Reid ME. Some concepts relating to the molecular genetic basis of certain MNS blood group antigens. Transf Med 1994;4:99–111.10.1111/j.1365-3148.1994.tb00250.x7921055
Huang C-H, Blumenfeld OO. MNSs blood groups and major glycophorins: molecular basis for allelic variation. In: Cartron J-P, Rouger P, eds. Molecular basis of human blood group antigens. New York: Plenum Press, 1995;153-88.
Blumenfeld OO, Huang C-H. Molecular genetics of the glycophorin gene family. The antigens for MNSs blood groups; multiple gene rearrangements and modulation of splice site usage result in extensive diversification. Hum Mutation 1995;6:199–209.10.1002/humu.13800603028535438
Daniels GL, Anstee DJ, Cartron J-P, et al. Blood group terminology 1995. ISBT working party on terminology for red cell surface antigens. Vox Sang 1995;69:265–79.
Daniels G, Flegel WA, Fletcher A, et al. International Society of Blood Transfusion committee on terminology for red cell surface antigens: Cape Town report. Vox Sang 2007;92:250–3.10.1111/j.1423-0410.2007.00887.x17348875
Chasis JA, Mohandas N, Shohet SB. Erythrocyte membrane rigidity induced by glycophorin A-ligand interaction. Evidence for a ligand-induced association between glycophorin A and skeletal proteins. J Clin Invest 1985;75:1919–26.10.1172/JCI1119074255494008645
Lublin DM. Functional roles of blood group antigens. In: Silberstein LE, ed. Molecular and functional aspects of blood group antigens. Bethesda, MD: American Association of Blood Banks, 1995;163-92.
Cartron J-P, Prou O, Luilier M, Soulier JP. Susceptibility to invasion by Plasmodium falciparum of some human erythrocytes carrying rare blood group antigens. Br J Haematol 1983;55:639–47.10.1111/j.1365-2141.1983.tb02846.x6200133
Pasvol G, Chasis JA, Mohandas N, et al. Inhibition of malarial parasite invasion by monoclonal antibodies against glycophorin A correlates with reduction in red cell membrane deformability. Blood 1989;74:1836–43.10.1182/blood.V74.5.1836.1836
Hadley TJ. Invasion of erythrocytes by malaria parasites: a cellular and molecular overview. Annu Rev Microbiol 1986;40:451–77.10.1146/annurev.mi.40.100186.0023153535649
Groves JD, Tanner MJ. Glycophorin A facilitates the expression of human band 3-mediated anion transport in Xenopus oocytes. J Biol Chem 1992;267:22163–70.10.1016/S0021-9258(18)41649-3
Groves JD, Tanner MJ. The effects of glycophorin A on the expression of the human red cell anion transporter (band 3) in Xenopus oocytes. J Membr Biol 1994;140:81–8.
Rahuel C, London J, Vignal A, et al. Erythrocyte glycophorin B deficiency may occur by two distinct gene alterations. Am J Hematol 1991;37:57–8.10.1002/ajh.2830370115
Huang C-H, Reid ME, Blumenfeld OO. Remodeling of the transmembrane segment in human glycophorin by aberrant RNA splicing. J Biol Chem 1994;269:10804–12.10.1016/S0021-9258(17)34131-5
Maizels N. Might gene conversion be the mechanism of somatic hypermutation of mammalian immunoglobulin genes? Trends Genet 1989;5:4–8.10.1016/0168-9525(89)90004-8
Dahr W, Knuppertz G, Beyreuther K, et al. Studies on the structures of the Tm, Sj, M1, Can, Sext and Hu blood group antigens. Biol Chem Hoppe-Seyler 1991;372:573–84.10.1515/bchm3.1991.372.2.5731958316
Morel PA, Bergren MO, Hill V, et al. M and N specific hemagglutinins of human erythrocytes stored in glucose solutions. Transfusion 1981;21:652–62.10.1046/j.1537-2995.1981.21682085751.x6171920
Reid ME, Ellisor SS, Barker JM, et al. Characteristics of an antibody causing agglutination of M-positive nonenzymatically glycosylated human red cells. Vox Sang 1981;41:85–90.10.1111/j.1423-0410.1981.tb01019.x7331284
Drzeniek Z, Kusnierz G, Lisowska E. A human antiserum reacting with modified blood group M determinants. Immunol Invest 1981;10:185–97.10.3109/088201381090506966169632
Fassbinder W, Seidl S, Koch KM. The role of formaldehyde in the formation of haemodialysis-associated anti-N-like antibodies. Vox Sang 1978;35:41–8.10.1111/j.1423-0410.1978.tb02899.x566486
Lynen R, Rothe M, Gallasch E. Characterization of formaldehyde-related antibodies encountered in hemodialysis patients at different stages of immunization. Vox Sang 1983;44:81–9.10.1111/j.1423-0410.1983.tb04106.x6402858
Furuhjelm U, Nevanlinna HR, Pirkola A. A second Finnish En(a-) propositus with anti-Ena. Vox Sang 1973;24:545–9.10.1111/j.1423-0410.1973.tb03498.x4722837
Postoway N, Anstee DJ, Wortman M, Garratty G. A severe transfusion reaction associated with anti-EnaTS in a patient with an abnormal alpha-like red cell sialoglycoprotein. Transfusion 1988;28:77–80.10.1046/j.1537-2995.1988.28188127961.x3341073
Garratty G, Arndt P, Domen R, et al. Severe autoimmune hemolytic anemia associated with IgM warm autoantibodies directed against determinants on or associated with glycophorin A. Vox Sang 1997;72:124–30.10.1046/j.1423-0410.1997.7220124.x9088083
Jensen RH, Reynolds JC, Robbins J, et al. Glycophorin A as a biological dosimeter for radiation dose to the bone marrow from iodine-131. Radiat Res 1997;147:747–52.10.2307/3579490
Jensen RH, Langlois RG, Bigbee WL, et al. Elevated frequency of glycophorin A mutations in erythrocytes from Chernobyl accident victims. Radiat Res 1995;141:129–35.10.2307/3579040
Langlois RG, Bigbee WL, Jensen RH, German J. Evidence for increased in vivo mutation and somatic recombination in Bloom’s syndrome. Proc Natl Acad Sci U S A 1989;86:670–4.10.1073/pnas.86.2.6702865352911598
Langlois RG, Bigbee WL, Kyoizumi S, et al. Evidence for increased somatic cell mutations at the glycophorin A locus in atomic bomb survivors. Science 1987;236:445–8.10.1126/science.35635203563520