PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15313217-4	2004	Structural studies based on nanoflow electrospray-ionization tandem mass spectrometry and earlier reported data on the carbohydrate moiety of GPA and ABH antigens allowed us to conclude that these blood group epitopes are elongations of the beta-GlcNAc branch attached to C-6 of the reducing GalNAc.	N-acetylgalactosaminuronic acid	292-298	glycophorin A (MNS blood group)	Homo sapiens	142-145	
9136905-0	1997	Blood group MN-dependent difference in degree of galactosylation of O-glycans of glycophorin A is restricted to the GalNAc residues located on amino acid residues 2-4 of the glycophorin polypeptide chain.	N-acetylgalactosaminuronic acid	116-122	glycophorin A (MNS blood group)	Homo sapiens	81-94	
9136905-1	1997	Glycophorin A (GPA) of human erythrocytes contains a minor number of unsubstituted GalNAc residues (Tn receptors) which are recognized by Moluccella laevis lectin (MLL).	N-acetylgalactosaminuronic acid	83-89	glycophorin A (MNS blood group)	Homo sapiens	0-19	
9136905-4	1997	The asialoglycopeptides 1-39 and 1-8 derived from GPA-N showed about 2 and 4 times higher content of non-galactosylated GalNAc residues, respectively, and higher reactivity with MLL than their counterparts derived from GPA-M, while asialoglycopeptides 9-39 of GPA-M and GPA-N did not show such differences.	N-acetylgalactosaminuronic acid	120-126	glycophorin A (MNS blood group)	Homo sapiens	50-53	
9136905-5	1997	These results demonstrate that higher expression of non-galactosylated GalNAc in GPA-N than in GPA-M is confined to GalNAc residues located in the amino-terminal portion of GPA polypeptide chain, between the blood group M- and N-specific amino acid residues 1 and 5.	N-acetylgalactosaminuronic acid	71-77	glycophorin A (MNS blood group)	Homo sapiens	81-84	
9136905-5	1997	These results demonstrate that higher expression of non-galactosylated GalNAc in GPA-N than in GPA-M is confined to GalNAc residues located in the amino-terminal portion of GPA polypeptide chain, between the blood group M- and N-specific amino acid residues 1 and 5.	N-acetylgalactosaminuronic acid	71-77	glycophorin A (MNS blood group)	Homo sapiens	95-98	
9136905-5	1997	These results demonstrate that higher expression of non-galactosylated GalNAc in GPA-N than in GPA-M is confined to GalNAc residues located in the amino-terminal portion of GPA polypeptide chain, between the blood group M- and N-specific amino acid residues 1 and 5.	N-acetylgalactosaminuronic acid	71-77	glycophorin A (MNS blood group)	Homo sapiens	95-98	
9136905-5	1997	These results demonstrate that higher expression of non-galactosylated GalNAc in GPA-N than in GPA-M is confined to GalNAc residues located in the amino-terminal portion of GPA polypeptide chain, between the blood group M- and N-specific amino acid residues 1 and 5.	N-acetylgalactosaminuronic acid	116-122	glycophorin A (MNS blood group)	Homo sapiens	81-84	
9136905-5	1997	These results demonstrate that higher expression of non-galactosylated GalNAc in GPA-N than in GPA-M is confined to GalNAc residues located in the amino-terminal portion of GPA polypeptide chain, between the blood group M- and N-specific amino acid residues 1 and 5.	N-acetylgalactosaminuronic acid	116-122	glycophorin A (MNS blood group)	Homo sapiens	95-98	
9136905-5	1997	These results demonstrate that higher expression of non-galactosylated GalNAc in GPA-N than in GPA-M is confined to GalNAc residues located in the amino-terminal portion of GPA polypeptide chain, between the blood group M- and N-specific amino acid residues 1 and 5.	N-acetylgalactosaminuronic acid	116-122	glycophorin A (MNS blood group)	Homo sapiens	95-98	
6195088-0	1983	Immunochemistry of O-glycosidically-linked Gal(beta 1 leads to 3) GalNAc on fragments of human glycophorin A.	N-acetylgalactosaminuronic acid	66-72	glycophorin A (MNS blood group)	Homo sapiens	95-108	
8598452-9	1996	When N-terminal octapeptides from human glycophorin A that bore NeuAc alpha 2-3 Gal beta 1-3 (NeuAc alpha 2-6) GalNAc and its sequentially deglycosylated derivatives were compared, glycopeptides carrying three constitutive GalNAc-Ser/Thr (Tn Ag) strongly bound to the recombinant human macrophage lectin.	N-acetylgalactosaminuronic acid	111-117	glycophorin A (MNS blood group)	Homo sapiens	40-53	
2167157-4	1990	Beside gangliosides, both antibodies recognized the carbohydrate determinant carried by glycophorin A on very rare Cad-positive human RBC; the structure of which is GalNAc beta 1----4(NeuAc alpha 2----3)Gal beta 1----3(NeuAc alpha 2---- 6)GalNAc alpha 1----Ser/Thr.	N-acetylgalactosaminuronic acid	165-171	glycophorin A (MNS blood group)	Homo sapiens	88-101	
2167157-4	1990	Beside gangliosides, both antibodies recognized the carbohydrate determinant carried by glycophorin A on very rare Cad-positive human RBC; the structure of which is GalNAc beta 1----4(NeuAc alpha 2----3)Gal beta 1----3(NeuAc alpha 2---- 6)GalNAc alpha 1----Ser/Thr.	N-acetylgalactosaminuronic acid	239-245	glycophorin A (MNS blood group)	Homo sapiens	88-101