메뉴 건너뛰기




Volumn 36, Issue 3, 1997, Pages 246-252

Physical properties of dystrophin rod domain

Author keywords

dystrophin; spectrin repeats

Indexed keywords

DYSTROPHIN; MONOMER; SPECTRIN;

EID: 0031052652     PISSN: 08861544     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0169(1997)36:3<246::AID-CM5>3.0.CO;2-5     Document Type: Article
Times cited : (20)

References (29)
  • 1
    • 0027470203 scopus 로고
    • The structural and functional diversity of dystrophin
    • Ahn, A.H., and Kunkel, L.M. (1993): The structural and functional diversity of dystrophin. Nature Genet. 3:283-291.
    • (1993) Nature Genet. , vol.3 , pp. 283-291
    • Ahn, A.H.1    Kunkel, L.M.2
  • 2
    • 0014817347 scopus 로고
    • Use of dimethylsuberimidute, a cross-linking reagent, in studying the subunit structure of oliaomeric proteins
    • Davis, G.E., and Stark, G.R. (1970): Use of dimethylsuberimidute, a cross-linking reagent, in studying the subunit structure of oliaomeric proteins. Proc. Natl. Acad. Sci. U.S.A. 66:651-657.
    • (1970) Proc. Natl. Acad. Sci. U.S.A. , vol.66 , pp. 651-657
    • Davis, G.E.1    Stark, G.R.2
  • 4
    • 0029093546 scopus 로고
    • Association of structural repeats in the α-actinin rod domain. Alignment of inter-subunit interactions
    • Flood, G., Kahana, E., Gilmore, A.P., Rowe, A.J., Gratzer, W.B., and Critchley, D.R. (1995): Association of structural repeats in the α-actinin rod domain. Alignment of inter-subunit interactions. J. Mol. Biol. 252:227-234.
    • (1995) J. Mol. Biol. , vol.252 , pp. 227-234
    • Flood, G.1    Kahana, E.2    Gilmore, A.P.3    Rowe, A.J.4    Gratzer, W.B.5    Critchley, D.R.6
  • 5
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N., and Fasman, G.D. (1969): Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8:4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 6
    • 1842360354 scopus 로고
    • Atassi-Gaudlin sedimentation coefficient and molecular weight relationship
    • Halsall, H.B. (1967): Atassi-Gaudlin sedimentation coefficient and molecular weight relationship. Nature 215:880-882.
    • (1967) Nature , vol.215 , pp. 880-882
    • Halsall, H.B.1
  • 7
    • 0024278676 scopus 로고
    • Substructure and higher structure of chicken smooth muscle α-actinin molecule
    • Imamura, M., Endo, T., Kuroda, M., Tanaka, T., and Masaki, T. (1988): Substructure and higher structure of chicken smooth muscle α-actinin molecule. J. Biol. Chem. 263:7800-7805.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7800-7805
    • Imamura, M.1    Endo, T.2    Kuroda, M.3    Tanaka, T.4    Masaki, T.5
  • 8
    • 0025750757 scopus 로고
    • Properties of the spectrin-like element of smooth muscle α-actinin
    • Kahana, E., and Gratzer, W.B. (1991): Properties of the spectrin-like element of smooth muscle α-actinin. Cell Motil. Cytoskeleton 20:242-248.
    • (1991) Cell Motil. Cytoskeleton , vol.20 , pp. 242-248
    • Kahana, E.1    Gratzer, W.B.2
  • 9
    • 0029063876 scopus 로고
    • Minimum folding unit of dystrophin rod domain
    • Kahanu, E., and Gratzer, W.B. (1995): Minimum folding unit of dystrophin rod domain. Biochemistry 34:8110-8114.
    • (1995) Biochemistry , vol.34 , pp. 8110-8114
    • Kahanu, E.1    Gratzer, W.B.2
  • 10
    • 0028213713 scopus 로고
    • Conformation and phasing of dystrophin structural repeats
    • Kahana, E., Marsh, P.J., Henry, A.J., Way, M., and Gratzer, W.B. (1994): Conformation and phasing of dystrophin structural repeats. J. Mol. Biol. 235:1271-1277.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1271-1277
    • Kahana, E.1    Marsh, P.J.2    Henry, A.J.3    Way, M.4    Gratzer, W.B.5
  • 12
    • 0025217703 scopus 로고
    • Detailed analysis of the repeat domain of dystrophin reveals four potential hinge segments that may confer flexibility
    • Koenig, M., and Kunkel, L.M. (1990): Detailed analysis of the repeat domain of dystrophin reveals four potential hinge segments that may confer flexibility. J. Biol. Chem. 265:4560-4566.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4560-4566
    • Koenig, M.1    Kunkel, L.M.2
  • 13
    • 0029149757 scopus 로고
    • Interactions between dystrophin glycoprotein complex proteins
    • Madhavan, R., and Jarrett, H.W. (1995): Interactions between dystrophin glycoprotein complex proteins. Biochemistry 34:12204-12209.
    • (1995) Biochemistry , vol.34 , pp. 12204-12209
    • Madhavan, R.1    Jarrett, H.W.2
  • 14
    • 0026785988 scopus 로고
    • Dystrophin at the plasma membrane of human muscle fibers shows a costameric localization
    • Minetti, C., Beltrame, F., Marcenaro, G., and Bonilla, E. (1992): Dystrophin at the plasma membrane of human muscle fibers shows a costameric localization. Neuromusc. Disord. 2:99-109.
    • (1992) Neuromusc. Disord. , vol.2 , pp. 99-109
    • Minetti, C.1    Beltrame, F.2    Marcenaro, G.3    Bonilla, E.4
  • 15
    • 0030026119 scopus 로고    scopus 로고
    • Towards an understanding of the dystrophinglycoprotein complex: Linkage between the extracellular matrix and the membrane cytoskcleton in muscle fibers
    • Ohlendieck. K. (1996): Towards an understanding of the dystrophinglycoprotein complex: Linkage between the extracellular matrix and the membrane cytoskcleton in muscle fibers. Eur. J. Cell Biol. 69:1-10.
    • (1996) Eur. J. Cell Biol. , vol.69 , pp. 1-10
    • Ohlendieck, K.1
  • 16
    • 0023049766 scopus 로고
    • Protein volumes and hydration effects. The calculation of partial specific volumes, neutron scattering match-points and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences
    • Perkins, S.J. (1986): Protein volumes and hydration effects. The calculation of partial specific volumes, neutron scattering match-points and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences. Eur. J. Biochem. 158:169-180.
    • (1986) Eur. J. Biochem. , vol.158 , pp. 169-180
    • Perkins, S.J.1
  • 18
    • 0026711133 scopus 로고
    • Dystrophin colocalizes with β-spectrin in distinct subsarcolemmal domains in mammalian skeletal muscle
    • Porter, G.A., Dmytrenko, G.M., Winkelmann, J.C., and Bloch, R.J. (1992): Dystrophin colocalizes with β-spectrin in distinct subsarcolemmal domains in mammalian skeletal muscle. J. Cell. Biol. 117:997-1005.
    • (1992) J. Cell. Biol. , vol.117 , pp. 997-1005
    • Porter, G.A.1    Dmytrenko, G.M.2    Winkelmann, J.C.3    Bloch, R.J.4
  • 19
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher, S.W., and Glöckner, J. (1981): Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20:33-37.
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glöckner, J.2
  • 21
    • 0018742616 scopus 로고
    • The molecular structure of human erythrocyte spectrin. Biophysical and electron microscopic studies
    • Shotton, D.M., Burke, B.E., and Branton, D. (1979): The molecular structure of human erythrocyte spectrin. Biophysical and electron microscopic studies. J. Mol. Biol. 131:303-329.
    • (1979) J. Mol. Biol. , vol.131 , pp. 303-329
    • Shotton, D.M.1    Burke, B.E.2    Branton, D.3
  • 22
    • 0026653822 scopus 로고
    • Properties of human red cell spectrin heterodimer (side-to-side) assembly and identification of an essential nucleation site
    • Speicher, D.W., Weglarz, L., and DeSilva, T.M. (1992): Properties of human red cell spectrin heterodimer (side-to-side) assembly and identification of an essential nucleation site. J. Biol. Chem. 267:14775-14782.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14775-14782
    • Speicher, D.W.1    Weglarz, L.2    DeSilva, T.M.3
  • 23
    • 0026453372 scopus 로고
    • Direct visualization of the dystrophin network on skeletal muscle fiber membrane
    • Straub, V., Bittner, R.E., Léger, J.J., and Voit, T. (1992): Direct visualization of the dystrophin network on skeletal muscle fiber membrane. J. Cell Biol. 119:1183-1191.
    • (1992) J. Cell Biol. , vol.119 , pp. 1183-1191
    • Straub, V.1    Bittner, R.E.2    Léger, J.J.3    Voit, T.4
  • 24
    • 0029913841 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, J.A., Kotula, L., DeSilva, T.M., Curtis, P.J., and Speicher, D.W. (1966): 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. 271:6636-6644.
    • (1966) 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
  • 25
    • 0028000263 scopus 로고
    • Interchain binding at the tail end of the Drosophila spectrin molecule
    • Viel, A., and Branton, D. (1994): Interchain binding at the tail end of the Drosophila spectrin molecule. Proc. Natl. Acad. Sci. U.S.A. 91:10839-10843.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 10839-10843
    • Viel, A.1    Branton, D.2
  • 26
    • 0025093899 scopus 로고
    • Identification of a region in segment 1 of gelsolin critical for actin binding
    • Way, M., Pope, B., Gooch, J., Hawkins, M., and Weeds, A.G. (1990): Identification of a region in segment 1 of gelsolin critical for actin binding. EMBO J. 9:4103-4109.
    • (1990) EMBO J. , vol.9 , pp. 4103-4109
    • Way, M.1    Pope, B.2    Gooch, J.3    Hawkins, M.4    Weeds, A.G.5
  • 28
    • 0029934409 scopus 로고    scopus 로고
    • Low probability of dystrophin and utrophin coiled coil regions forming dimers
    • Winder, S.J., Gibson, T.J., and Kendrick-Jones, J. (1996): Low probability of dystrophin and utrophin coiled coil regions forming dimers. Biochem. Soc. Trans. 24:280S.
    • (1996) Biochem. Soc. Trans. , vol.24
    • Winder, S.J.1    Gibson, T.J.2    Kendrick-Jones, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.