메뉴 건너뛰기




Volumn 4, Issue 1, 2016, Pages

New insights into the protein aggregation pathology in myotilinopathy by combined proteomic and immunolocalization analyses

Author keywords

Immunolocalization study; Laser microdissection; Mass spectrometry; Myofibrillar myopathy; Myotilinopathy; Protein aggregation

Indexed keywords

MUSCLE PROTEIN;

EID: 85013618076     PISSN: None     EISSN: 20515960     Source Type: Journal    
DOI: 10.1186/s40478-016-0280-0     Document Type: Article
Times cited : (49)

References (64)
  • 1
    • 0029875349 scopus 로고    scopus 로고
    • Myofibrillar myopathy with abnormal foci of desmin positivity I. Light and electron microscopy analysis of 10 cases
    • Nakano S, Engel AG, Waclawik AJ, Emslie-Smith AM, Busis NA. Myofibrillar myopathy with abnormal foci of desmin positivity. I. Light and electron microscopy analysis of 10 cases. J Neuropathol Exp Neurol. 1996;55(5):549-62
    • (1996) J Neuropathol Exp Neurol , vol.55 , Issue.5 , pp. 549-562
    • Nakano, S.1    Engel, A.G.2    Waclawik, A.J.3    Emslie-Smith, A.M.4    Busis, N.A.5
  • 2
    • 0029925575 scopus 로고    scopus 로고
    • Myofibrillar myopathy with abnormal foci of desmin positivity II. Immunocytochemical analysis reveals accumulation of multiple other proteins
    • de Bleecker JL, Engel AG, Ertl BB. Myofibrillar myopathy with abnormal foci of desmin positivity II. Immunocytochemical analysis reveals accumulation of multiple other proteins. J NeuropatholExp Neurol. 1996;55(5):563-77
    • (1996) J NeuropatholExp Neurol , vol.55 , Issue.5 , pp. 563-577
    • de Bleecker, J.L.1    Engel, A.G.2    Ertl, B.B.3
  • 3
    • 0742305818 scopus 로고    scopus 로고
    • Myofibrillar myopathy: clinical, morphological and genetic studies in 63 patients
    • Selcen D, Ohno K, Engel AG. Myofibrillar myopathy: clinical, morphological and genetic studies in 63 patients. Brain. 2004;127(Pt 2):439-51. doi:10.1093/brain/awh052
    • (2004) Brain , vol.127 , pp. 439-451
    • Selcen, D.1    Ohno, K.2    Engel, A.G.3
  • 4
    • 1942473823 scopus 로고    scopus 로고
    • Mutations in myotilin cause myofibrillar myopathy
    • Selcen D, Engel AG. Mutations in myotilin cause myofibrillar myopathy. Neurology. 2004;62(8):1363-71
    • (2004) Neurology , vol.62 , Issue.8 , pp. 1363-1371
    • Selcen, D.1    Engel, A.G.2
  • 5
    • 79960928910 scopus 로고    scopus 로고
    • Clinical and myopathological evaluation of early-and late-onset subtypes of myofibrillar myopathy
    • Olivé M, Odgerel Z, Martínez A, Poza JJ, Bragado FG, Zabalza RJ, et al. Clinical and myopathological evaluation of early-and late-onset subtypes of myofibrillar myopathy. Neuromuscul Disord. 2011;21(8):533-42. doi:10.1016/j.nmd.2011.05.002
    • (2011) Neuromuscul Disord , vol.21 , Issue.8 , pp. 533-542
    • Olivé, M.1    Odgerel, Z.2    Martínez, A.3    Poza, J.J.4    Bragado, F.G.5    Zabalza, R.J.6
  • 6
    • 0344759163 scopus 로고    scopus 로고
    • Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded by a candidate gene for limb-girdle muscular dystrophy
    • Salmikangas P, Mykkänen OM, Grönholm M, Heiska L, Kere J, Carpén O. Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded by a candidate gene for limb-girdle muscular dystrophy. Hum Mol Genet. 1999;8(7):1329-36
    • (1999) Hum Mol Genet , vol.8 , Issue.7 , pp. 1329-1336
    • Salmikangas, P.1    Mykkänen, O.M.2    Grönholm, M.3    Heiska, L.4    Kere, J.5    Carpén, O.6
  • 7
    • 0037439275 scopus 로고    scopus 로고
    • Myotilin, the limb-girdle muscular dystrophy 1A (LGMD1A) protein, cross-links actin filaments and controls sarcomere assembly
    • Salmikangas P, van der Ven PFM, Lalowski M, Taivainen A, Zhao F, Suila H, et al. Myotilin, the limb-girdle muscular dystrophy 1A (LGMD1A) protein, cross-links actin filaments and controls sarcomere assembly. Hum Mol Genet. 2003;12(2):189-203
    • (2003) Hum Mol Genet , vol.12 , Issue.2 , pp. 189-203
    • Salmikangas, P.1    van der Ven, P.F.M.2    Lalowski, M.3    Taivainen, A.4    Zhao, F.5    Suila, H.6
  • 8
    • 0034675887 scopus 로고    scopus 로고
    • Indications for a novel muscular dystrophy pathway. gamma-filamin, the muscle-specific filamin isoform, interacts with myotilin
    • van der Ven PF, Wiesner S, Salmikangas P, Auerbach D, Himmel M, Kempa S, et al. Indications for a novel muscular dystrophy pathway. gamma-filamin, the muscle-specific filamin isoform, interacts with myotilin. J Cell Biol. 2000;151(2):235-48
    • (2000) J Cell Biol , vol.151 , Issue.2 , pp. 235-248
    • van der Ven, P.F.1    Wiesner, S.2    Salmikangas, P.3    Auerbach, D.4    Himmel, M.5    Kempa, S.6
  • 9
    • 24944550989 scopus 로고    scopus 로고
    • The Z-disc proteins myotilin and FATZ-1 interact with each other and are connected to the sarcolemma via muscle-specific filamins
    • Gontier Y, Taivainen A, Fontao L, Sonnenberg A, van der Flier A, Carpen O, et al. The Z-disc proteins myotilin and FATZ-1 interact with each other and are connected to the sarcolemma via muscle-specific filamins. J Cell Sci. 2005;118(Pt 16):3739-49. doi:10.1242/jcs.02484
    • (2005) J Cell Sci , vol.118 , pp. 3739-3749
    • Gontier, Y.1    Taivainen, A.2    Fontao, L.3    Sonnenberg, A.4    van der Flier, A.5    Carpen, O.6
  • 10
    • 59249091710 scopus 로고    scopus 로고
    • A class III PDZ binding motif in the myotilin and FATZ families binds enigma family proteins: a common link for Z-disc myopathies
    • von Nandelstadh P, Ismail M, Gardin C, Suila H, Zara I, Belgrano A, et al. A class III PDZ binding motif in the myotilin and FATZ families binds enigma family proteins: a common link for Z-disc myopathies. Mol Cell Biol. 2009;29(3):822-34. doi:10.1128/MCB.01454-08
    • (2009) Mol Cell Biol , vol.29 , Issue.3 , pp. 822-834
    • von Nandelstadh, P.1    Ismail, M.2    Gardin, C.3    Suila, H.4    Zara, I.5    Belgrano, A.6
  • 11
    • 26044435388 scopus 로고    scopus 로고
    • Myotilinopathy: refining the clinical and myopathological phenotype
    • Olivé M, Goldfarb LG, Shatunov A, Fischer D, Ferrer I. Myotilinopathy: refining the clinical and myopathological phenotype. Brain. 2005;128(Pt 10):2315-26. doi:10.1093/brain/awh576
    • (2005) Brain , vol.128 , pp. 2315-2326
    • Olivé, M.1    Goldfarb, L.G.2    Shatunov, A.3    Fischer, D.4    Ferrer, I.5
  • 12
    • 66949173652 scopus 로고    scopus 로고
    • Myofibrillar myopathies: a clinical and myopathological guide
    • Schröder R, Schoser B. Myofibrillar myopathies: a clinical and myopathological guide. Brain Pathol. 2009;19(3):483-92. doi:10.1111/j.1750-3639.2009.00289.x
    • (2009) Brain Pathol , vol.19 , Issue.3 , pp. 483-492
    • Schröder, R.1    Schoser, B.2
  • 13
    • 66949120632 scopus 로고    scopus 로고
    • Extralysosomal protein degradation in myofibrillar myopathies
    • Olivé M. Extralysosomal protein degradation in myofibrillar myopathies. Brain Pathol. 2009;19(3):507-15. doi:10.1111/j.1750-3639.2009.00288.x
    • (2009) Brain Pathol , vol.19 , Issue.3 , pp. 507-515
    • Olivé, M.1
  • 16
    • 61349154811 scopus 로고    scopus 로고
    • Differential involvement of sarcomeric proteins in myofibrillar myopathies: a morphological and immunohistochemical study
    • Claeys KG, van der Ven PFM, Behin A, Stojkovic T, Eymard B, Dubourg O, et al. Differential involvement of sarcomeric proteins in myofibrillar myopathies: a morphological and immunohistochemical study. Acta Neuropathol. 2009;117(3):293-307. doi:10.1007/s00401-008-0479-7
    • (2009) Acta Neuropathol , vol.117 , Issue.3 , pp. 293-307
    • Claeys, K.G.1    van der Ven, P.F.M.2    Behin, A.3    Stojkovic, T.4    Eymard, B.5    Dubourg, O.6
  • 17
    • 84871880606 scopus 로고    scopus 로고
    • A combined laser microdissection and mass spectrometry approach reveals new disease relevant proteins accumulating in aggregates of filaminopathy patients
    • Kley RA, Maerkens A, Leber Y, Theis V, Schreiner A, van der Ven PFM, et al. A combined laser microdissection and mass spectrometry approach reveals new disease relevant proteins accumulating in aggregates of filaminopathy patients. Mol Cell Proteomics. 2013;12(1):215-27. doi:10.1074/mcp.M112.023176
    • (2013) Mol Cell Proteomics , vol.12 , Issue.1 , pp. 215-227
    • Kley, R.A.1    Maerkens, A.2    Leber, Y.3    Theis, V.4    Schreiner, A.5    van der Ven, P.F.M.6
  • 18
    • 84882686603 scopus 로고    scopus 로고
    • Differential proteomic analysis of abnormal intramyoplasmic aggregates in desminopathy
    • Maerkens A, Kley RA, Olivé M, Theis V, van der Ven PFM, Reimann J, et al. Differential proteomic analysis of abnormal intramyoplasmic aggregates in desminopathy. J Proteomics. 2013;90:14-27. doi:10.1016/j.jprot.2013.04.026
    • (2013) J Proteomics , vol.90 , pp. 14-27
    • Maerkens, A.1    Kley, R.A.2    Olivé, M.3    Theis, V.4    van der Ven, P.F.M.5    Reimann, J.6
  • 20
    • 33745101996 scopus 로고    scopus 로고
    • Different early pathogenesis in myotilinopathy compared to primary desminopathy
    • Fischer D, Clemen CS, Olivé M, Ferrer I, Goudeau B, Roth U, et al. Different early pathogenesis in myotilinopathy compared to primary desminopathy. Neuromuscul Disord. 2006;16(6):361-7. doi:10.1016/j.nmd. 2006.03.007
    • (2006) Neuromuscul Disord , vol.16 , Issue.6 , pp. 361-367
    • Fischer, D.1    Clemen, C.S.2    Olivé, M.3    Ferrer, I.4    Goudeau, B.5    Roth, U.6
  • 22
    • 0033515454 scopus 로고    scopus 로고
    • A high molecular weight intermediate filament-associated protein in BHK-21 cells is nestin, a type VI intermediate filament protein. Limited co-assembly in vitro to form heteropolymers with type III vimentin and type IV alpha-internexin
    • Steinert PM, Chou YH, Prahlad V, Parry DA, Marekov LN, Wu KC, et al. A high molecular weight intermediate filament-associated protein in BHK-21 cells is nestin, a type VI intermediate filament protein. Limited co-assembly in vitro to form heteropolymers with type III vimentin and type IV alpha-internexin. J Biol Chem. 1999;274(14):9881-90
    • (1999) J Biol Chem , vol.274 , Issue.14 , pp. 9881-9890
    • Steinert, P.M.1    Chou, Y.H.2    Prahlad, V.3    Parry, D.A.4    Marekov, L.N.5    Wu, K.C.6
  • 23
    • 0036479311 scopus 로고    scopus 로고
    • Association of syncoilin and desmin: linking intermediate filament proteins to the dystrophin-associated protein complex
    • Poon E, Howman EV, Newey SE, Davies KE. Association of syncoilin and desmin: linking intermediate filament proteins to the dystrophin-associated protein complex. J Biol Chem. 2002;277(5):3433-9. doi:10.1074/jbc. M105273200
    • (2002) J Biol Chem , vol.277 , Issue.5 , pp. 3433-3439
    • Poon, E.1    Howman, E.V.2    Newey, S.E.3    Davies, K.E.4
  • 24
    • 0037295486 scopus 로고    scopus 로고
    • Plectin tethers desmin intermediate filaments onto subsarcolemmal dense plaques containing dystrophin and vinculin
    • Hijikata T, Murakami T, Ishikawa H, Yorifuji H. Plectin tethers desmin intermediate filaments onto subsarcolemmal dense plaques containing dystrophin and vinculin. Histochem Cell Biol. 2003;119(2):109-23. doi:10. 1007/s00418-003-0496-5
    • (2003) Histochem Cell Biol , vol.119 , Issue.2 , pp. 109-123
    • Hijikata, T.1    Murakami, T.2    Ishikawa, H.3    Yorifuji, H.4
  • 25
    • 33744941082 scopus 로고    scopus 로고
    • Unusual splicing events result in distinct Xin isoforms that associate differentially with filamin c and Mena/VASP
    • van der Ven PFM, Ehler E, Vakeel P, Eulitz S, Schenk JA, Milting H, et al. Unusual splicing events result in distinct Xin isoforms that associate differentially with filamin c and Mena/VASP. Exp Cell Res. 2006;312(11):2154-67. doi:10.1016/j.yexcr.2006.03.015
    • (2006) Exp Cell Res , vol.312 , Issue.11 , pp. 2154-2167
    • van der Ven, P.F.M.1    Ehler, E.2    Vakeel, P.3    Eulitz, S.4    Schenk, J.A.5    Milting, H.6
  • 26
    • 0038348502 scopus 로고    scopus 로고
    • Archvillin, a muscle-specific isoform of supervillin, is an early expressed component of the costameric membrane skeleton
    • Oh SW, Pope RK, Smith KP, Crowley JL, Nebl T, Lawrence JB, et al. Archvillin, a muscle-specific isoform of supervillin, is an early expressed component of the costameric membrane skeleton. J Cell Sci. 2003;116(Pt 11):2261-75. doi:10.1242/jcs.00422
    • (2003) J Cell Sci , vol.116 , pp. 2261-2275
    • Oh, S.W.1    Pope, R.K.2    Smith, K.P.3    Crowley, J.L.4    Nebl, T.5    Lawrence, J.B.6
  • 28
    • 0026694490 scopus 로고
    • Alpha B-crystallin in cardiac tissue. Association with actin and desmin filaments
    • Bennardini F, Wrzosek A, Chiesi M. Alpha B-crystallin in cardiac tissue. Association with actin and desmin filaments. Circ Res. 1992;71(2):288-94
    • (1992) Circ Res , vol.71 , Issue.2 , pp. 288-294
    • Bennardini, F.1    Wrzosek, A.2    Chiesi, M.3
  • 29
    • 0026774629 scopus 로고
    • Copurification of small heat shock protein with alpha B crystallin from human skeletal muscle
    • Kato K, Shinohara H, Goto S, Inaguma Y, Morishita R, Asano T. Copurification of small heat shock protein with alpha B crystallin from human skeletal muscle. J Biol Chem. 1992;267(11):7718-25
    • (1992) J Biol Chem , vol.267 , Issue.11 , pp. 7718-7725
    • Kato, K.1    Shinohara, H.2    Goto, S.3    Inaguma, Y.4    Morishita, R.5    Asano, T.6
  • 30
    • 0026632361 scopus 로고
    • Heat shock protein 27 and alpha B-crystallin can form a complex, which dissociates by heat shock
    • Zantema A, Verlaan-De Vries M, Maasdam D, Bol S, van der Eb A. Heat shock protein 27 and alpha B-crystallin can form a complex, which dissociates by heat shock. J Biol Chem. 1992;267(18):12936-41
    • (1992) J Biol Chem , vol.267 , Issue.18 , pp. 12936-12941
    • Zantema, A.1    Verlaan-De Vries, M.2    Maasdam, D.3    Bol, S.4    van der Eb, A.5
  • 31
    • 36749069412 scopus 로고    scopus 로고
    • Clinical and morphological phenotype of the filamin myopathy: a study of 31 German patients
    • Kley RA, Hellenbroich Y, van der Ven PFM, Fürst DO, Huebner A, Bruchertseifer V, et al. Clinical and morphological phenotype of the filamin myopathy: a study of 31 German patients. Brain. 2007;130(Pt 12):3250-64. doi:10.1093/brain/awm271
    • (2007) Brain , vol.130 , pp. 3250-3264
    • Kley, R.A.1    Hellenbroich, Y.2    van der Ven, P.F.M.3    Fürst, D.O.4    Huebner, A.5    Bruchertseifer, V.6
  • 32
    • 51349145767 scopus 로고    scopus 로고
    • Molecular pathology of myofibrillar myopathies
    • Ferrer I, Olivé M. Molecular pathology of myofibrillar myopathies. Expert Rev Mol Med. 2008;10, e25. doi:10.1017/S1462399408000793
    • (2008) Expert Rev Mol Med , vol.10
    • Ferrer, I.1    Olivé, M.2
  • 33
    • 33947722764 scopus 로고    scopus 로고
    • Plectin 1f scaffolding at the sarcolemma of dystrophic (mdx) muscle fibers through multiple interactions with beta-dystroglycan
    • Rezniczek GA, Konieczny P, Nikolic B, Reipert S, Schneller D, Abrahamsberg C, et al. Plectin 1f scaffolding at the sarcolemma of dystrophic (mdx) muscle fibers through multiple interactions with beta-dystroglycan. J Cell Biol. 2007;176(7):965-77. doi:10.1083/jcb.200604179
    • (2007) J Cell Biol , vol.176 , Issue.7 , pp. 965-977
    • Rezniczek, G.A.1    Konieczny, P.2    Nikolic, B.3    Reipert, S.4    Schneller, D.5    Abrahamsberg, C.6
  • 34
    • 42949160078 scopus 로고    scopus 로고
    • Muscle interstitial fibroblasts are the main source of collagen VI synthesis in skeletal muscle: implications for congenital muscular dystrophy types Ullrich and Bethlem
    • Zou Y, Zhang R, Sabatelli P, Chu M, Bönnemann CG. Muscle interstitial fibroblasts are the main source of collagen VI synthesis in skeletal muscle: implications for congenital muscular dystrophy types Ullrich and Bethlem. J Neuropathol Exp Neurol. 2008;67(2):144-54. doi:10.1097/nen. 0b013e3181634ef7
    • (2008) J Neuropathol Exp Neurol , vol.67 , Issue.2 , pp. 144-154
    • Zou, Y.1    Zhang, R.2    Sabatelli, P.3    Chu, M.4    Bönnemann, C.G.5
  • 35
    • 2442651500 scopus 로고    scopus 로고
    • Proteasomal expression, induction of immunoproteasome subunits, and local MHC class I presentation in myofibrillar myopathy and inclusion body myositis
    • Ferrer I, Martín B, Castaño JG, Lucas JJ, Moreno D, Olivé M. Proteasomal expression, induction of immunoproteasome subunits, and local MHC class I presentation in myofibrillar myopathy and inclusion body myositis. J Neuropathol Exp Neurol. 2004;63(5):484-98
    • (2004) J Neuropathol Exp Neurol , vol.63 , Issue.5 , pp. 484-498
    • Ferrer, I.1    Martín, B.2    Castaño, J.G.3    Lucas, J.J.4    Moreno, D.5    Olivé, M.6
  • 36
    • 84866360574 scopus 로고    scopus 로고
    • Pathophysiology of protein aggregation and extended phenotyping in filaminopathy
    • Kley RA, Serdaroglu-Oflazer P, Leber Y, Odgerel Z, van der Ven PFM, Olivé M, et al. Pathophysiology of protein aggregation and extended phenotyping in filaminopathy. Brain. 2012;135(Pt 9):2642-60. doi:10.1093/brain/aws200
    • (2012) Brain , vol.135 , pp. 2642-2660
    • Kley, R.A.1    Serdaroglu-Oflazer, P.2    Leber, Y.3    Odgerel, Z.4    van der Ven, P.F.M.5    Olivé, M.6
  • 37
    • 84904691818 scopus 로고    scopus 로고
    • Instructive roles of extracellular matrix on autophagy
    • Neill T, Schaefer L, Iozzo RV. Instructive roles of extracellular matrix on autophagy. Am J Pathol. 2014;184(8):2146-53. doi:10.1016/j.ajpath.2014.05.010
    • (2014) Am J Pathol , vol.184 , Issue.8 , pp. 2146-2153
    • Neill, T.1    Schaefer, L.2    Iozzo, R.V.3
  • 38
    • 84934298725 scopus 로고    scopus 로고
    • Amino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding
    • Cha-Molstad H, Sung KS, Hwang J, Kim KA, Yu JE, Yoo YD, et al. Amino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding. Nat Cell Biol. 2015;17(7):917-29. doi:10.1038/ncb3177
    • (2015) Nat Cell Biol , vol.17 , Issue.7 , pp. 917-929
    • Cha-Molstad, H.1    Sung, K.S.2    Hwang, J.3    Kim, K.A.4    Yu, J.E.5    Yoo, Y.D.6
  • 39
    • 74549133523 scopus 로고    scopus 로고
    • Chaperone-assisted selective autophagy is essential for muscle maintenance
    • Arndt V, Dick N, Tawo R, Dreiseidler M, Wenzel D, Hesse M, et al. Chaperone-assisted selective autophagy is essential for muscle maintenance. Curr Biol. 2010;20(2):143-8. doi:10.1016/j.cub.2009.11.022
    • (2010) Curr Biol , vol.20 , Issue.2 , pp. 143-148
    • Arndt, V.1    Dick, N.2    Tawo, R.3    Dreiseidler, M.4    Wenzel, D.5    Hesse, M.6
  • 40
    • 84875210317 scopus 로고    scopus 로고
    • Cellular mechanotransduction relies on tension-induced and chaperoneassisted autophagy
    • Ulbricht A, Eppler FJ, Tapia VE, van der Ven PFM, Hampe N, Hersch N, et al. Cellular mechanotransduction relies on tension-induced and chaperoneassisted autophagy. Curr Biol. 2013;23(5):430-5. doi:10.1016/j.cub.2013.01.064
    • (2013) Curr Biol , vol.23 , Issue.5 , pp. 430-435
    • Ulbricht, A.1    Eppler, F.J.2    Tapia, V.E.3    van der Ven, P.F.M.4    Hampe, N.5    Hersch, N.6
  • 41
    • 84922042515 scopus 로고    scopus 로고
    • Ascribing novel functions to the sarcomeric protein, myosin binding protein H (MyBPH) in cardiac sarcomere contraction
    • Mouton J, Loos B, Moolman-Smook JC, Kinnear CJ. Ascribing novel functions to the sarcomeric protein, myosin binding protein H (MyBPH) in cardiac sarcomere contraction. Exp Cell Res. 2015;331(2):338-51. doi:10.1016/j.yexcr.2014.11.006
    • (2015) Exp Cell Res , vol.331 , Issue.2 , pp. 338-351
    • Mouton, J.1    Loos, B.2    Moolman-Smook, J.C.3    Kinnear, C.J.4
  • 43
    • 78349273136 scopus 로고    scopus 로고
    • Heat shock proteins: cell protection through protein triage
    • Lanneau D, Wettstein G, Bonniaud P, Garrido C. Heat shock proteins: cell protection through protein triage. ScientificWorldJournal. 2010;10:1543-52. doi:10.1100/tsw.2010.152
    • (2010) ScientificWorldJournal , vol.10 , pp. 1543-1552
    • Lanneau, D.1    Wettstein, G.2    Bonniaud, P.3    Garrido, C.4
  • 44
    • 0035847115 scopus 로고    scopus 로고
    • Interaction between alphaB-crystallin and the human 20S proteasomal subunit C8/alpha7
    • Boelens WC, Croes Y, de Jong WW. Interaction between alphaB-crystallin and the human 20S proteasomal subunit C8/alpha7. Biochim Biophys Acta. 2001;1544(1-2):311-9
    • (2001) Biochim Biophys Acta , vol.1544 , Issue.1-2 , pp. 311-319
    • Boelens, W.C.1    Croes, Y.2    de Jong, W.W.3
  • 45
    • 0242637569 scopus 로고    scopus 로고
    • AlphaB-crystallin modulates protein aggregation of abnormal desmin
    • Wang X, Klevitsky R, Huang W, Glasford J, Li F, Robbins J. AlphaB-crystallin modulates protein aggregation of abnormal desmin. Circ Res. 2003;93(10): 998-1005. doi:10.1161/01.RES.0000102401.77712.ED
    • (2003) Circ Res , vol.93 , Issue.10 , pp. 998-1005
    • Wang, X.1    Klevitsky, R.2    Huang, W.3    Glasford, J.4    Li, F.5    Robbins, J.6
  • 46
    • 33645055949 scopus 로고    scopus 로고
    • Aberrant protein aggregation is essential for a mutant desmin to impair the proteolytic function of the ubiquitinproteasome system in cardiomyocytes
    • Liu J, Tang M, Mestril R, Wang X. Aberrant protein aggregation is essential for a mutant desmin to impair the proteolytic function of the ubiquitinproteasome system in cardiomyocytes. J Mol Cell Cardiol. 2006;40(4):451-4. doi:10.1016/j.yjmcc.2005.12.011
    • (2006) J Mol Cell Cardiol , vol.40 , Issue.4 , pp. 451-454
    • Liu, J.1    Tang, M.2    Mestril, R.3    Wang, X.4
  • 47
    • 0038104369 scopus 로고    scopus 로고
    • Distinct chaperone mechanisms can delay the formation of aggresomes by the myopathy-causing R120G alphaB-crystallin mutant
    • Chavez Zobel AT, Loranger A, Marceau N, Theriault JR, Lambert H, Landry J. Distinct chaperone mechanisms can delay the formation of aggresomes by the myopathy-causing R120G alphaB-crystallin mutant. Hum Mol Genet. 2003;12(13):1609-20
    • (2003) Hum Mol Genet , vol.12 , Issue.13 , pp. 1609-1620
    • Chavez Zobel, A.T.1    Loranger, A.2    Marceau, N.3    Theriault, J.R.4    Lambert, H.5    Landry, J.6
  • 49
    • 65449170415 scopus 로고    scopus 로고
    • Protective effect of geranylgeranylacetone via enhancement of HSPB8 induction in desmin-related cardiomyopathy
    • Sanbe A, Daicho T, Mizutani R, Endo T, Miyauchi N, Yamauchi J, et al. Protective effect of geranylgeranylacetone via enhancement of HSPB8 induction in desmin-related cardiomyopathy. PLoS One. 2009;4(4), e5351. doi:10.1371/journal.pone.0005351
    • (2009) PLoS One , vol.4 , Issue.4
    • Sanbe, A.1    Daicho, T.2    Mizutani, R.3    Endo, T.4    Miyauchi, N.5    Yamauchi, J.6
  • 50
    • 35148847303 scopus 로고    scopus 로고
    • Oxidative stress in desminopathies and myotilinopathies: a link between oxidative damage and abnormal protein aggregation
    • Janué A, Olivé M, Ferrer I. Oxidative stress in desminopathies and myotilinopathies: a link between oxidative damage and abnormal protein aggregation. Brain Pathol. 2007;17(4):377-88. doi:10.1111/j.1750-3639.2007.00087.x
    • (2007) Brain Pathol , vol.17 , Issue.4 , pp. 377-388
    • Janué, A.1    Olivé, M.2    Ferrer, I.3
  • 51
    • 38549169530 scopus 로고    scopus 로고
    • The two faces of protein misfolding: gain-and loss-of-function in neurodegenerative diseases
    • Winklhofer KF, Tatzelt J, Haass C. The two faces of protein misfolding: gain-and loss-of-function in neurodegenerative diseases. EMBO J. 2008;27(2):336-49. doi:10.1038/sj.emboj.7601930
    • (2008) EMBO J , vol.27 , Issue.2 , pp. 336-349
    • Winklhofer, K.F.1    Tatzelt, J.2    Haass, C.3
  • 52
    • 84155167265 scopus 로고    scopus 로고
    • Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration
    • Lee EB, Lee VM, Trojanowski JQ. Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration. Nat Rev Neurosci. 2012;13(1):38-50. doi:10.1038/nrn3121
    • (2012) Nat Rev Neurosci , vol.13 , Issue.1 , pp. 38-50
    • Lee, E.B.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 53
    • 78549244048 scopus 로고    scopus 로고
    • BAG3 and Hsc70 interact with actin capping protein CapZ to maintain myofibrillar integrity under mechanical stress
    • Hishiya A, Kitazawa T, Takayama S. BAG3 and Hsc70 interact with actin capping protein CapZ to maintain myofibrillar integrity under mechanical stress. Circ Res. 2010;107(10):1220-31. doi:10.1161/CIRCRESAHA.110.225649
    • (2010) Circ Res , vol.107 , Issue.10 , pp. 1220-1231
    • Hishiya, A.1    Kitazawa, T.2    Takayama, S.3
  • 54
    • 84855913811 scopus 로고    scopus 로고
    • Scaffolds and chaperones in myofibril assembly: putting the striations in striated muscle
    • Crawford GL, Horowits R. Scaffolds and chaperones in myofibril assembly: putting the striations in striated muscle. Biophys Rev. 2011;3(1):25-32. doi:10.1007/s12551-011-0043-x
    • (2011) Biophys Rev , vol.3 , Issue.1 , pp. 25-32
    • Crawford, G.L.1    Horowits, R.2
  • 55
    • 0033104818 scopus 로고    scopus 로고
    • Binding of the stress protein alpha B-crystallin to cardiac myofibrils correlates with the degree of myocardial damage during ischemia/reperfusion in vivo
    • Golenhofen N, Htun P, Ness W, Koob R, Schaper W, Drenckhahn D. Binding of the stress protein alpha B-crystallin to cardiac myofibrils correlates with the degree of myocardial damage during ischemia/reperfusion in vivo. J Mol Cell Cardiol. 1999;31(3):569-80. doi:10.1006/jmcc.1998.0892
    • (1999) J Mol Cell Cardiol , vol.31 , Issue.3 , pp. 569-580
    • Golenhofen, N.1    Htun, P.2    Ness, W.3    Koob, R.4    Schaper, W.5    Drenckhahn, D.6
  • 56
    • 43249119946 scopus 로고    scopus 로고
    • MURC, a muscle-restricted coiled-coil protein that modulates the Rho/ROCK pathway, induces cardiac dysfunction and conduction disturbance
    • Ogata T, Ueyama T, Isodono K, Tagawa M, Takehara N, Kawashima T, et al. MURC, a muscle-restricted coiled-coil protein that modulates the Rho/ROCK pathway, induces cardiac dysfunction and conduction disturbance. Mol Cell Biol. 2008;28(10):3424-36. doi:10.1128/MCB.02186-07
    • (2008) Mol Cell Biol , vol.28 , Issue.10 , pp. 3424-3436
    • Ogata, T.1    Ueyama, T.2    Isodono, K.3    Tagawa, M.4    Takehara, N.5    Kawashima, T.6
  • 57
    • 84855162727 scopus 로고    scopus 로고
    • Tropomodulin capping of actin filaments in striated muscle development and physiology
    • Gokhin DS, Fowler VM. Tropomodulin capping of actin filaments in striated muscle development and physiology. J Biomed Biotechnol. 2011;2011:103069. doi:10.1155/2011/103069
    • (2011) J Biomed Biotechnol , vol.2011
    • Gokhin, D.S.1    Fowler, V.M.2
  • 58
    • 84904480041 scopus 로고    scopus 로고
    • Human muscle LIM protein dimerizes along the actin cytoskeleton and cross-links actin filaments
    • Hoffmann C, Moreau F, Moes M, Luthold C, Dieterle M, Goretti E, et al. Human muscle LIM protein dimerizes along the actin cytoskeleton and cross-links actin filaments. Mol Cell Biol. 2014;34(16):3053-65. doi:10.1128/ MCB.00651-14
    • (2014) Mol Cell Biol , vol.34 , Issue.16 , pp. 3053-3065
    • Hoffmann, C.1    Moreau, F.2    Moes, M.3    Luthold, C.4    Dieterle, M.5    Goretti, E.6
  • 59
    • 0033952929 scopus 로고    scopus 로고
    • Characterization of muscle filamin isoforms suggests a possible role of gamma-filamin/ABP-L in sarcomeric Z-disc formation
    • van der Ven PF, Obermann WM, Lemke B, Gautel M, Weber K, Furst DO. Characterization of muscle filamin isoforms suggests a possible role of gamma-filamin/ABP-L in sarcomeric Z-disc formation. Cell Motil Cytoskeleton. 2000;45(2):149-62. doi:10.1002/(SICI)1097-0169(200002)45: 2<149:AID-CM6>3.0.CO;2-G
    • (2000) Cell Motil Cytoskeleton , vol.45 , Issue.2 , pp. 149-162
    • van der Ven, P.F.1    Obermann, W.M.2    Lemke, B.3    Gautel, M.4    Weber, K.5    Furst, D.O.6
  • 60
    • 0035938225 scopus 로고    scopus 로고
    • Structural and functional aspects of filamins
    • van der Flier A, Sonnenberg A. Structural and functional aspects of filamins. Biochim Biophys Acta. 2001;1538(2-3):99-117
    • (2001) Biochim Biophys Acta , vol.1538 , Issue.2-3 , pp. 99-117
    • van der Flier, A.1    Sonnenberg, A.2
  • 61
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: from stress pathway to homeostatic regulation
    • Walter P, Ron D. The unfolded protein response: from stress pathway to homeostatic regulation. Science. 2011;334(6059):1081-6. doi:10.1126/science. 1209038
    • (2011) Science , vol.334 , Issue.6059 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 62
    • 34447296195 scopus 로고    scopus 로고
    • The pathomechanism of filaminopathy: altered biochemical properties explain the cellular phenotype of a protein aggregation myopathy
    • Lowe T, Kley RA, van der Ven PFM, Himmel M, Huebner A, Vorgerd M, et al. The pathomechanism of filaminopathy: altered biochemical properties explain the cellular phenotype of a protein aggregation myopathy. Hum Mol Genet. 2007;16(11):1351-8. doi:10.1093/hmg/ddm085
    • (2007) Hum Mol Genet , vol.16 , Issue.11 , pp. 1351-1358
    • Lowe, T.1    Kley, R.A.2    van der Ven, P.F.M.3    Himmel, M.4    Huebner, A.5    Vorgerd, M.6
  • 63
    • 84885618582 scopus 로고    scopus 로고
    • Identification of Xin-repeat proteins as novel ligands of the SH3 domains of nebulin and nebulette and analysis of their interaction during myofibril formation and remodeling
    • Eulitz S, Sauer F, Pelissier M, Boisguerin P, Molt S, Schuld J, et al. Identification of Xin-repeat proteins as novel ligands of the SH3 domains of nebulin and nebulette and analysis of their interaction during myofibril formation and remodeling. Mol Biol Cell. 2013;24(20):3215-26. doi:10.1091/mbc.E13-04-0202
    • (2013) Mol Biol Cell , vol.24 , Issue.20 , pp. 3215-3226
    • Eulitz, S.1    Sauer, F.2    Pelissier, M.3    Boisguerin, P.4    Molt, S.5    Schuld, J.6
  • 64
    • 84888306075 scopus 로고    scopus 로고
    • Xin is a marker of skeletal muscle damage severity in myopathies
    • Nilsson MI, Nissar AA, Al-Sajee D, Tarnopolsky MA, Parise G, Lach B, et al. Xin is a marker of skeletal muscle damage severity in myopathies. Am J Pathol. 2013;183(6):1703-9. doi:10.1016/j.ajpath.2013.08.010
    • (2013) Am J Pathol , vol.183 , Issue.6 , pp. 1703-1709
    • Nilsson, M.I.1    Nissar, A.A.2    Al-Sajee, D.3    Tarnopolsky, M.A.4    Parise, G.5    Lach, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.