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Volumn 6, Issue 3, 2001, Pages 571-585

Studies of the erythrocyte spectrin tetramerization region

Author keywords

EPR; Erythrocyte; NMR; Recombinant Peptides; Spectrin; Tetramerization

Indexed keywords

GALLUS GALLUS;

EID: 0035236645     PISSN: 14258153     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (7)

References (27)
  • 2
    • 0033588274 scopus 로고    scopus 로고
    • Structures of two-repeats of spectrin suggest models of flexibility
    • Grum, V.L., Li, D., MacDonald, R.I. and Mondragon, A. Structures of two-repeats of spectrin suggest models of flexibility. Cell 98 (1999) 523-535.
    • (1999) Cell , vol.98 , pp. 523-535
    • Grum, V.L.1    Li, D.2    MacDonald, R.I.3    Mondragon, A.4
  • 3
    • 0031592935 scopus 로고    scopus 로고
    • Solution structure of the spectrin repeat: A left-handed antiparallel triple-helical coiled-coil
    • Pascual, J., Pfuhl, M., Walther, D., Saraste, M. and Nilges, M. Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil. J. Mol. Biol. 273 (1997) 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
  • 4
    • 0026653822 scopus 로고
    • Properties of human red cell spectrin heterodimer (site-to-site) assembly and identification of an essential nucleation site
    • Speicher, D.W., Weglarz, L. and DeSilva, T.M. Properties of human red cell spectrin heterodimer (site-to-site) assembly and identification of an essential nucleation site. J. Biol. Chem. 267 (1992) 14775-14782.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14775-14782
    • Speicher, D.W.1    Weglarz, L.2    Desilva, T.M.3
  • 6
    • 0033593331 scopus 로고    scopus 로고
    • Interactions of the alpha-spectrin N-terminal region with beta-spectrin. Implications for the spectrin tetramerization reaction
    • Cherry, L.C., Menhart, N. and Fung, L.W.-M. Interactions of the alpha-spectrin N-terminal region with beta-spectrin. Implications for the spectrin tetramerization reaction. J. Biol. Chem. 274 (1999), 2077-2084.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2077-2084
    • Cherry, L.C.1    Menhart, N.2    Fung, L.W.-M.3
  • 7
    • 0021022472 scopus 로고
    • Structure of human erythrocyte spectrin. II. The sequence of the α-I domain
    • Speicher, D.W., Davis, G. and Marchesi, V.T. Structure of human erythrocyte spectrin. II. The sequence of the α-I domain. J. Biol. Chem. 258 (1983) 14938-14947.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14938-14947
    • Speicher, D.W.1    Davis, G.2    Marchesi, V.T.3
  • 8
    • 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, D.W., DeSilva, T.M., Speicher, K.D., Ursitti, J.A., Hembach, P. and 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 (1993) 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
  • 9
    • 0034602955 scopus 로고    scopus 로고
    • Initiation of spectrin dimerization involves complementary electrostatic interactions between paired triple-helical bundles
    • Begg, G.E., Harper, S.L., Morris, M.B. and Speicher, D.W. Initiation of spectrin dimerization involves complementary electrostatic interactions between paired triple-helical bundles. J. Biol. Chem. 275 (2000) 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
  • 10
    • 0020051666 scopus 로고
    • Spectrin tetramer-dimer equilibrium in hereditary elliptocytosis
    • Coetzer, T. and Zail S. Spectrin tetramer-dimer equilibrium in hereditary elliptocytosis. Blood 59 (1982) 900-905.
    • (1982) Blood , vol.59 , pp. 900-905
    • Coetzer, T.1    Zail, S.2
  • 12
    • 0019166431 scopus 로고
    • Identification of proteolytically resistant domains of human erythrocyte spectrin
    • Speicher, D.W., Morrow, J.S., Knowles, W.J. and Marchesi, V.T. Identification of proteolytically resistant domains of human erythrocyte spectrin. Proc. Natl. Acad. Sci. USA. 77 (1980) 5673-5677.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 5673-5677
    • Speicher, D.W.1    Morrow, J.S.2    Knowles, W.J.3    Marchesi, V.T.4
  • 13
    • 0027478129 scopus 로고
    • Mutations involving the spectrin heterodimer contact site: Clinical expression and alterations in specific function
    • Delaunay, J. and Dhermy, D. Mutations involving the spectrin heterodimer contact site: clinical expression and alterations in specific function. Semin. Hematol. 30 (1993) 21-33.
    • (1993) Semin. Hematol. , vol.30 , pp. 21-33
    • Delaunay, J.1    Dhermy, D.2
  • 15
    • 0029825450 scopus 로고    scopus 로고
    • Peptides with more than one 106-amino-acid sequence motif are needed to mimic the structural stability of spectrin
    • Menhart, N.M., Mitchell, T., Lusitani, D., Topouzian, N. and Fung, L.W.-M. Peptides with more than one 106-amino-acid sequence motif are needed to mimic the structural stability of spectrin J. Biol. Chem. 271 (1996) 30410-30416.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30410-30416
    • Menhart, N.M.1    Mitchell, T.2    Lusitani, D.3    Topouzian, N.4    Fung, L.W.-M.5
  • 16
    • 0032564376 scopus 로고    scopus 로고
    • Ionic strength effect on the thermal unfolding of a-spectrin peptides
    • Lusitani, D., Menhart, N.M., Keiderling, T.A. and Fung, L.W.-M. Ionic strength effect on the thermal unfolding of a-spectrin peptides. Biochemistry 37 (1998) 16546-16554.
    • (1998) Biochemistry , vol.37 , pp. 16546-16554
    • Lusitani, D.1    Menhart, N.M.2    Keiderling, T.A.3    Fung, L.W.-M.4
  • 18
    • 0033978990 scopus 로고    scopus 로고
    • Spin-Label EPR Structural studies of the N-terminus of a-spectrin
    • Cherry, L. Menhart, N. and Fung, L.W.-M. Spin-Label EPR Structural studies of the N-terminus of a-spectrin, FEBS Lett. 466 (2000) 341-345.
    • (2000) FEBS Lett. , vol.466 , pp. 341-345
    • Cherry, L.1    Menhart, N.2    Fung, L.W.-M.3
  • 19
    • 0033233331 scopus 로고    scopus 로고
    • 13C NMR backbone assignments of the N terminal region of human erythrocyte alpha spectrin including one structural domain
    • 13C NMR backbone assignments of the N terminal region of human erythrocyte alpha spectrin including one structural domain. J. Biomol. NMR 15 (1999) 345-346.
    • (1999) J. Biomol. NMR , vol.15 , pp. 345-346
    • Park, S.1    Liao, X.2    Fung, L.W.-M.3    Johnson, M.E.4
  • 20
    • 0034680758 scopus 로고    scopus 로고
    • NMR analysis of secondary structure and dynamics of a recombinant peptide from the N-terminal region of human erythroid α-spectrin
    • Park, S., Johnson, M.E. and Fung, L. W.-M. NMR analysis of secondary structure and dynamics of a recombinant peptide from the N-terminal region of human erythroid α-spectrin. FEBS Lett. 485 (2000) 81-86.
    • (2000) FEBS Lett. , vol.485 , pp. 81-86
    • Park, S.1    Johnson, M.E.2    Fung, L.W.-M.3
  • 21
    • 0030066743 scopus 로고    scopus 로고
    • Erythrocyte spectrin maintains its segmental motions upon oxidation: A spin label EPR study
    • Fung, L. W.-M., Kalaw, B.O., Hatfield, R.M. and Dias, M.N. Erythrocyte spectrin maintains its segmental motions upon oxidation: A spin label EPR study. Biophys. J. 70 (1996) 841-851.
    • (1996) Biophys. J. , vol.70 , pp. 841-851
    • Fung, L.W.-M.1    Kalaw, B.O.2    Hatfield, R.M.3    Dias, M.N.4
  • 22
    • 12044252858 scopus 로고
    • Methodological advances in protein
    • Bax, A. and Grzesiek, S. Methodological advances in protein NMR. Acc. Chem. Res. 26 (1993) 131-138.
    • (1993) NMR. Acc. Chem. Res. , vol.26 , pp. 131-138
    • Bax, A.1    Grzesiek, S.2
  • 24
    • 0026470325 scopus 로고
    • Analysis of human red cell spectrin tetramer (head-to-head) assembly using complementary univalent peptides
    • DeSilva, T.M., Peng, K.C. and Speicher, D.W. Analysis of human red cell spectrin tetramer (head-to-head) assembly using complementary univalent peptides. Biochem. 31 (1992) 10872-10878.
    • (1992) Biochem. , vol.31 , pp. 10872-10878
    • DeSilva, T.M.1    Peng, K.C.2    Speicher, D.W.3
  • 25
    • 0026589161 scopus 로고
    • A common type of the spectrin αI46-50a kDa peptide abnormality in hereditary elliptocytosis is associated with a mutation distant from the proteolytic cleavage site. Evidence for the functional importance of the triple helical model of spectrin
    • Gallagher, P.G., Tse, W.T. and Goetzer, T. A common type of the spectrin αI46-50a kDa peptide abnormality in hereditary elliptocytosis is associated with a mutation distant from the proteolytic cleavage site. Evidence for the functional importance of the triple helical model of spectrin. J. Clin. Invest. 89 (1992) 892-898.
    • (1992) J. Clin. Invest. , vol.89 , pp. 892-898
    • Gallagher, P.G.1    Tse, W.T.2    Goetzer, T.3
  • 27
    • 0035900013 scopus 로고    scopus 로고
    • αβ spectrin coiled coil association at the tetramerization site
    • in press
    • Mehboob, S., Luo, B.-H., Patel, B. and Fung, L.W.-M. αβ spectrin coiled coil association at the tetramerization site. Biochemistry (2001) in press.
    • (2001) Biochemistry
    • Mehboob, S.1    Luo, B.-H.2    Patel, B.3    Fung, L.W.-M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.