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Gene Information

Gene symbol: GYPA

Gene name: glycophorin A (MNS blood group)

HGNC ID: 4702

Synonyms: GPA, MN, CD235a

Related Genes

# Gene Symbol Number of hits
1 ABO 1 hits
2 GYPB 1 hits
3 NEU1 1 hits

Related Sentences

# PMID Sentence
1 814753 [Connection between the group factors of the blood systems ABO, MNSs, and rhesus and peculiarities of the vaccination process in children immunized against smallpox].
2 814753 The ahthors present new data on the character of the vaccine process in children associated with the characteristics of the blood group ABO, MNSs and Rh systems.
3 814753 [Connection between the group factors of the blood systems ABO, MNSs, and rhesus and peculiarities of the vaccination process in children immunized against smallpox].
4 814753 The ahthors present new data on the character of the vaccine process in children associated with the characteristics of the blood group ABO, MNSs and Rh systems.
5 8009226 Region II, which contains a cysteine-rich motif, and native EBA-175 bind specifically to glycophorin A, but not to glycophorin B, on the erythrocyte membrane.
6 9584138 Using nulls lacking glycophorin A [En(a-)], glycophorin B (S-s-U-) or a combination of glycophorin A and B (Mk/Mk) we showed that erythrocytes lacking glycophorin B retain the ability to bind but a lack of glycophorin A reduced adherence by exflagellating microgametes.
7 9712768 The peptide, EBA(aa1076-96), also bound to desialylated glycophorin A and glycophorin B when tested by ELISA.
8 10531229 Of the 15 field isolates tested, 5 multiply in both neuraminidase and trypsin-treated erythrocytes, 3 multiply in neuraminidase-treated but not trypsin-treated erythrocytes, and 4 multiply in trypsin-treated but not neuraminidase-treated erythrocytes; 12 of the 15 field isolates tested use alternate invasion pathways that are not dependent on sialic acid residues of glycophorin A.
9 18063920 Glycophorin B, the next in terms of amount, can take on the role of glycophorin A as the receptor, but the glycophorin B- and sialic acid-dependent invasion of erythrocytes by Plasmodium falciparum involves a different parasite ligand.