메뉴 건너뛰기




Volumn 111, Issue 12, 2008, Pages 5712-5720

Structural and functional effects of hereditary hemolytic anemia-associated point mutations in the alpha spectrin tetramer site

Author keywords

[No Author keywords available]

Indexed keywords

FODRIN; MUTANT PROTEIN; RECOMBINANT PROTEIN; TETRAMER; SPECTRIN;

EID: 47049089420     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2007-11-122457     Document Type: Article
Times cited : (42)

References (64)
  • 1
    • 0032907043 scopus 로고    scopus 로고
    • Red blood cell membrane disorders
    • Tse WT. Lux SE. Red blood cell membrane disorders. BrJ Haematol. 1999;104:2-13.
    • (1999) BrJ Haematol , vol.104 , pp. 2-13
    • Tse, W.T.1    Lux, S.E.2
  • 3
    • 1942445176 scopus 로고    scopus 로고
    • Hereditary elliptocytosis: Spectrin and protein 4.1 R
    • Gallagher PG. Hereditary elliptocytosis: spectrin and protein 4.1 R. Semin Hematol. 2004;41:142-164.
    • (2004) Semin Hematol , vol.41 , pp. 142-164
    • Gallagher, P.G.1
  • 4
    • 33846274937 scopus 로고    scopus 로고
    • The molecular basis of hereditary red cell membrane disorders
    • Delaunay J. The molecular basis of hereditary red cell membrane disorders. Blood Rev. 2007;21:1- 20.
    • (2007) Blood Rev , vol.21 , pp. 1-20
    • Delaunay, J.1
  • 5
    • 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. 1984;311:177-180.
    • (1984) Nature , vol.311 , pp. 177-180
    • Speicher, D.W.1    Marchesi, V.T.2
  • 6
    • 0025215706 scopus 로고
    • The complete cDNA and polypeptide sequences of human ery-throid alpha-spectrin
    • Sahr KE, Laurila P, Kotula L, et al. The complete cDNA and polypeptide sequences of human ery-throid alpha-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
  • 9
    • 0026653822 scopus 로고
    • Properties of human red cell spectrin heterodimer (side-to-side) assembly and identification of an essential nucleation site
    • Speicher DW, Weglarz L, DeSilva TM. Properties of human red cell spectrin heterodimer (side-to-side) assembly and identification of an essential nucleation site. J Biol Chem. 1992;267:14775-14782.
    • (1992) J Biol Chem , vol.267 , pp. 14775-14782
    • Speicher, D.W.1    Weglarz, L.2    DeSilva, T.M.3
  • 10
    • 0028000263 scopus 로고
    • Interchain binding at the tail of the Drosophila spectrin molecule
    • Viel A, Branton D. Interchain binding at the tail of the Drosophila spectrin molecule. Proc Natl Acad Sci U S A 1994;91:10839-10843.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 10839-10843
    • Viel, A.1    Branton, D.2
  • 11
    • 0029913841 scopus 로고    scopus 로고
    • Mapping the human erythrocyte beta-spectrin dimer initiation site using recombinant peptides and correlation of its phasing with the alpha-actinin dimer site
    • Ursitti JA, Kotula L, DeSilvaTM, Curtis PJ, Speicher DW. Mapping the human erythrocyte beta-spectrin dimer initiation site using recombinant peptides and correlation of its phasing with the alpha-actinin dimer site. J Biol Chem. 1996; 271:6636-6644.
    • (1996) J Biol Chem , vol.271 , pp. 6636-6644
    • Ursitti, J.A.1    Kotula, L.2    DeSilva, T.M.3    Curtis, P.J.4    Speicher, D.W.5
  • 12
    • 0018099901 scopus 로고
    • Self-association of human spectrin: A thermodynamic and kinetic study
    • Ungewickell E, GratzerW. Self-association of human spectrin: a thermodynamic and kinetic study. Eur J Biochem. 1978;88:379-385.
    • (1978) Eur J Biochem , vol.88 , pp. 379-385
    • Ungewickell, E.1    GratzerW2
  • 13
    • 0018188805 scopus 로고
    • Physical-chemical studies of spectrin
    • Ralston GB. Physical-chemical studies of spectrin. J Supramol Struct. 1978;8:361-373.
    • (1978) J Supramol Struct , vol.8 , pp. 361-373
    • Ralston, G.B.1
  • 14
    • 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
  • 15
    • 0026470325 scopus 로고    scopus 로고
    • DeSilvaTM, Peng KC. Speicher KD, Speicher DW. Analysis of human red cell spectrin tetramer (head-to-head) assembly using complementary univalent peptides. Biochemistry. 1992;31:10872-10878.
    • DeSilvaTM, Peng KC. Speicher KD, Speicher DW. Analysis of human red cell spectrin tetramer (head-to-head) assembly using complementary univalent peptides. Biochemistry. 1992;31:10872-10878.
  • 16
    • 0027419729 scopus 로고
    • Location of the human red cell spectrin tetramer binding site and detection of a related ''closed hairpin loop dimer using proteolyticfootprinting
    • 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 proteolyticfootprinting. 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
  • 17
    • 0023150141 scopus 로고
    • Visualization of the hexagonal lattice in the erythrocyte membrane skeleton
    • Liu SC, DerickLH, Palek J. Visualization of the hexagonal lattice in the erythrocyte membrane skeleton. J Cell Biol. 1987;104:527-536.
    • (1987) J Cell Biol , vol.104 , pp. 527-536
    • Liu, S.C.1    Derick, L.H.2    Palek, J.3
  • 18
    • 0022344550 scopus 로고
    • Visualization of the protein associations in the erythrocyte membrane skeleton
    • Byers TJ, Branton D. Visualization of the protein associations in the erythrocyte membrane skeleton. Proc Natl Acad Sci U S A 1985;82:6153-6157.
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 6153-6157
    • Byers, T.J.1    Branton, D.2
  • 19
    • 0018759538 scopus 로고
    • The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes
    • Bennett V, Stenbuck PJ. The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes. Nature. 1979;280:468-473.
    • (1979) Nature , vol.280 , pp. 468-473
    • Bennett, V.1    Stenbuck, P.J.2
  • 20
    • 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
  • 21
    • 23244437029 scopus 로고    scopus 로고
    • Identification and functional characterization of protein 4.1 R and actin-binding sites in erythrocyte beta spectrin: Regulation of the interactions by phosphatidylinositol-4,5- bisphosphate
    • An X, Debnath G, Guo X, et al. Identification and functional characterization of protein 4.1 R and actin-binding sites in erythrocyte beta spectrin: regulation of the interactions by phosphatidylinositol-4,5- bisphosphate. Biochemistry. 2005;44:10681-10688.
    • (2005) Biochemistry , vol.44 , pp. 10681-10688
    • An, X.1    Debnath, G.2    Guo, X.3
  • 22
    • 0028917977 scopus 로고
    • Identification of the protein 4.1 binding interface on glycophorin C and p55, a homologue of the Drosophila discs-large tumor suppressor protein
    • Marfatia SM, Leu RA, Branton D, Chishti AH. Identification of the protein 4.1 binding interface on glycophorin C and p55, a homologue of the Drosophila discs-large tumor suppressor protein. J Biol Chem. 1995;270:715-719.
    • (1995) J Biol Chem , vol.270 , pp. 715-719
    • Marfatia, S.M.1    Leu, R.A.2    Branton, D.3    Chishti, A.H.4
  • 23
    • 0028944110 scopus 로고
    • Identification of the membrane attachment sites for protein 4.1 in the human erythrocyte
    • Hemming NJ, Anstee DJ, Staricoff MA, Tanner MJ, Mohandas N. Identification of the membrane attachment sites for protein 4.1 in the human erythrocyte. J Biol Chem. 1995;270:5360-5366.
    • (1995) J Biol Chem , vol.270 , pp. 5360-5366
    • Hemming, N.J.1    Anstee, D.J.2    Staricoff, M.A.3    Tanner, M.J.4    Mohandas, N.5
  • 24
    • 0037200093 scopus 로고    scopus 로고
    • Shear-response of the spectrin dimer- tetramer equilibrium in the red blood cell membrane
    • An X, Lecomte MC, Chasis JA, Mohandas N, Gratzer W. Shear-response of the spectrin dimer- tetramer equilibrium in the red blood cell membrane. J Biol Chem. 2002;277:31796-31800.
    • (2002) J Biol Chem , vol.277 , pp. 31796-31800
    • An, X.1    Lecomte, M.C.2    Chasis, J.A.3    Mohandas, N.4    Gratzer, W.5
  • 25
    • 0009509734 scopus 로고
    • Defective spectrin dimer-dimer association with hereditary elliptocy- tosis
    • Liu SC. Palek J, Prchal JT. Defective spectrin dimer-dimer association with hereditary elliptocy- tosis. Proc Natl Acad Sci USA. 1982;79:2072- 2076.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 2072-2076
    • Liu, S.C.1    Palek, J.2    Prchal, J.T.3
  • 26
    • 0020051666 scopus 로고
    • Spectrin tetramer-dimer equilibrium in hereditary elliptocytosis
    • Coetzer T. Zail S. Spectrin tetramer-dimer equilibrium in hereditary elliptocytosis. Blood. 1982;59: 900-905.
    • (1982) Blood , vol.59 , pp. 900-905
    • Coetzer, T.1    Zail, S.2
  • 27
    • 0019967052 scopus 로고
    • Spectrin beta-chain variant associated with hereditary elliptocytosis
    • Dhermy D, Lecomte MC, Garbarz M, et al. Spectrin beta-chain variant associated with hereditary elliptocytosis. J Clin Invest. 1982;70:707-715.
    • (1982) J Clin Invest , vol.70 , pp. 707-715
    • Dhermy, D.1    Lecomte, M.C.2    Garbarz, M.3
  • 28
    • 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
  • 29
    • 0031017565 scopus 로고    scopus 로고
    • Mutation of a highly conserved residue of betal spectrin associated with fatal and near-fatal neonatal hemolytic anemia
    • Gallagher PG, Petruzzi MJ, Weed SA, et al. Mutation of a highly conserved residue of betal spectrin associated with fatal and near-fatal neonatal hemolytic anemia. J Clin Invest. 1997;99:267- 277.
    • (1997) J Clin Invest , vol.99 , pp. 267-277
    • Gallagher, P.G.1    Petruzzi, M.J.2    Weed, S.A.3
  • 30
    • 0027438310 scopus 로고
    • Spectrin ca- gliari: 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. Spectrin ca- gliari: 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
  • 31
    • 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
  • 32
    • 10244232936 scopus 로고    scopus 로고
    • Epidemiologic studies of spectrin mutations related to hereditary elliptocytosis and spectrin polymorphisms in Benin
    • Glele-Kakai C, Garbarz M, Lecomte MC, et al. Epidemiologic 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
  • 33
    • 0030945744 scopus 로고    scopus 로고
    • Spectrin Cosenza: A novel beta chain variant associated with Sp alphal/74 hereditary elliptocytosis
    • Qualtieri A, Pasqua A, Bisconte MG, Le Pera M, Brancati C. Spectrin Cosenza: a novel beta chain variant associated with Sp alphal/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
  • 34
    • 0025859449 scopus 로고
    • Occurrence of the alpha I 22Arg→His (CGT→CAT) spectrin mutation in Tunisia: Potential association with severe elliptopoikilocytosis
    • Baklouti F, Marechal J, Morle L, et al. Occurrence of the alpha I 22Arg→His (CGT→CAT) spectrin mutation in Tunisia: potential association with severe elliptopoikilocytosis. 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
  • 35
    • 0025934799 scopus 로고
    • Fourdifferent mutations in codon 28 of alpha spectrin are associated with structurally and functionally abnormal spectrin alpha I/74 in hereditary elliptocytosis
    • Coetzer TL, Sahr K, Prchal J, et al. Fourdifferent mutations in codon 28 of alpha spectrin are associated with structurally and functionally abnormal spectrin alpha I/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
  • 36
    • 0028032248 scopus 로고
    • Avari-ant of spectrin low-expression allele alpha LELY carrying a hereditary elliptocytosis mutation in codon 28
    • Randon J, Boulanger L. Marechal J. et al. Avari-ant 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
  • 37
    • 0026076633 scopus 로고
    • Heterogeneity of the molecular basis of hereditary pyropoikilocytosis and hereditary elliptocytosis associated with increased levels of the spectrin alpha I/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 alpha I/74-kilodalton tryptic peptide. Blood. 1991 ;78:1364-1372.
    • (1991) Blood , vol.78 , pp. 1364-1372
    • Floyd, P.B.1    Gallagher, P.G.2    Valentino LA Davis, M.3    Marchesi, S.L.4    Forget, B.G.5
  • 38
    • 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
  • 39
    • 0028206127 scopus 로고
    • Mild elliptocytosis associated with the alpha 34 Arg→Trp mutation in spectrin Geneva (alpha I/74)
    • Perrotta S, Miraglia del Giudice E, Alloisio N, et al. Mild elliptocytosis associated with the alpha 34 Arg→Trp mutation in spectrin Geneva (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
  • 40
    • 0024348471 scopus 로고    scopus 로고
    • Morle L, Morle F RouxAF, et al. Spectrin Tunis (Sp alpha I/78), an elliptocytogenic variant, is due to the CGG→TGG codon change (Arg→Trp) at position 35 of the alpha I domain. Blood. 1989;74: 828-832.
    • Morle L, Morle F RouxAF, et al. Spectrin Tunis (Sp alpha I/78), an elliptocytogenic variant, is due to the CGG→TGG codon change (Arg→Trp) at position 35 of the alpha I domain. Blood. 1989;74: 828-832.
  • 41
    • 0024314456 scopus 로고
    • Sp alpha I/78: A mutation of the alpha I spectrin domain in a white kindred with HE and HPP phe-notypes
    • Lecomte MG, 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 phe-notypes. Blood. 1989;74:1126-1133.
    • (1989) Blood , vol.74 , pp. 1126-1133
    • Lecomte, M.G.1    Garbarz, M.2    Grandchamp, B.3
  • 42
    • 0028899466 scopus 로고
    • Spectrin Anastasia (alpha I/78): A new spectrin variant (alpha 45 Arg→Thr) with moderate elliptocytogenic potential
    • Perrotta S, lolascon A, DeAngelis F, etal. 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    lolascon, A.2    DeAngelis, F.3
  • 43
    • 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, RouxAF 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    RouxAF Alloisio, N.2
  • 44
    • 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. 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
  • 45
    • 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, Féo 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    Féo, C.3
  • 46
    • 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, et al. An alpha-spectrin mutation responsible for hereditary elliptocytosis associated in cis with the alpha v/41 polymorphism. Hum Genet. 1993;90:641-644.
    • (1993) Hum Genet , vol.90 , pp. 641-644
    • Dalla Venezia, N.1    Wilmotte, R.2    Morle, L.3
  • 47
    • 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 skip-ping of exon 46
    • Wilmotte R, Maréchal J, Morlé 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 skip-ping of exon 46. J Clin Invest. 1993;91:2091-2096.
    • (1993) J Clin Invest , vol.91 , pp. 2091-2096
    • Wilmotte, R.1    Maréchal, J.2    Morlé, L.3
  • 48
    • 0036660204 scopus 로고    scopus 로고
    • Nuclear magnetic resonance studies of mutations at the tetramer- ization region of human alpha spectrin
    • Park S, Johnson ME, Fung LW. Nuclear magnetic resonance studies of mutations at the tetramer- ization region of human alpha spectrin. Blood. 2002;100:283-288.
    • (2002) Blood , vol.100 , pp. 283-288
    • Park, S.1    Johnson, M.E.2    Fung, L.W.3
  • 49
    • 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
  • 50
    • 0027181238 scopus 로고
    • Molecular basis of spectrin deficiency in hereditary pyropoikilocytosis
    • Hanspal M, Hanspal JS, Sahr KE, Fibach E, Nachman J, Palek J. Molecular basis of spectrin deficiency in hereditary pyropoikilocytosis. Blood. 1993;82:1652-1660.
    • (1993) Blood , vol.82 , pp. 1652-1660
    • Hanspal, M.1    Hanspal, J.S.2    Sahr, K.E.3    Fibach, E.4    Nachman, J.5    Palek, J.6
  • 51
    • 0027181844 scopus 로고
    • Functional characterization of recombinant human red cell alpha-spectrin polypeptides containing the tetramer binding site
    • Kotula L, DeSilvaTM, Speicher DW, Curtis PJ. Functional characterization of recombinant human red cell alpha-spectrin polypeptides containing the tetramer binding site. J Biol Ghem. 1993; 268:14788-14793.
    • (1993) J Biol Ghem , vol.268 , pp. 14788-14793
    • Kotula, L.1    DeSilva, T.M.2    Speicher, D.W.3    Curtis, P.J.4
  • 52
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace CN, Vajdos F, Fee L, Grimsley G, Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 1995;4:2411-2423.
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 53
    • 0035928821 scopus 로고    scopus 로고
    • Role of terminal nonhomologous domains in initiation of human red cell spectrin dimerization
    • Harper SL, Begg G E, Speicher DW. Role of terminal nonhomologous domains in initiation of human red cell spectrin dimerization. Biochemistry. 2001 ;40:9935-9943.
    • (2001) Biochemistry , vol.40 , pp. 9935-9943
    • Harper, S.L.1    Begg, G.E.2    Speicher, D.W.3
  • 54
    • 0034602955 scopus 로고    scopus 로고
    • Initiation of spectrin dimerization involves complementary electrostatic interactions between paired triple-helical bundles
    • Begg GE, Harper SL, Morris MB, Speicher DW. Initiation of spectrin dimerization involves complementary electrostatic interactions between paired triple-helical bundles. J Biol Chem. 2000; 275:3279-3287.
    • (2000) J Biol Chem , vol.275 , pp. 3279-3287
    • Begg, G.E.1    Harper, S.L.2    Morris, M.B.3    Speicher, D.W.4
  • 55
    • 0001038767 scopus 로고
    • Equilibrium ultracentrifugation of dilute solutions
    • Yphantis DA. Equilibrium ultracentrifugation of dilute solutions. Biochemistry. 1964;3:297-317.
    • (1964) Biochemistry , vol.3 , pp. 297-317
    • Yphantis, D.A.1
  • 56
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultracen- trifuge by nonlinear least-squares techniques
    • Johnson ML, Correia JJ, Yphantis DA, Halvorson HR. Analysis of data from the analytical ultracen- trifuge by nonlinear least-squares techniques. Biophys J. 1981 ;36:575-588.
    • (1981) Biophys J , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4
  • 57
    • 34548767082 scopus 로고    scopus 로고
    • Initiation and propagation of spectrin heterodimer assembly involves distinct energetic processes
    • Li D, Harper S, Speicher DW. Initiation and propagation of spectrin heterodimer assembly involves distinct energetic processes. Biochemistry. 2007;46:10585-10594.
    • (2007) Biochemistry , vol.46 , pp. 10585-10594
    • Li, D.1    Harper, S.2    Speicher, D.W.3
  • 58
    • 0023019557 scopus 로고
    • Analysis of the self- association of human red cell spectrin
    • Shahbakhti F, Gratzer WB. Analysis of the self- association of human red cell spectrin. Biochemistry. 1986;25:5969-5975.
    • (1986) Biochemistry , vol.25 , pp. 5969-5975
    • Shahbakhti, F.1    Gratzer, W.B.2
  • 59
    • 0027930961 scopus 로고
    • The concentration dependence of the activity coefficient of the human spectrin heterodimer: A quantitative test of the Adams-Fujita approximation
    • Ralston GB. The concentration dependence of the activity coefficient of the human spectrin heterodimer: a quantitative test of the Adams-Fujita approximation. Biophys Chem. 1994;52:51-61.
    • (1994) Biophys Chem , vol.52 , pp. 51-61
    • Ralston, G.B.1
  • 60
    • 0141679134 scopus 로고    scopus 로고
    • Spectrin alpha II and beta II isoforms interact with high affinity at the tetramerization site
    • Bignone PA, Baines AJ. Spectrin alpha II and beta II isoforms interact with high affinity at the tetramerization site. Biochem J. 2003;374:613-624.
    • (2003) Biochem J , vol.374 , pp. 613-624
    • Bignone, P.A.1    Baines, A.J.2
  • 61
    • 34147151815 scopus 로고    scopus 로고
    • Pathogenic proline mutation in the linker between spectrin repeats: Disease caused by spectrin unfolding
    • Johnson CP, Gaetani M, Ortiz V, et al. Pathogenic proline mutation in the linker between spectrin repeats: disease caused by spectrin unfolding. Blood. 2007;109:3538-3543.
    • (2007) Blood , vol.109 , pp. 3538-3543
    • Johnson, C.P.1    Gaetani, M.2    Ortiz, V.3
  • 62
    • 31444453626 scopus 로고    scopus 로고
    • Mammalian al-spectrin is a neo-functionalized polypeptide adapted to small highly deformable erythrocytes
    • Salomao M, An X, Guo X, Gratzer WB, Mohansas N, Baines AJ. Mammalian al-spectrin is a neo-functionalized polypeptide adapted to small highly deformable erythrocytes. Proc Natl Acad Sci USA. 2006;103:643-648.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 643-648
    • Salomao, M.1    An, X.2    Guo, X.3    Gratzer, W.B.4    Mohansas, N.5    Baines, A.J.6
  • 63
    • 0035885947 scopus 로고    scopus 로고
    • Dynamic molecular modeling of pathogenic mutations in the spectrin self-association domain
    • Zhang Z, Weed SA, Gallagher PG, Morrow JS. Dynamic molecular modeling of pathogenic mutations in the spectrin self-association domain. Blood. 2001;98:1645-1653.
    • (2001) Blood , vol.98 , pp. 1645-1653
    • Zhang, Z.1    Weed, S.A.2    Gallagher, P.G.3    Morrow, J.S.4
  • 64
    • 84869242126 scopus 로고    scopus 로고
    • National Center for Biotechnology Information database, Accessed December 12, 2007
    • National Center for Biotechnology Information database, http://www.ncbi.nlm.nih.gov/blast/Blast.cgi. Accessed December 12, 2007.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.