메뉴 건너뛰기




Volumn 98, Issue 6, 2001, Pages 1645-1653

Dynamic molecular modeling of pathogenic mutations in the spectrin self-association domain

Author keywords

[No Author keywords available]

Indexed keywords

FODRIN; SPECTRIN;

EID: 0035885947     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.V98.6.1645     Document Type: Article
Times cited : (35)

References (56)
  • 1
    • 0033880909 scopus 로고    scopus 로고
    • Spectrin tethers and mesh in the biosynthetic pathway
    • De Matteis MA, Morrow JS. Spectrin tethers and mesh in the biosynthetic pathway. J Cell Sci. 2000;113:2331-2343.
    • (2000) J Cell Sci , vol.113 , pp. 2331-2343
    • De Matteis, M.A.1    Morrow, J.S.2
  • 3
    • 0032907043 scopus 로고    scopus 로고
    • Red blood cell membrane disorders
    • Tse WT, Lux SE. Red blood cell membrane disorders. Br J Haematol. 1999;104:2-13.
    • (1999) Br J Haematol , vol.104 , pp. 2-13
    • Tse, W.T.1    Lux, S.E.2
  • 4
    • 0028141959 scopus 로고
    • Differential control of band 3 lateral and rotational mobility in intact red cells
    • Corbett JD, Agre P, Palek J, Golan DE. Differential control of band 3 lateral and rotational mobility in intact red cells. J Clin Invest. 1994;94:683-688.
    • (1994) J Clin Invest , vol.94 , pp. 683-688
    • Corbett, J.D.1    Agre, P.2    Palek, J.3    Golan, D.E.4
  • 5
    • 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
  • 6
    • 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;30:21-33.
    • (1993) Semin Hematol , vol.30 , pp. 21-33
    • Delaunay, J.1    Dhermy, D.2
  • 7
    • 0002077443 scopus 로고    scopus 로고
    • Red cell membrane disorders
    • Hoffman R, Benz EJ Jr, Shattil SJ, et al. eds. New York, NY: Churchill Livingstone
    • Gallagher PG, Jarolim P. Red cell membrane disorders. In: Hoffman R, Benz EJ Jr, Shattil SJ, et al, eds. Hematology: Basic Principles and Practice. 3rd ed. New York, NY: Churchill Livingstone; 2000:576-610.
    • (2000) Hematology: Basic Principles and Practice. 3rd ed. , pp. 576-610
    • Gallagher, P.G.1    Jarolim, P.2
  • 8
    • 0027301038 scopus 로고
    • Erythroid and nonerythroid spectrins
    • Winkelmann JC, Forget BG. Erythroid and nonerythroid spectrins. Blood. 1993;81:3173-3185.
    • (1993) Blood , vol.81 , pp. 3173-3185
    • Winkelmann, J.C.1    Forget, B.G.2
  • 9
    • 0025215706 scopus 로고
    • The complete cDNA and polypeptide sequences of human erythroid α-spectrin
    • Sahr KE, Laurila P, Kotula L, et al. The complete cDNA and polypeptide sequences of human erythroid α-spectrin. J Biol Chem. 1990;265:4434-4443.
    • (1990) J Biol Chem , vol.265 , pp. 4434-4443
    • Sahr, K.E.1    Laurila, P.2    Kotula, L.3
  • 12
    • 0019522402 scopus 로고
    • Self-assembly of spectrin oligomers in vitro: A basis for a dynamic cytoskeleton
    • Morrow JS, Marchesi VT. Self-assembly of spectrin oligomers in vitro: a basis for a dynamic cytoskeleton. J Cell Biol. 1981;88:463-468.
    • (1981) J Cell Biol , vol.88 , pp. 463-468
    • Morrow, J.S.1    Marchesi, V.T.2
  • 14
    • 0020571635 scopus 로고
    • Molecular and functional changes in spectrin from patients with hereditary pyropoikilocytosis
    • Knowles WJ, Morrow JS, Speicher DW, et al. Molecular and functional changes in spectrin from patients with hereditary pyropoikilocytosis. J Clin Invest. 1983;71:1867-1877.
    • (1983) J Clin Invest , vol.71 , pp. 1867-1877
    • Knowles, W.J.1    Morrow, J.S.2    Speicher, D.W.3
  • 15
    • 0003147477 scopus 로고
    • Disorders of the red cell membrane
    • Handin RI, Lux SE, Stossel TP, eds. Philadelphia, PA: Lippincott
    • Lux SE, Palek J. Disorders of the red cell membrane. In: Handin RI, Lux SE, Stossel TP, eds. Blood: Principles and Practice of Hematology. Philadelphia, PA: Lippincott; 1995:1701-1816.
    • (1995) Blood: Principles and Practice of hematology , pp. 1701-1816
    • Lux, S.E.1    Palek, J.2
  • 16
    • 0021272595 scopus 로고
    • Erythrocyte spectrin is comprised of many homologous triple helical segments
    • Speicher DW, Marchesi VT. Erythrocyte spectrin is comprised of many homologous triple helical segments. Nature (London). 1984;311:177-180.
    • (1984) Nature (London) , vol.311 , pp. 177-180
    • Speicher, D.W.1    Marchesi, V.T.2
  • 18
    • 0029863942 scopus 로고    scopus 로고
    • The spectrin repeat folds into a three-helix bundle in solution
    • Pascual J, Pfuhl M, Rivas G, Pastore A, Saraste M. The spectrin repeat folds into a three-helix bundle in solution. FEBS Lett. 1996;383:201-207.
    • (1996) FEBS Lett , vol.383 , pp. 201-207
    • Pascual, J.1    Pfuhl, M.2    Rivas, G.3    Pastore, A.4    Saraste, M.5
  • 19
    • 0031592935 scopus 로고    scopus 로고
    • Solution structure of the spectrin repeat: A left-handed antiparallel triple-helical coiled-coll
    • Pascual J, Pfuhl M, Walther D, Saraste M, Nilges M. Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coll. J Mol Biol. 1997;273:740-751.
    • (1997) J Mol Biol , vol.273 , pp. 740-751
    • Pascual, J.1    Pfuhl, M.2    Walther, D.3    Saraste, M.4    Nilges, M.5
  • 20
    • 0018777694 scopus 로고
    • Salt and temperature-dependent conformation changes in spectrin from human erythrocyte membranes
    • Ralston GB, Dunbar JC. Salt and temperature-dependent conformation changes in spectrin from human erythrocyte membranes. Biochim Biophys Acta. 1979;579:20-30.
    • (1979) Biochim Biophys Acta , vol.579 , pp. 20-30
    • Ralston, G.B.1    Dunbar, J.C.2
  • 22
    • 0027433507 scopus 로고
    • Fourier transform infrared spectroscopic studies of the secondary structure of spectrin under different ionic strengths
    • LaBrake CC, Wang L, Keiderling TA, Fung LW. Fourier transform infrared spectroscopic studies of the secondary structure of spectrin under different ionic strengths. Biochemistry. 1993;32: 10296-10302.
    • (1993) Biochemistry , vol.32 , pp. 10296-10302
    • LaBrake, C.C.1    Wang, L.2    Keiderling, T.A.3    Fung, L.W.4
  • 23
    • 0033588274 scopus 로고    scopus 로고
    • Structures of two repeats of spectrin suggest models of flexibility
    • Grum VL, Li D, MacDonald RI, Mondragon A. Structures of two repeats of spectrin suggest models of flexibility. Cell. 1999;98:523-535.
    • (1999) Cell , vol.98 , pp. 523-535
    • Grum, V.L.1    Li, D.2    MacDonald, R.I.3    Mondragon, A.4
  • 24
    • 0024993498 scopus 로고
    • Point mutation in the beta-spectrin gene associated with alpha I/74 hereditary elliptocytosis: Implications for the mechanism of spectrin dimer self-association
    • Tse WT, Lecomte MC, Costa FF, et al. Point mutation in the beta-spectrin gene associated with alpha I/74 hereditary elliptocytosis: implications for the mechanism of spectrin dimer self-association. J Clin Invest. 1990;86:909-916.
    • (1990) J Clin Invest , vol.86 , pp. 909-916
    • Tse, W.T.1    Lecomte, M.C.2    Costa, F.F.3
  • 25
    • 0032524188 scopus 로고    scopus 로고
    • Spectrin self-association site: Characterization and study of beta-spectrin mutations associated with hereditary elliptocytosis
    • Nicolas G, Pedroni S, Fournier C, et al. Spectrin self-association site: characterization and study of beta-spectrin mutations associated with hereditary elliptocytosis. Biochem J. 1998;332:81-89.
    • (1998) Biochem J , vol.332 , pp. 81-89
    • Nicolas, G.1    Pedroni, S.2    Fournier, C.3
  • 26
    • 0027419729 scopus 로고
    • Location of the human red cell spectrin tetramer binding site and detection of a related "closed" hairpin loop dimer using proteolytic footprinting
    • Speicher DW, DeSilva TM, Speicher KD, Ursitti JA, Hembach P, Weglarz L. Location of the human red cell spectrin tetramer binding site and detection of a related "closed" hairpin loop dimer using proteolytic footprinting. J Biol Chem. 1993;268:4227-4235.
    • (1993) J Biol Chem , vol.268 , pp. 4227-4235
    • Speicher, D.W.1    DeSilva, T.M.2    Speicher, K.D.3    Ursitti, J.A.4    Hembach, P.5    Weglarz, L.6
  • 27
    • 0028245275 scopus 로고
    • A partial structural repeat forms the heterodimer self-association site of all β-spectrins
    • Kennedy SP, Weed SA, Forget BG, Morrow JS. A partial structural repeat forms the heterodimer self-association site of all β-spectrins. J Biol Chem. 1994;269:11400-11408.
    • (1994) J Biol Chem , vol.269 , pp. 11400-11408
    • Kennedy, S.P.1    Weed, S.A.2    Forget, B.G.3    Morrow, J.S.4
  • 28
    • 0033593331 scopus 로고    scopus 로고
    • Interactions of the alpha-spectrin N-terminal region with beta-spectrin: Implications for the spectrin tetramerization reaction
    • Cherry L, Menhart N, Fung LW. Interactions of the alpha-spectrin N-terminal region with beta-spectrin: implications for the spectrin tetramerization reaction. J Biol Chem. 1999;274:2077-2084.
    • (1999) J Biol Chem , vol.274 , pp. 2077-2084
    • Cherry, L.1    Menhart, N.2    Fung, L.W.3
  • 29
    • 0032960680 scopus 로고    scopus 로고
    • Properties of normal and mutant polypeptide fragments from the dimer self-association sites of human red cell spectrin
    • Lecomte MC, Nicolas G, Dhermy D, Pinder JC, Gratzer WB. Properties of normal and mutant polypeptide fragments from the dimer self-association sites of human red cell spectrin. Eur Biophys J. 1999;28:208-215.
    • (1999) Eur Biophys J , vol.28 , pp. 208-215
    • Lecomte, M.C.1    Nicolas, G.2    Dhermy, D.3    Pinder, J.C.4    Gratzer, W.B.5
  • 30
    • 4244147936 scopus 로고    scopus 로고
    • Dynamic molecular modeling of pathogenic mutations in the spectrin self-association domain
    • Zhang Z, Weed SA, Morrow JS. Dynamic molecular modeling of pathogenic mutations in the spectrin self-association domain [abstract]. FASEB J. 1999;13:A1394.
    • (1999) FASEB J , vol.13
    • Zhang, Z.1    Weed, S.A.2    Morrow, J.S.3
  • 31
    • 0003769049 scopus 로고
    • (ed X-plor pre-release version 3.851, available via the Internet [1996]). New Haven, CT: Yale University Press
    • Brünger AT. X-Plor: A system for x-ray crystallography and NMR (ed X-plor pre-release version 3.851, available via the Internet [1996]). New Haven, CT: Yale University Press; 1992.
    • (1992) X-Plor: A system for x-ray crystallography and NMR
    • Brünger, A.T.1
  • 33
    • 22944467757 scopus 로고
    • Computer experiments on classical fluid, I: Thermodynamical properties of Lennard-Jones molecules
    • Veriet L. Computer experiments on classical fluid, I: thermodynamical properties of Lennard-Jones molecules. Physical Rev. 1967;159:98-103.
    • (1967) Physical Rev , vol.159 , pp. 98-103
    • Veriet, L.1
  • 34
    • 33846446220 scopus 로고
    • Restart procedures for the conjugate gradient method
    • Powell MJD. Restart procedures for the conjugate gradient method. Mathematical Programming. 1977;12:141-254.
    • (1977) Mathematical Programming , vol.12 , pp. 141-254
    • Powell, M.J.D.1
  • 35
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux J, Haeberli P, Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 1984;12:387-395.
    • (1984) Nucleic Acids Res , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 36
    • 0031031730 scopus 로고    scopus 로고
    • Site-directed mutagenesis of αII spectrin (fodrin) reveals determinants of its μ-calpain susceptibility
    • Stabach PR, Cianci CD, Glantz SB, Zhang Z, Morrow JS. Site-directed mutagenesis of αII spectrin (fodrin) reveals determinants of its μ-calpain susceptibility. Biochemistry. 1997;36:57-65.
    • (1997) Biochemistry , vol.36 , pp. 57-65
    • Stabach, P.R.1    Cianci, C.D.2    Glantz, S.B.3    Zhang, Z.4    Morrow, J.S.5
  • 37
    • 0028927524 scopus 로고
    • Recurrent fatal hydrops fetalis associated with a nucleotide substitution in the erythrocyte beta-spectrin gene
    • Gallagher PG, Weed SA, Tse WT, et al. Recurrent fatal hydrops fetalis associated with a nucleotide substitution in the erythrocyte beta-spectrin gene [see comments]. J Clin Invest. 1995;95:1174-1182.
    • (1995) J Clin Invest , vol.95 , pp. 1174-1182
    • Gallagher, P.G.1    Weed, S.A.2    Tse, W.T.3
  • 38
    • 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 MC, Feo 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;75:1691-1698.
    • (1990) Blood , vol.75 , pp. 1691-1698
    • Garbarz, M.1    Lecomte, M.C.2    Feo, C.3
  • 39
    • 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, 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;91:2091-2096.
    • (1993) J Clin Invest , vol.91 , pp. 2091-2096
    • Wilmotte, R.1    Marechal, J.2    Morle, L.3
  • 41
    • 0030391717 scopus 로고    scopus 로고
    • Hematologically important mutations: Spectrin variants in hereditary elliptocytosis and hereditary pyropoikilocytosis
    • Gallagher PG, Forget BG. Hematologically important mutations: spectrin variants in hereditary elliptocytosis and hereditary pyropoikilocytosis. Blood Cells Mol Dis. 1996;22:254-258.
    • (1996) Blood Cells Mol Dis , vol.22 , pp. 254-258
    • Gallagher, P.G.1    Forget, B.G.2
  • 43
    • 0027438310 scopus 로고
    • Spectin Cagliari: An Ala→Gly substitution in helix 1 of beta spectrin repeat 17 that severely disrupts the structure and self-association of the erythrocyte spectrin heterodimer
    • Sahr KE, Coetzer TL, Moy LS, et al. Spectin Cagliari: an Ala→Gly substitution in helix 1 of beta spectrin repeat 17 that severely disrupts the structure and self-association of the erythrocyte spectrin heterodimer. J Biol Chem. 1993;268: 22656-22662.
    • (1993) J Biol Chem , vol.268 , pp. 22656-22662
    • Sahr, K.E.1    Coetzer, T.L.2    Moy, L.S.3
  • 44
    • 0028240888 scopus 로고
    • Identification of three novel spectrin alpha I/74 mutations in hereditary elliptocytosis: Further support for a triple-stranded folding unit model of the spectrin heterodimer contact site
    • Parquet N, Devaux I, Boulanger L, et al. Identification of three novel spectrin alpha I/74 mutations in hereditary elliptocytosis: further support for a triple-stranded folding unit model of the spectrin heterodimer contact site. Blood. 1994;84:303-308.
    • (1994) Blood , vol.84 , pp. 303-308
    • Parquet, N.1    Devaux, I.2    Boulanger, L.3
  • 45
    • 10244232936 scopus 로고    scopus 로고
    • Epidemiological studies of spectrin mutations related to hereditary elliptocytosis and spectrin polymorphisms in Benin
    • Glele-Kakai C, Garbarz M, Lecomte MC, et al. Epidemiological studies of spectrin mutations related to hereditary elliptocytosis and spectrin polymorphisms in Benin. Br J Haematol. 1996;95: 57-66.
    • (1996) Br J Haematol , vol.95 , pp. 57-66
    • Glele-Kakai, C.1    Garbarz, M.2    Lecomte, M.C.3
  • 46
    • 0030945744 scopus 로고    scopus 로고
    • Spectrin Cosenza: A novel beta chain variant associated with Sp alpha1/74 hereditary elliptocytosis
    • Qualtieri A, Pasqua A, Bisconte MG, Le Pera M, Brancati C. Spectrin Cosenza: a novel beta chain variant associated with Sp alpha1/74 hereditary elliptocytosis. Br J Haematol. 1997;97:273-278.
    • (1997) Br J Haematol , vol.97 , pp. 273-278
    • Qualtieri, A.1    Pasqua, A.2    Bisconte, M.G.3    Le Pera, M.4    Brancati, C.5
  • 47
    • 0025859449 scopus 로고
    • Occurrence of the alpha I 22 Arg→His (CGT→CAT) spectrin mutation in Tunisia: Potential association with severe elliptocytosis
    • Baklouti F, Marechal J, Morle L, et al. Occurrence of the alpha I 22 Arg→His (CGT→CAT) spectrin mutation in Tunisia: potential association with severe elliptocytosis. Br J Haematol. 1991;78:108-113.
    • (1991) Br J Haematol , vol.78 , pp. 108-113
    • Baklouti, F.1    Marechal, J.2    Morle, L.3
  • 48
    • 0025934799 scopus 로고
    • Four different mutations in codon 28 alpha spectrin are associated with structurally and functionally abnormal spectrin alpha1/74 in hereditary elliptocytosis
    • Coetzer TL, Sahr K, Prchal J, et al. Four different mutations in codon 28 alpha spectrin are associated with structurally and functionally abnormal spectrin alpha1/74 in hereditary elliptocytosis. J Clin Invest. 1991;88:743-749.
    • (1991) J Clin Invest , vol.88 , pp. 743-749
    • Coetzer, T.L.1    Sahr, K.2    Prchal, J.3
  • 49
    • 0028032248 scopus 로고
    • A variant of spectrin low-expression allele alpha LELY carrying a hereditary elliptocytosis mutation in codon 28
    • Randon J, Boulanger L, Marechal J, et al. A variant of spectrin low-expression allele alpha LELY carrying a hereditary elliptocytosis mutation in codon 28. Br J Haematol. 1994;88:534-540.
    • (1994) Br J Haematol , vol.88 , pp. 534-540
    • Randon, J.1    Boulanger, L.2    Marechal, J.3
  • 50
    • 0026076633 scopus 로고
    • Heterogeneity of the molecular basis of hereditary pyropoikilocytosis and hereditary elliptocytosis associated with increased levels of the spectrin alpha1/74-kilodalton tryptic peptide
    • Floyd PB, Gallagher PG, Valentino LA, Davis M, Marchesi SL, Forget BG. Heterogeneity of the molecular basis of hereditary pyropoikilocytosis and hereditary elliptocytosis associated with increased levels of the spectrin alpha1/74-kilodalton tryptic peptide. Blood. 1991;78:1365-1372.
    • (1991) Blood , vol.78 , pp. 1365-1372
    • Floyd, P.B.1    Gallagher, P.G.2    Valentino, L.A.3    Davis, M.4    Marchesi, S.L.5    Forget, B.G.6
  • 51
    • 0027525861 scopus 로고
    • Severe poikilocytosis associated with a de novo alpha 28 Arg→Cys mutation in spectrin
    • Lorenzo F, Miraglia del Giudice E, Alloisio N, et al. Severe poikilocytosis associated with a de novo alpha 28 Arg→Cys mutation in spectrin. Br J Haematol. 1993;83:152-157.
    • (1993) Br J Haematol , vol.83 , pp. 152-157
    • Lorenzo, F.1    Miraglia del Giudice, E.2    Alloisio, N.3
  • 52
    • 0028206127 scopus 로고
    • Mild elliptocytosis associated with the alpha 34 Arg→Trp mutation in Genova (alpha I/74)
    • Perrotta S, Miraglia del Giudice E, Alloisio N, et al. Mild elliptocytosis associated with the alpha 34 Arg→Trp mutation in Genova (alpha I/74). Blood. 1994;83:3346-3349.
    • (1994) Blood , vol.83 , pp. 3346-3349
    • Perrotta, S.1    Miraglia del Giudice, E.2    Alloisio, N.3
  • 53
    • 0024348471 scopus 로고
    • Spectrin Tunis (Sp alpha I/78), an elliptocytogenic variant, is due to the CGG→TGG condon change (Arg→Trp) at position 35 of the alpha I domain
    • Morle L, Morle F, Roux AF, et al. Spectrin Tunis (Sp alpha I/78), an elliptocytogenic variant, is due to the CGG→TGG condon change (Arg→Trp) at position 35 of the alpha I domain. Blood. 1989;74: 828-832.
    • (1989) Blood , vol.74 , pp. 828-832
    • Morle, L.1    Morle, F.2    Roux, A.F.3
  • 54
    • 0024314456 scopus 로고
    • Sp alpha I/78: A mutation of the alpha I spectrin domain in a white kindred with HE and HPP phenotypes
    • Lecomte MC, Garbarz M, Grandchamp B, et al. Sp alpha I/78: a mutation of the alpha I spectrin domain in a white kindred with HE and HPP phenotypes. Blood. 1989;74:1126-1133.
    • (1989) Blood , vol.74 , pp. 1126-1133
    • Lecomte, M.C.1    Garbarz, M.2    Grandchamp, B.3
  • 55
    • 0028899466 scopus 로고
    • Spectrin Anastasia (alpha I/78): A new spectrin variant (alpha 45 Arg→Thr) with moderate elliptocytogenic potential
    • Perrotta S, Iolascon A, De Angelis F, et al. Spectrin Anastasia (alpha I/78): a new spectrin variant (alpha 45 Arg→Thr) with moderate elliptocytogenic potential. Br J Haematol. 1995;89:933-936.
    • (1995) Br J Haematol , vol.89 , pp. 933-936
    • Perrotta, S.1    Iolascon, A.2    De Angelis, F.3
  • 56
    • 11944274698 scopus 로고
    • Two elliptocytogenic alpha I/74 variants of the spectrin alpha I domain: Spectrin Culoz (GGT→GTT; alpha I 40 Gly→Val) and spectrin Lyon (CTT→TTT, alpha I 43 Leu→Phe)
    • Morle L, Roux AF, Alloisio N, et al. Two elliptocytogenic alpha I/74 variants of the spectrin alpha I domain: Spectrin Culoz (GGT→GTT; alpha I 40 Gly→Val) and spectrin Lyon (CTT→TTT, alpha I 43 Leu→Phe). J Clin Invest. 1990;86:548-554.
    • (1990) J Clin Invest , vol.86 , pp. 548-554
    • Morle, L.1    Roux, A.F.2    Alloisio, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.