PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
32298669-5	2020	MALDI-MS was used for N-glycan analysis of IgA1 samples.	n-glycan	22-30	immunoglobulin heavy constant alpha 1	Homo sapiens	43-47	
27302155-8	2016	Pregnancy associated changes of N-glycan bisection were different for IgA1 as compared to IgG-Fc described earlier.	n-glycan	32-40	immunoglobulin heavy constant alpha 1	Homo sapiens	70-74	
20431350-0	2010	Differences in N-glycan structures found on recombinant IgA1 and IgA2 produced in murine myeloma and CHO cell lines.	n-glycan	15-23	immunoglobulin heavy constant alpha 1	Homo sapiens	56-60	
18264945-0	2008	Similarities between N-glycan glycoform of tonsillar IgA1 and that of aberrant IgA1 abundant in IgA nephropathy patient serum.	n-glycan	21-29	immunoglobulin heavy constant alpha 1	Homo sapiens	53-57	
18264945-4	2008	Therefore, analyses of the N-glycan glycoform on serum IgA1, aberrant IgA1 and tonsillar IgA1 were carried out using the 3-dimensional mapping method.	n-glycan	27-35	immunoglobulin heavy constant alpha 1	Homo sapiens	55-59	
18264945-4	2008	Therefore, analyses of the N-glycan glycoform on serum IgA1, aberrant IgA1 and tonsillar IgA1 were carried out using the 3-dimensional mapping method.	n-glycan	27-35	immunoglobulin heavy constant alpha 1	Homo sapiens	70-74	
18264945-4	2008	Therefore, analyses of the N-glycan glycoform on serum IgA1, aberrant IgA1 and tonsillar IgA1 were carried out using the 3-dimensional mapping method.	n-glycan	27-35	immunoglobulin heavy constant alpha 1	Homo sapiens	70-74	
18264945-7	2008	The neutral complex-type N-glycan chain with fucose was higher in both the aberrant IgA1 and tonsillar IgA1 than in the serum IgA1.	n-glycan	25-33	immunoglobulin heavy constant alpha 1	Homo sapiens	84-88	
18264945-7	2008	The neutral complex-type N-glycan chain with fucose was higher in both the aberrant IgA1 and tonsillar IgA1 than in the serum IgA1.	n-glycan	25-33	immunoglobulin heavy constant alpha 1	Homo sapiens	103-107	
18264945-7	2008	The neutral complex-type N-glycan chain with fucose was higher in both the aberrant IgA1 and tonsillar IgA1 than in the serum IgA1.	n-glycan	25-33	immunoglobulin heavy constant alpha 1	Homo sapiens	103-107	
10211705-2	1998	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.	n-glycan	189-197	immunoglobulin heavy constant alpha 1	Homo sapiens	85-89	
31362986-2	2019	Little is known about the impact of N-glycan modifications of IgA1 and IgA2 on binding to the Fcalpha receptor (FcalphaRI), which is also heavily glycosylated at its extracellular domain.	n-glycan	36-44	immunoglobulin heavy constant alpha 1	Homo sapiens	62-66	
18826328-4	2008	Analytical ultracentrifugation revealed wide variation in the distribution of polymeric species between IgA1 samples, and Fourier transform ion cyclotron resonance mass spectrometry showed overlapping but distinct populations of N-glycan species between IgA1 samples.	n-glycan	229-237	immunoglobulin heavy constant alpha 1	Homo sapiens	254-258