메뉴 건너뛰기




Volumn 1824, Issue 10, 2012, Pages 1080-1089

Exon edited dystrophin rods in the hinge 3 region

Author keywords

Duchenne muscular dystrophy; Dystrophin; Exon skipping; Lipid; Stability

Indexed keywords

ANTISENSE OLIGONUCLEOTIDE; DYSTROPHIN; LIPID; RECOMBINANT DYSTROPHIN; UNCLASSIFIED DRUG;

EID: 84864068462     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.06.011     Document Type: Article
Times cited : (11)

References (39)
  • 2
    • 77956322846 scopus 로고    scopus 로고
    • Change in natural history of Duchenne muscular dystrophy with long-term corticosteroid treatment: Implications for management
    • R.T. Moxley III, S. Pandya, E. Ciafaloni, D.J. Fox, and K. Campbell Change in natural history of Duchenne muscular dystrophy with long-term corticosteroid treatment: implications for management J. Child Neurol. 25 2010 1116 1129
    • (2010) J. Child Neurol. , vol.25 , pp. 1116-1129
    • Moxley III, R.T.1    Pandya, S.2    Ciafaloni, E.3    Fox, D.J.4    Campbell, K.5
  • 3
    • 67649849595 scopus 로고    scopus 로고
    • Enhanced exon-skipping induced by U7 snRNA carrying a splicing silencer sequence: Promising tool for DMD therapy
    • A. Goyenvalle, A. Babbs, G.J. van Ommen, L. Garcia, and K.E. Davies Enhanced exon-skipping induced by U7 snRNA carrying a splicing silencer sequence: promising tool for DMD therapy Mol. Ther. 17 2009 1234 1240
    • (2009) Mol. Ther. , vol.17 , pp. 1234-1240
    • Goyenvalle, A.1    Babbs, A.2    Van Ommen, G.J.3    Garcia, L.4    Davies, K.E.5
  • 4
    • 78650916689 scopus 로고    scopus 로고
    • The status of exon skipping as a therapeutic approach to Duchenne muscular dystrophy
    • Q.L. Lu, T. Yokota, S. Takeda, L. Garcia, F. Muntoni, and T. Partridge The status of exon skipping as a therapeutic approach to Duchenne muscular dystrophy Mol. Ther. 19 2011 9 15
    • (2011) Mol. Ther. , vol.19 , pp. 9-15
    • Lu, Q.L.1    Yokota, T.2    Takeda, S.3    Garcia, L.4    Muntoni, F.5    Partridge, T.6
  • 13
    • 53149120329 scopus 로고    scopus 로고
    • Stability of dystrophin STR fragments in relation to junction helicity
    • A. Mirza, and N. Menhart Stability of dystrophin STR fragments in relation to junction helicity Biochim. Biophys. Acta 1784 2008 1301 1309
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1301-1309
    • Mirza, A.1    Menhart, N.2
  • 14
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • S.C. Gill, and P.H. von Hippel Calculation of protein extinction coefficients from amino acid sequence data Anal. Biochem. 182 1989 319 326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 15
    • 0017555826 scopus 로고
    • Dynamic light scattering of biopolymers and biocolloids
    • J.M. Schurr Dynamic light scattering of biopolymers and biocolloids CRC Crit. Rev. Biochem. 4 1977 371 431
    • (1977) CRC Crit. Rev. Biochem. , vol.4 , pp. 371-431
    • Schurr, J.M.1
  • 16
    • 33646524933 scopus 로고    scopus 로고
    • Structural cooperativity in spectrin type repeats motifs of dystrophin
    • L. Saadat, L. Pittman, and N. Menhart Structural cooperativity in spectrin type repeats motifs of dystrophin Biochim. Biophys. Acta 1764 2006 943 954
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 943-954
    • Saadat, L.1    Pittman, L.2    Menhart, N.3
  • 17
    • 0037458618 scopus 로고    scopus 로고
    • Interaction of dystrophin rod domain with membrane phospholipids. Evidence of a close proximity between tryptophan residues and lipids
    • E. Le Rumeur, Y. Fichou, S. Pottier, F. Gaboriau, C. Rondeau-Mouro, M. Vincent, J. Gallay, and A. Bondon Interaction of dystrophin rod domain with membrane phospholipids. Evidence of a close proximity between tryptophan residues and lipids J. Biol. Chem. 278 2003 5993 6001
    • (2003) J. Biol. Chem. , vol.278 , pp. 5993-6001
    • Le Rumeur, E.1    Fichou, Y.2    Pottier, S.3    Gaboriau, F.4    Rondeau-Mouro, C.5    Vincent, M.6    Gallay, J.7    Bondon, A.8
  • 19
    • 0026795513 scopus 로고
    • Synthetic model proteins. Positional effects of interchain hydrophobic interactions on stability of two-stranded alpha-helical coiled-coils
    • N.E. Zhou, C.M. Kay, and R.S. Hodges Synthetic model proteins. Positional effects of interchain hydrophobic interactions on stability of two-stranded alpha-helical coiled-coils J. Biol. Chem. 267 1992 2664 2670
    • (1992) J. Biol. Chem. , vol.267 , pp. 2664-2670
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3
  • 20
    • 0025689272 scopus 로고
    • The effect of conformation on the CD of interacting helices: A theoretical study of tropomyosin
    • T.M. Cooper, and R.W. Woody The effect of conformation on the CD of interacting helices: a theoretical study of tropomyosin Biopolymers 30 1990 657 676
    • (1990) Biopolymers , vol.30 , pp. 657-676
    • Cooper, T.M.1    Woody, R.W.2
  • 21
    • 0021431509 scopus 로고
    • Multiexponential, multicompartmental, and noncompartmental modeling. II. Data analysis and statistical considerations
    • E.M. Landaw, and J.J. DiStefano III Multiexponential, multicompartmental, and noncompartmental modeling. II. Data analysis and statistical considerations Am. J. Physiol. 246 1984 R665 R677
    • (1984) Am. J. Physiol. , vol.246
    • Landaw, E.M.1    Distefano III, J.J.2
  • 22
    • 33745215797 scopus 로고    scopus 로고
    • Hybrid spectrin type repeats produced by exon-skipping in dystrophin
    • N. Menhart Hybrid spectrin type repeats produced by exon-skipping in dystrophin Biochim. Biophys. Acta 1764 2006 993 999
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 993-999
    • Menhart, N.1
  • 24
    • 0025217703 scopus 로고
    • Detailed analysis of the repeat domain of dystrophin reveals four potential hinge segments that may confer flexibility
    • M. Koenig, and L.M. Kunkel Detailed analysis of the repeat domain of dystrophin reveals four potential hinge segments that may confer flexibility J. Biol. Chem. 265 1990 4560 4566
    • (1990) J. Biol. Chem. , vol.265 , pp. 4560-4566
    • Koenig, M.1    Kunkel, L.M.2
  • 26
    • 77953692026 scopus 로고    scopus 로고
    • Specific anchoring modes of two distinct dystrophin rod sub-domains interacting in phospholipid Langmuir films studied by atomic force microscopy and PM-IRRAS
    • V. Vie, S. Legardinier, L. Chieze, O. Le Bihan, Y. Qin, J. Sarkis, J.F. Hubert, A. Renault, B. Desbat, and E. Le Rumeur Specific anchoring modes of two distinct dystrophin rod sub-domains interacting in phospholipid Langmuir films studied by atomic force microscopy and PM-IRRAS Biochim. Biophys. Acta 1798 1503 1511
    • (1798) Biochim. Biophys. Acta , pp. 1503-1511
    • Vie, V.1    Legardinier, S.2    Chieze, L.3    Le Bihan, O.4    Qin, Y.5    Sarkis, J.6    Hubert, J.F.7    Renault, A.8    Desbat, B.9    Le Rumeur, E.10
  • 27
    • 77953692026 scopus 로고    scopus 로고
    • Specific anchoring modes of two distinct dystrophin rod sub-domains interacting in phospholipid Langmuir films studied by atomic force microscopy and PM-IRRAS
    • V. Vie, S. Legardinier, L. Chieze, O. Le Bihan, Y. Qin, J. Sarkis, J.F. Hubert, A. Renault, B. Desbat, and E. Le Rumeur Specific anchoring modes of two distinct dystrophin rod sub-domains interacting in phospholipid Langmuir films studied by atomic force microscopy and PM-IRRAS Biochim. Biophys. Acta 1798 2010 1503 1511
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1503-1511
    • Vie, V.1    Legardinier, S.2    Chieze, L.3    Le Bihan, O.4    Qin, Y.5    Sarkis, J.6    Hubert, J.F.7    Renault, A.8    Desbat, B.9    Le Rumeur, E.10
  • 29
    • 46749083416 scopus 로고    scopus 로고
    • Cooperativity and specificity in enzyme kinetics: A single-molecule time-based perspective
    • H. Qian Cooperativity and specificity in enzyme kinetics: a single-molecule time-based perspective Biophys. J. 95 2008 10 17
    • (2008) Biophys. J. , vol.95 , pp. 10-17
    • Qian, H.1
  • 30
    • 67349085538 scopus 로고    scopus 로고
    • Differential stabilities of alternative exon-skipped rod motifs of dystrophin
    • C. Ruszczak, A. Mirza, and N. Menhart Differential stabilities of alternative exon-skipped rod motifs of dystrophin Biochim. Biophys. Acta 1794 2009 921 928
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 921-928
    • Ruszczak, C.1    Mirza, A.2    Menhart, N.3
  • 32
    • 0029063876 scopus 로고
    • Minimum folding unit of dystrophin rod domain
    • E. Kahana, and W.B. Gratzer Minimum folding unit of dystrophin rod domain Biochemistry 34 1995 8110 8114
    • (1995) Biochemistry , vol.34 , pp. 8110-8114
    • Kahana, E.1    Gratzer, W.B.2
  • 34
    • 0036667981 scopus 로고    scopus 로고
    • Spectrin-like repeats from dystrophin and alpha-actinin-2 are not functionally interchangeable
    • S.Q. Harper, R.W. Crawford, C. DelloRusso, and J.S. Chamberlain Spectrin-like repeats from dystrophin and alpha-actinin-2 are not functionally interchangeable Hum. Mol. Genet. 11 2002 1807 1815
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1807-1815
    • Harper, S.Q.1    Crawford, R.W.2    Dellorusso, C.3    Chamberlain, J.S.4
  • 39
    • 84856546632 scopus 로고    scopus 로고
    • Restoration of the dystrophin-associated glycoprotein complex after exon skipping therapy in Duchenne muscular dystrophy
    • S. Cirak, L. Feng, K. Anthony, V. Arechavala-Gomeza, S. Torelli, C. Sewry, J.E. Morgan, and F. Muntoni Restoration of the dystrophin-associated glycoprotein complex after exon skipping therapy in Duchenne muscular dystrophy Mol. Ther. 20 2012 462 467
    • (2012) Mol. Ther. , vol.20 , pp. 462-467
    • Cirak, S.1    Feng, L.2    Anthony, K.3    Arechavala-Gomeza, V.4    Torelli, S.5    Sewry, C.6    Morgan, J.E.7    Muntoni, F.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.