메뉴 건너뛰기




Volumn , Issue , 2011, Pages 55-87

Functional symbiosis between the intermediate filament cytoskeleton and small heat shock proteins

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84895325708     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (2)

References (230)
  • 1
    • 34447318642 scopus 로고    scopus 로고
    • Evolution of the cytoskeleton
    • Jul
    • Erickson HP. Evolution of the cytoskeleton. Bioessays. 2007 Jul;29(7):668-77.
    • (2007) Bioessays. , vol.29 , Issue.7 , pp. 668-677
    • Erickson, H.P.1
  • 2
    • 0030030256 scopus 로고    scopus 로고
    • Degradation of nuclear matrix and DNA cleavage in apoptotic thymocytes
    • Weaver VM, Carson CE, Walker PR, Chaly N, Lach B, Raymond Y, et al. Degradation of nuclear matrix and DNA cleavage in apoptotic thymocytes. J Cell Sci. 1996;109(Pt 1):45-56.
    • (1996) J Cell Sci. , vol.109 , Issue.PART 1 , pp. 45-56
    • Weaver, V.M.1    Carson, C.E.2    Walker, P.R.3    Chaly, N.4    Lach, B.5    Raymond, Y.6
  • 3
    • 65449137972 scopus 로고    scopus 로고
    • Bacterial intermediate filaments: in vivo assembly, organization, and dynamics of crescentin
    • May 1
    • Charbon G, Cabeen MT, Jacobs-Wagner C. Bacterial intermediate filaments: in vivo assembly, organization, and dynamics of crescentin. Genes Dev. 2009 May 1;23(9):1131-44.
    • (2009) Genes Dev. , vol.23 , Issue.9 , pp. 1131-1144
    • Charbon, G.1    Cabeen, M.T.2    Jacobs-Wagner, C.3
  • 4
    • 62949149564 scopus 로고    scopus 로고
    • Assembly of the MreB-associated cytoskeletal ring of Escherichia coli
    • Apr
    • Vats P, Shih YL, Rothfield L. Assembly of the MreB-associated cytoskeletal ring of Escherichia coli. Mol Microbiol. 2009 Apr;72(1):170-82.
    • (2009) Mol Microbiol. , vol.72 , Issue.1 , pp. 170-182
    • Vats, P.1    Shih, Y.L.2    Rothfield, L.3
  • 5
    • 41749083933 scopus 로고    scopus 로고
    • Novel coiled-coil cell division factor ZapB stimulates Z ring assembly and cell division
    • May
    • Ebersbach G, Galli E, Moller-Jensen J, Lowe J, Gerdes K. Novel coiled-coil cell division factor ZapB stimulates Z ring assembly and cell division. Mol Microbiol. 2008 May;68(3):720-35.
    • (2008) Mol Microbiol. , vol.68 , Issue.3 , pp. 720-735
    • Ebersbach, G.1    Galli, E.2    Moller-Jensen, J.3    Lowe, J.4    Gerdes, K.5
  • 6
    • 54249099195 scopus 로고    scopus 로고
    • Intermediate filament-like proteins in bacteria and a cytoskeletal function in Streptomyces
    • Nov
    • Bagchi S, Tomenius H, Belova LM, Ausmees N. Intermediate filament-like proteins in bacteria and a cytoskeletal function in Streptomyces. Mol Microbiol. 2008 Nov;70(4):1037-50.
    • (2008) Mol Microbiol. , vol.70 , Issue.4 , pp. 1037-1050
    • Bagchi, S.1    Tomenius, H.2    Belova, L.M.3    Ausmees, N.4
  • 7
    • 0032818827 scopus 로고    scopus 로고
    • Intermediate filament interactions can be altered by HSP27 and alphaB-crystallin
    • Jul
    • Perng MD, Cairns L, van den IP, Prescott A, Hutcheson AM, Quinlan RA. Intermediate filament interactions can be altered by HSP27 and alphaB-crystallin. J Cell Sci. 1999 Jul;112 (Pt 13):2099-112.
    • (1999) J Cell Sci. , vol.112 , Issue.PART 13 , pp. 2099-2112
    • Perng, M.D.1    Cairns, L.2    van den, I.P.3    Prescott, A.4    Hutcheson, A.M.5    Quinlan, R.A.6
  • 8
    • 57349200349 scopus 로고    scopus 로고
    • GFAP Filaments Can Tolerate the Incorporation of Assembly-compromised GFAP-{delta}, but with Consequences for Filament Organization and {alpha}B-crystallin Association
    • Aug 13
    • Perng MD, Wen SF, Gibbon T, Middeldorp J, Sluijs JA, Hol EM, et al. GFAP Filaments Can Tolerate the Incorporation of Assembly-compromised GFAP-{delta}, but with Consequences for Filament Organization and {alpha}B-crystallin Association. Mol Biol Cell, 2008 Aug 13.
    • (2008) Mol Biol Cell
    • Perng, M.D.1    Wen, S.F.2    Gibbon, T.3    Middeldorp, J.4    Sluijs, J.A.5    Hol, E.M.6
  • 9
    • 0036366525 scopus 로고    scopus 로고
    • Cytoskeletal competence requires protein chaperones
    • Quinlan R. Cytoskeletal competence requires protein chaperones. Prog Mol Subcell Biol. 2002;28:219-33.
    • (2002) Prog Mol Subcell Biol. , vol.28 , pp. 219-233
    • Quinlan, R.1
  • 10
    • 65649100437 scopus 로고    scopus 로고
    • Bacterial cell curvature through mechanical control of cell growth
    • May 6
    • Cabeen MT, Charbon G, Vollmer W, Born P, Ausmees N, Weibel DB, et al. Bacterial cell curvature through mechanical control of cell growth. EMBO J. 2009 May 6;28(9):1208-19.
    • (2009) EMBO J. , vol.28 , Issue.9 , pp. 1208-1219
    • Cabeen, M.T.1    Charbon, G.2    Vollmer, W.3    Born, P.4    Ausmees, N.5    Weibel, D.B.6
  • 11
    • 33745610496 scopus 로고    scopus 로고
    • Regulation of Streptomyces development: reach for the sky! Trends Microbiol
    • Jul
    • Claessen D, de Jong W, Dijkhuizen L, Wosten HA. Regulation of Streptomyces development: reach for the sky! Trends Microbiol. 2006 Jul;14(7):313-9.
    • (2006) , vol.14 , Issue.7 , pp. 313-319
    • Claessen, D.1    de Jong, W.2    Dijkhuizen, L.3    Wosten, H.A.4
  • 12
    • 58949096499 scopus 로고    scopus 로고
    • Syncoilin isoform organization and differential expression in murine striated muscle
    • Mar
    • Kemp MW, Edwards B, Burgess M, Clarke WT, Nicholson G, Parry DA, et al. Syncoilin isoform organization and differential expression in murine striated muscle. J Struct Biol. 2009 Mar;165(3):196-203.
    • (2009) J Struct Biol. , vol.165 , Issue.3 , pp. 196-203
    • Kemp, M.W.1    Edwards, B.2    Burgess, M.3    Clarke, W.T.4    Nicholson, G.5    Parry, D.A.6
  • 13
    • 0035794230 scopus 로고    scopus 로고
    • Syncoilin, a novel member of the intermediate filament superfamily that interacts with alpha-dystrobrevin in skeletal muscle
    • Mar 2
    • Newey SE, Howman EV, Ponting CP, Benson MA, Nawrotzki R, Loh NY, et al. Syncoilin, a novel member of the intermediate filament superfamily that interacts with alpha-dystrobrevin in skeletal muscle. J Biol Chem. 2001 Mar 2;276(9):6645-55.
    • (2001) J Biol Chem. , vol.276 , Issue.9 , pp. 6645-6655
    • Newey, S.E.1    Howman, E.V.2    Ponting, C.P.3    Benson, M.A.4    Nawrotzki, R.5    Loh, N.Y.6
  • 14
    • 34249781403 scopus 로고    scopus 로고
    • Intermediate filaments and stress
    • Jun 10
    • Pekny M, Lane EB. Intermediate filaments and stress. Exp Cell Res. 2007 Jun 10;313(10):2244-54.
    • (2007) Exp Cell Res. , vol.313 , Issue.10 , pp. 2244-2254
    • Pekny, M.1    Lane, E.B.2
  • 15
  • 17
    • 0023649685 scopus 로고
    • Rearrangement of the vimentin cytoskeleton during adipose conversion: formation of an intermediate filament cage around lipid globules
    • Franke WW, Hergt M, Grund C. Rearrangement of the vimentin cytoskeleton during adipose conversion: formation of an intermediate filament cage around lipid globules. Cell, 1987;49(1):131-41.
    • (1987) Cell , vol.49 , Issue.1 , pp. 131-141
    • Franke, W.W.1    Hergt, M.2    Grund, C.3
  • 18
    • 0028905818 scopus 로고
    • Vimentin and CP49 / Filensin form distinct networks in the lens which are independantly modulated during lens fibre cell differentiation
    • Sandilands A, Prescott AR, Carter JM, Hutcheson AM, Quinlan RA, Richards J, et al. Vimentin and CP49 / Filensin form distinct networks in the lens which are independantly modulated during lens fibre cell differentiation. J Cell Sci. 1995;108:1397-406.
    • (1995) J Cell Sci. , vol.108 , pp. 1397-1406
    • Sandilands, A.1    Prescott, A.R.2    Carter, J.M.3    Hutcheson, A.M.4    Quinlan, R.A.5    Richards, J.6
  • 19
    • 68849097388 scopus 로고    scopus 로고
    • Functions of the intermediate filament cytoskeleton in the eye lens
    • Jul
    • Song S, Landsbury A, Dahm R, Liu Y, Zhang Q, Quinlan RA. Functions of the intermediate filament cytoskeleton in the eye lens. J Clin Invest. 2009 Jul;119(7):1837-48.
    • (2009) J Clin Invest. , vol.119 , Issue.7 , pp. 1837-1848
    • Song, S.1    Landsbury, A.2    Dahm, R.3    Liu, Y.4    Zhang, Q.5    Quinlan, R.A.6
  • 20
    • 0035943673 scopus 로고    scopus 로고
    • Synemin may function to directly link muscle cell intermediate filaments to both myofibrillar Z-lines and costameres
    • Aug 24
    • Bellin RM, Huiatt TW, Critchley DR, Robson RM. Synemin may function to directly link muscle cell intermediate filaments to both myofibrillar Z-lines and costameres. J Biol Chem. 2001 Aug 24;276(34):32330-7.
    • (2001) J Biol Chem. , vol.276 , Issue.34 , pp. 32330-32337
    • Bellin, R.M.1    Huiatt, T.W.2    Critchley, D.R.3    Robson, R.M.4
  • 22
    • 34347374872 scopus 로고    scopus 로고
    • Intermediate filament scaffolds fulfill mechanical, organizational, and signaling functions in the cytoplasm
    • Jul 1
    • Kim S, Coulombe PA. Intermediate filament scaffolds fulfill mechanical, organizational, and signaling functions in the cytoplasm. Genes Dev. 2007 Jul 1;21(13):1581-97.
    • (2007) Genes Dev. , vol.21 , Issue.13 , pp. 1581-1597
    • Kim, S.1    Coulombe, P.A.2
  • 23
    • 60749130274 scopus 로고    scopus 로고
    • Cell fate regulation by coupling mechanical cycles to biochemical signaling pathways
    • Feb
    • Vogel V, Sheetz MP. Cell fate regulation by coupling mechanical cycles to biochemical signaling pathways. Curr Opin Cell Biol. 2009 Feb;21(1):38-46.
    • (2009) Curr Opin Cell Biol. , vol.21 , Issue.1 , pp. 38-46
    • Vogel, V.1    Sheetz, M.P.2
  • 24
    • 68849112456 scopus 로고    scopus 로고
    • Intermediate filaments: primary determinants of cell architecture and plasticity
    • Jul
    • Herrmann H, Strelkov SV, Burkhard P, Aebi U. Intermediate filaments: primary determinants of cell architecture and plasticity. J Clin Invest. 2009 Jul;119(7):1772-83.
    • (2009) J Clin Invest. , vol.119 , Issue.7 , pp. 1772-1783
    • Herrmann, H.1    Strelkov, S.V.2    Burkhard, P.3    Aebi, U.4
  • 25
    • 0037076399 scopus 로고    scopus 로고
    • Microrheometry of semiflexible actin networks through enforced single-filament reptation: frictional coupling and heterogeneities in entangled networks
    • May 14
    • Dichtl MA, Sackmann E. Microrheometry of semiflexible actin networks through enforced single-filament reptation: frictional coupling and heterogeneities in entangled networks. Proc Natl Acad Sci U S A. 2002 May 14;99(10):6533-8.
    • (2002) Proc Natl Acad Sci U S A. , vol.99 , Issue.10 , pp. 6533-6538
    • Dichtl, M.A.1    Sackmann, E.2
  • 26
    • 2342455798 scopus 로고    scopus 로고
    • Desmin aggregate formation by R120G alphaB-crystallin is caused by altered filament interactions and is dependent upon network status in cells
    • May
    • Perng MD, Wen SF, van den IP, Prescott AR, Quinlan RA. Desmin aggregate formation by R120G alphaB-crystallin is caused by altered filament interactions and is dependent upon network status in cells. Mol Biol Cell,. 2004 May;15(5):2335-46.
    • (2004) Mol Biol Cell,. , vol.15 , Issue.5 , pp. 2335-2346
    • Perng, M.D.1    Wen, S.F.2    van den, I.P.3    Prescott, A.R.4    Quinlan, R.A.5
  • 27
    • 17344361902 scopus 로고    scopus 로고
    • A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy
    • Vicart P, Caron A, Guicheney P, Li Z, Prevost MC, Faure A, et al. A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy. Nat Genet. 1998;20(1):92-5.
    • (1998) Nat Genet. , vol.20 , Issue.1 , pp. 92-95
    • Vicart, P.1    Caron, A.2    Guicheney, P.3    Li, Z.4    Prevost, M.C.5    Faure, A.6
  • 28
    • 0020804195 scopus 로고
    • "Prompt" heat shock proteins: translationally regulated synthesis of new proteins associated with the nuclear matrix-intermediate filaments as an early response to heat shock
    • Aug
    • Reiter T, Penman S. "Prompt" heat shock proteins: translationally regulated synthesis of new proteins associated with the nuclear matrix-intermediate filaments as an early response to heat shock. Proc Natl Acad Sci U S A. 1983 Aug;80(15):4737-41.
    • (1983) Proc Natl Acad Sci U S A. , vol.80 , Issue.15 , pp. 4737-4741
    • Reiter, T.1    Penman, S.2
  • 30
    • 57349153151 scopus 로고    scopus 로고
    • Effects of heat shock on the distribution and expression levels of nuclear proteins in HeLa S3 cells
    • Dec 15
    • Haddad N, Paulin-Levasseur M. Effects of heat shock on the distribution and expression levels of nuclear proteins in HeLa S3 cells. J Cell Biochem. 2008 Dec 15;105(6):1485-500.
    • (2008) J Cell Biochem. , vol.105 , Issue.6 , pp. 1485-1500
    • Haddad, N.1    Paulin-Levasseur, M.2
  • 31
    • 0031887317 scopus 로고    scopus 로고
    • alpha B-crystallin is associated with intermediate filaments in astrocytoma cells
    • Wisniewski T, Goldman JE. alpha B-crystallin is associated with intermediate filaments in astrocytoma cells. Neurochemical Research, 1998;23(3):385-92.
    • (1998) Neurochemical Research , vol.23 , Issue.3 , pp. 385-392
    • Wisniewski, T.1    Goldman, J.E.2
  • 32
    • 0043205911 scopus 로고    scopus 로고
    • Nuclear speckle localisation of the small heat shock protein alpha B-crystallin and its inhibition by the R120G cardiomyopathy-linked mutation
    • Jul 15
    • van den Ijssel P, Wheelock R, Prescott A, Russell P, Quinlan RA. Nuclear speckle localisation of the small heat shock protein alpha B-crystallin and its inhibition by the R120G cardiomyopathy-linked mutation. Exp Cell Res. 2003 Jul 15;287(2):249-61.
    • (2003) Exp Cell Res. , vol.287 , Issue.2 , pp. 249-261
    • van den Ijssel, P.1    Wheelock, R.2    Prescott, A.3    Russell, P.4    Quinlan, R.A.5
  • 33
    • 4444246913 scopus 로고    scopus 로고
    • Heat stress-induced localization of small heat shock proteins in mouse myoblasts: intranuclear lamin A/C speckles as target for alphaB-crystallin and Hsp25
    • Oct 1
    • Adhikari AS, Sridhar Rao K, Rangaraj N, Parnaik VK, Mohan Rao C. Heat stress-induced localization of small heat shock proteins in mouse myoblasts: intranuclear lamin A/C speckles as target for alphaB-crystallin and Hsp25. Exp Cell Res. 2004 Oct 1;299(2):393-403.
    • (2004) Exp Cell Res. , vol.299 , Issue.2 , pp. 393-403
    • Adhikari, A.S.1    Sridhar Rao, K.2    Rangaraj, N.3    Parnaik, V.K.4    Mohan Rao, C.5
  • 34
    • 0027392709 scopus 로고
    • Responses to heat shock of alpha B crystallin and HSP28 in U373 MG human glioma cells
    • Kato K, Goto S, Hasegawa K, Shinohara H, Inaguma Y. Responses to heat shock of alpha B crystallin and HSP28 in U373 MG human glioma cells. Biochim Biophys Acta, 1993;1175(3):257-62.
    • (1993) Biochim Biophys Acta , vol.1175 , Issue.3 , pp. 257-262
    • Kato, K.1    Goto, S.2    Hasegawa, K.3    Shinohara, H.4    Inaguma, Y.5
  • 35
    • 0025167955 scopus 로고
    • Cardiac alpha-crystallin. III. Involvement during heart ischemia
    • Chiesi M, Longoni S, Limbruno U. Cardiac alpha-crystallin. III. Involvement during heart ischemia. Mol Cell Biochem. 1990;97(2):129-36.
    • (1990) Mol Cell Biochem. , vol.97 , Issue.2 , pp. 129-136
    • Chiesi, M.1    Longoni, S.2    Limbruno, U.3
  • 36
    • 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.
    • (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
  • 37
    • 0024521440 scopus 로고
    • AB-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain
    • Iwaki T, Kume-Iwaki A, Liem RKH, Goldman JE. AB-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain. Cell. 1989;57:71-8.
    • (1989) Cell. , vol.57 , pp. 71-78
    • Iwaki, T.1    Kume-Iwaki, A.2    Liem, R.K.H.3    Goldman, J.E.4
  • 38
    • 0027742866 scopus 로고
    • Alpha-b-crystallin and 27-kd heat-shock protein are regulated by stress conditions in the central-nervous-system and accumulate in rosenthal fibers
    • Iwaki T, Iwaki A, Tateishi J, Sakaki Y, Goldman JE. Alpha-b-crystallin and 27-kd heat-shock protein are regulated by stress conditions in the central-nervous-system and accumulate in rosenthal fibers. Am J Path. 1993; 143(2):487-95.
    • (1993) Am J Path. , vol.143 , Issue.2 , pp. 487-495
    • Iwaki, T.1    Iwaki, A.2    Tateishi, J.3    Sakaki, Y.4    Goldman, J.E.5
  • 39
    • 0026541969 scopus 로고
    • Alpha B crystallin expression in non-lenticular tissues and selective presence in ubiquitinated inclusion bodies in human disease
    • Jan
    • Lowe J, McDermott H, Pike I, Spendlove I, Landon M, Mayer RJ. Alpha B crystallin expression in non-lenticular tissues and selective presence in ubiquitinated inclusion bodies in human disease. J Pathol. 1992 Jan; 166(1):61-8.
    • (1992) J Pathol. , vol.166 , Issue.1 , pp. 61-68
    • Lowe, J.1    McDermott, H.2    Pike, I.3    Spendlove, I.4    Landon, M.5    Mayer, R.J.6
  • 40
    • 0030724879 scopus 로고    scopus 로고
    • alpha B-crystallin interacts with intermediate filaments in response to stress
    • Djabali K, deNechaud B, Landon F, Portier MM. alpha B-crystallin interacts with intermediate filaments in response to stress. J Cell Sci. 1997;110(Pt 21):2759-69.
    • (1997) J Cell Sci. , vol.110 , Issue.PART 21 , pp. 2759-2769
    • Djabali, K.1    deNechaud, B.2    Landon, F.3    Portier, M.M.4
  • 42
    • 0032582722 scopus 로고    scopus 로고
    • Effect of mutations of murine lens alphaB crystallin on transfected neural cell viability and cellular translocation in response to stress
    • Oct 30
    • Wiesmann KE, Coop A, Goode D, Hepburne-Scott HW, Crabbe MJ. Effect of mutations of murine lens alphaB crystallin on transfected neural cell viability and cellular translocation in response to stress. FEBS Lett. 1998 Oct 30;438(1-2):25-31.
    • (1998) FEBS Lett. , vol.438 , Issue.1-2 , pp. 25-31
    • Wiesmann, K.E.1    Coop, A.2    Goode, D.3    Hepburne-Scott, H.W.4    Crabbe, M.J.5
  • 43
    • 35748947791 scopus 로고    scopus 로고
    • Regulation of stress-induced intracellular sorting and chaperone function of Hsp27 (HspB1) in mammalian cells
    • Nov 1
    • Bryantsev AL, Kurchashova SY, Golyshev SA, Polyakov VY, Wunderink HF, Kanon B, et al. Regulation of stress-induced intracellular sorting and chaperone function of Hsp27 (HspB1) in mammalian cells. Biochem J. 2007 Nov 1;407(3):407-17.
    • (2007) Biochem J. , vol.407 , Issue.3 , pp. 407-417
    • Bryantsev, A.L.1    Kurchashova, S.Y.2    Golyshev, S.A.3    Polyakov, V.Y.4    Wunderink, H.F.5    Kanon, B.6
  • 44
    • 0028176579 scopus 로고
    • Chaperone activity of a-crystallins modulates intermediate filament assembly
    • Nicholl ID, Quinlan RA. Chaperone activity of a-crystallins modulates intermediate filament assembly. EMBO J. 1994;13:945-53.
    • (1994) EMBO J. , vol.13 , pp. 945-953
    • Nicholl, I.D.1    Quinlan, R.A.2
  • 45
    • 0032965815 scopus 로고    scopus 로고
    • Oxidative refolding chromatography: folding of the scorpion toxin Cn5 [see comments]
    • Altamirano MM, Garcia C, Possani LD, Fersht AR. Oxidative refolding chromatography: folding of the scorpion toxin Cn5 [see comments]. Nat Biotechnol. 1999;17(2):187-91.
    • (1999) Nat Biotechnol. , vol.17 , Issue.2 , pp. 187-191
    • Altamirano, M.M.1    Garcia, C.2    Possani, L.D.3    Fersht, A.R.4
  • 47
    • 0032587169 scopus 로고    scopus 로고
    • aB-crystallin selectively targets intermediate filament proteins during thermal stress
    • Muchowski PJ, Valdez MM, Clark JI. aB-crystallin selectively targets intermediate filament proteins during thermal stress. Invest Ophthalmol Vis Sci. 1999;40:951-8.
    • (1999) Invest Ophthalmol Vis Sci. , vol.40 , pp. 951-958
    • Muchowski, P.J.1    Valdez, M.M.2    Clark, J.I.3
  • 48
    • 0000843475 scopus 로고    scopus 로고
    • The cardiomyopathy and lens cataract mutation in aB-crystallin compromises secondary, tertiary and quaternary protein structure and reduces in vitro chaperone activity
    • Perng MD, Muchowski PJ, van den Ijssel P, Wu GJS, Clark JI, Quinlan RA. The cardiomyopathy and lens cataract mutation in aB-crystallin compromises secondary, tertiary and quaternary protein structure and reduces in vitro chaperone activity. J Biol Chem. 1999; 274:33235-43.
    • (1999) J Biol Chem. , vol.274 , pp. 33235-33243
    • Perng, M.D.1    Muchowski, P.J.2    van den Ijssel, P.3    Wu, G.J.S.4    Clark, J.I.5    Quinlan, R.A.6
  • 49
    • 33645055949 scopus 로고    scopus 로고
    • Aberrant protein aggregation is essential for a mutant desmin to impair the proteolytic function of the ubiquitin-proteasome system in cardiomyocytes
    • Apr
    • Liu J, Tang M, Mestril R, Wang X. Aberrant protein aggregation is essential for a mutant desmin to impair the proteolytic function of the ubiquitin-proteasome system in cardiomyocytes. J Mol Cell Cardiol. 2006 Apr; 40(4):451-4.
    • (2006) J Mol Cell Cardiol. , vol.40 , Issue.4 , pp. 451-454
    • Liu, J.1    Tang, M.2    Mestril, R.3    Wang, X.4
  • 51
    • 48249145765 scopus 로고    scopus 로고
    • Adaptive autophagy in Alexander disease-affected astrocytes
    • Sep-Oct
    • Tang G, Yue Z, Talloczy Z, Goldman JE. Adaptive autophagy in Alexander disease-affected astrocytes. Autophagy, 2008 Sep-Oct;4(5):701-3.
    • (2008) Autophagy , vol.4 , Issue.5 , pp. 701-703
    • Tang, G.1    Yue, Z.2    Talloczy, Z.3    Goldman, J.E.4
  • 52
    • 33644883329 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system in desminopathy mouse hearts
    • Feb
    • Liu J, Chen Q, Huang W, Horak KM, Zheng H, Mestril R, et al. Impairment of the ubiquitin-proteasome system in desminopathy mouse hearts. FASEB J. 2006 Feb; 20(2):362-4.
    • (2006) FASEB J. , vol.20 , Issue.2 , pp. 362-364
    • Liu, J.1    Chen, Q.2    Huang, W.3    Horak, K.M.4    Zheng, H.5    Mestril, R.6
  • 53
    • 63049138899 scopus 로고    scopus 로고
    • Properties of astrocytes cultured from GFAP over-expressing and GFAP mutant mice
    • Apr 15
    • Cho W, Messing A. Properties of astrocytes cultured from GFAP over-expressing and GFAP mutant mice. Exp Cell Res. 2009 Apr 15; 315(7):1260-72.
    • (2009) Exp Cell Res. , vol.315 , Issue.7 , pp. 1260-1272
    • Cho, W.1    Messing, A.2
  • 54
    • 1342346544 scopus 로고    scopus 로고
    • An autocrine/paracrine loop linking keratin 14 aggregates to tumor necrosis factor alpha-mediated cytotoxicity in a keratinocyte model of epidermolysis bullosa simplex
    • Feb 20
    • Yoneda K, Furukawa T, Zheng YJ, Momoi T, Izawa I, Inagaki M, et al. An autocrine/paracrine loop linking keratin 14 aggregates to tumor necrosis factor alpha-mediated cytotoxicity in a keratinocyte model of epidermolysis bullosa simplex. J Biol Chem. 2004 Feb 20; 279(8):7296-303.
    • (2004) J Biol Chem. , vol.279 , Issue.8 , pp. 7296-7303
    • Yoneda, K.1    Furukawa, T.2    Zheng, Y.J.3    Momoi, T.4    Izawa, I.5    Inagaki, M.6
  • 55
    • 42649136545 scopus 로고    scopus 로고
    • Autophagy modulates keratin-containing inclusion formation and apoptosis in cell culture in a context-dependent fashion
    • May 1
    • Harada M, Strnad P, Toivola DM, Omary MB. Autophagy modulates keratin-containing inclusion formation and apoptosis in cell culture in a context-dependent fashion. Exp Cell Res. 2008 May 1; 314(8):1753-64.
    • (2008) Exp Cell Res. , vol.314 , Issue.8 , pp. 1753-1764
    • Harada, M.1    Strnad, P.2    Toivola, D.M.3    Omary, M.B.4
  • 56
    • 0034194388 scopus 로고    scopus 로고
    • Keratins turn over by ubiquitination in a phosphorylation-modulated fashion
    • May 1
    • Ku NO, Omary MB. Keratins turn over by ubiquitination in a phosphorylation-modulated fashion. J Cell Biol. 2000 May 1; 149(3):547-52.
    • (2000) J Cell Biol. , vol.149 , Issue.3 , pp. 547-552
    • Ku, N.O.1    Omary, M.B.2
  • 58
    • 34548041439 scopus 로고    scopus 로고
    • Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human alphaA-, alphaB- and R120G alphaB-crystallins
    • Sep 14
    • Meehan S, Knowles TP, Baldwin AJ, Smith JF, Squires AM, Clements P, et al. Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human alphaA-, alphaB- and R120G alphaB-crystallins. J Mol Biol. 2007 Sep 14; 372(2):470-84.
    • (2007) J Mol Biol. , vol.372 , Issue.2 , pp. 470-484
    • Meehan, S.1    Knowles, T.P.2    Baldwin, A.J.3    Smith, J.F.4    Squires, A.M.5    Clements, P.6
  • 59
    • 27944450427 scopus 로고    scopus 로고
    • Intrasarcoplasmic amyloidosis impairs proteolytic function of proteasomes in cardiomyocytes by compromising substrate uptake
    • Nov 11
    • Chen Q, Liu JB, Horak KM, Zheng H, Kumarapeli AR, Li J, et al. Intrasarcoplasmic amyloidosis impairs proteolytic function of proteasomes in cardiomyocytes by compromising substrate uptake. Circ Res. 2005 Nov 11;97(10):1018-26.
    • (2005) Circ Res. , vol.97 , Issue.10 , pp. 1018-1026
    • Chen, Q.1    Liu, J.B.2    Horak, K.M.3    Zheng, H.4    Kumarapeli, A.R.5    Li, J.6
  • 60
    • 0036239489 scopus 로고    scopus 로고
    • Inhibition of Proteasomes Induces Accumulation, Phosphorylation, and Recruitment of HSP27 and alphaB-Crystallin to Aggresomes
    • Apr
    • Ito H, Kamei K, Iwamoto I, Inaguma Y, Garcia-Mata R, Sztul E, et al. Inhibition of Proteasomes Induces Accumulation, Phosphorylation, and Recruitment of HSP27 and alphaB-Crystallin to Aggresomes. J Biochem. (Tokyo). 2002 Apr; 131(4):593-603.
    • (2002) J Biochem. (Tokyo). , vol.131 , Issue.4 , pp. 593-603
    • Ito, H.1    Kamei, K.2    Iwamoto, I.3    Inaguma, Y.4    Garcia-Mata, R.5    Sztul, E.6
  • 62
    • 58149136255 scopus 로고    scopus 로고
    • Cellular vimentin content regulates the protein level of hepatitis C virus core protein and the hepatitis C virus production in cultured cells
    • Jan 20
    • Nitahara-Kasahara Y, Fukasawa M, Shinkai-Ouchi F, Sato S, Suzuki T, Murakami K, et al. Cellular vimentin content regulates the protein level of hepatitis C virus core protein and the hepatitis C virus production in cultured cells. Virology, 2009 Jan 20; 383(2):319-27.
    • (2009) Virology , vol.383 , Issue.2 , pp. 319-327
    • Nitahara-Kasahara, Y.1    Fukasawa, M.2    Shinkai-Ouchi, F.3    Sato, S.4    Suzuki, T.5    Murakami, K.6
  • 63
    • 8644246567 scopus 로고    scopus 로고
    • Mimicking phosphorylation of the small heat-shock protein alphaB-crystallin recruits the F-box protein FBX4 to nuclear SC35 speckles
    • Nov
    • den Engelsman J, Bennink EJ, Doerwald L, Onnekink C, Wunderink L, Andley UP, et al. Mimicking phosphorylation of the small heat-shock protein alphaB-crystallin recruits the F-box protein FBX4 to nuclear SC35 speckles. Eur J Biochem. 2004 Nov; 271(21):4195-203.
    • (2004) Eur J Biochem. , vol.271 , Issue.21 , pp. 4195-4203
    • den Engelsman, J.1    Bennink, E.J.2    Doerwald, L.3    Onnekink, C.4    Wunderink, L.5    Andley, U.P.6
  • 64
    • 44849103123 scopus 로고    scopus 로고
    • Truncation of alphaB-crystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells
    • Apr 18
    • Hayes VH, Devlin G, Quinlan RA. Truncation of alphaB-crystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells. J Biol Chem. 2008 Apr 18;283(16):10500-12.
    • (2008) J Biol Chem. , vol.283 , Issue.16 , pp. 10500-10512
    • Hayes, V.H.1    Devlin, G.2    Quinlan, R.A.3
  • 65
    • 34548241302 scopus 로고    scopus 로고
    • Interactive sequences in the stress protein and molecular chaperone human alphaB crystallin recognize and modulate the assembly of filaments
    • Ghosh JG, Houck SA, Clark JI. Interactive sequences in the stress protein and molecular chaperone human alphaB crystallin recognize and modulate the assembly of filaments. Int J Biochem Cell Biol. 2007; 39(10):1804-15.
    • (2007) Int J Biochem Cell Biol. , vol.39 , Issue.10 , pp. 1804-1815
    • Ghosh, J.G.1    Houck, S.A.2    Clark, J.I.3
  • 66
    • 0344664368 scopus 로고    scopus 로고
    • Myofibrillar myopathy caused by novel dominant negative alpha B-crystallin mutations
    • Dec
    • Selcen D, Engel AG. Myofibrillar myopathy caused by novel dominant negative alpha B-crystallin mutations. Ann Neurol. 2003 Dec; 54(6):804-10.
    • (2003) Ann Neurol. , vol.54 , Issue.6 , pp. 804-810
    • Selcen, D.1    Engel, A.G.2
  • 67
    • 34548041439 scopus 로고    scopus 로고
    • Characterisation of Amyloid Fibril Formation by Small Heat-shock Chaperone Proteins Human alphaA-, alphaB- and R120G alphaB-Crystallins
    • Jun 29
    • Meehan S, Knowles TP, Baldwin AJ, Smith JF, Squires AM, Clements P, et al. Characterisation of Amyloid Fibril Formation by Small Heat-shock Chaperone Proteins Human alphaA-, alphaB- and R120G alphaB-Crystallins. J Mol Biol. 2007 Jun 29.
    • (2007) J Mol Biol.
    • Meehan, S.1    Knowles, T.P.2    Baldwin, A.J.3    Smith, J.F.4    Squires, A.M.5    Clements, P.6
  • 68
    • 13444260973 scopus 로고    scopus 로고
    • R120G alphaB-crystallin promotes the unfolding of reduced alpha-lactalbumin and is inherently unstable
    • Feb
    • Treweek TM, Rekas A, Lindner RA, Walker MJ, Aquilina JA, Robinson CV, et al. R120G alphaB-crystallin promotes the unfolding of reduced alpha-lactalbumin and is inherently unstable. Febs J. 2005 Feb; 272(3):711-24.
    • (2005) Febs J. , vol.272 , Issue.3 , pp. 711-724
    • Treweek, T.M.1    Rekas, A.2    Lindner, R.A.3    Walker, M.J.4    Aquilina, J.A.5    Robinson, C.V.6
  • 70
    • 68849104798 scopus 로고    scopus 로고
    • Tragedy in a heartbeat: malfunctioning desmin causes skeletal and cardiac muscle disease
    • Jul
    • Goldfarb LG, Dalakas MC. Tragedy in a heartbeat: malfunctioning desmin causes skeletal and cardiac muscle disease. J Clin Invest. 2009 Jul;119(7):1806-13.
    • (2009) J Clin Invest. , vol.119 , Issue.7 , pp. 1806-1813
    • Goldfarb, L.G.1    Dalakas, M.C.2
  • 71
    • 27244439232 scopus 로고    scopus 로고
    • Severe muscle disease-causing desmin mutations interfere with in vitro filament assembly at distinct stages
    • Oct 18
    • Bar H, Mucke N, Kostareva A, Sjoberg G, Aebi U, Herrmann H. Severe muscle disease-causing desmin mutations interfere with in vitro filament assembly at distinct stages. Proc Natl Acad Sci U S A. 2005 Oct 18;102(42):15099-104.
    • (2005) Proc Natl Acad Sci U S A. , vol.102 , Issue.42 , pp. 15099-15104
    • Bar, H.1    Mucke, N.2    Kostareva, A.3    Sjoberg, G.4    Aebi, U.5    Herrmann, H.6
  • 72
    • 58149352273 scopus 로고    scopus 로고
    • Severe myopathy mutations modify the nanomechanics of desmin intermediate filaments
    • Jan 30
    • Kreplak L, Bar H. Severe myopathy mutations modify the nanomechanics of desmin intermediate filaments. J Mol Biol. 2009 Jan 30;385(4):1043-51.
    • (2009) J Mol Biol. , vol.385 , Issue.4 , pp. 1043-1051
    • Kreplak, L.1    Bar, H.2
  • 74
    • 66949173652 scopus 로고    scopus 로고
    • Myofibrillar myopathies: a clinical and myopathological guide
    • Jul
    • Schroder R, Schoser B. Myofibrillar myopathies: a clinical and myopathological guide. Brain Pathol. 2009 Jul; 19(3):483-92.
    • (2009) Brain Pathol. , vol.19 , Issue.3 , pp. 483-492
    • Schroder, R.1    Schoser, B.2
  • 76
    • 20044372525 scopus 로고    scopus 로고
    • Glial fibrillary acidic protein mutations in infantile, juvenile, and adult forms of Alexander disease
    • Mar
    • Li R, Johnson AB, Salomons G, Goldman JE, Naidu S, Quinlan R, et al. Glial fibrillary acidic protein mutations in infantile, juvenile, and adult forms of Alexander disease. Ann Neurol. 2005 Mar;57(3):310-26.
    • (2005) Ann Neurol. , vol.57 , Issue.3 , pp. 310-326
    • Li, R.1    Johnson, A.B.2    Salomons, G.3    Goldman, J.E.4    Naidu, S.5    Quinlan, R.6
  • 77
    • 2642539919 scopus 로고    scopus 로고
    • Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy
    • Jun
    • Irobi J, Van Impe K, Seeman P, Jordanova A, Dierick I, Verpoorten N, et al. Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy. Nat Genet. 2004 Jun; 36(6):597-601.
    • (2004) Nat Genet. , vol.36 , Issue.6 , pp. 597-601
    • Irobi, J.1    Van Impe, K.2    Seeman, P.3    Jordanova, A.4    Dierick, I.5    Verpoorten, N.6
  • 78
    • 2642563501 scopus 로고    scopus 로고
    • Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy
    • Jun
    • Evgrafov OV, Mersiyanova I, Irobi J, Van Den Bosch L, Dierick I, Leung CL, et al. Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy. Nat Genet. 2004 Jun; 36(6):602-6.
    • (2004) Nat Genet. , vol.36 , Issue.6 , pp. 602-606
    • Evgrafov, O.V.1    Mersiyanova, I.2    Irobi, J.3    Van Den Bosch, L.4    Dierick, I.5    Leung, C.L.6
  • 79
    • 63149096739 scopus 로고    scopus 로고
    • Suppression of GFAP toxicity by alphaB-crystallin in mouse models of Alexander disease
    • Apr 1
    • Hagemann TL, Boelens WC, Wawrousek EF, Messing A. Suppression of GFAP toxicity by alphaB-crystallin in mouse models of Alexander disease. Hum Mol Genet. 2009 Apr 1; 18(7):1190-9.
    • (2009) Hum Mol Genet. , vol.18 , Issue.7 , pp. 1190-1199
    • Hagemann, T.L.1    Boelens, W.C.2    Wawrousek, E.F.3    Messing, A.4
  • 80
    • 0035163913 scopus 로고    scopus 로고
    • Mutations in GFAP, encoding glial fibrillary acidic protein are associated with Alexander Disease
    • Brenner M, Johnson AB, Boespflug-Tanguay O, Rodriguez D, Goldman JE. Mutations in GFAP, encoding glial fibrillary acidic protein are associated with Alexander Disease. Nat Gen. 2001;27:117-20.
    • (2001) Nat Gen. , vol.27 , pp. 117-120
    • Brenner, M.1    Johnson, A.B.2    Boespflug-Tanguay, O.3    Rodriguez, D.4    Goldman, J.E.5
  • 81
    • 33746485560 scopus 로고    scopus 로고
    • The Alexander disease-causing glial fibrillary acidic protein mutant, R416W, accumulates into Rosenthal fibers by a pathway that involves filament aggregation and the association of alpha B-crystallin and HSP27
    • Aug
    • Der Perng M, Su M, Wen SF, Li R, Gibbon T, Prescott AR, et al. The Alexander disease-causing glial fibrillary acidic protein mutant, R416W, accumulates into Rosenthal fibers by a pathway that involves filament aggregation and the association of alpha B-crystallin and HSP27. Am J Hum Genet. 2006 Aug;79(2):197-213.
    • (2006) Am J Hum Genet. , vol.79 , Issue.2 , pp. 197-213
    • Der Perng, M.1    Su, M.2    Wen, S.F.3    Li, R.4    Gibbon, T.5    Prescott, A.R.6
  • 82
    • 33846002775 scopus 로고    scopus 로고
    • Synergistic effects of the SAPK/JNK and the proteasome pathway on glial fibrillary acidic protein (GFAP) accumulation in Alexander disease
    • Dec 15
    • Tang G, Xu Z, Goldman JE. Synergistic effects of the SAPK/JNK and the proteasome pathway on glial fibrillary acidic protein (GFAP) accumulation in Alexander disease. J Biol Chem. 2006 Dec 15; 281(50):38634-43.
    • (2006) J Biol Chem. , vol.281 , Issue.50 , pp. 38634-38643
    • Tang, G.1    Xu, Z.2    Goldman, J.E.3
  • 85
    • 19444366359 scopus 로고    scopus 로고
    • Alexander-disease mutation of GFAP causes filament disorganization and decreased solubility of GFAP
    • May 1
    • Hsiao VC, Tian R, Long H, Der Perng M, Brenner M, Quinlan RA, et al. Alexander-disease mutation of GFAP causes filament disorganization and decreased solubility of GFAP. J Cell Sci. 2005 May 1;118(Pt 9):2057-65.
    • (2005) J Cell Sci. , vol.118 , Issue.PART 9 , pp. 2057-2065
    • Hsiao, V.C.1    Tian, R.2    Long, H.3    Der Perng, M.4    Brenner, M.5    Quinlan, R.A.6
  • 86
    • 33644642950 scopus 로고    scopus 로고
    • Plectin regulates the organization of glial fibrillary acidic protein in Alexander disease
    • Mar
    • Tian R, Gregor M, Wiche G, Goldman JE. Plectin regulates the organization of glial fibrillary acidic protein in Alexander disease. Am J Pathol. 2006 Mar;168(3):888-97.
    • (2006) Am J Pathol. , vol.168 , Issue.3 , pp. 888-897
    • Tian, R.1    Gregor, M.2    Wiche, G.3    Goldman, J.E.4
  • 87
    • 0032956263 scopus 로고    scopus 로고
    • Formation of GFAP cytoplasmic inclusions in astrocytes and their disaggregation by alphaB-crystallin [In Process Citation]
    • Koyama Y, Goldman JE. Formation of GFAP cytoplasmic inclusions in astrocytes and their disaggregation by alphaB-crystallin [In Process Citation]. Am J Pathol. 1999; 154(5):1563-72.
    • (1999) Am J Pathol. , vol.154 , Issue.5 , pp. 1563-1572
    • Koyama, Y.1    Goldman, J.E.2
  • 88
    • 0242637569 scopus 로고    scopus 로고
    • AlphaB-crystallin modulates protein aggregation of abnormal desmin
    • Nov 14
    • Wang X, Klevitsky R, Huang W, Glasford J, Li F, Robbins J. AlphaB-crystallin modulates protein aggregation of abnormal desmin. Circ Res. 2003 Nov 14;93(10):998-1005.
    • (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
  • 89
    • 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.
    • (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
  • 91
    • 0024212723 scopus 로고
    • Characterization of an inhibitor of actin polymerization in vinculin- rich fraction of turkey gizzard smooth-muscle
    • Miron T, Wilchek M, Geiger B. Characterization of an inhibitor of actin polymerization in vinculin- rich fraction of turkey gizzard smooth-muscle. Eur J Biochem. 1988; 178(2):543-53.
    • (1988) Eur J Biochem. , vol.178 , Issue.2 , pp. 543-553
    • Miron, T.1    Wilchek, M.2    Geiger, B.3
  • 92
    • 0036556697 scopus 로고    scopus 로고
    • Actin cytoskeleton and small heat shock proteins: how do they interact?
    • Apr
    • Mounier N, Arrigo AP. Actin cytoskeleton and small heat shock proteins: how do they interact? Cell Stress Chaperones, 2002 Apr;7(2):167-76.
    • (2002) Cell Stress Chaperones , vol.7 , Issue.2 , pp. 167-176
    • Mounier, N.1    Arrigo, A.P.2
  • 93
    • 0025813543 scopus 로고
    • A 25-kd inhibitor of actin polymerization is a low-molecular mass heat-shock protein
    • Miron T, Vancompernolle K, Vandekerckhove J, Wilchek M, Geiger B. A 25-kd inhibitor of actin polymerization is a low-molecular mass heat-shock protein. J Cell Biol. 1991; 114(2):255-61.
    • (1991) J Cell Biol. , vol.114 , Issue.2 , pp. 255-261
    • Miron, T.1    Vancompernolle, K.2    Vandekerckhove, J.3    Wilchek, M.4    Geiger, B.5
  • 94
    • 0028071812 scopus 로고
    • Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity
    • Benndorf R, Hayess K, Ryazantsev S, Wieske M, Behlke J, Lutsch G. Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity. J Biol Chem. 1994; 269(32):20780-4.
    • (1994) J Biol Chem. , vol.269 , Issue.32 , pp. 20780-20784
    • Benndorf, R.1    Hayess, K.2    Ryazantsev, S.3    Wieske, M.4    Behlke, J.5    Lutsch, G.6
  • 95
    • 0031056783 scopus 로고    scopus 로고
    • Regulation of actin filament dynamics by p38 map kinase-mediated phosphorylation of heat shock protein 27
    • Guay J, Lambert H, GingrasBreton G, Lavoie JN, Huot J, Landry J. Regulation of actin filament dynamics by p38 map kinase-mediated phosphorylation of heat shock protein 27. J Cell Sci. 1997; 110(Pt 3):357-68.
    • (1997) J Cell Sci. , vol.110 , Issue.PART 3 , pp. 357-368
    • Guay, J.1    Lambert, H.2    GingrasBreton, G.3    Lavoie, J.N.4    Huot, J.5    Landry, J.6
  • 96
    • 0037338308 scopus 로고    scopus 로고
    • Interaction of the small heat shock protein with molecular mass 25 kDa (hsp25) with actin
    • Mar
    • Panasenko OO, Kim MV, Marston SB, Gusev NB. Interaction of the small heat shock protein with molecular mass 25 kDa (hsp25) with actin. Eur J Biochem. 2003 Mar; 270(5):892-901.
    • (2003) Eur J Biochem. , vol.270 , Issue.5 , pp. 892-901
    • Panasenko, O.O.1    Kim, M.V.2    Marston, S.B.3    Gusev, N.B.4
  • 97
    • 35748965834 scopus 로고    scopus 로고
    • Small heat shock protein Hsp27 prevents heat-induced aggregation of F-actin by forming soluble complexes with denatured actin
    • Nov
    • Pivovarova AV, Chebotareva NA, Chernik IS, Gusev NB, Levitsky DI. Small heat shock protein Hsp27 prevents heat-induced aggregation of F-actin by forming soluble complexes with denatured actin. FEBS J. 2007 Nov; 274(22):5937-48.
    • (2007) FEBS J. , vol.274 , Issue.22 , pp. 5937-5948
    • Pivovarova, A.V.1    Chebotareva, N.A.2    Chernik, I.S.3    Gusev, N.B.4    Levitsky, D.I.5
  • 98
    • 0033373475 scopus 로고    scopus 로고
    • HSP27 expression regulates CCK-induced changes of the actin cytoskeleton in CHO-CCK-A cells
    • Dec
    • Schafer C, Clapp P, Welsh MJ, Benndorf R, Williams JA. HSP27 expression regulates CCK-induced changes of the actin cytoskeleton in CHO-CCK-A cells. Am J Physiol. 1999 Dec; 277(6 Pt 1):C1032-43.
    • (1999) Am J Physiol. , vol.277 , Issue.6 PART 1
    • Schafer, C.1    Clapp, P.2    Welsh, M.J.3    Benndorf, R.4    Williams, J.A.5
  • 99
    • 0029658123 scopus 로고    scopus 로고
    • a-crystallin stabilises actin filaments and prevents cytochalasin-induced depolymerisation in a phosphorylation-dependent manner
    • Wang K, Spector A. a-crystallin stabilises actin filaments and prevents cytochalasin-induced depolymerisation in a phosphorylation-dependent manner. Eur J Biochem. 1996; 242:56-66.
    • (1996) Eur J Biochem. , vol.242 , pp. 56-66
    • Wang, K.1    Spector, A.2
  • 100
    • 0034843626 scopus 로고    scopus 로고
    • Defined sequence segments of the small heat shock proteins HSP25 and alphaB-crystallin inhibit actin polymerization
    • Apr
    • Wieske M, Benndorf R, Behlke J, Dolling R, Grelle G, Bielka H, et al. Defined sequence segments of the small heat shock proteins HSP25 and alphaB-crystallin inhibit actin polymerization. Eur J Biochem. 2001 Apr; 268(7):2083-90.
    • (2001) Eur J Biochem. , vol.268 , Issue.7 , pp. 2083-2090
    • Wieske, M.1    Benndorf, R.2    Behlke, J.3    Dolling, R.4    Grelle, G.5    Bielka, H.6
  • 101
    • 33846618592 scopus 로고    scopus 로고
    • Association of alphaB-crystallin, a small heat shock protein, with actin: role in modulating actin filament dynamics in vivo
    • Feb 23
    • Singh BN, Rao KS, Ramakrishna T, Rangaraj N, Rao Ch M. Association of alphaB-crystallin, a small heat shock protein, with actin: role in modulating actin filament dynamics in vivo. J Mol Biol. 2007 Feb 23; 366(3):756-67.
    • (2007) J Mol Biol. , vol.366 , Issue.3 , pp. 756-767
    • Singh, B.N.1    Rao, K.S.2    Ramakrishna, T.3    Rangaraj, N.4    Rao Ch, M.5
  • 102
    • 0028365799 scopus 로고
    • Sense and antisense modification of glial alpha B-crystallin production results in alterations of stress fiber formation and thermoresistance
    • Iwaki T, Iwaki A, Tateishi J, Goldman JE. Sense and antisense modification of glial alpha B-crystallin production results in alterations of stress fiber formation and thermoresistance. J Cell Biol. 1994; 125(6):1385-93.
    • (1994) J Cell Biol. , vol.125 , Issue.6 , pp. 1385-1393
    • Iwaki, T.1    Iwaki, A.2    Tateishi, J.3    Goldman, J.E.4
  • 103
    • 0026440390 scopus 로고
    • Binding of actin to lens alpha crystallins
    • Gopalakrishnan S, Takemoto L. Binding of actin to lens alpha crystallins. Curr Eye Res. 1992;11(9):929-33.
    • (1992) Curr Eye Res. , vol.11 , Issue.9 , pp. 929-933
    • Gopalakrishnan, S.1    Takemoto, L.2
  • 104
    • 0033016897 scopus 로고    scopus 로고
    • The small heat shock-related protein-20 is an actin-associated protein
    • Brophy CM, Lamb S, Graham A. The small heat shock-related protein-20 is an actin-associated protein. J Vasc Surg. 1999; 29(2):326-33.
    • (1999) J Vasc Surg. , vol.29 , Issue.2 , pp. 326-333
    • Brophy, C.M.1    Lamb, S.2    Graham, A.3
  • 105
    • 28444497458 scopus 로고    scopus 로고
    • Small heat shock protein with apparent molecular mass 20 kDa (Hsp20, HspB6) is not a genuine actin-binding protein
    • Bukach OV, Marston SB, Gusev NB. Small heat shock protein with apparent molecular mass 20 kDa (Hsp20, HspB6) is not a genuine actin-binding protein. J Muscle Res Cell Motil. 2005;26(4-5):175-81.
    • (2005) J Muscle Res Cell Motil. , vol.26 , Issue.4-5 , pp. 175-181
    • Bukach, O.V.1    Marston, S.B.2    Gusev, N.B.3
  • 106
    • 21544444439 scopus 로고    scopus 로고
    • Molecular mechanism of actomyosin-based motility
    • Jul
    • Geeves MA, Fedorov R, Manstein DJ. Molecular mechanism of actomyosin-based motility. Cell Mol Life Sci. 2005 Jul; 62(13):1462-77.
    • (2005) Cell Mol Life Sci. , vol.62 , Issue.13 , pp. 1462-1477
    • Geeves, M.A.1    Fedorov, R.2    Manstein, D.J.3
  • 107
    • 0026530409 scopus 로고
    • Inactivation, subunit dissociation, aggregation, and unfolding of myosin subfragment 1 during guanidine denaturation
    • Feb 4
    • Nozais M, Bechet JJ, Houadjeto M. Inactivation, subunit dissociation, aggregation, and unfolding of myosin subfragment 1 during guanidine denaturation. Biochemistry, 1992 Feb 4; 31(4):1210-5.
    • (1992) Biochemistry , vol.31 , Issue.4 , pp. 1210-1215
    • Nozais, M.1    Bechet, J.J.2    Houadjeto, M.3
  • 108
    • 33646042860 scopus 로고    scopus 로고
    • AlphaB-crystallin maintains skeletal muscle myosin enzymatic activity and prevents its aggregation under heat-shock stress
    • May 5
    • Melkani GC, Cammarato A, Bernstein SI. AlphaB-crystallin maintains skeletal muscle myosin enzymatic activity and prevents its aggregation under heat-shock stress. J Mol Biol. 2006 May 5; 358(3):635-45.
    • (2006) J Mol Biol. , vol.358 , Issue.3 , pp. 635-645
    • Melkani, G.C.1    Cammarato, A.2    Bernstein, S.I.3
  • 109
    • 0141780839 scopus 로고    scopus 로고
    • Serial analysis of gene expression in the skeletal muscle of endurance athletes compared to sedentary men
    • Oct
    • Yoshioka M, Tanaka H, Shono N, Snyder EE, Shindo M, St-Amand J. Serial analysis of gene expression in the skeletal muscle of endurance athletes compared to sedentary men. FASEB J. 2003 Oct; 17(13):1812-9.
    • (2003) FASEB J. , vol.17 , Issue.13 , pp. 1812-1819
    • Yoshioka, M.1    Tanaka, H.2    Shono, N.3    Snyder, E.E.4    Shindo, M.5    St-Amand, J.6
  • 110
    • 0042839620 scopus 로고    scopus 로고
    • Titin: properties and family relationships
    • Sep
    • Tskhovrebova L, Trinick J. Titin: properties and family relationships. Nat Rev Mol Cell Biol. 2003 Sep; 4(9):679-89.
    • (2003) Nat Rev Mol Cell Biol. , vol.4 , Issue.9 , pp. 679-689
    • Tskhovrebova, L.1    Trinick, J.2
  • 111
    • 1242342244 scopus 로고    scopus 로고
    • The giant protein titin: a major player in myocardial mechanics, signaling, and disease
    • Feb 20
    • Granzier HL, Labeit S. The giant protein titin: a major player in myocardial mechanics, signaling, and disease. Circ Res. 2004 Feb 20;94(3):284-95.
    • (2004) Circ Res. , vol.94 , Issue.3 , pp. 284-295
    • Granzier, H.L.1    Labeit, S.2
  • 112
    • 0031795571 scopus 로고    scopus 로고
    • A spring tale: new facts on titin elasticity
    • Dec
    • Linke WA, Granzier H. A spring tale: new facts on titin elasticity. Biophys J. 1998 Dec; 75(6):2613-4.
    • (1998) Biophys J. , vol.75 , Issue.6 , pp. 2613-2614
    • Linke, W.A.1    Granzier, H.2
  • 113
    • 0034509442 scopus 로고    scopus 로고
    • Changes in titin and collagen underlie diastolic stiffness diversity of cardiac muscle
    • Dec
    • Wu Y, Cazorla O, Labeit D, Labeit S, Granzier H. Changes in titin and collagen underlie diastolic stiffness diversity of cardiac muscle. J Mol Cell Cardiol. 2000 Dec; 32(12):2151-62.
    • (2000) J Mol Cell Cardiol. , vol.32 , Issue.12 , pp. 2151-2162
    • Wu, Y.1    Cazorla, O.2    Labeit, D.3    Labeit, S.4    Granzier, H.5
  • 114
    • 0033546073 scopus 로고    scopus 로고
    • Mechanically driven contour-length adjustment in rat cardiac titin's unique N2B sequence: titin is an adjustable spring
    • Jun 11
    • Helmes M, Trombitas K, Centner T, Kellermayer M, Labeit S, Linke WA, et al. Mechanically driven contour-length adjustment in rat cardiac titin's unique N2B sequence: titin is an adjustable spring. Circ Res. 1999 Jun 11; 84(11):1339-52.
    • (1999) Circ Res. , vol.84 , Issue.11 , pp. 1339-1352
    • Helmes, M.1    Trombitas, K.2    Centner, T.3    Kellermayer, M.4    Labeit, S.5    Linke, W.A.6
  • 115
    • 0036517816 scopus 로고    scopus 로고
    • Ischemia-induced association of the stress protein alpha B-crystallin with I-band portion of cardiac titin
    • Mar
    • Golenhofen N, Arbeiter A, Koob R, Drenckhahn D. Ischemia-induced association of the stress protein alpha B-crystallin with I-band portion of cardiac titin. J Mol Cell Cardiol. 2002 Mar;34(3):309-19.
    • (2002) J Mol Cell Cardiol. , vol.34 , Issue.3 , pp. 309-319
    • Golenhofen, N.1    Arbeiter, A.2    Koob, R.3    Drenckhahn, D.4
  • 116
    • 1542349941 scopus 로고    scopus 로고
    • Association of the chaperone alphaB-crystallin with titin in heart muscle
    • Feb 27
    • Bullard B, Ferguson C, Minajeva A, Leake MC, Gautel M, Labeit D, et al. Association of the chaperone alphaB-crystallin with titin in heart muscle. J Biol Chem. 2004 Feb 27; 279(9):7917-24.
    • (2004) J Biol Chem. , vol.279 , Issue.9 , pp. 7917-7924
    • Bullard, B.1    Ferguson, C.2    Minajeva, A.3    Leake, M.C.4    Gautel, M.5    Labeit, D.6
  • 117
    • 67649399290 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of the cardiac titin N2B element: effects of the molecular chaperone alphaB-crystallin with disease-causing mutations
    • May 15
    • Zhu Y, Bogomolovas J, Labeit S, Granzier H. Single molecule force spectroscopy of the cardiac titin N2B element: effects of the molecular chaperone alphaB-crystallin with disease-causing mutations. J Biol Chem. 2009 May 15; 284(20):13914-23.
    • (2009) J Biol Chem. , vol.284 , Issue.20 , pp. 13914-13923
    • Zhu, Y.1    Bogomolovas, J.2    Labeit, S.3    Granzier, H.4
  • 118
    • 12944328888 scopus 로고    scopus 로고
    • Comparison of the small heat shock proteins alphaB-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle
    • Nov
    • Golenhofen N, Perng MD, Quinlan RA, Drenckhahn D. Comparison of the small heat shock proteins alphaB-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle. Histochem Cell Biol. 2004 Nov; 122(5):415-25.
    • (2004) Histochem Cell Biol. , vol.122 , Issue.5 , pp. 415-425
    • Golenhofen, N.1    Perng, M.D.2    Quinlan, R.A.3    Drenckhahn, D.4
  • 119
    • 9644258538 scopus 로고    scopus 로고
    • Genetic modification of the heart: chaperones and the cytoskeleton
    • Dec
    • Kumarapeli AR, Wang X. Genetic modification of the heart: chaperones and the cytoskeleton. J Mol Cell Cardiol. 2004 Dec;37(6):1097-109.
    • (2004) J Mol Cell Cardiol. , vol.37 , Issue.6 , pp. 1097-1109
    • Kumarapeli, A.R.1    Wang, X.2
  • 120
    • 33749123682 scopus 로고    scopus 로고
    • Cell signaling pathways to alphaB-crystallin following stresses of the cytoskeleton
    • Nov 1
    • Launay N, Goudeau B, Kato K, Vicart P, Lilienbaum A. Cell signaling pathways to alphaB-crystallin following stresses of the cytoskeleton. Exp Cell Res. 2006 Nov 1;312(18):3570-84.
    • (2006) Exp Cell Res. , vol.312 , Issue.18 , pp. 3570-3584
    • Launay, N.1    Goudeau, B.2    Kato, K.3    Vicart, P.4    Lilienbaum, A.5
  • 122
    • 0036478897 scopus 로고    scopus 로고
    • Mutations of TTN, encoding the giant muscle filament titin, cause familial dilated cardiomyopathy
    • Feb
    • Gerull B, Gramlich M, Atherton J, McNabb M, Trombitas K, Sasse-Klaassen S, et al. Mutations of TTN, encoding the giant muscle filament titin, cause familial dilated cardiomyopathy. Nat Genet. 2002 Feb;30(2):201-4.
    • (2002) Nat Genet. , vol.30 , Issue.2 , pp. 201-204
    • Gerull, B.1    Gramlich, M.2    Atherton, J.3    McNabb, M.4    Trombitas, K.5    Sasse-Klaassen, S.6
  • 123
    • 41149138739 scopus 로고    scopus 로고
    • alpha B-crystallin is a cytoplasmic interaction partner of the kidney-specific cadherin-16
    • Apr 18
    • Thedieck C, Kalbacher H, Kratzer U, Lammers R, Stevanovic S, Klein G. alpha B-crystallin is a cytoplasmic interaction partner of the kidney-specific cadherin-16. J Mol Biol. 2008 Apr 18; 378(1):145-53.
    • (2008) J Mol Biol. , vol.378 , Issue.1 , pp. 145-153
    • Thedieck, C.1    Kalbacher, H.2    Kratzer, U.3    Lammers, R.4    Stevanovic, S.5    Klein, G.6
  • 124
    • 34249891883 scopus 로고    scopus 로고
    • Not so simple: the complexity of phosphotyrosine signaling at cadherin adhesive contacts
    • Jun
    • McLachlan RW, Yap AS. Not so simple: the complexity of phosphotyrosine signaling at cadherin adhesive contacts. J Mol Med. 2007 Jun;85(6):545-54.
    • (2007) J Mol Med. , vol.85 , Issue.6 , pp. 545-554
    • McLachlan, R.W.1    Yap, A.S.2
  • 125
    • 2342439076 scopus 로고    scopus 로고
    • alphaB-Crystallin-coated MAP microtubule resists nocodazole and calcium-induced disassembly
    • Apr 1
    • Fujita Y, Ohto E, Katayama E, Atomi Y. alphaB-Crystallin-coated MAP microtubule resists nocodazole and calcium-induced disassembly. J Cell Sci. 2004 Apr 1; 117(Pt 9):1719-26.
    • (2004) J Cell Sci. , vol.117 , Issue.PART 9 , pp. 1719-1726
    • Fujita, Y.1    Ohto, E.2    Katayama, E.3    Atomi, Y.4
  • 126
    • 34548028021 scopus 로고    scopus 로고
    • Analysis of the alphaB-crystallin domain responsible for inhibiting tubulin aggregation
    • Summer
    • Ohto-Fujita E, Fujita Y, Atomi Y. Analysis of the alphaB-crystallin domain responsible for inhibiting tubulin aggregation. Cell Stress Chaperones. 2007 Summer; 12(2):163-71.
    • (2007) Cell Stress Chaperones. , vol.12 , Issue.2 , pp. 163-171
    • Ohto-Fujita, E.1    Fujita, Y.2    Atomi, Y.3
  • 127
    • 0034728761 scopus 로고    scopus 로고
    • Small heat shock protein 27 (HSP27) associates with tubulin/microtubules in HeLa cells
    • Apr 29
    • Hino M, Kurogi K, Okubo MA, Murata-Hori M, Hosoya H. Small heat shock protein 27 (HSP27) associates with tubulin/microtubules in HeLa cells. Biochem Biophys Res Commun. 2000 Apr 29; 271(1):164-9.
    • (2000) Biochem Biophys Res Commun. , vol.271 , Issue.1 , pp. 164-169
    • Hino, M.1    Kurogi, K.2    Okubo, M.A.3    Murata-Hori, M.4    Hosoya, H.5
  • 128
    • 0031457379 scopus 로고    scopus 로고
    • Chaperone activity of alpha B-crystallin suppresses tubulin aggregation through complex formation
    • Arai H, Atomi Y. Chaperone activity of alpha B-crystallin suppresses tubulin aggregation through complex formation. Cell Structure and Function, 1997; 22(5):539-44.
    • (1997) Cell Structure and Function , vol.22 , Issue.5 , pp. 539-544
    • Arai, H.1    Atomi, Y.2
  • 129
    • 0029662027 scopus 로고    scopus 로고
    • Synthesis and accumulation of alpha-b-crystallin in c6 glioma-cells is induced by agents that promote the disassembly of microtubules
    • Kato K, Ito H, Inaguma Y, Okamoto K, Saga S. Synthesis and accumulation of alpha-b-crystallin in c6 glioma-cells is induced by agents that promote the disassembly of microtubules. Journal of Biological Chemistry, 1996;271(43):26989-94.
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.43 , pp. 26989-26994
    • Kato, K.1    Ito, H.2    Inaguma, Y.3    Okamoto, K.4    Saga, S.5
  • 130
    • 0041525250 scopus 로고    scopus 로고
    • A small heat shock/alpha-crystallin protein from encysted Artemia embryos suppresses tubulin denaturation
    • Summer
    • Day RM, Gupta JS, MacRae TH. A small heat shock/alpha-crystallin protein from encysted Artemia embryos suppresses tubulin denaturation. Cell Stress Chaperones. 2003 Summer; 8(2):183-93.
    • (2003) Cell Stress Chaperones. , vol.8 , Issue.2 , pp. 183-193
    • Day, R.M.1    Gupta, J.S.2    MacRae, T.H.3
  • 131
    • 33744475377 scopus 로고    scopus 로고
    • Alpha-crystallin expression affects microtubule assembly and prevents their aggregation
    • May
    • Xi JH, Bai F, McGaha R, Andley UP. Alpha-crystallin expression affects microtubule assembly and prevents their aggregation. FASEB J. 2006 May;20(7):846-57.
    • (2006) FASEB J. , vol.20 , Issue.7 , pp. 846-857
    • Xi, J.H.1    Bai, F.2    McGaha, R.3    Andley, U.P.4
  • 132
    • 33750857016 scopus 로고    scopus 로고
    • Specific heat shock proteins protect microtubules during simulated ischemia in cardiac myocytes
    • Bluhm WF, Martin JL, Mestril R, Dillmann WH. Specific heat shock proteins protect microtubules during simulated ischemia in cardiac myocytes. Am J Physiol. 1998;275(6 Pt 2):H2243-9.
    • (1998) Am J Physiol. , vol.275 , Issue.6 PART 2 , pp. 2243-2249
    • Bluhm, W.F.1    Martin, J.L.2    Mestril, R.3    Dillmann, W.H.4
  • 133
    • 40149111037 scopus 로고    scopus 로고
    • Interactive domains in the molecular chaperone human alphaB crystallin modulate microtubule assembly and disassembly
    • Ghosh JG, Houck SA, Clark JI. Interactive domains in the molecular chaperone human alphaB crystallin modulate microtubule assembly and disassembly. PLoS One, 2007;2(6):e498.
    • (2007) PLoS One , vol.2 , Issue.6
    • Ghosh, J.G.1    Houck, S.A.2    Clark, J.I.3
  • 134
    • 40149107721 scopus 로고    scopus 로고
    • Interactive sequences in the molecular chaperone, human alphaB crystallin modulate the fibrillation of amyloidogenic proteins
    • Ghosh JG, Houck SA, Clark JI. Interactive sequences in the molecular chaperone, human alphaB crystallin modulate the fibrillation of amyloidogenic proteins. Int J Biochem Cell Biol. 2008;40(5):954-67.
    • (2008) Int J Biochem Cell Biol. , vol.40 , Issue.5 , pp. 954-967
    • Ghosh, J.G.1    Houck, S.A.2    Clark, J.I.3
  • 136
  • 137
    • 14044272992 scopus 로고    scopus 로고
    • Mechanism of chaperone function in small heat shock proteins: dissociation of the HSP27 oligomer is required for recognition and binding of destabilized T4 lysozyme
    • Feb 18
    • Shashidharamurthy R, Koteiche HA, Dong J, McHaourab HS. Mechanism of chaperone function in small heat shock proteins: dissociation of the HSP27 oligomer is required for recognition and binding of destabilized T4 lysozyme. J Biol Chem. 2005 Feb 18;280(7):5281-9.
    • (2005) J Biol Chem. , vol.280 , Issue.7 , pp. 5281-5289
    • Shashidharamurthy, R.1    Koteiche, H.A.2    Dong, J.3    McHaourab, H.S.4
  • 138
    • 3142543752 scopus 로고    scopus 로고
    • Phosphorylation of alphaB-crystallin alters chaperone function through loss of dimeric substructure
    • Jul 2
    • Aquilina JA, Benesch JL, Ding LL, Yaron O, Horwitz J, Robinson CV. Phosphorylation of alphaB-crystallin alters chaperone function through loss of dimeric substructure. J Biol Chem. 2004 Jul 2;279(27):28675-80.
    • (2004) J Biol Chem. , vol.279 , Issue.27 , pp. 28675-28680
    • Aquilina, J.A.1    Benesch, J.L.2    Ding, L.L.3    Yaron, O.4    Horwitz, J.5    Robinson, C.V.6
  • 139
    • 70349470609 scopus 로고    scopus 로고
    • Substrate binding site flexibility of the small heat shock protein molecular chaperones
    • Aug 26
    • Jaya N, Garcia V, Vierling E. Substrate binding site flexibility of the small heat shock protein molecular chaperones. Proc Natl Acad Sci U S A. 2009 Aug 26.
    • (2009) Proc Natl Acad Sci U S A.
    • Jaya, N.1    Garcia, V.2    Vierling, E.3
  • 140
    • 0035718677 scopus 로고    scopus 로고
    • Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones
    • van Montfort R, Slingsby C, Vierling E. Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones. Adv Protein Chem. 2001;59:105-56.
    • (2001) Adv Protein Chem. , vol.59 , pp. 105-156
    • van Montfort, R.1    Slingsby, C.2    Vierling, E.3
  • 142
    • 33644692738 scopus 로고    scopus 로고
    • Studies of alphaB crystallin subunit dynamics by surface plasmon resonance
    • Mar 15
    • Liu L, Ghosh JG, Clark JI, Jiang S. Studies of alphaB crystallin subunit dynamics by surface plasmon resonance. Anal Biochem. 2006 Mar 15;350(2):186-95.
    • (2006) Anal Biochem. , vol.350 , Issue.2 , pp. 186-195
    • Liu, L.1    Ghosh, J.G.2    Clark, J.I.3    Jiang, S.4
  • 143
    • 0346463052 scopus 로고    scopus 로고
    • Interactions between small heat shock protein subunits and substrate in small heat shock protein-substrate complexes
    • Jan 9
    • Friedrich KL, Giese KC, Buan NR, Vierling E. Interactions between small heat shock protein subunits and substrate in small heat shock protein-substrate complexes. J Biol Chem. 2004 Jan 9;279(2):1080-9.
    • (2004) J Biol Chem. , vol.279 , Issue.2 , pp. 1080-1089
    • Friedrich, K.L.1    Giese, K.C.2    Buan, N.R.3    Vierling, E.4
  • 144
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: cellular functions and molecular mechanism
    • Mar
    • Mayer MP, Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci. 2005 Mar;62(6):670-84.
    • (2005) Cell Mol Life Sci. , vol.62 , Issue.6 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 146
    • 0242582458 scopus 로고    scopus 로고
    • Mechanism of chaperone function in small heat-shock proteins. Fluorescence studies of the conformations of T4 lysozyme bound to alphaB-crystallin
    • Nov 7
    • Sathish HA, Stein RA, Yang G, McHaourab HS. Mechanism of chaperone function in small heat-shock proteins. Fluorescence studies of the conformations of T4 lysozyme bound to alphaB-crystallin. J Biol Chem. 2003 Nov 7;278(45):44214-21.
    • (2003) J Biol Chem. , vol.278 , Issue.45 , pp. 44214-44221
    • Sathish, H.A.1    Stein, R.A.2    Yang, G.3    McHaourab, H.S.4
  • 147
    • 34250810346 scopus 로고    scopus 로고
    • Chemical cross-linking of the chloroplast localized small heat-shock protein, Hsp21, and the model substrate citrate synthase
    • Jul
    • Ahrman E, Lambert W, Aquilina JA, Robinson CV, Emanuelsson CS. Chemical cross-linking of the chloroplast localized small heat-shock protein, Hsp21, and the model substrate citrate synthase. Protein Sci. 2007 Jul;16(7):1464-78.
    • (2007) Protein Sci. , vol.16 , Issue.7 , pp. 1464-1478
    • Ahrman, E.1    Lambert, W.2    Aquilina, J.A.3    Robinson, C.V.4    Emanuelsson, C.S.5
  • 148
    • 34249749409 scopus 로고    scopus 로고
    • Interactions between important regulatory proteins and human alphaB crystallin
    • May 29
    • Ghosh JG, Shenoy AK, Jr., Clark JI. Interactions between important regulatory proteins and human alphaB crystallin. Biochemistry, 2007 May 29;46(21):6308-17.
    • (2007) Biochemistry , vol.46 , Issue.21 , pp. 6308-6317
    • Ghosh, J.G.1    Shenoy Jr., A.K.2    Clark, J.I.3
  • 149
    • 55549133282 scopus 로고    scopus 로고
    • Insights into small heat shock protein and substrate structure during chaperone action derived from hydrogen/deuterium exchange and mass spectrometry
    • Sep 26
    • Cheng G, Basha E, Wysocki VH, Vierling E. Insights into small heat shock protein and substrate structure during chaperone action derived from hydrogen/deuterium exchange and mass spectrometry. J Biol Chem. 2008 Sep 26;283(39):26634-42.
    • (2008) J Biol Chem. , vol.283 , Issue.39 , pp. 26634-26642
    • Cheng, G.1    Basha, E.2    Wysocki, V.H.3    Vierling, E.4
  • 150
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heat-shock protein
    • Kim KK, Kim R, Kim SH. Crystal structure of a small heat-shock protein. Nature, 1998;394(6693):595-9.
    • (1998) Nature , vol.394 , Issue.6693 , pp. 595-599
    • Kim, K.K.1    Kim, R.2    Kim, S.H.3
  • 151
    • 0032549677 scopus 로고    scopus 로고
    • The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure
    • Haley DA, Horwitz J, Stewart PL. The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure. J Mol Biol. 1998;277(1):27-35.
    • (1998) J Mol Biol. , vol.277 , Issue.1 , pp. 27-35
    • Haley, D.A.1    Horwitz, J.2    Stewart, P.L.3
  • 152
    • 0141703310 scopus 로고    scopus 로고
    • Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in alphaB-crystallin
    • Sep 16
    • Aquilina JA, Benesch JL, Bateman OA, Slingsby C, Robinson CV. Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in alphaB-crystallin. Proc Natl Acad Sci U S A. 2003 Sep 16;100(19):10611-6.
    • (2003) Proc Natl Acad Sci U S A. , vol.100 , Issue.19 , pp. 10611-10616
    • Aquilina, J.A.1    Benesch, J.L.2    Bateman, O.A.3    Slingsby, C.4    Robinson, C.V.5
  • 153
    • 34547681313 scopus 로고    scopus 로고
    • Human alpha B-crystallin mutation causes oxido-reductive stress and protein aggregation cardiomyopathy in mice
    • Aug 10
    • Rajasekaran NS, Connell P, Christians ES, Yan LJ, Taylor RP, Orosz A, et al. Human alpha B-crystallin mutation causes oxido-reductive stress and protein aggregation cardiomyopathy in mice. Cell, 2007 Aug 10;130(3):427-39.
    • (2007) Cell , vol.130 , Issue.3 , pp. 427-439
    • Rajasekaran, N.S.1    Connell, P.2    Christians, E.S.3    Yan, L.J.4    Taylor, R.P.5    Orosz, A.6
  • 154
    • 27744485379 scopus 로고    scopus 로고
    • Interactive domains for chaperone activity in the small heat shock protein, human alphaB crystallin
    • Nov 15
    • Ghosh JG, Estrada MR, Clark JI. Interactive domains for chaperone activity in the small heat shock protein, human alphaB crystallin. Biochemistry, 2005 Nov 15;44(45):14854-69.
    • (2005) Biochemistry , vol.44 , Issue.45 , pp. 14854-14869
    • Ghosh, J.G.1    Estrada, M.R.2    Clark, J.I.3
  • 156
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Dec
    • Emsley P, Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32.
    • (2004) Acta Crystallogr D Biol Crystallogr. , vol.60 , Issue.PART 12 PT 1 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 157
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Dec
    • Krissinel E, Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2256-68.
    • (2004) Acta Crystallogr D Biol Crystallogr. , vol.60 , Issue.PART 12 PT 1 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 158
    • 44949255090 scopus 로고    scopus 로고
    • Relative contribution of mutations in genes for autosomal dominant distal hereditary motor neuropathies: a genotype-phenotype correlation study
    • May
    • Dierick I, Baets J, Irobi J, Jacobs A, De Vriendt E, Deconinck T, et al. Relative contribution of mutations in genes for autosomal dominant distal hereditary motor neuropathies: a genotype-phenotype correlation study. Brain, 2008 May;131(Pt 5):1217-27.
    • (2008) Brain , vol.131 , Issue.PART 5 , pp. 1217-1227
    • Dierick, I.1    Baets, J.2    Irobi, J.3    Jacobs, A.4    De Vriendt, E.5    Deconinck, T.6
  • 159
    • 58149243285 scopus 로고    scopus 로고
    • Mutations in the HSP27 (HSPB1) gene cause dominant, recessive, and sporadic distal HMN/CMT type 2
    • Nov 18
    • Houlden H, Laura M, Wavrant-De Vrieze F, Blake J, Wood N, Reilly MM. Mutations in the HSP27 (HSPB1) gene cause dominant, recessive, and sporadic distal HMN/CMT type 2. Neurology, 2008 Nov 18;71(21):1660-8.
    • (2008) Neurology , vol.71 , Issue.21 , pp. 1660-1668
    • Houlden, H.1    Laura, M.2    Wavrant-De Vrieze, F.3    Blake, J.4    Wood, N.5    Reilly, M.M.6
  • 160
    • 41149089652 scopus 로고    scopus 로고
    • Asymmetrical late onset motor neuropathy associated with a novel mutation in the small heat shock protein HSPB1 (HSP27)
    • Apr
    • James PA, Rankin J, Talbot K. Asymmetrical late onset motor neuropathy associated with a novel mutation in the small heat shock protein HSPB1 (HSP27). J Neurol Neurosurg Psychiatry, 2008 Apr;79(4):461-3.
    • (2008) J Neurol Neurosurg Psychiatry , vol.79 , Issue.4 , pp. 461-463
    • James, P.A.1    Rankin, J.2    Talbot, K.3
  • 161
    • 22644433190 scopus 로고    scopus 로고
    • Mutation analysis of the small heat shock protein 27 gene in chinese patients with Charcot-Marie-Tooth disease
    • Aug
    • Tang B, Liu X, Zhao G, Luo W, Xia K, Pan Q, et al. Mutation analysis of the small heat shock protein 27 gene in chinese patients with Charcot-Marie-Tooth disease. Arch Neurol. 2005 Aug;62(8):1201-7.
    • (2005) Arch Neurol. , vol.62 , Issue.8 , pp. 1201-1207
    • Tang, B.1    Liu, X.2    Zhao, G.3    Luo, W.4    Xia, K.5    Pan, Q.6
  • 162
    • 58149299834 scopus 로고    scopus 로고
    • A clinical phenotype of distal hereditary motor neuronopathy type II with a novel HSPB1 mutation
    • Feb 15
    • Ikeda Y, Abe A, Ishida C, Takahashi K, Hayasaka K, Yamada M. A clinical phenotype of distal hereditary motor neuronopathy type II with a novel HSPB1 mutation. J Neurol Sci. 2009 Feb 15;277(1-2):9-12.
    • (2009) J Neurol Sci. , vol.277 , Issue.1-2 , pp. 9-12
    • Ikeda, Y.1    Abe, A.2    Ishida, C.3    Takahashi, K.4    Hayasaka, K.5    Yamada, M.6
  • 163
    • 31144453053 scopus 로고    scopus 로고
    • A mutation in the small heat-shock protein HSPB1 leading to distal hereditary motor neuronopathy disrupts neurofilament assembly and the axonal transport of specific cellular cargoes
    • Jan 15
    • Ackerley S, James PA, Kalli A, French S, Davies KE, Talbot K. A mutation in the small heat-shock protein HSPB1 leading to distal hereditary motor neuronopathy disrupts neurofilament assembly and the axonal transport of specific cellular cargoes. Hum Mol Genet. 2006 Jan 15;15(2):347-54.
    • (2006) Hum Mol Genet. , vol.15 , Issue.2 , pp. 347-354
    • Ackerley, S.1    James, P.A.2    Kalli, A.3    French, S.4    Davies, K.E.5    Talbot, K.6
  • 164
    • 26944431622 scopus 로고    scopus 로고
    • Small heat shock protein 27 mutation in a Japanese patient with distal hereditary motor neuropathy
    • Kijima K, Numakura C, Goto T, Takahashi T, Otagiri T, Umetsu K, et al. Small heat shock protein 27 mutation in a Japanese patient with distal hereditary motor neuropathy. J Hum Genet. 2005;50(9):473-6.
    • (2005) J Hum Genet. , vol.50 , Issue.9 , pp. 473-476
    • Kijima, K.1    Numakura, C.2    Goto, T.3    Takahashi, T.4    Otagiri, T.5    Umetsu, K.6
  • 165
    • 34548239171 scopus 로고    scopus 로고
    • Genetic variant in the HSPB1 promoter region impairs the HSP27 stress response
    • Aug
    • Dierick I, Irobi J, Janssens S, Theuns J, Lemmens R, Jacobs A, et al. Genetic variant in the HSPB1 promoter region impairs the HSP27 stress response. Hum Mutat. 2007 Aug;28(8):830.
    • (2007) Hum Mutat. , vol.28 , Issue.8 , pp. 830
    • Dierick, I.1    Irobi, J.2    Janssens, S.3    Theuns, J.4    Lemmens, R.5    Jacobs, A.6
  • 166
    • 0033771250 scopus 로고    scopus 로고
    • A nonsense mutation (W9X) in CRYAA causes autosomal recessive cataract in an inbred Jewish Persian family
    • Oct
    • Pras E, Frydman M, Levy-Nissenbaum E, Bakhan T, Raz J, Assia EI, et al. A nonsense mutation (W9X) in CRYAA causes autosomal recessive cataract in an inbred Jewish Persian family. Invest Ophthalmol Vis Sci. 2000 Oct;41(11):3511-5.
    • (2000) Invest Ophthalmol Vis Sci. , vol.41 , Issue.11 , pp. 3511-3515
    • Pras, E.1    Frydman, M.2    Levy-Nissenbaum, E.3    Bakhan, T.4    Raz, J.5    Assia, E.I.6
  • 167
    • 35148832522 scopus 로고    scopus 로고
    • Genetic heterogeneity in microcornea-cataract: five novel mutations in CRYAA, CRYGD, and GJA8
    • Sep
    • Hansen L, Yao W, Eiberg H, Kjaer KW, Baggesen K, Hejtmancik JF, et al. Genetic heterogeneity in microcornea-cataract: five novel mutations in CRYAA, CRYGD, and GJA8. Invest Ophthalmol Vis Sci. 2007 Sep;48(9):3937-44.
    • (2007) Invest Ophthalmol Vis Sci. , vol.48 , Issue.9 , pp. 3937-3944
    • Hansen, L.1    Yao, W.2    Eiberg, H.3    Kjaer, K.W.4    Baggesen, K.5    Hejtmancik, J.F.6
  • 169
    • 33746912684 scopus 로고    scopus 로고
    • Congenital cataract and macular hypoplasia in humans associated with a de novo mutation in CRYAA and compound heterozygous mutations in P
    • Aug
    • Graw J, Klopp N, Illig T, Preising MN, Lorenz B. Congenital cataract and macular hypoplasia in humans associated with a de novo mutation in CRYAA and compound heterozygous mutations in P. Graefes Arch Clin Exp Ophthalmol. 2006 Aug;244(8):912-9.
    • (2006) Graefes Arch Clin Exp Ophthalmol. , vol.244 , Issue.8 , pp. 912-919
    • Graw, J.1    Klopp, N.2    Illig, T.3    Preising, M.N.4    Lorenz, B.5
  • 170
    • 0242287938 scopus 로고    scopus 로고
    • Cell death triggered by a novel mutation in the alphaA-crystallin gene underlies autosomal dominant cataract linked to chromosome 21q
    • Oct
    • Mackay DS, Andley UP, Shiels A. Cell death triggered by a novel mutation in the alphaA-crystallin gene underlies autosomal dominant cataract linked to chromosome 21q. Eur J Hum Genet. 2003 Oct;11(10):784-93.
    • (2003) Eur J Hum Genet. , vol.11 , Issue.10 , pp. 784-793
    • Mackay, D.S.1    Andley, U.P.2    Shiels, A.3
  • 171
    • 36249024863 scopus 로고    scopus 로고
    • Recessive congenital total cataract with microcornea and heterozygote carrier signs caused by a novel missense CRYAA mutation (R54C)
    • Dec
    • Khan AO, Aldahmesh MA, Meyer B. Recessive congenital total cataract with microcornea and heterozygote carrier signs caused by a novel missense CRYAA mutation (R54C). Am J Ophthalmol. 2007 Dec;144(6):949-52.
    • (2007) Am J Ophthalmol. , vol.144 , Issue.6 , pp. 949-952
    • Khan, A.O.1    Aldahmesh, M.A.2    Meyer, B.3
  • 172
    • 33745913948 scopus 로고    scopus 로고
    • Identification of a novel, putative cataract-causing allele in CRYAA (G98R) in an Indian family
    • Santhiya ST, Soker T, Klopp N, Illig T, Prakash MV, Selvaraj B, et al. Identification of a novel, putative cataract-causing allele in CRYAA (G98R) in an Indian family. Mol Vis. 2006;12:768-73.
    • (2006) Mol Vis. , vol.12 , pp. 768-773
    • Santhiya, S.T.1    Soker, T.2    Klopp, N.3    Illig, T.4    Prakash, M.V.5    Selvaraj, B.6
  • 173
    • 0031934121 scopus 로고    scopus 로고
    • Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA
    • Litt M, Kramer P, LaMorticella DM, Murphey W, Lovrien EW, Weleber RG. Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA. Hum Mol Genet. 1998;7(3):471-4.
    • (1998) Hum Mol Genet. , vol.7 , Issue.3 , pp. 471-474
    • Litt, M.1    Kramer, P.2    LaMorticella, D.M.3    Murphey, W.4    Lovrien, E.W.5    Weleber, R.G.6
  • 174
    • 33846993052 scopus 로고    scopus 로고
    • New phenotype associated with an Arg116Cys mutation in the CRYAA gene: nuclear cataract, iris coloboma, and microphthalmia
    • Feb
    • Beby F, Commeaux C, Bozon M, Denis P, Edery P, Morle L. New phenotype associated with an Arg116Cys mutation in the CRYAA gene: nuclear cataract, iris coloboma, and microphthalmia. Arch Ophthalmol. 2007 Feb;125(2):213-6.
    • (2007) Arch Ophthalmol. , vol.125 , Issue.2 , pp. 213-216
    • Beby, F.1    Commeaux, C.2    Bozon, M.3    Denis, P.4    Edery, P.5    Morle, L.6
  • 175
    • 33646888160 scopus 로고    scopus 로고
    • A novel fan-shaped cataract-microcornea syndrome caused by a mutation of CRYAA in an Indian family
    • Vanita V, Singh JR, Hejtmancik JF, Nuernberg P, Hennies HC, Singh D, et al. A novel fan-shaped cataract-microcornea syndrome caused by a mutation of CRYAA in an Indian family. Mol Vis. 2006;12:518-22.
    • (2006) Mol Vis. , vol.12 , pp. 518-522
    • Vanita, V.1    Singh, J.R.2    Hejtmancik, J.F.3    Nuernberg, P.4    Hennies, H.C.5    Singh, D.6
  • 176
    • 41849150778 scopus 로고    scopus 로고
    • Clinical variability of autosomal dominant cataract, microcornea and corneal opacity and novel mutation in the alpha A crystallin gene (CRYAA)
    • Apr 1
    • Richter L, Flodman P, Barria von-Bischhoffshausen F, Burch D, Brown S, Nguyen L, et al. Clinical variability of autosomal dominant cataract, microcornea and corneal opacity and novel mutation in the alpha A crystallin gene (CRYAA). Am J Med Genet A. 2008 Apr 1;146(7):833-42.
    • (2008) Am J Med Genet A. , vol.146 , Issue.7 , pp. 833-842
    • Richter, L.1    Flodman, P.2    Barria von-Bischhoffshausen, F.3    Burch, D.4    Brown, S.5    Nguyen, L.6
  • 177
    • 49849089879 scopus 로고    scopus 로고
    • A novel mutation in AlphaA-crystallin (CRYAA) caused autosomal dominant congenital cataract in a large Chinese family
    • May
    • Gu F, Luo W, Li X, Wang Z, Lu S, Zhang M, et al. A novel mutation in AlphaA-crystallin (CRYAA) caused autosomal dominant congenital cataract in a large Chinese family. Hum Mutat. 2008 May;29(5):769.
    • (2008) Hum Mutat. , vol.29 , Issue.5 , pp. 769
    • Gu, F.1    Luo, W.2    Li, X.3    Wang, Z.4    Lu, S.5    Zhang, M.6
  • 178
    • 33748109601 scopus 로고    scopus 로고
    • Identification of a CRYAB mutation associated with autosomal dominant posterior polar cataract in a Chinese family
    • Aug
    • Liu M, Ke T, Wang Z, Yang Q, Chang W, Jiang F, et al. Identification of a CRYAB mutation associated with autosomal dominant posterior polar cataract in a Chinese family. Invest Ophthalmol Vis Sci. 2006 Aug;47(8):3461-6.
    • (2006) Invest Ophthalmol Vis Sci. , vol.47 , Issue.8 , pp. 3461-3466
    • Liu, M.1    Ke, T.2    Wang, Z.3    Yang, Q.4    Chang, W.5    Jiang, F.6
  • 179
    • 65949103211 scopus 로고    scopus 로고
    • Identification of a novel CRYAB mutation associated with autosomal recessive juvenile cataract in a Saudi family
    • Safieh LA, Khan AO, Alkuraya FS. Identification of a novel CRYAB mutation associated with autosomal recessive juvenile cataract in a Saudi family. Mol Vis. 2009;15:980-4.
    • (2009) Mol Vis. , vol.15 , pp. 980-984
    • Safieh, L.A.1    Khan, A.O.2    Alkuraya, F.S.3
  • 180
    • 33645401324 scopus 로고    scopus 로고
    • A novel alphaB-crystallin mutation associated with autosomal dominant congenital lamellar cataract
    • Mar
    • Liu Y, Zhang X, Luo L, Wu M, Zeng R, Cheng G, et al. A novel alphaB-crystallin mutation associated with autosomal dominant congenital lamellar cataract. Invest Ophthalmol Vis Sci. 2006 Mar;47(3):1069-75.
    • (2006) Invest Ophthalmol Vis Sci. , vol.47 , Issue.3 , pp. 1069-1075
    • Liu, Y.1    Zhang, X.2    Luo, L.3    Wu, M.4    Zeng, R.5    Cheng, G.6
  • 181
    • 0034765821 scopus 로고    scopus 로고
    • Alpha-B crystallin gene (CRYAB) mutation causes dominant congenital posterior polar cataract in humans
    • Nov
    • Berry V, Francis P, Reddy MA, Collyer D, Vithana E, MacKay I, et al. Alpha-B crystallin gene (CRYAB) mutation causes dominant congenital posterior polar cataract in humans. Am J Hum Genet. 2001 Nov;69(5):1141-5.
    • (2001) Am J Hum Genet. , vol.69 , Issue.5 , pp. 1141-1145
    • Berry, V.1    Francis, P.2    Reddy, M.A.3    Collyer, D.4    Vithana, E.5    MacKay, I.6
  • 182
    • 57749119543 scopus 로고    scopus 로고
    • Human mutation in the anti-apoptotic heat shock protein 20 abrogates its cardioprotective effects
    • Nov 28
    • Nicolaou P, Knoll R, Haghighi K, Fan GC, Dorn GW, 2nd, Hasenfub G, et al. Human mutation in the anti-apoptotic heat shock protein 20 abrogates its cardioprotective effects. J Biol Chem. 2008 Nov 28;283(48):33465-71.
    • (2008) J Biol Chem. , vol.283 , Issue.48 , pp. 33465-33471
    • Nicolaou, P.1    Knoll, R.2    Haghighi, K.3    Fan, G.C.4    Dorn II, G.W.5    Hasenfub, G.6
  • 183
    • 19944433659 scopus 로고    scopus 로고
    • Small heat-shock protein 22 mutated in autosomal dominant Charcot-Marie-Tooth disease type 2L
    • Feb
    • Tang BS, Zhao GH, Luo W, Xia K, Cai F, Pan Q, et al. Small heat-shock protein 22 mutated in autosomal dominant Charcot-Marie-Tooth disease type 2L. Hum Genet. 2005 Feb;116(3):222-4.
    • (2005) Hum Genet. , vol.116 , Issue.3 , pp. 222-224
    • Tang, B.S.1    Zhao, G.H.2    Luo, W.3    Xia, K.4    Cai, F.5    Pan, Q.6
  • 184
    • 0037359564 scopus 로고    scopus 로고
    • The sperm outer dense fiber protein is the 10th member of the superfamily of mammalian small stress proteins
    • Spring
    • Fontaine JM, Rest JS, Welsh MJ, Benndorf R. The sperm outer dense fiber protein is the 10th member of the superfamily of mammalian small stress proteins. Cell Stress Chaperones, 2003 Spring;8(1):62-9.
    • (2003) Cell Stress Chaperones , vol.8 , Issue.1 , pp. 62-69
    • Fontaine, J.M.1    Rest, J.S.2    Welsh, M.J.3    Benndorf, R.4
  • 185
    • 61849111847 scopus 로고    scopus 로고
    • Dominant cataract formation in association with a vimentin assembly disrupting mutation
    • Mar 15
    • Müller M, Bhattacharya SS, Moore T, Prescott Q, Wedig T, Herrmann H, et al. Dominant cataract formation in association with a vimentin assembly disrupting mutation. Hum Mol Genet. 2009 Mar 15;18(6):1052-7.
    • (2009) Hum Mol Genet. , vol.18 , Issue.6 , pp. 1052-1057
    • Müller, M.1    Bhattacharya, S.S.2    Moore, T.3    Prescott, Q.4    Wedig, T.5    Herrmann, H.6
  • 186
    • 34147101803 scopus 로고    scopus 로고
    • Autosomal recessive juvenile onset cataract associated with mutation in BFSP1
    • May
    • Ramachandran RD, Perumalsamy V, Hejtmancik JF. Autosomal recessive juvenile onset cataract associated with mutation in BFSP1. Hum Genet. 2007 May;121(3-4):475-82.
    • (2007) Hum Genet. , vol.121 , Issue.3-4 , pp. 475-482
    • Ramachandran, R.D.1    Perumalsamy, V.2    Hejtmancik, J.F.3
  • 187
    • 0033942142 scopus 로고    scopus 로고
    • Autosomal-Dominant Congenital Cataract Associated with a Deletion Mutation in the Human Beaded Filament Protein Gene BFSP2
    • Jakobs PM, Hess JF, FitzGerald PG, Kramer P, Weleber RG, Litt M. Autosomal-Dominant Congenital Cataract Associated with a Deletion Mutation in the Human Beaded Filament Protein Gene BFSP2. Am J Hum Genet. 2000;66(4):1432-6.
    • (2000) Am J Hum Genet. , vol.66 , Issue.4 , pp. 1432-1436
    • Jakobs, P.M.1    Hess, J.F.2    FitzGerald, P.G.3    Kramer, P.4    Weleber, R.G.5    Litt, M.6
  • 188
    • 16644393713 scopus 로고    scopus 로고
    • Clinical description and genome wide linkage study of Y-sutural cataract and myopia in a Chinese family
    • Nov 17
    • Zhang Q, Guo X, Xiao X, Yi J, Jia X, Hejtmancik JF. Clinical description and genome wide linkage study of Y-sutural cataract and myopia in a Chinese family. Mol Vis. 2004 Nov 17;10:890-900.
    • (2004) Mol Vis. , vol.17 , Issue.10 , pp. 890-900
    • Zhang, Q.1    Guo, X.2    Xiao, X.3    Yi, J.4    Jia, X.5    Hejtmancik, J.F.6
  • 189
    • 35548990168 scopus 로고    scopus 로고
    • The E233del mutation in BFSP2 causes a progressive autosomal dominant congenital cataract in a Chinese family
    • Cui X, Gao L, Jin Y, Zhang Y, Bai J, Feng G, et al. The E233del mutation in BFSP2 causes a progressive autosomal dominant congenital cataract in a Chinese family. Mol Vis. 2007;13:2023-9.
    • (2007) Mol Vis. , vol.13 , pp. 2023-2029
    • Cui, X.1    Gao, L.2    Jin, Y.3    Zhang, Y.4    Bai, J.5    Feng, G.6
  • 190
    • 0033942141 scopus 로고    scopus 로고
    • A Juvenile-Onset, Progressive Cataract Locus on Chromosome 3q21-q22 Is Associated with a Missense Mutation in the Beaded Filament Structural Protein-2
    • Conley YP, Erturk D, Keverline A, Mah TS, Keravala A, Barnes LR, et al. A Juvenile-Onset, Progressive Cataract Locus on Chromosome 3q21-q22 Is Associated with a Missense Mutation in the Beaded Filament Structural Protein-2. Am J Hum Genet. 2000;66(4):1426-31.
    • (2000) Am J Hum Genet. , vol.66 , Issue.4 , pp. 1426-1431
    • Conley, Y.P.1    Erturk, D.2    Keverline, A.3    Mah, T.S.4    Keravala, A.5    Barnes, L.R.6
  • 191
    • 55349139316 scopus 로고    scopus 로고
    • A new mutation in BFSP2 (G1091A) causes autosomal dominant congenital lamellar cataracts
    • Ma X, Li FF, Wang SZ, Gao C, Zhang M, Zhu SQ. A new mutation in BFSP2 (G1091A) causes autosomal dominant congenital lamellar cataracts. Mol Vis. 2008; 14:1906-11.
    • (2008) Mol Vis. , vol.14 , pp. 1906-1911
    • Ma, X.1    Li, F.F.2    Wang, S.Z.3    Gao, C.4    Zhang, M.5    Zhu, S.Q.6
  • 192
    • 0035136847 scopus 로고    scopus 로고
    • Further evidence that neurofilament light chain gene mutations can cause Charcot-Marie-Tooth disease type 2E
    • Feb
    • De Jonghe P, Mersivanova I, Nelis E, Del Favero J, Martin JJ, Van Broeckhoven C, et al. Further evidence that neurofilament light chain gene mutations can cause Charcot-Marie-Tooth disease type 2E. Ann Neurol. 2001 Feb;49(2):245-9.
    • (2001) Ann Neurol. , vol.49 , Issue.2 , pp. 245-249
    • De Jonghe, P.1    Mersivanova, I.2    Nelis, E.3    Del Favero, J.4    Martin, J.J.5    Van Broeckhoven, C.6
  • 193
    • 5444267945 scopus 로고    scopus 로고
    • Phenotypic analysis of neurofilament light gene mutations linked to Charcot-Marie-Tooth disease in cell culture models
    • Oct 1
    • Perez-Olle R, Jones ST, Liem RK. Phenotypic analysis of neurofilament light gene mutations linked to Charcot-Marie-Tooth disease in cell culture models. Hum Mol Genet. 2004 Oct 1; 13(19):2207-20.
    • (2004) Hum Mol Genet. , vol.13 , Issue.19 , pp. 2207-2220
    • Perez-Olle, R.1    Jones, S.T.2    Liem, R.K.3
  • 195
    • 0037370894 scopus 로고    scopus 로고
    • Mutations in the neurofilament light chain gene (NEFL) cause early onset severe Charcot-Marie-Tooth disease
    • Mar
    • Jordanova A, De Jonghe P, Boerkoel CF, Takashima H, De Vriendt E, Ceuterick C, et al. Mutations in the neurofilament light chain gene (NEFL) cause early onset severe Charcot-Marie-Tooth disease. Brain, 2003 Mar; 126(Pt 3):590-7.
    • (2003) Brain , vol.126 , Issue.PART 3 , pp. 590-597
    • Jordanova, A.1    De Jonghe, P.2    Boerkoel, C.F.3    Takashima, H.4    De Vriendt, E.5    Ceuterick, C.6
  • 196
    • 33646079176 scopus 로고    scopus 로고
    • A novel duplication/insertion mutation of NEFL in a patient with Charcot-Marie-Tooth disease
    • May 1
    • Leung CL, Nagan N, Graham TH, Liem RK. A novel duplication/insertion mutation of NEFL in a patient with Charcot-Marie-Tooth disease. Am J Med Genet A. 2006 May 1; 140(9):1021-5.
    • (2006) Am J Med Genet A. , vol.140 , Issue.9 , pp. 1021-1025
    • Leung, C.L.1    Nagan, N.2    Graham, T.H.3    Liem, R.K.4
  • 198
    • 1942473714 scopus 로고    scopus 로고
    • Giant axon and neurofilament accumulation in Charcot-Marie-Tooth disease type 2E
    • Apr 27
    • Fabrizi GM, Cavallaro T, Angiari C, Bertolasi L, Cabrini I, Ferrarini M, et al. Giant axon and neurofilament accumulation in Charcot-Marie-Tooth disease type 2E. Neurology, 2004 Apr 27; 62(8):1429-31.
    • (2004) Neurology , vol.62 , Issue.8 , pp. 1429-1431
    • Fabrizi, G.M.1    Cavallaro, T.2    Angiari, C.3    Bertolasi, L.4    Cabrini, I.5    Ferrarini, M.6
  • 199
    • 60749123443 scopus 로고    scopus 로고
    • Neurofilament light chain polypeptide gene mutations in Charcot-Marie-Tooth disease: nonsense mutation probably causes a recessive phenotype
    • Abe A, Numakura C, Saito K, Koide H, Oka N, Honma A, et al. Neurofilament light chain polypeptide gene mutations in Charcot-Marie-Tooth disease: nonsense mutation probably causes a recessive phenotype. J Hum Genet. 2009; 54(2):94-7.
    • (2009) J Hum Genet. , vol.54 , Issue.2 , pp. 94-97
    • Abe, A.1    Numakura, C.2    Saito, K.3    Koide, H.4    Oka, N.5    Honma, A.6
  • 200
    • 0742305818 scopus 로고    scopus 로고
    • Myofibrillar myopathy: clinical, morphological and genetic studies in 63 patients
    • Feb
    • Selcen D, Ohno K, Engel AG. Myofibrillar myopathy: clinical, morphological and genetic studies in 63 patients. Brain, 2004 Feb; 127(Pt 2):439-51.
    • (2004) Brain , vol.127 , Issue.PART 2 , pp. 439-451
    • Selcen, D.1    Ohno, K.2    Engel, A.G.3
  • 201
    • 34548745149 scopus 로고    scopus 로고
    • Two related Dutch families with a clinically variable presentation of cardioskeletal myopathy caused by a novel S13F mutation in the desmin gene
    • Sep-Oct
    • Bergman JE, Veenstra-Knol HE, van Essen AJ, van Ravenswaaij CM, den Dunnen WF, van den Wijngaard A, et al. Two related Dutch families with a clinically variable presentation of cardioskeletal myopathy caused by a novel S13F mutation in the desmin gene. Eur J Med Genet. 2007 Sep-Oct;50(5):355-66.
    • (2007) Eur J Med Genet. , vol.50 , Issue.5 , pp. 355-366
    • Bergman, J.E.1    Veenstra-Knol, H.E.2    van Essen, A.J.3    van Ravenswaaij, C.M.4    den Dunnen, W.F.5    van den Wijngaard, A.6
  • 202
    • 39649100186 scopus 로고    scopus 로고
    • Characterization of a novel S13F desmin mutation associated with desmin myopathy and heart block in a Chinese family
    • Feb
    • Pica EC, Kathirvel P, Pramono ZA, Lai PS, Yee WC. Characterization of a novel S13F desmin mutation associated with desmin myopathy and heart block in a Chinese family. Neuromuscul Disord. 2008 Feb; 18(2):178-82.
    • (2008) Neuromuscul Disord. , vol.18 , Issue.2 , pp. 178-182
    • Pica, E.C.1    Kathirvel, P.2    Pramono, Z.A.3    Lai, P.S.4    Yee, W.C.5
  • 203
    • 33747180877 scopus 로고    scopus 로고
    • Desmin accumulation restrictive cardiomyopathy and atrioventricular block associated with desmin gene defects
    • Aug
    • Arbustini E, Pasotti M, Pilotto A, Pellegrini C, Grasso M, Previtali S, et al. Desmin accumulation restrictive cardiomyopathy and atrioventricular block associated with desmin gene defects. Eur J Heart Fail. 2006 Aug; 8(5):477-83.
    • (2006) Eur J Heart Fail. , vol.8 , Issue.5 , pp. 477-483
    • Arbustini, E.1    Pasotti, M.2    Pilotto, A.3    Pellegrini, C.4    Grasso, M.5    Previtali, S.6
  • 204
  • 206
    • 0038669889 scopus 로고    scopus 로고
    • A dysfunctional desmin mutation in a patient with severe generalized myopathy [In Process Citation]
    • Munoz-Marmol AM, Strasser G, Isamat M, Coulombe PA, Yang Y, Roca X, et al. A dysfunctional desmin mutation in a patient with severe generalized myopathy [In Process Citation]. Proc Natl Acad Sci U S A. 1998;95(19):11312-7.
    • (1998) Proc Natl Acad Sci U S A. , vol.95 , Issue.19 , pp. 11312-11317
    • Munoz-Marmol, A.M.1    Strasser, G.2    Isamat, M.3    Coulombe, P.A.4    Yang, Y.5    Roca, X.6
  • 209
    • 18344374698 scopus 로고    scopus 로고
    • The enlarging spectrum of desminopathies: new morphological findings, eastward geographic spread, novel exon 3 desmin mutation
    • Apr
    • Vrabie A, Goldfarb LG, Shatunov A, Nagele A, Fritz P, Kaczmarek I, et al. The enlarging spectrum of desminopathies: new morphological findings, eastward geographic spread, novel exon 3 desmin mutation. Acta Neuropathol. 2005 Apr; 109(4):411-7.
    • (2005) Acta Neuropathol. , vol.109 , Issue.4 , pp. 411-417
    • Vrabie, A.1    Goldfarb, L.G.2    Shatunov, A.3    Nagele, A.4    Fritz, P.5    Kaczmarek, I.6
  • 210
    • 0034673647 scopus 로고    scopus 로고
    • Desmin myopathy, a skeletal myopathy with cardiomyopathy caused by mutations in the desmin gene
    • Mar 16
    • Dalakas MC, Park KY, Semino-Mora C, Lee HS, Sivakumar K, Goldfarb LG. Desmin myopathy, a skeletal myopathy with cardiomyopathy caused by mutations in the desmin gene. N Engl J Med. 2000 Mar 16;342(11):770-80.
    • (2000) N Engl J Med. , vol.342 , Issue.11 , pp. 770-780
    • Dalakas, M.C.1    Park, K.Y.2    Semino-Mora, C.3    Lee, H.S.4    Sivakumar, K.5    Goldfarb, L.G.6
  • 212
    • 0037444403 scopus 로고    scopus 로고
    • On noxious desmin: functional effects of a novel heterozygous desmin insertion mutation on the extrasarcomeric desmin cytoskeleton and mitochondria
    • Mar 15
    • Schroder R, Goudeau B, Simon MC, Fischer D, Eggermann T, Clemen CS, et al. On noxious desmin: functional effects of a novel heterozygous desmin insertion mutation on the extrasarcomeric desmin cytoskeleton and mitochondria. Hum Mol Genet. 2003 Mar 15; 12(6):657-69.
    • (2003) Hum Mol Genet. , vol.12 , Issue.6 , pp. 657-669
    • Schroder, R.1    Goudeau, B.2    Simon, M.C.3    Fischer, D.4    Eggermann, T.5    Clemen, C.S.6
  • 214
    • 3042778127 scopus 로고    scopus 로고
    • A missense mutation in the desmin rod domain is associated with autosomal dominant distal myopathy, and exerts a dominant negative effect on filament formation
    • Nov
    • Sjoberg G, Saavedra-Matiz CA, Rosen DR, Wijsman EM, Borg K, Horowitz SH, et al. A missense mutation in the desmin rod domain is associated with autosomal dominant distal myopathy, and exerts a dominant negative effect on filament formation. Hum Mol Genet. 1999 Nov; 8(12):2191-8.
    • (1999) Hum Mol Genet. , vol.8 , Issue.12 , pp. 2191-2198
    • Sjoberg, G.1    Saavedra-Matiz, C.A.2    Rosen, D.R.3    Wijsman, E.M.4    Borg, K.5    Horowitz, S.H.6
  • 215
    • 34250813063 scopus 로고    scopus 로고
    • Scapuloperoneal syndrome type Kaeser and a wide phenotypic spectrum of adult-onset, dominant myopathies are associated with the desmin mutation R350P
    • Jun
    • Walter MC, Reilich P, Huebner A, Fischer D, Schroder R, Vorgerd M, et al. Scapuloperoneal syndrome type Kaeser and a wide phenotypic spectrum of adult-onset, dominant myopathies are associated with the desmin mutation R350P. Brain, 2007 Jun;130(Pt 6):1485-96.
    • (2007) Brain , vol.130 , Issue.PART 6 , pp. 1485-1496
    • Walter, M.C.1    Reilich, P.2    Huebner, A.3    Fischer, D.4    Schroder, R.5    Vorgerd, M.6
  • 216
    • 19744363995 scopus 로고    scopus 로고
    • Pathogenic effects of a novel heterozygous R350P desmin mutation on the assembly of desmin intermediate filaments in vivo and in vitro
    • May 15
    • Bar H, Fischer D, Goudeau B, Kley RA, Clemen CS, Vicart P, et al. Pathogenic effects of a novel heterozygous R350P desmin mutation on the assembly of desmin intermediate filaments in vivo and in vitro. Hum Mol Genet. 2005 May 15; 14(10):1251-60.
    • (2005) Hum Mol Genet. , vol.14 , Issue.10 , pp. 1251-1260
    • Bar, H.1    Fischer, D.2    Goudeau, B.3    Kley, R.A.4    Clemen, C.S.5    Vicart, P.6
  • 218
    • 12444251022 scopus 로고    scopus 로고
    • Respiratory insufficiency in desminopathy patients caused by introduction of proline residues in desmin c-terminal alpha-helical segment
    • Jun
    • Dagvadorj A, Goudeau B, Hilton-Jones D, Blancato JK, Shatunov A, Simon-Casteras M, et al. Respiratory insufficiency in desminopathy patients caused by introduction of proline residues in desmin c-terminal alpha-helical segment. Muscle Nerve, 2003 Jun; 27(6):669-75.
    • (2003) Muscle Nerve , vol.27 , Issue.6 , pp. 669-675
    • Dagvadorj, A.1    Goudeau, B.2    Hilton-Jones, D.3    Blancato, J.K.4    Shatunov, A.5    Simon-Casteras, M.6
  • 219
    • 10744233465 scopus 로고    scopus 로고
    • Small deletions disturb desmin architecture leading to breakdown of muscle cells and development of skeletal or cardioskeletal myopathy
    • Feb
    • Kaminska A, Strelkov SV, Goudeau B, Olive M, Dagvadorj A, Fidzianska A, et al. Small deletions disturb desmin architecture leading to breakdown of muscle cells and development of skeletal or cardioskeletal myopathy. Hum Genet. 2004 Feb;114(3):306-13.
    • (2004) Hum Genet. , vol.114 , Issue.3 , pp. 306-313
    • Kaminska, A.1    Strelkov, S.V.2    Goudeau, B.3    Olive, M.4    Dagvadorj, A.5    Fidzianska, A.6
  • 220
    • 34249026071 scopus 로고    scopus 로고
    • Phenotypic patterns of desminopathy associated with three novel mutations in the desmin gene
    • Jun
    • Olive M, Armstrong J, Miralles F, Pou A, Fardeau M, Gonzalez L, et al. Phenotypic patterns of desminopathy associated with three novel mutations in the desmin gene. Neuromuscul Disord. 2007 Jun;17(6):443-50.
    • (2007) Neuromuscul Disord. , vol.17 , Issue.6 , pp. 443-450
    • Olive, M.1    Armstrong, J.2    Miralles, F.3    Pou, A.4    Fardeau, M.5    Gonzalez, L.6
  • 221
    • 0034633685 scopus 로고    scopus 로고
    • A novel de novo mutation in the desmin gene causes desmin myopathy with toxic aggregates
    • Oct 10
    • Sugawara M, Kato K, Komatsu M, Wada C, Kawamura K, Shindo PS, et al. A novel de novo mutation in the desmin gene causes desmin myopathy with toxic aggregates. Neurology, 2000 Oct 10;55(7):986-90.
    • (2000) Neurology , vol.55 , Issue.7 , pp. 986-990
    • Sugawara, M.1    Kato, K.2    Komatsu, M.3    Wada, C.4    Kawamura, K.5    Shindo, P.S.6
  • 222
  • 223
    • 0034120197 scopus 로고    scopus 로고
    • Sporadic cardiac and skeletal myopathy caused by a de novo desmin mutation
    • Jun
    • Park KY, Dalakas MC, Semino-Mora C, Lee HS, Litvak S, Takeda K, et al. Sporadic cardiac and skeletal myopathy caused by a de novo desmin mutation. Clin Genet. 2000 Jun; 57(6):423-9.
    • (2000) Clin Genet. , vol.57 , Issue.6 , pp. 423-429
    • Park, K.Y.1    Dalakas, M.C.2    Semino-Mora, C.3    Lee, H.S.4    Litvak, S.5    Takeda, K.6
  • 224
    • 12144286880 scopus 로고    scopus 로고
    • Desmin-related myopathy: clinical, electrophysiological, radiological, neuropathological and genetic studies
    • Apr 15
    • Olive M, Goldfarb L, Moreno D, Laforet E, Dagvadorj A, Sambuughin N, et al. Desmin-related myopathy: clinical, electrophysiological, radiological, neuropathological and genetic studies. J Neurol Sci. 2004 Apr 15; 219(1-2):125-37.
    • (2004) J Neurol Sci. , vol.219 , Issue.1-2 , pp. 125-137
    • Olive, M.1    Goldfarb, L.2    Moreno, D.3    Laforet, E.4    Dagvadorj, A.5    Sambuughin, N.6
  • 225
    • 10744229630 scopus 로고    scopus 로고
    • A series of West European patients with severe cardiac and skeletal myopathy associated with a de novo R406W mutation in desmin
    • Feb
    • Dagvadorj A, Olive M, Urtizberea JA, Halle M, Shatunov A, Bonnemann C, et al. A series of West European patients with severe cardiac and skeletal myopathy associated with a de novo R406W mutation in desmin. J Neurol. 2004 Feb; 251(2):143-9.
    • (2004) J Neurol. , vol.251 , Issue.2 , pp. 143-149
    • Dagvadorj, A.1    Olive, M.2    Urtizberea, J.A.3    Halle, M.4    Shatunov, A.5    Bonnemann, C.6
  • 226
    • 33947517125 scopus 로고    scopus 로고
    • Restrictive cardiomyopathy with atrioventricular conduction block resulting from a desmin mutation
    • Apr 25
    • Pruszczyk P, Kostera-Pruszczyk A, Shatunov A, Goudeau B, Draminska A, Takeda K, et al. Restrictive cardiomyopathy with atrioventricular conduction block resulting from a desmin mutation. Int J Cardiol. 2007 Apr 25;117(2):244-53.
    • (2007) Int J Cardiol. , vol.117 , Issue.2 , pp. 244-253
    • Pruszczyk, P.1    Kostera-Pruszczyk, A.2    Shatunov, A.3    Goudeau, B.4    Draminska, A.5    Takeda, K.6
  • 228
    • 0033730389 scopus 로고    scopus 로고
    • Epidemiology of desmin and cardiac actin gene mutations in a European population of dilated cardiomyopathy
    • Nov
    • Tesson F, Sylvius N, Pilotto A, Dubosq-Bidot L, Peuchmaurd M, Bouchier C, et al. Epidemiology of desmin and cardiac actin gene mutations in a European population of dilated cardiomyopathy. Eur Heart J. 2000 Nov; 21(22):1872-6.
    • (2000) Eur Heart J. , vol.21 , Issue.22 , pp. 1872-1876
    • Tesson, F.1    Sylvius, N.2    Pilotto, A.3    Dubosq-Bidot, L.4    Peuchmaurd, M.5    Bouchier, C.6
  • 229
    • 34047242886 scopus 로고    scopus 로고
    • Conspicuous involvement of desmin tail mutations in diverse cardiac and skeletal myopathies
    • Apr
    • Bar H, Goudeau B, Walde S, Casteras-Simon M, Mucke N, Shatunov A, et al. Conspicuous involvement of desmin tail mutations in diverse cardiac and skeletal myopathies. Hum Mutat. 2007 Apr; 28(4):374-86.
    • (2007) Hum Mutat. , vol.28 , Issue.4 , pp. 374-386
    • Bar, H.1    Goudeau, B.2    Walde, S.3    Casteras-Simon, M.4    Mucke, N.5    Shatunov, A.6
  • 230
    • 33646232231 scopus 로고    scopus 로고
    • Disease severity in dominant Emery Dreifuss is increased by mutations in both emerin and desmin proteins
    • May
    • Muntoni F, Bonne G, Goldfarb LG, Mercuri E, Piercy RJ, Burke M, et al. Disease severity in dominant Emery Dreifuss is increased by mutations in both emerin and desmin proteins. Brain, 2006 May; 129(Pt 5):1260-8.
    • (2006) Brain , vol.129 , Issue.PART 5 , pp. 1260-1268
    • Muntoni, F.1    Bonne, G.2    Goldfarb, L.G.3    Mercuri, E.4    Piercy, R.J.5    Burke, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.