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Volumn 80, Issue 5, 2012, Pages 1377-1392

Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin

Author keywords

Actin binding domain; Aggregation; Calponin homology domain; Disease; Dystrophin; Muscular dystrophy; Stability; Unfolding; Utrophin

Indexed keywords

DYSTROPHIN; UTROPHIN;

EID: 84862825847     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24033     Document Type: Article
Times cited : (14)

References (112)
  • 1
    • 0037160782 scopus 로고    scopus 로고
    • The muscular dystrophies
    • Emery AEH. The muscular dystrophies. Lancet 2002; 359: 687-695.
    • (2002) Lancet , vol.359 , pp. 687-695
    • Emery, A.E.H.1
  • 2
    • 0023614188 scopus 로고
    • Dystrophin: the protein product of the Duchenne muscular dystrophy locus
    • Hoffman EP, Brown J, Robert H., Kunkel LM. Dystrophin: the protein product of the Duchenne muscular dystrophy locus. Cell 1987; 51: 919-928.
    • (1987) Cell , vol.51 , pp. 919-928
    • Hoffman, E.P.1    Brown, J.2    Robert, H.3    Kunkel, L.M.4
  • 4
    • 0035037179 scopus 로고    scopus 로고
    • Protein family review: dystrophins and dystrobrevins
    • reviews
    • Roberts RG. Protein family review: dystrophins and dystrobrevins. Gen Biol 2001; 2:reviews 3006.3001-3006.3007.
    • (2001) Gen Biol , vol.2 , pp. 30063001-30063007
    • Roberts, R.G.1
  • 5
    • 33846271135 scopus 로고    scopus 로고
    • Dystrophin, its interactions with other proteins, and implications
    • Ervasti JM. Dystrophin, its interactions with other proteins, and implications. Biochim Biophys Acta 2007; 1772: 108-117.
    • (2007) Biochim Biophys Acta , vol.1772 , pp. 108-117
    • Ervasti, J.M.1
  • 7
    • 0028303798 scopus 로고
    • Searching for the 1 in 2,400,000: a review of dystrophin gene point mutations
    • Roberts RG, Gardner RJ, Bobrow M. Searching for the 1 in 2, 400, 000: a review of dystrophin gene point mutations. Hum Mutat 1994; 4: 1-11.
    • (1994) Hum Mutat , vol.4 , pp. 1-11
    • Roberts, R.G.1    Gardner, R.J.2    Bobrow, M.3
  • 10
    • 0344420060 scopus 로고    scopus 로고
    • Dystrophin and mutations: One gene, several proteins, multiple phenotypes
    • Muntoni F, Torelli S, Ferlini A. Dystrophin and mutations: One gene, several proteins, multiple phenotypes. Lancet Neurol 2003; 2: 731-740.
    • (2003) Lancet Neurol , vol.2 , pp. 731-740
    • Muntoni, F.1    Torelli, S.2    Ferlini, A.3
  • 11
    • 33746766278 scopus 로고    scopus 로고
    • Entries in the Leiden Duchenne muscular dystrophy mutation database: an overview of mutation types and paradoxical cases that confirm the reading-frame rule
    • Aaartsma-Rus A, van Deutekom JCT, Fokkema IF, van Ommen G-JB, Den Dennen JT. Entries in the Leiden Duchenne muscular dystrophy mutation database: an overview of mutation types and paradoxical cases that confirm the reading-frame rule. Muscle Nerve 2006; 34: 135-144.
    • (2006) Muscle Nerve , vol.34 , pp. 135-144
    • Aaartsma-Rus, A.1    van Deutekom, J.C.T.2    Fokkema, I.F.3    van Ommen, G.-J.4    Den Dennen, J.T.5
  • 13
    • 0025167294 scopus 로고
    • Identification of a chromosome 6-encoded dystrophin-related protein
    • Khurana TS, Hoffman EP, Kunkel L. Identification of a chromosome 6-encoded dystrophin-related protein. J Biol Chem 1990; 265: 16717-16720.
    • (1990) J Biol Chem , vol.265 , pp. 16717-16720
    • Khurana, T.S.1    Hoffman, E.P.2    Kunkel, L.3
  • 15
    • 0036087342 scopus 로고    scopus 로고
    • Function and genetics of dystrophin and dystrophin-related proteins in muscle
    • Blake DJ, Weir A, Newey SE, Davies KE. Function and genetics of dystrophin and dystrophin-related proteins in muscle. Physiol Rev 2002; 82: 291-329.
    • (2002) Physiol Rev , vol.82 , pp. 291-329
    • Blake, D.J.1    Weir, A.2    Newey, S.E.3    Davies, K.E.4
  • 17
    • 0031775820 scopus 로고    scopus 로고
    • Skeletal muscle-specific expression of a utrophin transgene rescues utrophin-dystrophin deficient mice
    • Rafael JA, Tinsley JM, Potter AC, Deconinck AE, Davies KE. Skeletal muscle-specific expression of a utrophin transgene rescues utrophin-dystrophin deficient mice. Nat Genet 1998; 19: 79-82.
    • (1998) Nat Genet , vol.19 , pp. 79-82
    • Rafael, J.A.1    Tinsley, J.M.2    Potter, A.C.3    Deconinck, A.E.4    Davies, K.E.5
  • 18
    • 0036796262 scopus 로고    scopus 로고
    • Gene therapy of muscular dystrophy
    • Chamberlain JS. Gene therapy of muscular dystrophy. Hum Mol Genet 2002; 11: 2355-2362.
    • (2002) Hum Mol Genet , vol.11 , pp. 2355-2362
    • Chamberlain, J.S.1
  • 19
    • 0141594934 scopus 로고    scopus 로고
    • Advances in Duchenne muscular dystrophy gene therapy
    • van Deutekom JCT, van Ommen G-JB. Advances in Duchenne muscular dystrophy gene therapy. Nat Rev Genet 2003; 4: 774-783.
    • (2003) Nat Rev Genet , vol.4 , pp. 774-783
    • van Deutekom, J.C.T.1    van Ommen, G.-J.2
  • 20
    • 33644975603 scopus 로고    scopus 로고
    • Utrophin upregulation for treating Duchenne or Becker muscular dystrophy: How close are we?
    • Miura P, Jasmin BJ. Utrophin upregulation for treating Duchenne or Becker muscular dystrophy: How close are we? Trends Mol Med 2006; 12: 122-129.
    • (2006) Trends Mol Med , vol.12 , pp. 122-129
    • Miura, P.1    Jasmin, B.J.2
  • 22
    • 50549098032 scopus 로고    scopus 로고
    • Microutrophin delivery through rAAV6 increases lifespan and improves muscle function in dystrophic dystrophin/utrophin-deficient mice
    • Odom GL, Gregorevic P, Allen JM, Finn E, Chamberlain JS. Microutrophin delivery through rAAV6 increases lifespan and improves muscle function in dystrophic dystrophin/utrophin-deficient mice. Mol Ther 2008; 16: 1539-1545.
    • (2008) Mol Ther , vol.16 , pp. 1539-1545
    • Odom, G.L.1    Gregorevic, P.2    Allen, J.M.3    Finn, E.4    Chamberlain, J.S.5
  • 26
    • 0026460270 scopus 로고
    • The dystrophin-related protein, utrophin, is expressed on the sarcolemma of regenerating human skeletal muscle fibers in dystrophies and inflammatory myopathies
    • Helliwell TR, Man NT, Morris GE, Davies KE. The dystrophin-related protein, utrophin, is expressed on the sarcolemma of regenerating human skeletal muscle fibers in dystrophies and inflammatory myopathies. Neuromusc Disord 1992; 2: 177-184.
    • (1992) Neuromusc Disord , vol.2 , pp. 177-184
    • Helliwell, T.R.1    Man, N.T.2    Morris, G.E.3    Davies, K.E.4
  • 27
    • 0029921129 scopus 로고    scopus 로고
    • Utrophin: a structural and functional comparison to dystrophin
    • Blake DJ, Tinsley JM, Davies KE. Utrophin: a structural and functional comparison to dystrophin. Brain Pathol 1996; 6: 37-47.
    • (1996) Brain Pathol , vol.6 , pp. 37-47
    • Blake, D.J.1    Tinsley, J.M.2    Davies, K.E.3
  • 29
    • 0031239725 scopus 로고    scopus 로고
    • Duchenne muscular dystrophy and the neuromuscular junction: the utrophin link
    • Gramolini AO, Jasmin BJ. Duchenne muscular dystrophy and the neuromuscular junction: the utrophin link. BioEssays 1997; 19: 747-750.
    • (1997) BioEssays , vol.19 , pp. 747-750
    • Gramolini, A.O.1    Jasmin, B.J.2
  • 30
    • 0033918661 scopus 로고    scopus 로고
    • Biochemical characterization of the actin-binding properties of utrophin
    • Moores CA, Kendrick-Jones J. Biochemical characterization of the actin-binding properties of utrophin. Cell Motil Cytoskeleton 2000; 46: 116-128.
    • (2000) Cell Motil Cytoskeleton , vol.46 , pp. 116-128
    • Moores, C.A.1    Kendrick-Jones, J.2
  • 31
    • 0025728005 scopus 로고
    • A homologue of dystrophin is expressed at the neuromuscular junctions of normal individuals and DMD patients, and of normal and mdx mice: immunological evidence
    • Pons F, Augier N, Léger JOC, Robert A, Tomé FMS, Fardeau M, Voit T, Nicholson LVB, Mornet D, Léger JJ. A homologue of dystrophin is expressed at the neuromuscular junctions of normal individuals and DMD patients, and of normal and mdx mice: immunological evidence. FEBS Lett 1991; 282: 161-165.
    • (1991) FEBS Lett , vol.282 , pp. 161-165
    • Pons, F.1    Augier, N.2    Léger, J.O.C.3    Robert, A.4    Tomé, F.M.S.5    Fardeau, M.6    Voit, T.7    Nicholson, L.V.B.8    Mornet, D.9    Léger, J.J.10
  • 32
    • 0026621608 scopus 로고
    • Association of dystrophin-related protein with dystrophin-associated proteins in mdx mouse muscle
    • Matsumura K, Ervasti JM, Ohlendieck K, Kahl SD, Campbell KP. Association of dystrophin-related protein with dystrophin-associated proteins in mdx mouse muscle. Nature 1992; 360: 588-591.
    • (1992) Nature , vol.360 , pp. 588-591
    • Matsumura, K.1    Ervasti, J.M.2    Ohlendieck, K.3    Kahl, S.D.4    Campbell, K.P.5
  • 34
    • 0035999982 scopus 로고    scopus 로고
    • Utrophin binds laterally along actin filaments and can couple costameric actin with sarcolemma when overexpressed in dystrophin-deficient muscle
    • Rybakova IN, Patel JR, Davies KE, Yurchenco PD, Ervasti JM. Utrophin binds laterally along actin filaments and can couple costameric actin with sarcolemma when overexpressed in dystrophin-deficient muscle. Mol Biol Cell 2002; 13: 1512-1521.
    • (2002) Mol Biol Cell , vol.13 , pp. 1512-1521
    • Rybakova, I.N.1    Patel, J.R.2    Davies, K.E.3    Yurchenco, P.D.4    Ervasti, J.M.5
  • 35
    • 1842429177 scopus 로고    scopus 로고
    • ZZ domain is essentially required for the physiological binding of dystrophin and utrophin to β-dystroglycan
    • Ishikawa-Sakurai M, Yoshida M, Imamura M, Davies KE, Ozawa E. ZZ domain is essentially required for the physiological binding of dystrophin and utrophin to β-dystroglycan. Hum Mol Genet 2004; 13: 693-702.
    • (2004) Hum Mol Genet , vol.13 , pp. 693-702
    • Ishikawa-Sakurai, M.1    Yoshida, M.2    Imamura, M.3    Davies, K.E.4    Ozawa, E.5
  • 36
    • 33744507184 scopus 로고    scopus 로고
    • Dystrophin and utrophin bind actin through distinct modes of contact
    • Rybakova IN, Humston JL, Sonnemann KJ, Ervasti JM. Dystrophin and utrophin bind actin through distinct modes of contact. J Biol Chem 2006; 281: 9996-10001.
    • (2006) J Biol Chem , vol.281 , pp. 9996-10001
    • Rybakova, I.N.1    Humston, J.L.2    Sonnemann, K.J.3    Ervasti, J.M.4
  • 37
    • 66049139116 scopus 로고    scopus 로고
    • Dystrophin and utrophin have distinct effects on the structural dynamics of actin
    • Prochniewicz E, Henderson D, Ervasti JM, Thomas DD. Dystrophin and utrophin have distinct effects on the structural dynamics of actin. Proc Natl Acad Sci USA 2009; 106: 7822-7827.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 7822-7827
    • Prochniewicz, E.1    Henderson, D.2    Ervasti, J.M.3    Thomas, D.D.4
  • 39
    • 0034641893 scopus 로고    scopus 로고
    • Mdx mice inducibly expressing dystrophin provide insights into the potential of gene therapy for Duchenne muscular dystrophy
    • Ahmad A, Brinson M, Hodges BL, Chamberlain JS, Amalfitano A. Mdx mice inducibly expressing dystrophin provide insights into the potential of gene therapy for Duchenne muscular dystrophy. Hum Mol Genet 2000; 9: 2507-2515.
    • (2000) Hum Mol Genet , vol.9 , pp. 2507-2515
    • Ahmad, A.1    Brinson, M.2    Hodges, B.L.3    Chamberlain, J.S.4    Amalfitano, A.5
  • 41
    • 0034657791 scopus 로고    scopus 로고
    • The structure of the N-terminal actin-binding domain of human dystrophin and how mutations in this domain may cause Duchenne or Becker muscular dystrophy
    • Norwood FL, Sutherland-Smith AJ, Keep NH, Kendrick-Jones J. The structure of the N-terminal actin-binding domain of human dystrophin and how mutations in this domain may cause Duchenne or Becker muscular dystrophy. Structure 2000; 8: 481-491.
    • (2000) Structure , vol.8 , pp. 481-491
    • Norwood, F.L.1    Sutherland-Smith, A.J.2    Keep, N.H.3    Kendrick-Jones, J.4
  • 42
    • 77956994292 scopus 로고    scopus 로고
    • Missense mutations in dystrophin that trigger muscular dystrophy decrease protein stability and lead to cross-β aggregates
    • Singh SM, Kongari N, Cabello-Villegas J, Mallela KMG. Missense mutations in dystrophin that trigger muscular dystrophy decrease protein stability and lead to cross-β aggregates. Proc Natl Acad Sci USA 2010; 107: 15069-15074.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 15069-15074
    • Singh, S.M.1    Kongari, N.2    Cabello-Villegas, J.3    Mallela, K.M.G.4
  • 43
    • 77953108170 scopus 로고    scopus 로고
    • Disease-causing missense mutations in actin binding domain 1 of dystrophin induce thermodynamic instability and protein aggregation
    • Henderson DM, Lee A, Ervasti JM. Disease-causing missense mutations in actin binding domain 1 of dystrophin induce thermodynamic instability and protein aggregation. Proc Natl Acad Sci USA 2010; 107: 9632-9637.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 9632-9637
    • Henderson, D.M.1    Lee, A.2    Ervasti, J.M.3
  • 46
    • 0030723508 scopus 로고    scopus 로고
    • Expression of truncated utrophin leads to major functional improvements in dystrophin-deficient muscles of mice
    • Deconinck N, Tinsley J, Backer FD, Fisher R, Kahn D, Phelps S, Davies K, Gillis J-M. Expression of truncated utrophin leads to major functional improvements in dystrophin-deficient muscles of mice. Nat Med 1997; 3: 1216-1221.
    • (1997) Nat Med , vol.3 , pp. 1216-1221
    • Deconinck, N.1    Tinsley, J.2    Backer, F.D.3    Fisher, R.4    Kahn, D.5    Phelps, S.6    Davies, K.7    Gillis, J.-M.8
  • 48
    • 0033994291 scopus 로고    scopus 로고
    • Prevention of the dystrophic phenotype in dystrophin/utrophin-deficient muscle following adenovirus-mediated transfer of a utrophin minigene
    • Wakefield PM, Tinsley JM, Wood MJA, Gilbert R, Karpati G, Davies KE. Prevention of the dystrophic phenotype in dystrophin/utrophin-deficient muscle following adenovirus-mediated transfer of a utrophin minigene. Gene Therapy 2000; 7: 201-204.
    • (2000) Gene Therapy , vol.7 , pp. 201-204
    • Wakefield, P.M.1    Tinsley, J.M.2    Wood, M.J.A.3    Gilbert, R.4    Karpati, G.5    Davies, K.E.6
  • 49
    • 0034610364 scopus 로고    scopus 로고
    • Adeno-associated virus vector carrying human minidystrophin genes effectively ameliorates muscular dystrophy in mdx mouse model
    • Wang B, Li J, Xiao X. Adeno-associated virus vector carrying human minidystrophin genes effectively ameliorates muscular dystrophy in mdx mouse model. Proc Natl Acad Sci USA 2000; 97: 13714-13719.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13714-13719
    • Wang, B.1    Li, J.2    Xiao, X.3
  • 51
    • 0036823730 scopus 로고    scopus 로고
    • Viral vectors for gene transfer of micro-, mini-, or full-length dystrophin
    • Scott JM, Li S, harper SQ. Viral vectors for gene transfer of micro-, mini-, or full-length dystrophin. Neuromuscular Disord 2002; 12: s23-s29.
    • (2002) Neuromuscular Disord , vol.12
    • Scott, J.M.1    Li, S.2    Harper, S.Q.3
  • 52
    • 0042170127 scopus 로고    scopus 로고
    • Gene therapy for muscular dystrophy-a review of promising progress
    • Gregorevic P, Chamberlain JS. Gene therapy for muscular dystrophy-a review of promising progress. Expert Opin Biol Ther 2003; 3: 803-814.
    • (2003) Expert Opin Biol Ther , vol.3 , pp. 803-814
    • Gregorevic, P.1    Chamberlain, J.S.2
  • 53
    • 33845218878 scopus 로고    scopus 로고
    • Gene therapy progress and prospects: Duchenne muscular dystrophy
    • Foster K, Foster H, Dickson JG. Gene therapy progress and prospects: Duchenne muscular dystrophy. Gene Ther 2006; 13: 1677-1685.
    • (2006) Gene Ther , vol.13 , pp. 1677-1685
    • Foster, K.1    Foster, H.2    Dickson, J.G.3
  • 54
    • 69149106708 scopus 로고    scopus 로고
    • Emerging strategies for cell and gene therapy of the muscular dystrophies
    • Muir LA, Chamberlain JS. Emerging strategies for cell and gene therapy of the muscular dystrophies. Expert Rev Mol Med 2009; 11: e18.
    • (2009) Expert Rev Mol Med , vol.11
    • Muir, L.A.1    Chamberlain, J.S.2
  • 55
    • 80055064588 scopus 로고    scopus 로고
    • Progress in therapy for Duchenne muscular dystrophy
    • Fairclough RJ, Bareja A, Davies KE. Progress in therapy for Duchenne muscular dystrophy. Exp Physiol 2011; 96: 1101-1113.
    • (2011) Exp Physiol , vol.96 , pp. 1101-1113
    • Fairclough, R.J.1    Bareja, A.2    Davies, K.E.3
  • 58
  • 60
    • 0041620499 scopus 로고    scopus 로고
    • Do the utrophin tandem calponin homology domains bind F-actin in a compact or extended conformation?
    • Galkin VE, Orlova A, VanLoock MS, Egelman EH. Do the utrophin tandem calponin homology domains bind F-actin in a compact or extended conformation? J Mol Biol 2003; 331: 967-972.
    • (2003) J Mol Biol , vol.331 , pp. 967-972
    • Galkin, V.E.1    Orlova, A.2    VanLoock, M.S.3    Egelman, E.H.4
  • 63
    • 79961213117 scopus 로고    scopus 로고
    • Large-scale opening of utrophin's tandem calponin homology (CH) domains upon actin binding by an induced-fit mechanism
    • Lin AY, Prochniewicz E, James ZM, Svensson B, Thomas DD. Large-scale opening of utrophin's tandem calponin homology (CH) domains upon actin binding by an induced-fit mechanism. Proc Natl Acad Sci USA 2011; 108: 12729-12733.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 12729-12733
    • Lin, A.Y.1    Prochniewicz, E.2    James, Z.M.3    Svensson, B.4    Thomas, D.D.5
  • 65
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • Greenfield NJ. Using circular dichroism spectra to estimate protein secondary structure. Nat Protocols 2006; 6: 2876-2890.
    • (2006) Nat Protocols , vol.6 , pp. 2876-2890
    • Greenfield, N.J.1
  • 67
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • Santoro MM, Bolen DW. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 1988; 27: 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 68
    • 0026754044 scopus 로고
    • A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range
    • Santoro MM, Bolen DW. A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range. Biochemistry 1992; 31: 4901-4907.
    • (1992) Biochemistry , vol.31 , pp. 4901-4907
    • Santoro, M.M.1    Bolen, D.W.2
  • 73
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding
    • Myers JK, Pace CN, Scholtz JM. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci 1995; 4: 2138-2148.
    • (1995) Protein Sci , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 75
    • 67349085538 scopus 로고    scopus 로고
    • Differential stabilities of alternative exon-skipped rod motifs of dystrophin
    • Ruszczak C, Mirza A, Menhart N. Differential stabilities of alternative exon-skipped rod motifs of dystrophin. Biochim Biophys Acta 2009; 1794: 921-928.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 921-928
    • Ruszczak, C.1    Mirza, A.2    Menhart, N.3
  • 76
    • 65849498675 scopus 로고    scopus 로고
    • A two-amino acid mutation encountered in Duchenne muscular dystrophy decreases stability of the rod domain 23 (R23) spectrin-like repeat of dystrophin
    • Legardinier S, Legrand B, Raguénès-Nicol C, Bondon A, Hardy S, Tascon C, Rumeur EL, Hubert J-F. A two-amino acid mutation encountered in Duchenne muscular dystrophy decreases stability of the rod domain 23 (R23) spectrin-like repeat of dystrophin. J Biol Chem 2009; 284: 8822-8832.
    • (2009) J Biol Chem , vol.284 , pp. 8822-8832
    • Legardinier, S.1    Legrand, B.2    Raguénès-Nicol, C.3    Bondon, A.4    Hardy, S.5    Tascon, C.6    Rumeur, E.L.7    Hubert, J.-F.8
  • 77
    • 33847306593 scopus 로고    scopus 로고
    • A unified mechanism for protein folding: predetermined pathways with optional errors
    • Krishna MMG, Englander SW. A unified mechanism for protein folding: predetermined pathways with optional errors. Protein Sci 2007; 16: 449-464.
    • (2007) Protein Sci , vol.16 , pp. 449-464
    • Krishna, M.M.G.1    Englander, S.W.2
  • 79
    • 6344285316 scopus 로고    scopus 로고
    • Probing the high energy states in proteins by proteolysis
    • Park C, Marqusee S. Probing the high energy states in proteins by proteolysis. J Mol Biol 2004; 343: 1467-1476.
    • (2004) J Mol Biol , vol.343 , pp. 1467-1476
    • Park, C.1    Marqusee, S.2
  • 81
    • 79960005237 scopus 로고    scopus 로고
    • Prediction of amyloid aggregation in vivo
    • Belli M, Ramazzotti M, Chiti F. Prediction of amyloid aggregation in vivo. EMBO Reports 2011; 12: 657-663.
    • (2011) EMBO Reports , vol.12 , pp. 657-663
    • Belli, M.1    Ramazzotti, M.2    Chiti, F.3
  • 82
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease {beta}-amyloid peptides: Detection of amyloid aggregation in solution
    • Levine-III H. Thioflavine T interaction with synthetic Alzheimer's disease {beta}-amyloid peptides: Detection of amyloid aggregation in solution. Protein Sci 1993; 2: 404-410.
    • (1993) Protein Sci , vol.2 , pp. 404-410
    • Levine III, H.1
  • 83
    • 0024352110 scopus 로고
    • Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleatedsheet conformation
    • Klunk WE, Pettegrew JW, Abraham DJ. Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleatedsheet conformation. J Histochem Cytochem 1989; 37: 1273-1281.
    • (1989) J Histochem Cytochem , vol.37 , pp. 1273-1281
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 85
    • 0028906307 scopus 로고
    • Mdx mice show progressive weakness and muscle deterioration with age
    • Pastoret C, Sebille A. Mdx mice show progressive weakness and muscle deterioration with age. J Neurol Sci 1995; 129: 97-105.
    • (1995) J Neurol Sci , vol.129 , pp. 97-105
    • Pastoret, C.1    Sebille, A.2
  • 86
    • 0022638233 scopus 로고
    • Skeletal muscle pathology in X chromosome-linked muscular dystrophy (mdx) mouse
    • Tanabe Y, Esaki K, Nomura T. Skeletal muscle pathology in X chromosome-linked muscular dystrophy (mdx) mouse. Acta Neuropathol 1986; 69: 91-95.
    • (1986) Acta Neuropathol , vol.69 , pp. 91-95
    • Tanabe, Y.1    Esaki, K.2    Nomura, T.3
  • 87
    • 0027461720 scopus 로고
    • Localization and quantitation of the chromosome 6-encoded dystrophin-related protein in normal and pathological human muscle
    • Karpati G, Carpenter S, Morris GE, Davies KE, Guerin C, Holland P. Localization and quantitation of the chromosome 6-encoded dystrophin-related protein in normal and pathological human muscle. J Neuropathol Exp Neurol 1993; 52: 119-128.
    • (1993) J Neuropathol Exp Neurol , vol.52 , pp. 119-128
    • Karpati, G.1    Carpenter, S.2    Morris, G.E.3    Davies, K.E.4    Guerin, C.5    Holland, P.6
  • 89
    • 0030848338 scopus 로고    scopus 로고
    • Skeletal and cardiac myopathies in mice lacking utrophin and dystrophin: a model for Duchenne muscular dystrophy
    • Grady RM, Teng HB, Nichol MC, Cunningham JC, Wilkinson RS, Sanes JR. Skeletal and cardiac myopathies in mice lacking utrophin and dystrophin: a model for Duchenne muscular dystrophy. Cell 1997; 90: 729-738.
    • (1997) Cell , vol.90 , pp. 729-738
    • Grady, R.M.1    Teng, H.B.2    Nichol, M.C.3    Cunningham, J.C.4    Wilkinson, R.S.5    Sanes, J.R.6
  • 90
    • 33846308923 scopus 로고    scopus 로고
    • Viral-mediated gene therapy for the muscular dystrophies: successes, limitations, and recent advances
    • Odom GL, Gregorevic P, Chamberlain JS. Viral-mediated gene therapy for the muscular dystrophies: successes, limitations, and recent advances. Biochim Biophys Acta 2007; 1772: 243-262.
    • (2007) Biochim Biophys Acta , vol.1772 , pp. 243-262
    • Odom, G.L.1    Gregorevic, P.2    Chamberlain, J.S.3
  • 92
    • 0024554228 scopus 로고
    • The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli
    • Parsell DA, Sauer RT. The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli. J Biol Chem 1989; 264: 7590-7595.
    • (1989) J Biol Chem , vol.264 , pp. 7590-7595
    • Parsell, D.A.1    Sauer, R.T.2
  • 93
    • 0031791519 scopus 로고    scopus 로고
    • Proteolysis as a measure of the free energy difference between cytochrome c and its derivatives
    • Wang L, Kallenbach NR. Proteolysis as a measure of the free energy difference between cytochrome c and its derivatives. Protein Sci 1998; 7: 2460-2464.
    • (1998) Protein Sci , vol.7 , pp. 2460-2464
    • Wang, L.1    Kallenbach, N.R.2
  • 94
    • 68849124510 scopus 로고    scopus 로고
    • Determining protein stability in cell lysates by pulse proteolysis and Western blotting
    • Kim M-S, Song J, Park C. Determining protein stability in cell lysates by pulse proteolysis and Western blotting. Protein Sci 2009; 18: 1051-1059.
    • (2009) Protein Sci , vol.18 , pp. 1051-1059
    • Kim, M.-S.1    Song, J.2    Park, C.3
  • 95
    • 77957970501 scopus 로고    scopus 로고
    • The proteasome antechamber maintains substrates in the unfolded state
    • Ruschak AM, Religa TL, Breuer S, Witt S, Kay LE. The proteasome antechamber maintains substrates in the unfolded state. Nature 2010; 467: 868-871.
    • (2010) Nature , vol.467 , pp. 868-871
    • Ruschak, A.M.1    Religa, T.L.2    Breuer, S.3    Witt, S.4    Kay, L.E.5
  • 97
    • 33744949000 scopus 로고    scopus 로고
    • Utrophin is a calpain substrate in muscle cells
    • Courdier-Fruh I, Briguet A. Utrophin is a calpain substrate in muscle cells. Muscle Nerve 2006; 33: 753-759.
    • (2006) Muscle Nerve , vol.33 , pp. 753-759
    • Courdier-Fruh, I.1    Briguet, A.2
  • 99
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation
    • Chi EY, Krishnan S, Randolph TW, Carpenter JF. Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation. Pharmaceut Res 2003; 20: 1325-1336.
    • (2003) Pharmaceut Res , vol.20 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 100
    • 34547687667 scopus 로고    scopus 로고
    • Correlation of levels of folded recombinant p53 in Escherichia coli with thermodynamic stability in vitro
    • Mayer S, Rüdiger S, Ang HC, Joerger AC, Fersht AR. Correlation of levels of folded recombinant p53 in Escherichia coli with thermodynamic stability in vitro. J Mol Biol 2007; 372: 268-276.
    • (2007) J Mol Biol , vol.372 , pp. 268-276
    • Mayer, S.1    Rüdiger, S.2    Ang, H.C.3    Joerger, A.C.4    Fersht, A.R.5
  • 101
    • 42649110014 scopus 로고    scopus 로고
    • The in vivo and in vitro aggregation properties of globular proteins correlate with their conformational stability: the SH3 case
    • Espargaró A, Castillo V, de Groot NS, Ventura S. The in vivo and in vitro aggregation properties of globular proteins correlate with their conformational stability: the SH3 case. J Mol Biol 2008; 378: 1116-1131.
    • (2008) J Mol Biol , vol.378 , pp. 1116-1131
    • Espargaró, A.1    Castillo, V.2    de Groot, N.S.3    Ventura, S.4
  • 106
    • 0030010809 scopus 로고    scopus 로고
    • Immunohistochemical study of utrophin and dystrophin at the motor end-plate in myasthenia gravis
    • Ito H, Yoshimura T, Satoh A, Takino H, Tsujihata M, Nagataki S. Immunohistochemical study of utrophin and dystrophin at the motor end-plate in myasthenia gravis. Acta Neuropathol 1996; 92: 14-18.
    • (1996) Acta Neuropathol , vol.92 , pp. 14-18
    • Ito, H.1    Yoshimura, T.2    Satoh, A.3    Takino, H.4    Tsujihata, M.5    Nagataki, S.6
  • 107
    • 0033817038 scopus 로고    scopus 로고
    • Immature end-plates and utrophin deficiency in congenital myasthemic syndrome caused by ε-AChR subunit truncating mutations
    • Sieb JP, Kraner S, Rauch M, Steinlein OK. Immature end-plates and utrophin deficiency in congenital myasthemic syndrome caused by ε-AChR subunit truncating mutations. Hum Genet 2000; 107: 160-164.
    • (2000) Hum Genet , vol.107 , pp. 160-164
    • Sieb, J.P.1    Kraner, S.2    Rauch, M.3    Steinlein, O.K.4
  • 108
  • 109
    • 0037173037 scopus 로고    scopus 로고
    • Deciphering peripheral nerve myelination by using Schwann cell expression profiling
    • Nagarajan R, Le N, Mahoney H, Araki T, Milbrandt J. Deciphering peripheral nerve myelination by using Schwann cell expression profiling. Proc Natl Acad Sci USA 2002; 99: 8998-9003.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8998-9003
    • Nagarajan, R.1    Le, N.2    Mahoney, H.3    Araki, T.4    Milbrandt, J.5
  • 112
    • 84862808113 scopus 로고    scopus 로고
    • Protein stability, folding, and aggregation of the N-terminal actin binding domains of dystrophin and utrophin
    • Mallela K, Singh S, Molas J, Cabello-Villegas J, Kongari N. Protein stability, folding, and aggregation of the N-terminal actin binding domains of dystrophin and utrophin. Protein Sci 2010; 19(S1): 180.
    • (2010) Protein Sci , vol.19 , Issue.S1 , pp. 180
    • Mallela, K.1    Singh, S.2    Molas, J.3    Cabello-Villegas, J.4    Kongari, N.5


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