PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18567790-5	2008	N-glycan analysis of alg3-2 and alg3-2 in the complex-glycan-less mutant background, which lacks N-acetylglucosaminyl-transferase I activity, reveals that when ALG3 activity is strongly reduced, almost all N-glycans transferred to proteins are aberrant, indicating that the Arabidopsis oligosaccharide transferase complex is remarkably substrate tolerant.	Polysaccharides	2-8	asparagine-linked glycosylation 3	Arabidopsis thaliana	21-25	
18567790-5	2008	N-glycan analysis of alg3-2 and alg3-2 in the complex-glycan-less mutant background, which lacks N-acetylglucosaminyl-transferase I activity, reveals that when ALG3 activity is strongly reduced, almost all N-glycans transferred to proteins are aberrant, indicating that the Arabidopsis oligosaccharide transferase complex is remarkably substrate tolerant.	Polysaccharides	2-8	asparagine-linked glycosylation 3	Arabidopsis thaliana	32-36	
18567790-5	2008	N-glycan analysis of alg3-2 and alg3-2 in the complex-glycan-less mutant background, which lacks N-acetylglucosaminyl-transferase I activity, reveals that when ALG3 activity is strongly reduced, almost all N-glycans transferred to proteins are aberrant, indicating that the Arabidopsis oligosaccharide transferase complex is remarkably substrate tolerant.	Polysaccharides	2-8	asparagine-linked glycosylation 3	Arabidopsis thaliana	160-164	
18567790-6	2008	In alg3-2 plants, the aberrant glycans on glycoproteins are recognized by endogenous mannosidase I and N-acetylglucosaminyltransferase I and efficiently processed into complex-type glycans.	Polysaccharides	31-38	asparagine-linked glycosylation 3	Arabidopsis thaliana	3-7	
18567790-6	2008	In alg3-2 plants, the aberrant glycans on glycoproteins are recognized by endogenous mannosidase I and N-acetylglucosaminyltransferase I and efficiently processed into complex-type glycans.	Polysaccharides	181-188	asparagine-linked glycosylation 3	Arabidopsis thaliana	3-7