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Hellberg Å, Westman JS, Thuresson B, Olsson ML. P1PK: the blood group system that changed its name and expanded. Immunohematology 2013;29:25–33.HellbergÅWestmanJSThuressonBOlssonML.P1PK: the blood group system that changed its name and expanded.Immunohematology2013;29:25–33.10.21307/immunohematology-2019-120Search in Google Scholar
Veldhuisen B, van der Schoot CE, de Haas M. Blood group genotyping: from patient to high-throughput donor screening. Vox Sang 2009;97:198–206.VeldhuisenBvan der SchootCEde HaasM.Blood group genotyping: from patient to high-throughput donor screening.Vox Sang2009;97:198–206.10.1111/j.1423-0410.2009.01209.xSearch in Google Scholar
Bezirgiannidou Z, Christoforidou A, Kontekaki E, et al. Hyperhemolytic syndrome complicating a delayed hemolytic transfusion reaction due to anti-P1 alloimmunization, in a pregnant woman with HbO-Arab/ß-thalassemia. Mediterr J Hematol Infect Dis 2016;8:e2016053.BezirgiannidouZChristoforidouAKontekakiE,Hyperhemolytic syndrome complicating a delayed hemolytic transfusion reaction due to anti-P1 alloimmunization, in a pregnant woman with HbO-Arab/ß-thalassemia.Mediterr J Hematol Infect Dis2016;8:e2016053.10.4084/mjhid.2016.053Search in Google Scholar
Smith D, Aye T, Er LS, Nester T, Delaney M. Acute hemolytic transfusion reaction due to anti-P1: a case report and review of institutional experience. Transfus Med Hemother 2019;46:381–4.SmithDAyeTErLSNesterTDelaneyM.Acute hemolytic transfusion reaction due to anti-P1: a case report and review of institutional experience.Transfus Med Hemother2019;46:381–4.10.1159/000490897Search in Google Scholar
Kaczmarek R, Duk M, Szymczak K, et al. Human Gb3/CD77 synthase reveals specificity toward two or four different acceptors depending on amino acid at position 211, creating P(k), P1 and NOR blood group antigens. Biochem Biophys Res Comm 2016;470:168–74.KaczmarekRDukMSzymczakK,Human Gb3/CD77 synthase reveals specificity toward two or four different acceptors depending on amino acid at position 211, creating P(k), P1 and NOR blood group antigens.Biochem Biophys Res Comm2016;470:168–74.10.1016/j.bbrc.2016.01.017Search in Google Scholar
Haselberger SG, Schenkel-Brunner H. Evidence for erythrocyte membrane glycoproteins being carriers of blood-group P1 determinants. FEBS Lett 1982;149:126–8.HaselbergerSGSchenkel-BrunnerH.Evidence for erythrocyte membrane glycoproteins being carriers of blood-group P1 determinants.FEBS Lett1982;149:126–8.10.1016/0014-5793(82)81086-7Search in Google Scholar
Yang Z, Bergström J, Karlsson K-A. Glycoproteins with Galalpha4Gal are absent from human erythrocyte membranes, indicating that glycolipids are the sole carriers of blood group P activities. J Biol Chem 1994;269:14620–4.YangZBergströmJKarlssonK-A.Glycoproteins with Galalpha4Gal are absent from human erythrocyte membranes, indicating that glycolipids are the sole carriers of blood group P activities.J Biol Chem1994;269:14620–4.10.1016/S0021-9258(17)36669-3Search in Google Scholar
Stenfelt L, Westman JS, Hellberg A, Olsson ML. The P1 histo-blood group antigen is present on human red blood cell glycoproteins. Transfusion 2019;59:1108–17.StenfeltLWestmanJSHellbergAOlssonML.The P1 histo-blood group antigen is present on human red blood cell glycoproteins.Transfusion2019;59:1108–17.10.1111/trf.1511530597575Search in Google Scholar
Szymczak-Kulus K, Weidler S, Bereznicka A, et al. Novel bisgalactosylated type of N-glycans as decoy receptors for Shiga toxin? Glycoconj J 2019;36:369.Szymczak-KulusKWeidlerSBereznickaA,Novel bisgalactosylated type of N-glycans as decoy receptors for Shiga toxin?Glycoconj J2019;36:369.Search in Google Scholar
Tsering D, Chen C, Ye J, et al. Enzymatic synthesis of human blood group P1 pentasaccharide antigen. Carbohydr Res 2017;438:39–43.TseringDChenCYeJ,Enzymatic synthesis of human blood group P1 pentasaccharide antigen.Carbohydr Res2017;438:39–43.10.1016/j.carres.2016.11.01927960098Search in Google Scholar
Jacob F, Alam S, Konantz M, et al. Transition of mesenchymal and epithelial cancer cells depends on alpha1-4 galactosyltransferase-mediated glycosphingolipids. Cancer Res 2018;78:2952–65.JacobFAlamSKonantzM,Transition of mesenchymal and epithelial cancer cells depends on alpha1-4 galactosyltransferase-mediated glycosphingolipids.Cancer Res2018;78:2952–65.10.1158/0008-5472.CAN-17-222329572228Search in Google Scholar
Breton C, Snajdrova L, Jeanneau C, Koca J, Imberty A. Structures and mechanisms of glycosyltransferases. Glycobiology 2006;16:29R–37R.BretonCSnajdrovaLJeanneauCKocaJImbertyA.Structures and mechanisms of glycosyltransferases.Glycobiology2006;16:29R–37R.10.1093/glycob/cwj01616037492Search in Google Scholar
Pacheco AR, Lazarus JE, Sit B, et al. CRISPR screen reveals that EHEC’s T3SS and shiga toxin rely on shared host factors for infection. MBio 2018;9:e011003–18.PachecoARLazarusJESitB,CRISPR screen reveals that EHEC’s T3SS and shiga toxin rely on shared host factors for infection.MBio2018;9:e011003–18.10.1128/mBio.01003-18601624329921669Search in Google Scholar
Tian S, Muneeruddin K, Choi MY, et al. Genome-wide CRISPR screens for Shiga toxins and ricin reveal Golgi proteins critical for glycosylation. PLoS Biol 2018;16:e2006951.TianSMuneeruddinKChoiMY,Genome-wide CRISPR screens for Shiga toxins and ricin reveal Golgi proteins critical for glycosylation.PLoS Biol2018;16:e2006951.10.1371/journal.pbio.2006951625847230481169Search in Google Scholar
Yamaji T, Sekizuka T, Tachida Y, et al. A CRISPR screen identifies LAPTM4A and TM9SF proteins as glycolipid-regulating factors. iScience 2019;11:409–24.YamajiTSekizukaTTachidaY,A CRISPR screen identifies LAPTM4A and TM9SF proteins as glycolipid-regulating factors.iScience2019;11:409–24.10.1016/j.isci.2018.12.039634830330660999Search in Google Scholar
Cabrita MA, Hobman TC, Hogue DL, King KM, Cass CE. Mouse transporter protein, a membrane protein that regulates cellular multidrug resistance, is localized to lysosomes. Cancer Res 1999;59:4890–7.CabritaMAHobmanTCHogueDLKingKMCassCE.Mouse transporter protein, a membrane protein that regulates cellular multidrug resistance, is localized to lysosomes.Cancer Res1999;59:4890–7.Search in Google Scholar
Möller M, Jöud M, Storry JR, Olsson ML. Erythrogene: a database for in-depth analysis of the extensive variation in 36 blood group systems in the 1000 Genomes Project. Blood Adv 2016;1:240–9.MöllerMJöudMStorryJROlssonML.Erythrogene: a database for in-depth analysis of the extensive variation in 36 blood group systems in the 1000 Genomes Project.Blood Adv2016;1:240–9.10.1182/bloodadvances.2016001867573716829296939Search in Google Scholar
Shastry S, Satyamoorthy K, Acharya KV, et al. Deletion in the A4GALT gene associated with rare “P null” phenotype: the first report from India. Transfus Med Hemother 2020;47:186–9.ShastrySSatyamoorthyKAcharyaKV,Deletion in the A4GALT gene associated with rare “P null” phenotype: the first report from India.Transfus Med Hemother2020;47:186–9.10.1159/000501916718482532355479Search in Google Scholar
Tilley L, McNeill A, Baglow L, et al. Two novel A4GALT null alleles detected in patients with the p phenotype (abstract). Br Blood Transfus Soc Ann Conf 2019;127.TilleyLMcNeillABaglowL,Two novel A4GALT null alleles detected in patients with the p phenotype (abstract).Br Blood Transfus Soc Ann Conf2019;127.Search in Google Scholar
Westman JS, Hellberg Å, Peyrard T, Thuresson B, Olsson ML. Large deletions involving the regulatory upstream regions of A4GALT give rise to principally novel P1PK-null alleles. Transfusion 2014;54:1831–5.WestmanJSHellberg Å, PeyrardTThuressonBOlssonML.Large deletions involving the regulatory upstream regions of A4GALT give rise to principally novel P1PK-null alleles.Transfusion2014;54:1831–5.10.1111/trf.1254324417201Search in Google Scholar
Thuresson B, Westman JS, Olsson ML. Identification of a novel A4GALT exon reveals the genetic basis of the P1/P2 histo-blood groups. Blood 2011;117:678–87.ThuressonBWestmanJSOlssonML.Identification of a novel A4GALT exon reveals the genetic basis of the P1/P2 histo-blood groups.Blood2011;117:678–87.10.1182/blood-2010-08-30133320971946Search in Google Scholar
Lai YJ, Wu WY, Yang CM, et al. A systematic study of single-nucleotide polymorphisms in the A4GALT gene suggests a molecular genetic basis for the P1/P2 blood groups. Transfusion 2014;54:3222–31.LaiYJWuWYYangCM,A systematic study of single-nucleotide polymorphisms in the A4GALT gene suggests a molecular genetic basis for the P1/P2 blood groups.Transfusion2014;54:3222–31.10.1111/trf.1277125041587Search in Google Scholar
Iwamura K, Furukawa K, Uchikawa M, et al. The blood group P1 synthase gene is identical to the Gb3/CD77 synthase gene: a clue to the solution of the P1/P2/p puzzle. J Biol Chem 2003;278:44429–38.IwamuraKFurukawaKUchikawaM,The blood group P1 synthase gene is identical to the Gb3/CD77 synthase gene: a clue to the solution of the P1/P2/p puzzle.J Biol Chem2003;278:44429–38.10.1074/jbc.M30160920012888565Search in Google Scholar
Eernstman J, Veldhuisen B, Heshusius S, et al. KLF1 regulates P1 expression through transcriptional control of A4GALT. Vox Sang 2017;112:25(3B-S06-2).EernstmanJVeldhuisenBHeshusiusS,KLF1 regulates P1 expression through transcriptional control of A4GALT.Vox Sang2017;112:25(3B-S06-2).Search in Google Scholar
Singleton BK, Burton NM, Green C, Brady RL, Anstee DJ. Mutations in EKLF/KLF1 form the molecular basis of the rare blood group In(Lu) phenotype. Blood 2008;112:2081–8.SingletonBKBurtonNMGreenCBradyRLAnsteeDJ.Mutations in EKLF/KLF1 form the molecular basis of the rare blood group In(Lu) phenotype.Blood2008;112:2081–8.10.1182/blood-2008-03-14567218487511Search in Google Scholar
Kawai M, Obara K, Onodera T, et al. Mutations of the KLF1 gene detected in Japanese with the In(Lu) phenotype. Transfusion 2017;57:1072–7.KawaiMObaraKOnoderaT,Mutations of the KLF1 gene detected in Japanese with the In(Lu) phenotype.Transfusion2017;57:1072–7.10.1111/trf.1399028194794Search in Google Scholar
Westman JS, Stenfelt L, Vidovic K, et al. Allele-selective RUNX1 binding regulates P1 blood group status by transcriptional control of A4GALT. Blood 2018;131:1611–6.WestmanJSStenfeltLVidovicK,Allele-selective RUNX1 binding regulates P1 blood group status by transcriptional control of A4GALT.Blood2018;131:1611–6.10.1182/blood-2017-08-80308029438961Search in Google Scholar
Yeh CC, Chang CJ, Twu YC, et al. The differential expression of the blood group P(1)-A4GALT and P(2)-A4GALT alleles is stimulated by the transcription factor early growth response 1. Transfusion 2018;58:1054–64.YehCCChangCJTwuYC,The differential expression of the blood group P(1)-A4GALT and P(2)-A4GALT alleles is stimulated by the transcription factor early growth response 1.Transfusion2018;58:1054–64.10.1111/trf.1451529399809Search in Google Scholar
Kaczmarek R, Szymczak-Kulus K, Bereznicka A, et al. Single nucleotide polymorphisms in A4GALT spur extra products of the human Gb3/CD77 synthase and underlie the P1PK blood group system. PLoS One 2018;13:e0196627.KaczmarekRSzymczak-KulusKBereznickaA,Single nucleotide polymorphisms in A4GALT spur extra products of the human Gb3/CD77 synthase and underlie the P1PK blood group system.PLoS One2018;13:e0196627.10.1371/journal.pone.0196627592744429709005Search in Google Scholar
Levine P. Illegitimate blood group antigens P1, A, and MN (T) in malignancy—a possible therapeutic approach with anti-Tja, anti-A, and anti-T. Ann N Y Acad Sci 1976;277:428–35.LevineP.Illegitimate blood group antigens P1, A, and MN (T) in malignancy—a possible therapeutic approach with anti-Tja, anti-A, and anti-T.Ann N Y Acad Sci1976;277:428–35.10.1111/j.1749-6632.1976.tb41719.x793484Search in Google Scholar
Jacob F, Goldstein DR, Bovin NV, et al. Serum antiglycan antibody detection of nonmucinous ovarian cancers by using a printed glycan array. Int J Cancer 2012;130:138–46.JacobFGoldsteinDRBovinNV,Serum antiglycan antibody detection of nonmucinous ovarian cancers by using a printed glycan array.Int J Cancer2012;130:138–46.10.1002/ijc.26002313766721351089Search in Google Scholar
Jacob F, Anugraham M, Pochechueva T, et al. The glycosphingolipid P(1) is an ovarian cancer-associated carbohydrate antigen involved in migration. Br J Cancer 2014;111:1634–45.JacobFAnugrahamMPochechuevaT,The glycosphingolipid P(1) is an ovarian cancer-associated carbohydrate antigen involved in migration.Br J Cancer2014;111:1634–45.10.1038/bjc.2014.455420009525167227Search in Google Scholar
Puri A, Rawat SS, Lin HM, et al. An inhibitor of glycosphingolipid metabolism blocks HIV-1 infection of primary T-cells. AIDS 2004;18:849–58.PuriARawatSSLinHM,An inhibitor of glycosphingolipid metabolism blocks HIV-1 infection of primary T-cells.AIDS2004;18:849–58.10.1097/00002030-200404090-0000215060432Search in Google Scholar
Hammache D, Yahi N, Maresca M, Pieroni G, Fantini J. Human erythrocyte glycosphingolipids as alternative cofactors for human immunodeficiency virus type 1 (HIV-1) entry: evidence for CD4-induced interactions between HIV-1 gp120 and reconstituted membrane microdomains of glycosphingolipids (Gb3 and GM3). J Virol 1999;73:5244–8.HammacheDYahiNMarescaMPieroniGFantiniJ.Human erythrocyte glycosphingolipids as alternative cofactors for human immunodeficiency virus type 1 (HIV-1) entry: evidence for CD4-induced interactions between HIV-1 gp120 and reconstituted membrane microdomains of glycosphingolipids (Gb3 and GM3).J Virol1999;73:5244–8.10.1128/JVI.73.6.5244-5248.199911257810233996Search in Google Scholar
Lund N, Olsson ML, Ramkumar S, et al. The human P(k) histo-blood group antigen provides protection against HIV-1 infection. Blood 2009;113:4980–91.LundNOlssonMLRamkumarS,The human P(k) histo-blood group antigen provides protection against HIV-1 infection.Blood2009;113:4980–91.10.1182/blood-2008-03-14339619139081Search in Google Scholar
Motswaledi MS, Kasvosve I, Oguntibeju OO. Blood group antigens C, Lub and P1 may have a role in HIV infection in Africans. PLoS One 2016;11:e0149883.MotswalediMSKasvosveIOguntibejuOO.Blood group antigens C, Lub and P1 may have a role in HIV infection in Africans.PLoS One2016;11:e0149883.10.1371/journal.pone.0149883476429526900853Search in Google Scholar