptide in which threonine has been substituted by epoxyethylglycine in the Asn-Xaa-Thr glycosylation triplet.	epoxyethylglycine	130-147	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	37-40
9078248-1	1997	Pig liver oligosaccharyltransferase (OST) is inactivated irreversibly by a hexapeptide in which threonine has been substituted by epoxyethylglycine in the Asn-Xaa-Thr glycosylation triplet.	asn-xaa-thr	155-166	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	10-35
9078248-1	1997	Pig liver oligosaccharyltransferase (OST) is inactivated irreversibly by a hexapeptide in which threonine has been substituted by epoxyethylglycine in the Asn-Xaa-Thr glycosylation triplet.	asn-xaa-thr	155-166	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	37-40
9078248-2	1997	Incubation of the enzyme in the presence of Dol-PP-linked [14C]oligosaccharides and the N-3,5-dinitrobenzoylated epoxy derivative leads to the double-labelling of two subunits (48 and 66 kDa) of the oligomeric OST complex, both of which are involved in the catalytic activity.	dol-pp-linked [14c]oligosaccharides	44-79	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	210-213
9078248-2	1997	Incubation of the enzyme in the presence of Dol-PP-linked [14C]oligosaccharides and the N-3,5-dinitrobenzoylated epoxy derivative leads to the double-labelling of two subunits (48 and 66 kDa) of the oligomeric OST complex, both of which are involved in the catalytic activity.	n-3,5-dinitrobenzoylated	88-112	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	210-213
9078248-3	1997	Labelling of both subunits was blocked competitively by the acceptor peptide N-benzoyl-Asu-Gly-Thr-NHCH3 and by the OST inhibitor N-benzoyl-alpha,gamma-diaminobutyric acid-Gly-Thr-NHCH3, but not by an analogue derived from the epoxy-inhibitor by replacing asparagine with glutamine.	n-benzoyl-alpha,gamma-diaminobutyric acid-gly-thr-nhch3	130-185	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	116-119
9078248-3	1997	Labelling of both subunits was blocked competitively by the acceptor peptide N-benzoyl-Asu-Gly-Thr-NHCH3 and by the OST inhibitor N-benzoyl-alpha,gamma-diaminobutyric acid-Gly-Thr-NHCH3, but not by an analogue derived from the epoxy-inhibitor by replacing asparagine with glutamine.	Asparagine	256-266	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	116-119
9078248-3	1997	Labelling of both subunits was blocked competitively by the acceptor peptide N-benzoyl-Asu-Gly-Thr-NHCH3 and by the OST inhibitor N-benzoyl-alpha,gamma-diaminobutyric acid-Gly-Thr-NHCH3, but not by an analogue derived from the epoxy-inhibitor by replacing asparagine with glutamine.	Glutamine	272-281	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	116-119
7782656-10	1995	Histologically, 1 alpha hydroxyvitamin D3 induced marked chondrogenetic differentiation in OST alone.	alfacalcidol	16-41	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	91-94
34462534-0	2022	The second DDOST-CDG patient with lactose intolerance, developmental delay, and situs inversus totalis.	Lactose	34-41	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	11-16
34462534-3	2022	In this study, we report a Chinese patient with a homozygous pathogenic variant in DDOST (c.1187G>A) and who presented with feeding difficulty, lactose intolerance, facial dysmorphism, failure to thrive, strabismus, high myopia, astigmatism, hypotonia, developmental delay and situs inversus totalis.	Lactose	144-151	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	83-88
34871448-13	2022	RESULTS: Consumption of a Mediterranean diet rich in monounsaturated fatty acids (MUFAs) and low in dietary AGEs reduced serum concentrations of AGEs, reduced expression of the receptor for AGE (RAGE), and increased expression of the AGE receptor 1 (AGER1) when compared with consumption of a Western diet rich in saturated fatty acids and dietary AGEs.	Fatty Acids, Monounsaturated	53-80	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	234-248
34871448-14	2022	Supplementation with omega-3 polyunsaturated fatty acids (PUFAs) resulted in decreased concentrations of fluorescent AGEs and decreased expression of RAGE as well as increased expression of AGER1.	omega-3 polyunsaturated fatty acids	21-56	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	190-195
34871448-14	2022	Supplementation with omega-3 polyunsaturated fatty acids (PUFAs) resulted in decreased concentrations of fluorescent AGEs and decreased expression of RAGE as well as increased expression of AGER1.	Fatty Acids, Unsaturated	58-63	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	190-195
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.	Oligosaccharides	42-57	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.	Oligosaccharides	42-57	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
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.	Asparagine	74-77	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.	Asparagine	74-77	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
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
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.	asn-x-ser	117-126	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.	asn-x-ser	117-126	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
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.	Threonine	127-130	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.	Threonine	127-130	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
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.	Proline	138-141	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.	Proline	138-141	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	27-30
34354228-3	2021	Here we determined the crystal structure of an archaeal OST in a complex with a sequon-containing peptide and dolichol-phosphate to a 2.7 A resolution.	Dolichol Phosphates	110-128	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	56-59
35173766-1	2021	Background: Dolichyl-diphosphooligosaccharide-protein glycosyltransferase non-catalytic subunit (DDOST) is an important enzyme in the process of high-mannose oligosaccharide transferring in cells.	Mannose	150-157	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	12-95
35173766-1	2021	Background: Dolichyl-diphosphooligosaccharide-protein glycosyltransferase non-catalytic subunit (DDOST) is an important enzyme in the process of high-mannose oligosaccharide transferring in cells.	Mannose	150-157	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	97-102
35173766-1	2021	Background: Dolichyl-diphosphooligosaccharide-protein glycosyltransferase non-catalytic subunit (DDOST) is an important enzyme in the process of high-mannose oligosaccharide transferring in cells.	Oligosaccharides	158-173	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	12-95
35173766-1	2021	Background: Dolichyl-diphosphooligosaccharide-protein glycosyltransferase non-catalytic subunit (DDOST) is an important enzyme in the process of high-mannose oligosaccharide transferring in cells.	Oligosaccharides	158-173	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	97-102
35173766-10	2021	GSEA suggested that DDOST is closely correlated with cell cycle and immune response via the PPAR signaling pathway.	gsea	0-4	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	20-25