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Volumn 90, Issue 10, 1997, Pages 4188-4196

The exon 46-encoded sequence is essential for stability of human erythroid α-spectrin and heterodimer formation

Author keywords

[No Author keywords available]

Indexed keywords

FODRIN; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; SPECTRIN; SULFUR 35;

EID: 0030781493     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v90.10.4188     Document Type: Article
Times cited : (23)

References (30)
  • 2
    • 0023840556 scopus 로고
    • The Duffy blood group is linked to the α-spectrin locus in a large pedigree with autosomal dominant inheritance of Charot-Marie-Tooth disease type 1
    • Raeymaekers P, Van Broeckhoven C, Backhovens H, Wehnert A, Muylle L, De Jonghe P, Gheuens J, Vandenberghe A: The Duffy blood group is linked to the α-spectrin locus in a large pedigree with autosomal dominant inheritance of Charot-Marie-Tooth disease type 1. Hum Genet 78:76, 1988
    • (1988) Hum Genet , vol.78 , pp. 76
    • Raeymaekers, P.1    Van Broeckhoven, C.2    Backhovens, H.3    Wehnert, A.4    Muylle, L.5    De Jonghe, P.6    Gheuens, J.7    Vandenberghe, A.8
  • 8
    • 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 311:177, 1984
    • (1984) Nature , vol.311 , pp. 177
    • Speicher, D.W.1    Marchesi, V.T.2
  • 12
    • 0022532739 scopus 로고
    • A calmodulin and α-subunit binding domain in human erythrocyte spectrin
    • Sears DE, Marchesi VT, Morrow JS: A calmodulin and α-subunit binding domain in human erythrocyte spectrin. Biochim Biophys Acta 870:432, 1986
    • (1986) Biochim Biophys Acta , vol.870 , pp. 432
    • Sears, D.E.1    Marchesi, V.T.2    Morrow, J.S.3
  • 13
    • 0025993140 scopus 로고
    • Characterization of the lateral interaction between human erythrocyte spectrin subunits
    • Yoshino H, Minari O: Characterization of the lateral interaction between human erythrocyte spectrin subunits. J Biochem 110:553, 1991
    • (1991) J Biochem , vol.110 , pp. 553
    • Yoshino, H.1    Minari, O.2
  • 14
    • 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 267:14775, 1992
    • (1992) J Biol Chem , vol.267 , pp. 14775
    • Speicher, D.W.1    Weglarz, L.2    DeSilva, T.M.3
  • 15
    • 0028000263 scopus 로고
    • Interchain binding at the tail end of the Drosophila spectrin molecule
    • Viel A, Branton D: Interchain binding at the tail end of the Drosophila spectrin molecule. Proc Natl Acad Sci USA 91:10839, 1994
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10839
    • Viel, A.1    Branton, D.2
  • 17
    • 0029913841 scopus 로고    scopus 로고
    • Mapping the human erythrocyte β-spectrin dimer initiation site using recombinant peptides and correlation of its phasing with the α-actinin dimer site
    • Ursitti JA, Kotula L, DeSilva TM, Curtis PJ, Speicher DW: Mapping the human erythrocyte β-spectrin dimer initiation site using recombinant peptides and correlation of its phasing with the α-actinin dimer site. J Biol Chem 271:6636, 1996
    • (1996) J Biol Chem , vol.271 , pp. 6636
    • Ursitti, J.A.1    Kotula, L.2    DeSilva, T.M.3    Curtis, P.J.4    Speicher, D.W.5
  • 20
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith DB, Johnson KS: Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67:31, 1988
    • (1988) Gene , vol.67 , pp. 31
    • Smith, D.B.1    Johnson, K.S.2
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680, 1970
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 22
    • 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 268:4227, 1993
    • (1993) J Biol Chem , vol.268 , pp. 4227
    • Speicher, D.W.1    DeSilva, T.M.2    Speicher, K.D.3    Ursitti, J.A.4    Hembach, P.5    Weglarz, L.6
  • 23
    • 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 4:2411, 1995
    • (1995) Protein Sci , vol.4 , pp. 2411
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 24
    • 0026521693 scopus 로고
    • High yield electroblotting onto polyvinylidene difluoride membranes from polyacrylamide gels
    • Mozdzanowski J, Hembach P, Speicher DW: High yield electroblotting onto polyvinylidene difluoride membranes from polyacrylamide gels. Electrophoresis 13:59, 1992
    • (1992) Electrophoresis , vol.13 , pp. 59
    • Mozdzanowski, J.1    Hembach, P.2    Speicher, D.W.3
  • 25
    • 0027982842 scopus 로고
    • A method for high-performance sequence analysis using polyvinylidene difluoride membranes with a biphasic reaction column sequencer
    • Reim DF, Speicher DW: A method for high-performance sequence analysis using polyvinylidene difluoride membranes with a biphasic reaction column sequencer. Anal Biochem 216:213, 1994
    • (1994) Anal Biochem , vol.216 , pp. 213
    • Reim, D.F.1    Speicher, D.W.2
  • 26
    • 0023646806 scopus 로고
    • From genes to structural morphogenesis: The genesis and epigenesis of a red blood cell
    • Lazarides E: From genes to structural morphogenesis: The genesis and epigenesis of a red blood cell. Cell 51:345, 1987
    • (1987) Cell , vol.51 , pp. 345
    • Lazarides, E.1
  • 27
    • 0023582256 scopus 로고
    • Synthesis and assembly of membrane skeletal proteins in mammalian red cell precursors
    • Hanspal M, Palek J: Synthesis and assembly of membrane skeletal proteins in mammalian red cell precursors. J Cell Biol 105:1417, 1987
    • (1987) J Cell Biol , vol.105 , pp. 1417
    • Hanspal, M.1    Palek, J.2
  • 30
    • 0003147477 scopus 로고
    • Disorders of the red cell membrane
    • Handin R, Lux SE, Stossel TP (eds): Philadelphia, PA, Lippincott
    • Lux SE, Palek J: Disorders of the red cell membrane, in Handin R, Lux SE, Stossel TP (eds): Blood: Principles and Practice of Hematology. Philadelphia, PA, Lippincott, 1995, p 1701
    • (1995) Blood: Principles and Practice of Hematology , pp. 1701
    • Lux, S.E.1    Palek, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.