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Volumn 27, Issue 4, 2013, Pages 167-178

Hereditary spherocytosis, elliptocytosis, and other red cell membrane disorders

Author keywords

Elliptocytosis; Hemolysis; Hereditary spherocytosis; Pyropoikilocytosis; Red cell membrane; Stomatocytosis

Indexed keywords

CELL MEMBRANE PROTEIN; SPECTRIN; ANKYRIN;

EID: 84881376528     PISSN: 0268960X     EISSN: 15321681     Source Type: Journal    
DOI: 10.1016/j.blre.2013.04.003     Document Type: Article
Times cited : (260)

References (145)
  • 1
    • 42049115740 scopus 로고    scopus 로고
    • Disorders of red cell membrane
    • An X., Mohandas N. Disorders of red cell membrane. Br J Haematol 2008, 141(3):367-375.
    • (2008) Br J Haematol , vol.141 , Issue.3 , pp. 367-375
    • An, X.1    Mohandas, N.2
  • 3
    • 45349107474 scopus 로고    scopus 로고
    • Red cell membrane disorders in pediatrics
    • Iolascon A., Piscopo C., Boschetto L. Red cell membrane disorders in pediatrics. Pediatr Ann 2008, 37(5):295-301.
    • (2008) Pediatr Ann , vol.37 , Issue.5 , pp. 295-301
    • Iolascon, A.1    Piscopo, C.2    Boschetto, L.3
  • 5
    • 58149158216 scopus 로고    scopus 로고
    • Red cell membrane: past, present, and future
    • Mohandas N., Gallagher P.G. Red cell membrane: past, present, and future. Blood 2008, 112(10):3939-3948.
    • (2008) Blood , vol.112 , Issue.10 , pp. 3939-3948
    • Mohandas, N.1    Gallagher, P.G.2
  • 6
    • 53749083690 scopus 로고    scopus 로고
    • Hereditary spherocytosis
    • Perrotta S., Gallagher P.G., Mohandas N. Hereditary spherocytosis. Lancet 2008, 372(9647):1411-1426.
    • (2008) Lancet , vol.372 , Issue.9647 , pp. 1411-1426
    • Perrotta, S.1    Gallagher, P.G.2    Mohandas, N.3
  • 7
    • 0025022555 scopus 로고
    • Recurrent acute splenic sequestration crisis due to interacting genetic defects: hemoglobin SC disease and hereditary spherocytosis
    • Warkentin T.E., Barr R.D., Ali M.A., Mohandas N. Recurrent acute splenic sequestration crisis due to interacting genetic defects: hemoglobin SC disease and hereditary spherocytosis. Blood 1990, 75(1):266-270.
    • (1990) Blood , vol.75 , Issue.1 , pp. 266-270
    • Warkentin, T.E.1    Barr, R.D.2    Ali, M.A.3    Mohandas, N.4
  • 8
    • 0026748544 scopus 로고
    • Splenic sequestration associated with sickle cell trait and hereditary spherocytosis
    • Yang Y.M., Donnell C., Wilborn W., Goodman S.R., Files B., Moore R.B., et al. Splenic sequestration associated with sickle cell trait and hereditary spherocytosis. Am J Hematol 1992, 40(2):110-116.
    • (1992) Am J Hematol , vol.40 , Issue.2 , pp. 110-116
    • Yang, Y.M.1    Donnell, C.2    Wilborn, W.3    Goodman, S.R.4    Files, B.5    Moore, R.B.6
  • 9
    • 11844299093 scopus 로고    scopus 로고
    • Phospholipid binding by proteins of the spectrin family: a comparative study
    • An X., Guo X., Gratzer W., Mohandas N. Phospholipid binding by proteins of the spectrin family: a comparative study. Biochem Biophys Res Commun 2005, 327(3):794-800.
    • (2005) Biochem Biophys Res Commun , vol.327 , Issue.3 , pp. 794-800
    • An, X.1    Guo, X.2    Gratzer, W.3    Mohandas, N.4
  • 10
    • 0345832247 scopus 로고    scopus 로고
    • Phosphatidylserine binding sites in erythroid spectrin: location and implications for membrane stability
    • An X., Guo X., Sum H., Morrow J., Gratzer W., Mohandas N. Phosphatidylserine binding sites in erythroid spectrin: location and implications for membrane stability. Biochemistry 2004, 43(2):310-315.
    • (2004) Biochemistry , vol.43 , Issue.2 , pp. 310-315
    • An, X.1    Guo, X.2    Sum, H.3    Morrow, J.4    Gratzer, W.5    Mohandas, N.6
  • 11
    • 33646478114 scopus 로고    scopus 로고
    • Phosphatidylinositol-4,5-biphosphate (PIP2) differentially regulates the interaction of human erythrocyte protein 4.1 (4.1R) with membrane proteins
    • An X., Zhang X., Debnath G., Baines A.J., Mohandas N. Phosphatidylinositol-4,5-biphosphate (PIP2) differentially regulates the interaction of human erythrocyte protein 4.1 (4.1R) with membrane proteins. Biochemistry 2006, 45(18):5725-5732.
    • (2006) Biochemistry , vol.45 , Issue.18 , pp. 5725-5732
    • An, X.1    Zhang, X.2    Debnath, G.3    Baines, A.J.4    Mohandas, N.5
  • 12
    • 77958563469 scopus 로고    scopus 로고
    • ATP-dependent mechanism protects spectrin against glycation in human erythrocytes
    • Manno S., Mohandas N., Takakuwa Y. ATP-dependent mechanism protects spectrin against glycation in human erythrocytes. J Biol Chem 2010, 285(44):33923-33929.
    • (2010) J Biol Chem , vol.285 , Issue.44 , pp. 33923-33929
    • Manno, S.1    Mohandas, N.2    Takakuwa, Y.3
  • 13
    • 0037133206 scopus 로고    scopus 로고
    • Identification of a functional role for lipid asymmetry in biological membranes: phosphatidylserine-skeletal protein interactions modulate membrane stability
    • Manno S., Takakuwa Y., Mohandas N. Identification of a functional role for lipid asymmetry in biological membranes: phosphatidylserine-skeletal protein interactions modulate membrane stability. Proc Natl Acad Sci U S A 2002, 99(4):1943-1948.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.4 , pp. 1943-1948
    • Manno, S.1    Takakuwa, Y.2    Mohandas, N.3
  • 14
    • 0026801368 scopus 로고
    • Red blood cell glycophorins
    • Chasis J.A., Mohandas N. Red blood cell glycophorins. Blood 1992, 80(8):1869-1879.
    • (1992) Blood , vol.80 , Issue.8 , pp. 1869-1879
    • Chasis, J.A.1    Mohandas, N.2
  • 15
    • 33646017711 scopus 로고    scopus 로고
    • New insights into function of red cell membrane proteins and their interaction with spectrin-based membrane skeleton
    • Mohandas N., An X. New insights into function of red cell membrane proteins and their interaction with spectrin-based membrane skeleton. Transfus Clin Biol 2006, 13(1-2):29-30.
    • (2006) Transfus Clin Biol , vol.13 , Issue.1-2 , pp. 29-30
    • Mohandas, N.1    An, X.2
  • 16
    • 1942509539 scopus 로고    scopus 로고
    • Red blood cell blood group antigens: structure and function
    • Reid M.E., Mohandas N. Red blood cell blood group antigens: structure and function. Semin Hematol 2004, 41(2):93-117.
    • (2004) Semin Hematol , vol.41 , Issue.2 , pp. 93-117
    • Reid, M.E.1    Mohandas, N.2
  • 17
    • 0037200093 scopus 로고    scopus 로고
    • Shear-response of the spectrin dimer-tetramer equilibrium in the red blood cell membrane
    • An X., Lecomte M.C., Chasis J.A., Mohandas N., Gratzer W. Shear-response of the spectrin dimer-tetramer equilibrium in the red blood cell membrane. J Biol Chem 2002, 277(35):31796-31800.
    • (2002) J Biol Chem , vol.277 , Issue.35 , pp. 31796-31800
    • An, X.1    Lecomte, M.C.2    Chasis, J.A.3    Mohandas, N.4    Gratzer, W.5
  • 18
    • 33846881356 scopus 로고    scopus 로고
    • Tropomyosin modulates erythrocyte membrane stability
    • An X., Salomao M., Guo X., Gratzer W., Mohandas N. Tropomyosin modulates erythrocyte membrane stability. Blood 2007, 109(3):1284-1288.
    • (2007) Blood , vol.109 , Issue.3 , pp. 1284-1288
    • An, X.1    Salomao, M.2    Guo, X.3    Gratzer, W.4    Mohandas, N.5
  • 19
    • 0021282226 scopus 로고
    • Rheological properties of antibody-coated red cells
    • Ballas S.K., Mohandas N., Clark M.R., Shohet S.B. Rheological properties of antibody-coated red cells. Transfusion 1984, 24(2):124-129.
    • (1984) Transfusion , vol.24 , Issue.2 , pp. 124-129
    • Ballas, S.K.1    Mohandas, N.2    Clark, M.R.3    Shohet, S.B.4
  • 20
    • 0026539641 scopus 로고
    • Molecular basis for red cell membrane viscoelastic properties
    • Mohandas N. Molecular basis for red cell membrane viscoelastic properties. Biochem Soc Trans 1992, 20(4):776-782.
    • (1992) Biochem Soc Trans , vol.20 , Issue.4 , pp. 776-782
    • Mohandas, N.1
  • 21
    • 0027272883 scopus 로고
    • Red blood cell deformability, membrane material properties and shape: regulation by transmembrane, skeletal and cytosolic proteins and lipids
    • Mohandas N., Chasis J.A. Red blood cell deformability, membrane material properties and shape: regulation by transmembrane, skeletal and cytosolic proteins and lipids. Semin Hematol 1993, 30(3):171-192.
    • (1993) Semin Hematol , vol.30 , Issue.3 , pp. 171-192
    • Mohandas, N.1    Chasis, J.A.2
  • 22
    • 0020790044 scopus 로고
    • The influence of membrane skeleton on red cell deformability, membrane material properties, and shape
    • Mohandas N., Chasis J.A., Shohet S.B. The influence of membrane skeleton on red cell deformability, membrane material properties, and shape. Semin Hematol 1983, 20(3):225-242.
    • (1983) Semin Hematol , vol.20 , Issue.3 , pp. 225-242
    • Mohandas, N.1    Chasis, J.A.2    Shohet, S.B.3
  • 23
    • 0028263839 scopus 로고
    • Mechanical properties of the red cell membrane in relation to molecular structure and genetic defects
    • Mohandas N., Evans E. Mechanical properties of the red cell membrane in relation to molecular structure and genetic defects. Annu Rev Biophys Biomol Struct 1994, 23:787-818.
    • (1994) Annu Rev Biophys Biomol Struct , vol.23 , pp. 787-818
    • Mohandas, N.1    Evans, E.2
  • 24
    • 0018390746 scopus 로고
    • Red blood cell deformability and hemolytic anemias
    • Mohandas N., Phillips W.M., Bessis M. Red blood cell deformability and hemolytic anemias. Semin Hematol 1979, 16(2):95-114.
    • (1979) Semin Hematol , vol.16 , Issue.2 , pp. 95-114
    • Mohandas, N.1    Phillips, W.M.2    Bessis, M.3
  • 25
    • 0018044039 scopus 로고
    • Control of red cell deformability and shape
    • Mohandas N., Shohet S.B. Control of red cell deformability and shape. Curr Top Hematol 1978, 1:71-125.
    • (1978) Curr Top Hematol , vol.1 , pp. 71-125
    • Mohandas, N.1    Shohet, S.B.2
  • 27
    • 33644508650 scopus 로고    scopus 로고
    • Rh proteins: key structural and functional components of the red cell membrane
    • Van Kim C.L., Colin Y., Cartron J.P. Rh proteins: key structural and functional components of the red cell membrane. Blood Rev 2006, 20(2):93-110.
    • (2006) Blood Rev , vol.20 , Issue.2 , pp. 93-110
    • Van Kim, C.L.1    Colin, Y.2    Cartron, J.P.3
  • 28
    • 0034921897 scopus 로고    scopus 로고
    • Structural and functional diversity of blood group antigens
    • Cartron J.P., Colin Y. Structural and functional diversity of blood group antigens. Transfus Clin Biol 2001, 8(3):163-199.
    • (2001) Transfus Clin Biol , vol.8 , Issue.3 , pp. 163-199
    • Cartron, J.P.1    Colin, Y.2
  • 29
    • 0028936298 scopus 로고
    • Erythrocyte blood group antigens: not so simple after all
    • Telen M.J. Erythrocyte blood group antigens: not so simple after all. Blood 1995, 85(2):299-306.
    • (1995) Blood , vol.85 , Issue.2 , pp. 299-306
    • Telen, M.J.1
  • 30
    • 70349254604 scopus 로고    scopus 로고
    • Adducin forms a bridge between the erythrocyte membrane and its cytoskeleton and regulates membrane cohesion
    • Anong W.A., Franco T., Chu H., Weis T.L., Devlin E.E., Bodine D.M., et al. Adducin forms a bridge between the erythrocyte membrane and its cytoskeleton and regulates membrane cohesion. Blood 2009, 114(9):1904-1912.
    • (2009) Blood , vol.114 , Issue.9 , pp. 1904-1912
    • Anong, W.A.1    Franco, T.2    Chu, H.3    Weis, T.L.4    Devlin, E.E.5    Bodine, D.M.6
  • 31
    • 0038157322 scopus 로고    scopus 로고
    • A band 3-based macrocomplex of integral and peripheral proteins in the RBC membrane
    • Bruce L.J., Beckmann R., Ribeiro M.L., Peters L.L., Chasis J.A., Delaunay J., et al. A band 3-based macrocomplex of integral and peripheral proteins in the RBC membrane. Blood 2003, 101(10):4180-4188.
    • (2003) Blood , vol.101 , Issue.10 , pp. 4180-4188
    • Bruce, L.J.1    Beckmann, R.2    Ribeiro, M.L.3    Peters, L.L.4    Chasis, J.A.5    Delaunay, J.6
  • 32
    • 14644395592 scopus 로고    scopus 로고
    • Blood group antigens in health and disease
    • Mohandas N., Narla A. Blood group antigens in health and disease. Curr Opin Hematol 2005, 12(2):135-140.
    • (2005) Curr Opin Hematol , vol.12 , Issue.2 , pp. 135-140
    • Mohandas, N.1    Narla, A.2
  • 34
    • 45849147331 scopus 로고    scopus 로고
    • Protein 4.1R-dependent multiprotein complex: new insights into the structural organization of the red blood cell membrane
    • Salomao M., Zhang X., Yang Y., Lee S., Hartwig J.H., Chasis J.A., et al. Protein 4.1R-dependent multiprotein complex: new insights into the structural organization of the red blood cell membrane. Proc Natl Acad Sci U S A 2008, 105(23):8026-8031.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.23 , pp. 8026-8031
    • Salomao, M.1    Zhang, X.2    Yang, Y.3    Lee, S.4    Hartwig, J.H.5    Chasis, J.A.6
  • 35
    • 0034663120 scopus 로고    scopus 로고
    • Severe hereditary spherocytosis and distal renal tubular acidosis associated with the total absence of band 3
    • Ribeiro M.L., Alloisio N., Almeida H., Gomes C., Texier P., Lemos C., et al. Severe hereditary spherocytosis and distal renal tubular acidosis associated with the total absence of band 3. Blood 2000, 96(4):1602-1604.
    • (2000) Blood , vol.96 , Issue.4 , pp. 1602-1604
    • Ribeiro, M.L.1    Alloisio, N.2    Almeida, H.3    Gomes, C.4    Texier, P.5    Lemos, C.6
  • 36
    • 0025719950 scopus 로고
    • Deficiency of alpha-spectrin synthesis in burst-forming units-erythroid in lethal hereditary spherocytosis
    • Whitfield C.F., Follweiler J.B., Lopresti-Morrow L., Miller B.A. Deficiency of alpha-spectrin synthesis in burst-forming units-erythroid in lethal hereditary spherocytosis. Blood 1991, 78(11):3043-3051.
    • (1991) Blood , vol.78 , Issue.11 , pp. 3043-3051
    • Whitfield, C.F.1    Follweiler, J.B.2    Lopresti-Morrow, L.3    Miller, B.A.4
  • 37
    • 0028927524 scopus 로고
    • Recurrent fatal hydrops fetalis associated with a nucleotide substitution in the erythrocyte beta-spectrin gene
    • Gallagher P.G., Weed S.A., Tse W.T., Benoit L., Morrow J.S., Marchesi S.L., et al. Recurrent fatal hydrops fetalis associated with a nucleotide substitution in the erythrocyte beta-spectrin gene. J Clin Invest 1995, 95(3):1174-1182.
    • (1995) J Clin Invest , vol.95 , Issue.3 , pp. 1174-1182
    • Gallagher, P.G.1    Weed, S.A.2    Tse, W.T.3    Benoit, L.4    Morrow, J.S.5    Marchesi, S.L.6
  • 38
    • 0030231133 scopus 로고    scopus 로고
    • Red cell abnormalities in hereditary spherocytosis: relevance to diagnosis and understanding of the variable expression of clinical severity
    • Cynober T., Mohandas N., Tchernia G. Red cell abnormalities in hereditary spherocytosis: relevance to diagnosis and understanding of the variable expression of clinical severity. J Lab Clin Med 1996, 128(3):259-269.
    • (1996) J Lab Clin Med , vol.128 , Issue.3 , pp. 259-269
    • Cynober, T.1    Mohandas, N.2    Tchernia, G.3
  • 39
    • 0035892116 scopus 로고    scopus 로고
    • Temporal differences in membrane loss lead to distinct reticulocyte features in hereditary spherocytosis and in immune hemolytic anemia
    • Da Costa L., Mohandas N., Sorette M., Grange M.J., Tchernia G., Cynober T. Temporal differences in membrane loss lead to distinct reticulocyte features in hereditary spherocytosis and in immune hemolytic anemia. Blood 2001, 98(10):2894-2899.
    • (2001) Blood , vol.98 , Issue.10 , pp. 2894-2899
    • Da Costa, L.1    Mohandas, N.2    Sorette, M.3    Grange, M.J.4    Tchernia, G.5    Cynober, T.6
  • 40
    • 0021914750 scopus 로고
    • Partial deficiency of erythrocyte spectrin in hereditary spherocytosis
    • Agre P., Casella J.F., Zinkham W.H., McMillan C., Bennett V. Partial deficiency of erythrocyte spectrin in hereditary spherocytosis. Nature 1985, 314(6009):380-383.
    • (1985) Nature , vol.314 , Issue.6009 , pp. 380-383
    • Agre, P.1    Casella, J.F.2    Zinkham, W.H.3    McMillan, C.4    Bennett, V.5
  • 41
    • 0036432768 scopus 로고    scopus 로고
    • Molecular basis of red cell membrane disorders
    • Delaunay J. Molecular basis of red cell membrane disorders. Acta Haematol 2002, 108(4):210-218.
    • (2002) Acta Haematol , vol.108 , Issue.4 , pp. 210-218
    • Delaunay, J.1
  • 42
    • 0029980108 scopus 로고    scopus 로고
    • Ankyrin Napoli: a de novo deletional frameshift mutation in exon 16 of ankyrin gene (ANK1) associated with spherocytosis
    • del Giudice E.M., Hayette S., Bozon M., Perrotta S., Alloisio N., Vallier A., et al. Ankyrin Napoli: a de novo deletional frameshift mutation in exon 16 of ankyrin gene (ANK1) associated with spherocytosis. Br J Haematol 1996, 93(4):828-834.
    • (1996) Br J Haematol , vol.93 , Issue.4 , pp. 828-834
    • del Giudice, E.M.1    Hayette, S.2    Bozon, M.3    Perrotta, S.4    Alloisio, N.5    Vallier, A.6
  • 43
    • 9044220232 scopus 로고    scopus 로고
    • Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis
    • Eber S.W., Gonzalez J.M., Lux M.L., Scarpa A.L., Tse W.T., Dornwell M., et al. Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis. Nat Genet 1996, 13(2):214-218.
    • (1996) Nat Genet , vol.13 , Issue.2 , pp. 214-218
    • Eber, S.W.1    Gonzalez, J.M.2    Lux, M.L.3    Scarpa, A.L.4    Tse, W.T.5    Dornwell, M.6
  • 44
    • 1942509531 scopus 로고    scopus 로고
    • Hereditary spherocytosis-defects in proteins that connect the membrane skeleton to the lipid bilayer
    • Eber S., Lux S.E. Hereditary spherocytosis-defects in proteins that connect the membrane skeleton to the lipid bilayer. Semin Hematol 2004, 41(2):118-141.
    • (2004) Semin Hematol , vol.41 , Issue.2 , pp. 118-141
    • Eber, S.1    Lux, S.E.2
  • 45
    • 0025338725 scopus 로고
    • Hereditary spherocytosis associated with deletion of human erythrocyte ankyrin gene on chromosome 8
    • Lux S.E., Tse W.T., Menninger J.C., John K.M., Harris P., Shalev O., et al. Hereditary spherocytosis associated with deletion of human erythrocyte ankyrin gene on chromosome 8. Nature 1990, 345(6277):736-739.
    • (1990) Nature , vol.345 , Issue.6277 , pp. 736-739
    • Lux, S.E.1    Tse, W.T.2    Menninger, J.C.3    John, K.M.4    Harris, P.5    Shalev, O.6
  • 46
    • 0020788331 scopus 로고
    • Red cell membrane skeletal defects in hereditary and acquired hemolytic anemias
    • Palek J., Lux S.E. Red cell membrane skeletal defects in hereditary and acquired hemolytic anemias. Semin Hematol 1983, 20(3):189-224.
    • (1983) Semin Hematol , vol.20 , Issue.3 , pp. 189-224
    • Palek, J.1    Lux, S.E.2
  • 47
    • 10544253080 scopus 로고    scopus 로고
    • Characterization of 13 novel band 3 gene defects in hereditary spherocytosis with band 3 deficiency
    • Jarolim P., Murray J.L., Rubin H.L., Taylor W.M., Prchal J.T., Ballas S.K., et al. Characterization of 13 novel band 3 gene defects in hereditary spherocytosis with band 3 deficiency. Blood 1996, 88(11):4366-4374.
    • (1996) Blood , vol.88 , Issue.11 , pp. 4366-4374
    • Jarolim, P.1    Murray, J.L.2    Rubin, H.L.3    Taylor, W.M.4    Prchal, J.T.5    Ballas, S.K.6
  • 48
    • 0030921079 scopus 로고    scopus 로고
    • Characterization of the underlying molecular defect in hereditary spherocytosis associated with spectrin deficiency
    • Hassoun H., Vassiliadis J.N., Murray J., Njolstad P.R., Rogus J.J., Ballas S.K., et al. Characterization of the underlying molecular defect in hereditary spherocytosis associated with spectrin deficiency. Blood 1997, 90(1):398-406.
    • (1997) Blood , vol.90 , Issue.1 , pp. 398-406
    • Hassoun, H.1    Vassiliadis, J.N.2    Murray, J.3    Njolstad, P.R.4    Rogus, J.J.5    Ballas, S.K.6
  • 49
    • 0015430071 scopus 로고
    • Red cell shapes. An illustrated classification and its rationale
    • Bessis M. Red cell shapes. An illustrated classification and its rationale. Nouv Rev Fr Hematol 1972, 12(6):721-745.
    • (1972) Nouv Rev Fr Hematol , vol.12 , Issue.6 , pp. 721-745
    • Bessis, M.1
  • 51
    • 0024434982 scopus 로고
    • Mean corpuscular hemoglobin concentration and cell deformability
    • Clark M.R. Mean corpuscular hemoglobin concentration and cell deformability. Ann N Y Acad Sci 1989, 565:284-294.
    • (1989) Ann N Y Acad Sci , vol.565 , pp. 284-294
    • Clark, M.R.1
  • 52
    • 0022543618 scopus 로고
    • Accurate and independent measurement of volume and hemoglobin concentration of individual red cells by laser light scattering
    • Mohandas N., Kim Y.R., Tycko D.H., Orlik J., Wyatt J., Groner W. Accurate and independent measurement of volume and hemoglobin concentration of individual red cells by laser light scattering. Blood 1986, 68(2):506-513.
    • (1986) Blood , vol.68 , Issue.2 , pp. 506-513
    • Mohandas, N.1    Kim, Y.R.2    Tycko, D.H.3    Orlik, J.4    Wyatt, J.5    Groner, W.6
  • 53
    • 83555165925 scopus 로고    scopus 로고
    • Guidelines for the diagnosis and management of hereditary spherocytosis-2011 update
    • Bolton-Maggs P.H., Langer J.C., Iolascon A., Tittensor P., King M.J. Guidelines for the diagnosis and management of hereditary spherocytosis-2011 update. Br J Haematol 2012, 156(1):37-49.
    • (2012) Br J Haematol , vol.156 , Issue.1 , pp. 37-49
    • Bolton-Maggs, P.H.1    Langer, J.C.2    Iolascon, A.3    Tittensor, P.4    King, M.J.5
  • 55
    • 0016121645 scopus 로고
    • Glycerol lysis time of incubated erythrocytes in the diagnosis of hereditary spherocytosis
    • Gottfried E.L., Robertson N.A. Glycerol lysis time of incubated erythrocytes in the diagnosis of hereditary spherocytosis. J Lab Clin Med 1974, 84(5):746-751.
    • (1974) J Lab Clin Med , vol.84 , Issue.5 , pp. 746-751
    • Gottfried, E.L.1    Robertson, N.A.2
  • 56
    • 0023917618 scopus 로고
    • Comparison of acidified glycerol lysis test, Pink test and osmotic fragility test in hereditary spherocytosis: effect of incubation
    • Bucx M.J., Breed W.P., Hoffmann J.J. Comparison of acidified glycerol lysis test, Pink test and osmotic fragility test in hereditary spherocytosis: effect of incubation. Eur J Haematol 1988, 40(3):227-231.
    • (1988) Eur J Haematol , vol.40 , Issue.3 , pp. 227-231
    • Bucx, M.J.1    Breed, W.P.2    Hoffmann, J.J.3
  • 57
    • 51249106670 scopus 로고    scopus 로고
    • Hereditary spherocytosis: guidelines for the diagnosis and management in children
    • Guitton C., Garcon L., Cynober T., Gauthier F., Tchernia G., Delaunay J., et al. Hereditary spherocytosis: guidelines for the diagnosis and management in children. Arch Pediatr 2008, 15(9):1464-1473.
    • (2008) Arch Pediatr , vol.15 , Issue.9 , pp. 1464-1473
    • Guitton, C.1    Garcon, L.2    Cynober, T.3    Gauthier, F.4    Tchernia, G.5    Delaunay, J.6
  • 58
    • 84859464017 scopus 로고    scopus 로고
    • Diagnostic power of laboratory tests for hereditary spherocytosis: a comparison study in 150 patients grouped according to molecular and clinical characteristics
    • Bianchi P., Fermo E., Vercellati C., Marcello A.P., Porretti L., Cortelezzi A., et al. Diagnostic power of laboratory tests for hereditary spherocytosis: a comparison study in 150 patients grouped according to molecular and clinical characteristics. Haematologica 2012, 97(4):516-523.
    • (2012) Haematologica , vol.97 , Issue.4 , pp. 516-523
    • Bianchi, P.1    Fermo, E.2    Vercellati, C.3    Marcello, A.P.4    Porretti, L.5    Cortelezzi, A.6
  • 60
    • 78649776046 scopus 로고    scopus 로고
    • Reliability of EMA binding test in the diagnosis of hereditary spherocytosis in Italian patients
    • D'Alcamo E., Agrigento V., Sclafani S., Vitrano A., Cuccia L., Maggio A., et al. Reliability of EMA binding test in the diagnosis of hereditary spherocytosis in Italian patients. Acta Haematol 2011, 125(3):136-140.
    • (2011) Acta Haematol , vol.125 , Issue.3 , pp. 136-140
    • D'Alcamo, E.1    Agrigento, V.2    Sclafani, S.3    Vitrano, A.4    Cuccia, L.5    Maggio, A.6
  • 61
    • 79952456632 scopus 로고    scopus 로고
    • Detection of hereditary pyropoikilocytosis by the eosin-5-maleimide (EMA)-binding test is attributable to a marked reduction in EMA-reactive transmembrane proteins
    • King M.J., Jepson M.A., Guest A., Mushens R. Detection of hereditary pyropoikilocytosis by the eosin-5-maleimide (EMA)-binding test is attributable to a marked reduction in EMA-reactive transmembrane proteins. Int J Lab Hematol 2011, 33(2):205-211.
    • (2011) Int J Lab Hematol , vol.33 , Issue.2 , pp. 205-211
    • King, M.J.1    Jepson, M.A.2    Guest, A.3    Mushens, R.4
  • 63
  • 65
    • 67949083657 scopus 로고    scopus 로고
    • Clinico-hematological profile of hereditary spherocytosis: experience from a tertiary care center in North India
    • Kar R., Rao S., Srinivas U.M., Mishra P., Pati H.P. Clinico-hematological profile of hereditary spherocytosis: experience from a tertiary care center in North India. Hematology 2009, 14(3):164-167.
    • (2009) Hematology , vol.14 , Issue.3 , pp. 164-167
    • Kar, R.1    Rao, S.2    Srinivas, U.M.3    Mishra, P.4    Pati, H.P.5
  • 66
    • 77449109504 scopus 로고    scopus 로고
    • Evaluation of eosin-5-maleimide flow cytometric test in diagnosis of hereditary spherocytosis
    • Kar R., Mishra P., Pati H.P. Evaluation of eosin-5-maleimide flow cytometric test in diagnosis of hereditary spherocytosis. Int J Lab Hematol 2010, 32(1 Pt 2):8-16.
    • (2010) Int J Lab Hematol , vol.32 , Issue.1 PART 2 , pp. 8-16
    • Kar, R.1    Mishra, P.2    Pati, H.P.3
  • 67
    • 47549102275 scopus 로고    scopus 로고
    • Using the eosin-5-maleimide binding test in the differential diagnosis of hereditary spherocytosis and hereditary pyropoikilocytosis
    • King M.J., Telfer P., MacKinnon H., Langabeer L., McMahon C., Darbyshire P., et al. Using the eosin-5-maleimide binding test in the differential diagnosis of hereditary spherocytosis and hereditary pyropoikilocytosis. Cytometry B Clin Cytom 2008, 74(4):244-250.
    • (2008) Cytometry B Clin Cytom , vol.74 , Issue.4 , pp. 244-250
    • King, M.J.1    Telfer, P.2    MacKinnon, H.3    Langabeer, L.4    McMahon, C.5    Darbyshire, P.6
  • 68
    • 0347064082 scopus 로고    scopus 로고
    • Eosin-5-maleimide binding to band 3 and Rh-related proteins forms the basis of a screening test for hereditary spherocytosis
    • King M.J., Smythe J.S., Mushens R. Eosin-5-maleimide binding to band 3 and Rh-related proteins forms the basis of a screening test for hereditary spherocytosis. Br J Haematol 2004, 124(1):106-113.
    • (2004) Br J Haematol , vol.124 , Issue.1 , pp. 106-113
    • King, M.J.1    Smythe, J.S.2    Mushens, R.3
  • 69
    • 0347504924 scopus 로고    scopus 로고
    • Experience with eosin-5'-maleimide as a diagnostic tool for red cell membrane cytoskeleton disorders
    • Kedar P.S., Colah R.B., Kulkarni S., Ghosh K., Mohanty D. Experience with eosin-5'-maleimide as a diagnostic tool for red cell membrane cytoskeleton disorders. Clin Lab Haematol 2003, 25(6):373-376.
    • (2003) Clin Lab Haematol , vol.25 , Issue.6 , pp. 373-376
    • Kedar, P.S.1    Colah, R.B.2    Kulkarni, S.3    Ghosh, K.4    Mohanty, D.5
  • 70
    • 0034494630 scopus 로고    scopus 로고
    • Rapid flow cytometric test for the diagnosis of membrane cytoskeleton-associated haemolytic anaemia
    • King M.J., Behrens J., Rogers C., Flynn C., Greenwood D., Chambers K. Rapid flow cytometric test for the diagnosis of membrane cytoskeleton-associated haemolytic anaemia. Br J Haematol 2000, 111(3):924-933.
    • (2000) Br J Haematol , vol.111 , Issue.3 , pp. 924-933
    • King, M.J.1    Behrens, J.2    Rogers, C.3    Flynn, C.4    Greenwood, D.5    Chambers, K.6
  • 71
    • 79956123277 scopus 로고    scopus 로고
    • A prospective study to assess the predictive value for hereditary spherocytosis using five laboratory tests (cryohemolysis test, eosin-5'-maleimide flow cytometry, osmotic fragility test, autohemolysis test, and SDS-PAGE) on 50 hereditary spherocytosis families in Argentina
    • Crisp R.L., Solari L., Vota D., Garcia E., Miguez G., Chamorro M.E., et al. A prospective study to assess the predictive value for hereditary spherocytosis using five laboratory tests (cryohemolysis test, eosin-5'-maleimide flow cytometry, osmotic fragility test, autohemolysis test, and SDS-PAGE) on 50 hereditary spherocytosis families in Argentina. Ann Hematol 2011, 90(6):625-634.
    • (2011) Ann Hematol , vol.90 , Issue.6 , pp. 625-634
    • Crisp, R.L.1    Solari, L.2    Vota, D.3    Garcia, E.4    Miguez, G.5    Chamorro, M.E.6
  • 72
    • 38349154864 scopus 로고    scopus 로고
    • Usefulness of the eosin-5'-maleimide cytometric method as a first-line screening test for the diagnosis of hereditary spherocytosis: comparison with ektacytometry and protein electrophoresis
    • Girodon F., Garcon L., Bergoin E., Largier M., Delaunay J., Feneant-Thibault M., et al. Usefulness of the eosin-5'-maleimide cytometric method as a first-line screening test for the diagnosis of hereditary spherocytosis: comparison with ektacytometry and protein electrophoresis. Br J Haematol 2008, 140(4):468-470.
    • (2008) Br J Haematol , vol.140 , Issue.4 , pp. 468-470
    • Girodon, F.1    Garcon, L.2    Bergoin, E.3    Largier, M.4    Delaunay, J.5    Feneant-Thibault, M.6
  • 74
    • 0018893223 scopus 로고
    • Ektacytometric analysis of factors regulating red cell deformability
    • Mohandas N., Clark M.R., Jacobs M.S., Groner W., Shohet S.B. Ektacytometric analysis of factors regulating red cell deformability. Blood Cells 1980, 6(3):329-334.
    • (1980) Blood Cells , vol.6 , Issue.3 , pp. 329-334
    • Mohandas, N.1    Clark, M.R.2    Jacobs, M.S.3    Groner, W.4    Shohet, S.B.5
  • 75
    • 0020080930 scopus 로고
    • A technique to detect reduced mechanical stability of red cell membranes: relevance to elliptocytic disorders
    • Mohandas N., Clark M.R., Health B.P., Rossi M., Wolfe L.C., Lux S.E., et al. A technique to detect reduced mechanical stability of red cell membranes: relevance to elliptocytic disorders. Blood 1982, 59(4):768-774.
    • (1982) Blood , vol.59 , Issue.4 , pp. 768-774
    • Mohandas, N.1    Clark, M.R.2    Health, B.P.3    Rossi, M.4    Wolfe, L.C.5    Lux, S.E.6
  • 76
    • 0015236352 scopus 로고
    • Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane
    • Fairbanks G., Steck T.L., Wallach D.F. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 1971, 10(13):2606-2617.
    • (1971) Biochemistry , vol.10 , Issue.13 , pp. 2606-2617
    • Fairbanks, G.1    Steck, T.L.2    Wallach, D.F.3
  • 77
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227(5259):680-685.
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 78
    • 0032791249 scopus 로고    scopus 로고
    • Hereditary dehydrated and overhydrated stomatocytosis: recent advances
    • Delaunay J., Stewart G., Iolascon A. Hereditary dehydrated and overhydrated stomatocytosis: recent advances. Curr Opin Hematol 1999, 6(2):110-114.
    • (1999) Curr Opin Hematol , vol.6 , Issue.2 , pp. 110-114
    • Delaunay, J.1    Stewart, G.2    Iolascon, A.3
  • 79
    • 0034488335 scopus 로고    scopus 로고
    • A recurrent frameshift mutation of the ankyrin gene associated with severe hereditary spherocytosis
    • Gallagher P.G., Ferreira J.D., Costa F.F., Saad S.T., Forget B.G. A recurrent frameshift mutation of the ankyrin gene associated with severe hereditary spherocytosis. Br J Haematol 2000, 111(4):1190-1193.
    • (2000) Br J Haematol , vol.111 , Issue.4 , pp. 1190-1193
    • Gallagher, P.G.1    Ferreira, J.D.2    Costa, F.F.3    Saad, S.T.4    Forget, B.G.5
  • 80
    • 0034988111 scopus 로고    scopus 로고
    • Band 3 Cape Town (E90K) causes severe hereditary spherocytosis in combination with band 3 Prague III
    • Bracher N.A., Lyons C.A., Wessels G., Mansvelt E., Coetzer T.L. Band 3 Cape Town (E90K) causes severe hereditary spherocytosis in combination with band 3 Prague III. Br J Haematol 2001, 113(3):689-693.
    • (2001) Br J Haematol , vol.113 , Issue.3 , pp. 689-693
    • Bracher, N.A.1    Lyons, C.A.2    Wessels, G.3    Mansvelt, E.4    Coetzer, T.L.5
  • 81
    • 0029763223 scopus 로고    scopus 로고
    • Hereditary spherocytosis with band 3 deficiency. Association with a nonsense mutation of the band 3 gene (allele Lyon), and aggravation by a low-expression allele occurring in trans (allele Genas)
    • Alloisio N., Maillet P., Carre G., Texier P., Vallier A., Baklouti F., et al. Hereditary spherocytosis with band 3 deficiency. Association with a nonsense mutation of the band 3 gene (allele Lyon), and aggravation by a low-expression allele occurring in trans (allele Genas). Blood 1996, 88(3):1062-1069.
    • (1996) Blood , vol.88 , Issue.3 , pp. 1062-1069
    • Alloisio, N.1    Maillet, P.2    Carre, G.3    Texier, P.4    Vallier, A.5    Baklouti, F.6
  • 82
    • 0031417692 scopus 로고    scopus 로고
    • Hematologically important mutations: band 3 and protein 4.2 variants in hereditary spherocytosis
    • Gallagher P.G., Forget B.G. Hematologically important mutations: band 3 and protein 4.2 variants in hereditary spherocytosis. Blood Cells Mol Dis 1997, 23(3):417-421.
    • (1997) Blood Cells Mol Dis , vol.23 , Issue.3 , pp. 417-421
    • Gallagher, P.G.1    Forget, B.G.2
  • 83
    • 0029834849 scopus 로고    scopus 로고
    • Combination of two mutant alpha spectrin alleles underlies a severe spherocytic hemolytic anemia
    • Wichterle H., Hanspal M., Palek J., Jarolim P. Combination of two mutant alpha spectrin alleles underlies a severe spherocytic hemolytic anemia. J Clin Invest 1996, 98(10):2300-2307.
    • (1996) J Clin Invest , vol.98 , Issue.10 , pp. 2300-2307
    • Wichterle, H.1    Hanspal, M.2    Palek, J.3    Jarolim, P.4
  • 84
    • 0028866823 scopus 로고
    • Beta spectrin PRAGUE: a truncated beta spectrin producing spectrin deficiency, defective spectrin heterodimer self-association and a phenotype of spherocytic elliptocytosis
    • Jarolim P., Wichterle H., Hanspal M., Murray J., Rubin H.L., Palek J. Beta spectrin PRAGUE: a truncated beta spectrin producing spectrin deficiency, defective spectrin heterodimer self-association and a phenotype of spherocytic elliptocytosis. Br J Haematol 1995, 91(2):502-510.
    • (1995) Br J Haematol , vol.91 , Issue.2 , pp. 502-510
    • Jarolim, P.1    Wichterle, H.2    Hanspal, M.3    Murray, J.4    Rubin, H.L.5    Palek, J.6
  • 85
  • 86
    • 4944237468 scopus 로고    scopus 로고
    • Different impacts of alleles alphaLEPRA and alphaLELY as assessed versus a novel, virtually null allele of the SPTA1 gene in trans
    • Delaunay J., Nouyrigat V., Proust A., Schischmanoff P.O., Cynober T., Yvart J., et al. Different impacts of alleles alphaLEPRA and alphaLELY as assessed versus a novel, virtually null allele of the SPTA1 gene in trans. Br J Haematol 2004, 127(1):118-122.
    • (2004) Br J Haematol , vol.127 , Issue.1 , pp. 118-122
    • Delaunay, J.1    Nouyrigat, V.2    Proust, A.3    Schischmanoff, P.O.4    Cynober, T.5    Yvart, J.6
  • 87
    • 0034584616 scopus 로고    scopus 로고
    • Recombinant erythropoietin therapy as an alternative to blood transfusions in infants with hereditary spherocytosis
    • Tchernia G., Delhommeau F., Perrotta S., Cynober T., Bader-Meunier B., Nobili B., et al. Recombinant erythropoietin therapy as an alternative to blood transfusions in infants with hereditary spherocytosis. Hematol J 2000, 1(3):146-152.
    • (2000) Hematol J , vol.1 , Issue.3 , pp. 146-152
    • Tchernia, G.1    Delhommeau, F.2    Perrotta, S.3    Cynober, T.4    Bader-Meunier, B.5    Nobili, B.6
  • 88
    • 0033763697 scopus 로고    scopus 로고
    • Technical advances in pediatric laparoscopy have had a beneficial impact on splenectomy
    • Danielson P.D., Shaul D.B., Phillips J.D., Stein J.E., Anderson K.D. Technical advances in pediatric laparoscopy have had a beneficial impact on splenectomy. J Pediatr Surg 2000, 35(11):1578-1581.
    • (2000) J Pediatr Surg , vol.35 , Issue.11 , pp. 1578-1581
    • Danielson, P.D.1    Shaul, D.B.2    Phillips, J.D.3    Stein, J.E.4    Anderson, K.D.5
  • 89
    • 34548487557 scopus 로고    scopus 로고
    • The prevention and management of infections in children with asplenia or hyposplenia
    • [viii-ix]
    • Price V.E., Blanchette V.S., Ford-Jones E.L. The prevention and management of infections in children with asplenia or hyposplenia. Infect Dis Clin North Am 2007, 21(3):697-710. [viii-ix].
    • (2007) Infect Dis Clin North Am , vol.21 , Issue.3 , pp. 697-710
    • Price, V.E.1    Blanchette, V.S.2    Ford-Jones, E.L.3
  • 90
    • 0027478257 scopus 로고
    • Initial assessment of the beneficial effect of partial splenectomy in hereditary spherocytosis
    • Tchernia G., Gauthier F., Mielot F., Dommergues J.P., Yvart J., Chasis J.A., et al. Initial assessment of the beneficial effect of partial splenectomy in hereditary spherocytosis. Blood 1993, 81(8):2014-2020.
    • (1993) Blood , vol.81 , Issue.8 , pp. 2014-2020
    • Tchernia, G.1    Gauthier, F.2    Mielot, F.3    Dommergues, J.P.4    Yvart, J.5    Chasis, J.A.6
  • 93
    • 85047693774 scopus 로고    scopus 로고
    • Clinical and hematologic benefits of partial splenectomy for congenital hemolytic anemias in children
    • Rice H.E., Oldham K.T., Hillery C.A., Skinner M.A., O'Hara S.M., Ware R.E. Clinical and hematologic benefits of partial splenectomy for congenital hemolytic anemias in children. Ann Surg 2003, 237(2):281-288.
    • (2003) Ann Surg , vol.237 , Issue.2 , pp. 281-288
    • Rice, H.E.1    Oldham, K.T.2    Hillery, C.A.3    Skinner, M.A.4    O'Hara, S.M.5    Ware, R.E.6
  • 94
    • 33750804497 scopus 로고    scopus 로고
    • A laparoscopic approach to partial splenectomy for children with hereditary spherocytosis
    • Dutta S., Price V.E., Blanchette V., Langer J.C. A laparoscopic approach to partial splenectomy for children with hereditary spherocytosis. Surg Endosc 2006, 20(11):1719-1724.
    • (2006) Surg Endosc , vol.20 , Issue.11 , pp. 1719-1724
    • Dutta, S.1    Price, V.E.2    Blanchette, V.3    Langer, J.C.4
  • 95
    • 81255197678 scopus 로고    scopus 로고
    • Splenectomy for hereditary spherocytosis: complete, partial or not at all?
    • Casale M., Perrotta S. Splenectomy for hereditary spherocytosis: complete, partial or not at all?. Expert Rev Hematol 2011, 4(6):627-635.
    • (2011) Expert Rev Hematol , vol.4 , Issue.6 , pp. 627-635
    • Casale, M.1    Perrotta, S.2
  • 97
    • 77955856705 scopus 로고    scopus 로고
    • Institutional experience with laparoscopic partial splenectomy for hereditary spherocytosis
    • Slater B.J., Chan F.P., Davis K., Dutta S. Institutional experience with laparoscopic partial splenectomy for hereditary spherocytosis. J Pediatr Surg 2010, 45(8):1682-1686.
    • (2010) J Pediatr Surg , vol.45 , Issue.8 , pp. 1682-1686
    • Slater, B.J.1    Chan, F.P.2    Davis, K.3    Dutta, S.4
  • 98
    • 77954426770 scopus 로고    scopus 로고
    • Hereditary spherocytosis and partial splenectomy in children: review of surgical technique and the role of imaging
    • Hollingsworth C.L., Rice H.E. Hereditary spherocytosis and partial splenectomy in children: review of surgical technique and the role of imaging. Pediatr Radiol 2010, 40(7):1177-1183.
    • (2010) Pediatr Radiol , vol.40 , Issue.7 , pp. 1177-1183
    • Hollingsworth, C.L.1    Rice, H.E.2
  • 99
    • 41149163283 scopus 로고    scopus 로고
    • Partial splenectomy for hereditary spherocytosis
    • [x]
    • Tracy E.T., Rice H.E. Partial splenectomy for hereditary spherocytosis. Pediatr Clin North Am 2008, 55(2):503-519. [x].
    • (2008) Pediatr Clin North Am , vol.55 , Issue.2 , pp. 503-519
    • Tracy, E.T.1    Rice, H.E.2
  • 100
    • 37749030888 scopus 로고    scopus 로고
    • Laparoscopic partial splenectomy: indications and results of a multicenter retrospective study
    • Hery G., Becmeur F., Mefat L., Kalfa D., Lutz P., Lutz L., et al. Laparoscopic partial splenectomy: indications and results of a multicenter retrospective study. Surg Endosc 2008, 22(1):45-49.
    • (2008) Surg Endosc , vol.22 , Issue.1 , pp. 45-49
    • Hery, G.1    Becmeur, F.2    Mefat, L.3    Kalfa, D.4    Lutz, P.5    Lutz, L.6
  • 101
    • 0032796195 scopus 로고    scopus 로고
    • The role of prophylactic cholecystectomy during splenectomy in children with hereditary spherocytosis
    • Sandler A., Winkel G., Kimura K., Soper R. The role of prophylactic cholecystectomy during splenectomy in children with hereditary spherocytosis. J Pediatr Surg 1999, 34(7):1077-1078.
    • (1999) J Pediatr Surg , vol.34 , Issue.7 , pp. 1077-1078
    • Sandler, A.1    Winkel, G.2    Kimura, K.3    Soper, R.4
  • 102
    • 0008435402 scopus 로고    scopus 로고
    • Coinheritance of Gilbert syndrome increases the risk for developing gallstones in patients with hereditary spherocytosis
    • del Giudice E.M., Perrotta S., Nobili B., Specchia C., d'Urzo G., Iolascon A. Coinheritance of Gilbert syndrome increases the risk for developing gallstones in patients with hereditary spherocytosis. Blood 1999, 94(7):2259-2262.
    • (1999) Blood , vol.94 , Issue.7 , pp. 2259-2262
    • del Giudice, E.M.1    Perrotta, S.2    Nobili, B.3    Specchia, C.4    d'Urzo, G.5    Iolascon, A.6
  • 103
    • 25644446874 scopus 로고    scopus 로고
    • Cholecystectomy and the risk of colorectal cancer
    • Shao T., Yang Y.X. Cholecystectomy and the risk of colorectal cancer. Am J Gastroenterol 2005, 100(8):1813-1820.
    • (2005) Am J Gastroenterol , vol.100 , Issue.8 , pp. 1813-1820
    • Shao, T.1    Yang, Y.X.2
  • 104
    • 77955236930 scopus 로고    scopus 로고
    • Is cholecystectomy really an indication for concomitant splenectomy in mild hereditary spherocytosis?
    • Alizai N.K., Richards E.M., Stringer M.D. Is cholecystectomy really an indication for concomitant splenectomy in mild hereditary spherocytosis?. Arch Dis Child 2010, 95(8):596-599.
    • (2010) Arch Dis Child , vol.95 , Issue.8 , pp. 596-599
    • Alizai, N.K.1    Richards, E.M.2    Stringer, M.D.3
  • 105
    • 0030465328 scopus 로고    scopus 로고
    • Molecular genetics of hereditary elliptocytosis and hereditary spherocytosis
    • Delaunay J., Alloisio N., Morle L., Baklouti F., Dalla Venezia N., Maillet P., et al. Molecular genetics of hereditary elliptocytosis and hereditary spherocytosis. Ann Genet 1996, 39(4):209-221.
    • (1996) Ann Genet , vol.39 , Issue.4 , pp. 209-221
    • Delaunay, J.1    Alloisio, N.2    Morle, L.3    Baklouti, F.4    Dalla Venezia, N.5    Maillet, P.6
  • 106
    • 0027478129 scopus 로고
    • Mutations involving the spectrin heterodimer contact site: clinical expression and alterations in specific function
    • Delaunay J., Dhermy D. Mutations involving the spectrin heterodimer contact site: clinical expression and alterations in specific function. Semin Hematol 1993, 30(1):21-33.
    • (1993) Semin Hematol , vol.30 , Issue.1 , pp. 21-33
    • Delaunay, J.1    Dhermy, D.2
  • 107
    • 1942445176 scopus 로고    scopus 로고
    • Hereditary elliptocytosis: spectrin and protein 4.1R
    • Gallagher P.G. Hereditary elliptocytosis: spectrin and protein 4.1R. Semin Hematol 2004, 41(2):142-164.
    • (2004) Semin Hematol , vol.41 , Issue.2 , pp. 142-164
    • Gallagher, P.G.1
  • 110
    • 0025035758 scopus 로고
    • Molecular analysis of insertion/deletion mutations in protein 4.1 in elliptocytosis. I. Biochemical identification of rearrangements in the spectrin/actin binding domain and functional characterizations
    • Marchesi S.L., Conboy J., Agre P., Letsinger J.T., Marchesi V.T., Speicher D.W., et al. Molecular analysis of insertion/deletion mutations in protein 4.1 in elliptocytosis. I. Biochemical identification of rearrangements in the spectrin/actin binding domain and functional characterizations. J Clin Invest 1990, 86(2):516-523.
    • (1990) J Clin Invest , vol.86 , Issue.2 , pp. 516-523
    • Marchesi, S.L.1    Conboy, J.2    Agre, P.3    Letsinger, J.T.4    Marchesi, V.T.5    Speicher, D.W.6
  • 111
    • 47049089420 scopus 로고    scopus 로고
    • Structural and functional effects of hereditary hemolytic anemia-associated point mutations in the alpha spectrin tetramer site
    • Gaetani M., Mootien S., Harper S., Gallagher P.G., Speicher D.W. Structural and functional effects of hereditary hemolytic anemia-associated point mutations in the alpha spectrin tetramer site. Blood 2008, 111(12):5712-5720.
    • (2008) Blood , vol.111 , Issue.12 , pp. 5712-5720
    • Gaetani, M.1    Mootien, S.2    Harper, S.3    Gallagher, P.G.4    Speicher, D.W.5
  • 112
    • 34147151815 scopus 로고    scopus 로고
    • Pathogenic proline mutation in the linker between spectrin repeats: disease caused by spectrin unfolding
    • Johnson C.P., Gaetani M., Ortiz V., Bhasin N., Harper S., Gallagher P.G., et al. Pathogenic proline mutation in the linker between spectrin repeats: disease caused by spectrin unfolding. Blood 2007, 109(8):3538-3543.
    • (2007) Blood , vol.109 , Issue.8 , pp. 3538-3543
    • Johnson, C.P.1    Gaetani, M.2    Ortiz, V.3    Bhasin, N.4    Harper, S.5    Gallagher, P.G.6
  • 113
    • 0025228664 scopus 로고
    • Hereditary pyropoikilocytosis and elliptocytosis in a white French family with the spectrin alpha I/74 variant related to a CGT to CAT codon change (Arg to His) at position 22 of the spectrin alpha I domain
    • Garbarz M., Lecomte M.C., Feo C., Devaux I., Picat C., Lefebvre C., et al. Hereditary pyropoikilocytosis and elliptocytosis in a white French family with the spectrin alpha I/74 variant related to a CGT to CAT codon change (Arg to His) at position 22 of the spectrin alpha I domain. Blood 1990, 75(8):1691-1698.
    • (1990) Blood , vol.75 , Issue.8 , pp. 1691-1698
    • Garbarz, M.1    Lecomte, M.C.2    Feo, C.3    Devaux, I.4    Picat, C.5    Lefebvre, C.6
  • 114
    • 0025908711 scopus 로고
    • Spectrin Rouen (beta 220-218), a novel shortened beta-chain variant in a kindred with hereditary elliptocytosis. Characterization of the molecular defect as exon skipping due to a splice site mutation
    • Garbarz M., Tse W.T., Gallagher P.G., Picat C., Lecomte M.C., Galibert F., et al. Spectrin Rouen (beta 220-218), a novel shortened beta-chain variant in a kindred with hereditary elliptocytosis. Characterization of the molecular defect as exon skipping due to a splice site mutation. J Clin Invest 1991, 88(1):76-81.
    • (1991) J Clin Invest , vol.88 , Issue.1 , pp. 76-81
    • Garbarz, M.1    Tse, W.T.2    Gallagher, P.G.3    Picat, C.4    Lecomte, M.C.5    Galibert, F.6
  • 115
    • 0026519395 scopus 로고
    • Molecular pathology of inherited erythrocyte membrane disorders: hereditary spherocytosis and elliptocytosis
    • Iolascon A., Miraglia del Giudice E., Camaschella C. Molecular pathology of inherited erythrocyte membrane disorders: hereditary spherocytosis and elliptocytosis. Haematologica 1992, 77(1):60-72.
    • (1992) Haematologica , vol.77 , Issue.1 , pp. 60-72
    • Iolascon, A.1    Miraglia del Giudice, E.2    Camaschella, C.3
  • 117
    • 1642499106 scopus 로고    scopus 로고
    • Hereditary pyropoikilocytosis and the spectrin St. Claude allele
    • Mootien S., Gallagher P.G. Hereditary pyropoikilocytosis and the spectrin St. Claude allele. Br J Haematol 2004, 124(2):251-252.
    • (2004) Br J Haematol , vol.124 , Issue.2 , pp. 251-252
    • Mootien, S.1    Gallagher, P.G.2
  • 118
    • 41449108263 scopus 로고    scopus 로고
    • Association between myeloid malignancies and acquired deficit in protein 4.1R: a retrospective analysis of six patients
    • Alanio-Brechot C., Schischmanoff P.O., Feneant-Thibault M., Cynober T., Tchernia G., Delaunay J., et al. Association between myeloid malignancies and acquired deficit in protein 4.1R: a retrospective analysis of six patients. Am J Hematol 2008, 83(4):275-278.
    • (2008) Am J Hematol , vol.83 , Issue.4 , pp. 275-278
    • Alanio-Brechot, C.1    Schischmanoff, P.O.2    Feneant-Thibault, M.3    Cynober, T.4    Tchernia, G.5    Delaunay, J.6
  • 119
    • 1242294601 scopus 로고    scopus 로고
    • Protein 4.1 deficiency and deletion of chromosome 20q are associated with acquired elliptocytosis in myelodysplastic syndrome
    • Hur M., Lee K.M., Cho H.C., Park Y.I., Kim S.H., Chang Y.W., et al. Protein 4.1 deficiency and deletion of chromosome 20q are associated with acquired elliptocytosis in myelodysplastic syndrome. Clin Lab Haematol 2004, 26(1):69-72.
    • (2004) Clin Lab Haematol , vol.26 , Issue.1 , pp. 69-72
    • Hur, M.1    Lee, K.M.2    Cho, H.C.3    Park, Y.I.4    Kim, S.H.5    Chang, Y.W.6
  • 120
    • 0027377369 scopus 로고
    • Abnormal erythrocyte band 4.1 protein in myelodysplastic syndrome with elliptocytosis
    • Ideguchi H., Yamada Y., Kondo S., Tamura K., Makino S., Hamasaki N. Abnormal erythrocyte band 4.1 protein in myelodysplastic syndrome with elliptocytosis. Br J Haematol 1993, 85(2):387-392.
    • (1993) Br J Haematol , vol.85 , Issue.2 , pp. 387-392
    • Ideguchi, H.1    Yamada, Y.2    Kondo, S.3    Tamura, K.4    Makino, S.5    Hamasaki, N.6
  • 121
    • 34247123673 scopus 로고    scopus 로고
    • Spectrin-based skeleton in red blood cells and malaria
    • Dhermy D., Schrevel J., Lecomte M.C. Spectrin-based skeleton in red blood cells and malaria. Curr Opin Hematol 2007, 14(3):198-202.
    • (2007) Curr Opin Hematol , vol.14 , Issue.3 , pp. 198-202
    • Dhermy, D.1    Schrevel, J.2    Lecomte, M.C.3
  • 122
    • 0031017565 scopus 로고    scopus 로고
    • Mutation of a highly conserved residue of betaI spectrin associated with fatal and near-fatal neonatal hemolytic anemia
    • Gallagher P.G., Petruzzi M.J., Weed S.A., Zhang Z., Marchesi S.L., Mohandas N., et al. Mutation of a highly conserved residue of betaI spectrin associated with fatal and near-fatal neonatal hemolytic anemia. J Clin Invest 1997, 99(2):267-277.
    • (1997) J Clin Invest , vol.99 , Issue.2 , pp. 267-277
    • Gallagher, P.G.1    Petruzzi, M.J.2    Weed, S.A.3    Zhang, Z.4    Marchesi, S.L.5    Mohandas, N.6
  • 123
    • 0023091092 scopus 로고
    • Modulation of erythrocyte membrane mechanical stability by 2,3-diphosphoglycerate in the neonatal poikilocytosis/elliptocytosis syndrome
    • Mentzer W.C., Iarocci T.A., Mohandas N., Lane P.A., Smith B., Lazerson J., et al. Modulation of erythrocyte membrane mechanical stability by 2,3-diphosphoglycerate in the neonatal poikilocytosis/elliptocytosis syndrome. J Clin Invest 1987, 79(3):943-949.
    • (1987) J Clin Invest , vol.79 , Issue.3 , pp. 943-949
    • Mentzer, W.C.1    Iarocci, T.A.2    Mohandas, N.3    Lane, P.A.4    Smith, B.5    Lazerson, J.6
  • 124
    • 0027408788 scopus 로고
    • An alpha-spectrin mutation responsible for hereditary elliptocytosis associated in cis with the alpha v/41 polymorphism
    • Dalla Venezia N., Wilmotte R., Morle L., Forissier A., Parquet N., Garbarz M., et al. An alpha-spectrin mutation responsible for hereditary elliptocytosis associated in cis with the alpha v/41 polymorphism. Hum Genet 1993, 90(6):641-644.
    • (1993) Hum Genet , vol.90 , Issue.6 , pp. 641-644
    • Dalla Venezia, N.1    Wilmotte, R.2    Morle, L.3    Forissier, A.4    Parquet, N.5    Garbarz, M.6
  • 125
    • 0027289475 scopus 로고
    • Low expression allele alpha LELY of red cell spectrin is associated with mutations in exon 40 (alpha V/41 polymorphism) and intron 45 and with partial skipping of exon 46
    • Wilmotte R., Marechal J., Morle L., Baklouti F., Philippe N., Kastally R., et al. Low expression allele alpha LELY of red cell spectrin is associated with mutations in exon 40 (alpha V/41 polymorphism) and intron 45 and with partial skipping of exon 46. J Clin Invest 1993, 91(5):2091-2096.
    • (1993) J Clin Invest , vol.91 , Issue.5 , pp. 2091-2096
    • Wilmotte, R.1    Marechal, J.2    Morle, L.3    Baklouti, F.4    Philippe, N.5    Kastally, R.6
  • 127
    • 84866669398 scopus 로고    scopus 로고
    • Reduced Risk of Plasmodium vivax malaria in Papua New Guinean children with Southeast Asian ovalocytosis in two cohorts and a case-control study
    • Rosanas-Urgell A., Lin E., Manning L., Rarau P., Laman M., Senn N., et al. Reduced Risk of Plasmodium vivax malaria in Papua New Guinean children with Southeast Asian ovalocytosis in two cohorts and a case-control study. PLoS Med 2012, 9(9):e1001305.
    • (2012) PLoS Med , vol.9 , Issue.9
    • Rosanas-Urgell, A.1    Lin, E.2    Manning, L.3    Rarau, P.4    Laman, M.5    Senn, N.6
  • 128
    • 0021262067 scopus 로고
    • Rigid membranes of Malayan ovalocytes: a likely genetic barrier against malaria
    • Mohandas N., Lie-Injo L.E., Friedman M., Mak J.W. Rigid membranes of Malayan ovalocytes: a likely genetic barrier against malaria. Blood 1984, 63(6):1385-1392.
    • (1984) Blood , vol.63 , Issue.6 , pp. 1385-1392
    • Mohandas, N.1    Lie-Injo, L.E.2    Friedman, M.3    Mak, J.W.4
  • 129
    • 0028027718 scopus 로고
    • The homozygous state for the band 3 protein mutation in Southeast Asian ovalocytosis may be lethal
    • Liu S.C., Jarolim P., Rubin H.L., Palek J., Amato D., Hassan K., et al. The homozygous state for the band 3 protein mutation in Southeast Asian ovalocytosis may be lethal. Blood 1994, 84(10):3590-3591.
    • (1994) Blood , vol.84 , Issue.10 , pp. 3590-3591
    • Liu, S.C.1    Jarolim, P.2    Rubin, H.L.3    Palek, J.4    Amato, D.5    Hassan, K.6
  • 130
    • 1942541308 scopus 로고    scopus 로고
    • The hereditary stomatocytoses: genetic disorders of the red cell membrane permeability to monovalent cations
    • Delaunay J. The hereditary stomatocytoses: genetic disorders of the red cell membrane permeability to monovalent cations. Semin Hematol 2004, 41(2):165-172.
    • (2004) Semin Hematol , vol.41 , Issue.2 , pp. 165-172
    • Delaunay, J.1
  • 131
    • 0034307365 scopus 로고    scopus 로고
    • Pleiotropic syndrome of dehydrated hereditary stomatocytosis, pseudohyperkalemia, and perinatal edema maps to 16q23-q24
    • Grootenboer S., Schischmanoff P.O., Laurendeau I., Cynober T., Tchernia G., Dommergues J.P., et al. Pleiotropic syndrome of dehydrated hereditary stomatocytosis, pseudohyperkalemia, and perinatal edema maps to 16q23-q24. Blood 2000, 96(7):2599-2605.
    • (2000) Blood , vol.96 , Issue.7 , pp. 2599-2605
    • Grootenboer, S.1    Schischmanoff, P.O.2    Laurendeau, I.3    Cynober, T.4    Tchernia, G.5    Dommergues, J.P.6
  • 133
    • 0038241178 scopus 로고    scopus 로고
    • Sub-lethal hydrops as a manifestation of dehydrated hereditary stomatocytosis in two consecutive pregnancies
    • Grootenboer-Mignot S., Cretien A., Laurendeau I., Poissonnier M.H., Doireau V., Brossard Y., et al. Sub-lethal hydrops as a manifestation of dehydrated hereditary stomatocytosis in two consecutive pregnancies. Prenat Diagn 2003, 23(5):380-384.
    • (2003) Prenat Diagn , vol.23 , Issue.5 , pp. 380-384
    • Grootenboer-Mignot, S.1    Cretien, A.2    Laurendeau, I.3    Poissonnier, M.H.4    Doireau, V.5    Brossard, Y.6
  • 134
    • 0032231446 scopus 로고    scopus 로고
    • Genomewide search for dehydrated hereditary stomatocytosis (hereditary xerocytosis): mapping of locus to chromosome 16 (16q23-qter)
    • Carella M., Stewart G., Ajetunmobi J.F., Perrotta S., Grootenboer S., Tchernia G., et al. Genomewide search for dehydrated hereditary stomatocytosis (hereditary xerocytosis): mapping of locus to chromosome 16 (16q23-qter). Am J Hum Genet 1998, 63(3):810-816.
    • (1998) Am J Hum Genet , vol.63 , Issue.3 , pp. 810-816
    • Carella, M.1    Stewart, G.2    Ajetunmobi, J.F.3    Perrotta, S.4    Grootenboer, S.5    Tchernia, G.6
  • 136
    • 84865279173 scopus 로고    scopus 로고
    • Mutations in the mechanotransduction protein PIEZO1 are associated with hereditary xerocytosis
    • Zarychanski R., Schulz V.P., Houston B.L., Maksimova Y., Houston D.S., Smith B., et al. Mutations in the mechanotransduction protein PIEZO1 are associated with hereditary xerocytosis. Blood 2012, 120(9):1908-1915.
    • (2012) Blood , vol.120 , Issue.9 , pp. 1908-1915
    • Zarychanski, R.1    Schulz, V.P.2    Houston, B.L.3    Maksimova, Y.4    Houston, D.S.5    Smith, B.6
  • 137
    • 77957332682 scopus 로고    scopus 로고
    • Piezo1 and Piezo2 are essential components of distinct mechanically activated cation channels
    • Coste B., Mathur J., Schmidt M., Earley T.J., Ranade S., Petrus M.J., et al. Piezo1 and Piezo2 are essential components of distinct mechanically activated cation channels. Science 2010, 330(6000):55-60.
    • (2010) Science , vol.330 , Issue.6000 , pp. 55-60
    • Coste, B.1    Mathur, J.2    Schmidt, M.3    Earley, T.J.4    Ranade, S.5    Petrus, M.J.6
  • 138
    • 38049179056 scopus 로고    scopus 로고
    • RhAG protein of the Rhesus complex is a CO2 channel in the human red cell membrane
    • Endeward V., Cartron J.P., Ripoche P., Gros G. RhAG protein of the Rhesus complex is a CO2 channel in the human red cell membrane. FASEB J 2008, 22(1):64-73.
    • (2008) FASEB J , vol.22 , Issue.1 , pp. 64-73
    • Endeward, V.1    Cartron, J.P.2    Ripoche, P.3    Gros, G.4
  • 139
    • 0033757434 scopus 로고    scopus 로고
    • The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast
    • Marini A.M., Matassi G., Raynal V., Andre B., Cartron J.P., Cherif-Zahar B. The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast. Nat Genet 2000, 26(3):341-344.
    • (2000) Nat Genet , vol.26 , Issue.3 , pp. 341-344
    • Marini, A.M.1    Matassi, G.2    Raynal, V.3    Andre, B.4    Cartron, J.P.5    Cherif-Zahar, B.6
  • 140
    • 60849116982 scopus 로고    scopus 로고
    • The monovalent cation leak in overhydrated stomatocytic red blood cells results from amino acid substitutions in the Rh-associated glycoprotein
    • Bruce L.J., Guizouarn H., Burton N.M., Gabillat N., Poole J., Flatt J.F., et al. The monovalent cation leak in overhydrated stomatocytic red blood cells results from amino acid substitutions in the Rh-associated glycoprotein. Blood 2009, 113(6):1350-1357.
    • (2009) Blood , vol.113 , Issue.6 , pp. 1350-1357
    • Bruce, L.J.1    Guizouarn, H.2    Burton, N.M.3    Gabillat, N.4    Poole, J.5    Flatt, J.F.6
  • 142
    • 0033134755 scopus 로고    scopus 로고
    • Familial pseudohyperkalemia maps to the same locus as dehydrated hereditary stomatocytosis (hereditary xerocytosis)
    • Iolascon A., Stewart G.W., Ajetunmobi J.F., Perrotta S., Delaunay J., Carella M., et al. Familial pseudohyperkalemia maps to the same locus as dehydrated hereditary stomatocytosis (hereditary xerocytosis). Blood 1999, 93(9):3120-3123.
    • (1999) Blood , vol.93 , Issue.9 , pp. 3120-3123
    • Iolascon, A.1    Stewart, G.W.2    Ajetunmobi, J.F.3    Perrotta, S.4    Delaunay, J.5    Carella, M.6
  • 143
    • 27644593833 scopus 로고    scopus 로고
    • Monovalent cation leaks in human red cells caused by single amino-acid substitutions in the transport domain of the band 3 chloride-bicarbonate exchanger, AE1
    • Bruce L.J., Robinson H.C., Guizouarn H., Borgese F., Harrison P., King M.J., et al. Monovalent cation leaks in human red cells caused by single amino-acid substitutions in the transport domain of the band 3 chloride-bicarbonate exchanger, AE1. Nat Genet 2005, 37(11):1258-1263.
    • (2005) Nat Genet , vol.37 , Issue.11 , pp. 1258-1263
    • Bruce, L.J.1    Robinson, H.C.2    Guizouarn, H.3    Borgese, F.4    Harrison, P.5    King, M.J.6
  • 144
    • 68049142292 scopus 로고    scopus 로고
    • A novel erythroid anion exchange variant (Gly796Arg) of hereditary stomatocytosis associated with dyserythropoiesis
    • Iolascon A., De Falco L., Borgese F., Esposito M.R., Avvisati R.A., Izzo P., et al. A novel erythroid anion exchange variant (Gly796Arg) of hereditary stomatocytosis associated with dyserythropoiesis. Haematologica 2009, 94(8):1049-1059.
    • (2009) Haematologica , vol.94 , Issue.8 , pp. 1049-1059
    • Iolascon, A.1    De Falco, L.2    Borgese, F.3    Esposito, M.R.4    Avvisati, R.A.5    Izzo, P.6
  • 145
    • 0026592344 scopus 로고
    • A case of congenital dyserythropoietic anaemia with stomatocytosis, reduced bands 7 and 8 and normal cation content
    • Olivieri O., Girelli D., Vettore L., Balercia G., Corrocher R. A case of congenital dyserythropoietic anaemia with stomatocytosis, reduced bands 7 and 8 and normal cation content. Br J Haematol 1992, 80(2):258-260.
    • (1992) Br J Haematol , vol.80 , Issue.2 , pp. 258-260
    • Olivieri, O.1    Girelli, D.2    Vettore, L.3    Balercia, G.4    Corrocher, R.5


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