PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8513978-1	1993	Two N-linked sites of glycosylation in the insulin receptor were examined for their contribution to insulin binding, tyrosine kinase activity, and receptor biosynthesis.	Nitrogen	4-5	insulin receptor	Homo sapiens	43-59	
21880708-4	2011	All N-methylated analogues showed impaired binding affinities to IR, which suggests a direct IR-interacting role for the respective amide hydrogens.	Nitrogen	4-5	insulin receptor	Homo sapiens	65-67	
21880708-4	2011	All N-methylated analogues showed impaired binding affinities to IR, which suggests a direct IR-interacting role for the respective amide hydrogens.	Nitrogen	4-5	insulin receptor	Homo sapiens	93-95	
17957771-1	2008	The human insulin receptor (IR) homodimer is heavily glycosylated and contains a total of 19 predicted N-linked glycosylation sites in each monomer.	Nitrogen	103-104	insulin receptor	Homo sapiens	10-26	
11118640-2	2000	To further explore the effect of aberrant (rather than absent) N-linked glycosylation of the insulin receptor, we examined the relationship of processing to function.	Nitrogen	63-64	insulin receptor	Homo sapiens	93-109	
10769182-0	2000	Mutational analysis of the N-linked glycosylation sites of the human insulin receptor.	Nitrogen	27-28	insulin receptor	Homo sapiens	69-85	
8027066-0	1994	The functions of the human insulin receptor are affected in different ways by mutation of each of the four N-glycosylation sites in the beta subunit.	Nitrogen	107-108	insulin receptor	Homo sapiens	27-43	
6346428-4	1983	Biosynthetic studies showing the incorporation of all four labeled monosaccharides (fucose, mannose, galactose and glucosamine) into the two major subunits of the insulin receptor suggested that both subunits were likely to contain carbohydrate chains of the complex, N-linked type.	Nitrogen	268-269	insulin receptor	Homo sapiens	163-179	
35450409-3	2022	In addition to the direct association between I-R and the release of reactive oxygen species and reactive nitrogen species, it is involved in developing mitochondrial oxidative damage.	Nitrogen	106-114	insulin receptor	Homo sapiens	46-49	
33316063-10	2021	Besides, INSR protein as an insulin receptor precursor showed a high potential site for posttranslation modifications, including phosphorylation and N-glycosylation.	Nitrogen	10-11	insulin receptor	Homo sapiens	28-44