메뉴 건너뛰기




Volumn 761, Issue , 2014, Pages 15-30

Neuropathy- and myopathy-associated mutations in human small heat shock proteins: Characteristics and evolutionary history of the mutation sites

Author keywords

Genetic dominance; Motor neuropathy; Mutation; Myopathy; Purifying selection; Small heat shock protein

Indexed keywords

ALPHA CRYSTALLIN; HEAT SHOCK PROTEIN 22; HEAT SHOCK PROTEIN 27; HSPB3 PROTEIN; SMALL HEAT SHOCK PROTEIN; UNCLASSIFIED DRUG;

EID: 84921856085     PISSN: 13835742     EISSN: 13882139     Source Type: Journal    
DOI: 10.1016/j.mrrev.2014.02.004     Document Type: Review
Times cited : (49)

References (107)
  • 1
    • 0037359564 scopus 로고    scopus 로고
    • The sperm outer dense fiber protein is the 10th member of the superfamily of mammalian small stress proteins
    • Fontaine J.-M., Rest J.S., Welsh M.J., Benndorf R. The sperm outer dense fiber protein is the 10th member of the superfamily of mammalian small stress proteins. Cell Stress Chaperones 2003, 8:62-69.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 62-69
    • Fontaine, J.-M.1    Rest, J.S.2    Welsh, M.J.3    Benndorf, R.4
  • 4
    • 0032077156 scopus 로고    scopus 로고
    • Genealogy of the alpha-crystallin-small heat shock protein superfamily
    • de Jong W.W., Caspers G.J., Leunissen J.A. Genealogy of the alpha-crystallin-small heat shock protein superfamily. Int. J. Biol. Macromol. 1998, 22:151-162.
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 151-162
    • de Jong, W.W.1    Caspers, G.J.2    Leunissen, J.A.3
  • 5
    • 80054747192 scopus 로고    scopus 로고
    • Large potentials of small heat shock proteins
    • Mymrikov E.V., Seit-Nebi A.S., Gusev N.B. Large potentials of small heat shock proteins. Physiol. Rev. 2011, 91:1123-1159.
    • (2011) Physiol. Rev. , vol.91 , pp. 1123-1159
    • Mymrikov, E.V.1    Seit-Nebi, A.S.2    Gusev, N.B.3
  • 6
    • 77955665257 scopus 로고    scopus 로고
    • Why proteins without an alpha-crystallin domain should not be included in the human small heat shock protein family HSPB
    • Kappé G., Boelens W.C., de Jong W.W. Why proteins without an alpha-crystallin domain should not be included in the human small heat shock protein family HSPB. Cell Stress Chaperones 2010, 15:457-461.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 457-461
    • Kappé, G.1    Boelens, W.C.2    de Jong, W.W.3
  • 7
    • 84934439863 scopus 로고    scopus 로고
    • The cellular 'networking' of mammalian Hsp27 and its functions in the control of protein folding, redox state and apoptosis
    • Arrigo A.-P. The cellular 'networking' of mammalian Hsp27 and its functions in the control of protein folding, redox state and apoptosis. Adv. Exp. Med. Biol. 2007, 594:14-26.
    • (2007) Adv. Exp. Med. Biol. , vol.594 , pp. 14-26
    • Arrigo, A.-P.1
  • 8
    • 46849116411 scopus 로고    scopus 로고
    • Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families
    • Vos M.J., Hageman J., Carra S., Kampinga H.H. Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families. Biochemistry 2008, 47:7001-7011.
    • (2008) Biochemistry , vol.47 , pp. 7001-7011
    • Vos, M.J.1    Hageman, J.2    Carra, S.3    Kampinga, H.H.4
  • 9
    • 84858003372 scopus 로고    scopus 로고
    • Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions
    • Basha E., O'Neill H., Vierling E. Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions. Trends Biochem. Sci. 2012, 37:106-117.
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 106-117
    • Basha, E.1    O'Neill, H.2    Vierling, E.3
  • 11
    • 84963732609 scopus 로고    scopus 로고
    • Small stress proteins in the central nervous system: From neurodegeneration to neuroprotection
    • Nova Science Publishers, New York, S. Simon, A.-P. Arrigo (Eds.)
    • Wyttenbach A., Hands S., O'Connor V. Small stress proteins in the central nervous system: From neurodegeneration to neuroprotection. Small Stress Proteins And Human Diseases 2012, 117-146. Nova Science Publishers, New York. S. Simon, A.-P. Arrigo (Eds.).
    • (2012) Small Stress Proteins And Human Diseases , pp. 117-146
    • Wyttenbach, A.1    Hands, S.2    O'Connor, V.3
  • 13
    • 84895308310 scopus 로고    scopus 로고
    • HSPB1 and HSPB8 mutations in neuropathies
    • Nova Science Publishers, New York, S. Simon, A.-P. Arrigo (Eds.)
    • Benndorf R. HSPB1 and HSPB8 mutations in neuropathies. Small stress proteins and human diseases 2012, 301-324. Nova Science Publishers, New York. S. Simon, A.-P. Arrigo (Eds.).
    • (2012) Small stress proteins and human diseases , pp. 301-324
    • Benndorf, R.1
  • 14
    • 57749119543 scopus 로고    scopus 로고
    • Human mutation in the anti-apoptotic heat shock protein 20 abrogates its cardioprotective effects
    • Nicolaou P., Knöll R., Haghighi K., Fan G.C., Dorn G.W., Hasenfuss G., Kranias E.G. Human mutation in the anti-apoptotic heat shock protein 20 abrogates its cardioprotective effects. J. Biol. Chem. 2008, 283:33465-33471.
    • (2008) J. Biol. Chem. , vol.283 , pp. 33465-33471
    • Nicolaou, P.1    Knöll, R.2    Haghighi, K.3    Fan, G.C.4    Dorn, G.W.5    Hasenfuss, G.6    Kranias, E.G.7
  • 15
    • 77957841871 scopus 로고    scopus 로고
    • Independent evolution of the core domain and its flanking sequences in small heat shock proteins
    • Kriehuber T., Rattei T., Weinmaier T., Bepperling A., Haslbeck M., Buchner J. Independent evolution of the core domain and its flanking sequences in small heat shock proteins. FASEB J. 2010, 24:3633-3642.
    • (2010) FASEB J. , vol.24 , pp. 3633-3642
    • Kriehuber, T.1    Rattei, T.2    Weinmaier, T.3    Bepperling, A.4    Haslbeck, M.5    Buchner, J.6
  • 17
    • 0027764344 scopus 로고
    • Protein sequence alignments: a strategy for the hierarchical analysis of residue conservation
    • Livingstone C.D., Barton G.J. Protein sequence alignments: a strategy for the hierarchical analysis of residue conservation. Comput. Appl. Biosci. 1993, 9:745-756.
    • (1993) Comput. Appl. Biosci. , vol.9 , pp. 745-756
    • Livingstone, C.D.1    Barton, G.J.2
  • 19
    • 0024598146 scopus 로고
    • Fast and sensitive multiple sequence alignments on a microcomputer
    • Higgins D.G., Sharp P.M. Fast and sensitive multiple sequence alignments on a microcomputer. Comput. Appl. Biosci. 1989, 5:151-153.
    • (1989) Comput. Appl. Biosci. , vol.5 , pp. 151-153
    • Higgins, D.G.1    Sharp, P.M.2
  • 20
    • 17744396121 scopus 로고    scopus 로고
    • Not so different after all: a comparison of methods for detecting amino acid sites under selection
    • Kosakovsky Pond S.L., Frost S.D. Not so different after all: a comparison of methods for detecting amino acid sites under selection. Mol. Biol. Evol. 2005, 22:1208-1222.
    • (2005) Mol. Biol. Evol. , vol.22 , pp. 1208-1222
    • Kosakovsky Pond, S.L.1    Frost, S.D.2
  • 21
    • 15844406550 scopus 로고    scopus 로고
    • HyPhy: hypothesis testing using phylogenies
    • Pond S.L., Frost S.D., Muse S.V. HyPhy: hypothesis testing using phylogenies. Bioinformatics 2005, 21:676-679.
    • (2005) Bioinformatics , vol.21 , pp. 676-679
    • Pond, S.L.1    Frost, S.D.2    Muse, S.V.3
  • 22
    • 17744395033 scopus 로고    scopus 로고
    • Datamonkey: rapid detection of selective pressure on individual sites of codon alignments
    • Pond S.L., Frost S.D. Datamonkey: rapid detection of selective pressure on individual sites of codon alignments. Bioinformatics 2005, 21:2531-2533.
    • (2005) Bioinformatics , vol.21 , pp. 2531-2533
    • Pond, S.L.1    Frost, S.D.2
  • 24
    • 35448989800 scopus 로고    scopus 로고
    • Effect of mutations in the beta5-beta7 loop on the structure and properties of human small heat shock protein HSP22 (HspB8, H11)
    • Kasakov A.S., Bukach O.V., Seit-Nebi A.S., Marston S.B., Gusev N.B. Effect of mutations in the beta5-beta7 loop on the structure and properties of human small heat shock protein HSP22 (HspB8, H11). FEBS J. 2007, 274:5628-5642.
    • (2007) FEBS J. , vol.274 , pp. 5628-5642
    • Kasakov, A.S.1    Bukach, O.V.2    Seit-Nebi, A.S.3    Marston, S.B.4    Gusev, N.B.5
  • 25
    • 0036258111 scopus 로고    scopus 로고
    • The IARC TP53 database: new online mutation analysis and recommendations to users
    • Olivier M., Eeles R., Hollstein M., Khan M.A., Harris C.C., Hainaut P. The IARC TP53 database: new online mutation analysis and recommendations to users. Hum. Mutat. 2002, 19:607-614.
    • (2002) Hum. Mutat. , vol.19 , pp. 607-614
    • Olivier, M.1    Eeles, R.2    Hollstein, M.3    Khan, M.A.4    Harris, C.C.5    Hainaut, P.6
  • 26
    • 84857129568 scopus 로고    scopus 로고
    • The role of intrinsically disordered regions in the structure and functioning of small heat shock proteins
    • Sudnitsyna M.V., Mymrikov E.V., Seit-Nebi A.S., Gusev N.B. The role of intrinsically disordered regions in the structure and functioning of small heat shock proteins. Curr. Protein Pept. Sci. 2012, 13:76-85.
    • (2012) Curr. Protein Pept. Sci. , vol.13 , pp. 76-85
    • Sudnitsyna, M.V.1    Mymrikov, E.V.2    Seit-Nebi, A.S.3    Gusev, N.B.4
  • 27
    • 30044445875 scopus 로고    scopus 로고
    • Evidence for an essential function of the N terminus of a small heat shock protein in vivo, independent of in vitro chaperone activity
    • Giese K.C., Basha E., Catague B.Y., Vierling E. Evidence for an essential function of the N terminus of a small heat shock protein in vivo, independent of in vitro chaperone activity. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:18896-18901.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 18896-18901
    • Giese, K.C.1    Basha, E.2    Catague, B.Y.3    Vierling, E.4
  • 28
    • 42349107955 scopus 로고    scopus 로고
    • Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formation
    • Treweek T.M., Ecroyd H., Williams D.M., Meehan S., Carver J.A., Walker M.J. Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formation. PLoS ONE 2007, 2:e1046.
    • (2007) PLoS ONE , vol.2 , pp. e1046
    • Treweek, T.M.1    Ecroyd, H.2    Williams, D.M.3    Meehan, S.4    Carver, J.A.5    Walker, M.J.6
  • 29
    • 84455168004 scopus 로고    scopus 로고
    • Roles of the N- and C-terminal sequences in Hsp27 self-association and chaperone activity
    • Lelj-Garolla B., Mauk A.G. Roles of the N- and C-terminal sequences in Hsp27 self-association and chaperone activity. Protein Sci. 2012, 21:122-133.
    • (2012) Protein Sci. , vol.21 , pp. 122-133
    • Lelj-Garolla, B.1    Mauk, A.G.2
  • 30
    • 84856820287 scopus 로고    scopus 로고
    • Sequence, structure, and dynamic determinants of Hsp27 (HspB1) equilibrium dissociation are encoded by the N-terminal domain
    • McDonald E.T., Bortolus M., Koteiche H.A., Mchaourab H.S. Sequence, structure, and dynamic determinants of Hsp27 (HspB1) equilibrium dissociation are encoded by the N-terminal domain. Biochemistry 2012, 51:1257-1268.
    • (2012) Biochemistry , vol.51 , pp. 1257-1268
    • McDonald, E.T.1    Bortolus, M.2    Koteiche, H.A.3    Mchaourab, H.S.4
  • 31
    • 84865569485 scopus 로고    scopus 로고
    • Structural aspects and chaperone activity of human HspB3: role of the 'C-Terminal Extension'
    • Asthana A., Raman B., Ramakrishna T., Rao C.M. Structural aspects and chaperone activity of human HspB3: role of the 'C-Terminal Extension'. Cell. Biochem. Biophys. 2012, 64:61-72.
    • (2012) Cell. Biochem. Biophys. , vol.64 , pp. 61-72
    • Asthana, A.1    Raman, B.2    Ramakrishna, T.3    Rao, C.M.4
  • 32
    • 0029956553 scopus 로고    scopus 로고
    • Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin
    • Plater M.L., Goode D., Crabbe M.J. Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin. J. Biol. Chem. 1996, 271:28558-28566.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28558-28566
    • Plater, M.L.1    Goode, D.2    Crabbe, M.J.3
  • 33
    • 0036299753 scopus 로고    scopus 로고
    • Mutation of COOH-terminal lysines in overexpressed alpha B-crystallin abrogates ischemic protection in cardiomyocytes
    • Martin J.L., Bluhm W.F., He H., Mestril R., Dillmann W.H. Mutation of COOH-terminal lysines in overexpressed alpha B-crystallin abrogates ischemic protection in cardiomyocytes. Am. J. Physiol. Heart Circ. Physiol. 2002, 283:H85-H91.
    • (2002) Am. J. Physiol. Heart Circ. Physiol. , vol.283 , pp. H85-H91
    • Martin, J.L.1    Bluhm, W.F.2    He, H.3    Mestril, R.4    Dillmann, W.H.5
  • 35
    • 0034294838 scopus 로고    scopus 로고
    • Five novel genetic variants in the promoter and coding region of the alpha B-crystallin gene (CRYAB): -652G>A, -650C>G, -249G>C, S41Y, P51L
    • Hahner A., Erdmann J., Kallisch H., Fleck E., Regitz-Zagrosek V. Five novel genetic variants in the promoter and coding region of the alpha B-crystallin gene (CRYAB): -652G>A, -650C>G, -249G>C, S41Y, P51L. Hum. Mutat. 2000, 16:374.
    • (2000) Hum. Mutat. , vol.16 , pp. 374
    • Hahner, A.1    Erdmann, J.2    Kallisch, H.3    Fleck, E.4    Regitz-Zagrosek, V.5
  • 37
    • 58149243285 scopus 로고    scopus 로고
    • Mutations in the HSP27 (HSPB1) gene cause dominant, recessive, and sporadic distal HMN/CMT type 2
    • Houlden H., Laura M., Wavrant-De Vrièze F., Blake J., Wood N., Reilly M.M. Mutations in the HSP27 (HSPB1) gene cause dominant, recessive, and sporadic distal HMN/CMT type 2. Neurology 2008, 71:1660-1668.
    • (2008) Neurology , vol.71 , pp. 1660-1668
    • Houlden, H.1    Laura, M.2    Wavrant-De Vrièze, F.3    Blake, J.4    Wood, N.5    Reilly, M.M.6
  • 43
    • 41149089652 scopus 로고    scopus 로고
    • Asymmetrical late onset motor neuropathy associated with a novel mutation in the small heat shock protein HSPB1 (HSP27)
    • James P.A., 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, 79:461-463.
    • (2008) J. Neurol. Neurosurg. Psychiatry , vol.79 , pp. 461-463
    • James, P.A.1    Rankin, J.2    Talbot, K.3
  • 44
    • 58149299834 scopus 로고    scopus 로고
    • A clinical phenotype of distal hereditary motor neuronopathy type II with a novel HSPB1 mutation
    • 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, 277:9-12.
    • (2009) J. Neurol. Sci. , vol.277 , pp. 9-12
    • Ikeda, Y.1    Abe, A.2    Ishida, C.3    Takahashi, K.4    Hayasaka, K.5    Yamada, M.6
  • 45
    • 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., Hayasaka K. Small heat shock protein 27 mutation in a Japanese patient with distal hereditary motor neuropathy. J. Hum. Genet. 2005, 50:473-476.
    • (2005) J. Hum. Genet. , vol.50 , pp. 473-476
    • Kijima, K.1    Numakura, C.2    Goto, T.3    Takahashi, T.4    Otagiri, T.5    Umetsu, K.6    Hayasaka, K.7
  • 51
    • 84880940762 scopus 로고    scopus 로고
    • A novel Lys141Thr mutation in small heat shock protein 22 (HSPB8) gene in Charcot-Marie-Tooth disease type 2L
    • Nakhro K., Park J.M., Kim Y.J., Yoon B.R., Yoo J.H., Koo H., Choi B.O., Chung K.W. A novel Lys141Thr mutation in small heat shock protein 22 (HSPB8) gene in Charcot-Marie-Tooth disease type 2L. Neuromuscul. Disord. 2013, 23:656-663.
    • (2013) Neuromuscul. Disord. , vol.23 , pp. 656-663
    • Nakhro, K.1    Park, J.M.2    Kim, Y.J.3    Yoon, B.R.4    Yoo, J.H.5    Koo, H.6    Choi, B.O.7    Chung, K.W.8
  • 55
    • 0018068469 scopus 로고
    • Une nouvelle affection musculaire familiale, definie par l'accumulation intra-sarco-plasmique d'un materiel granulo-filamentaire dense en microscopie electronique
    • Fardeau M., Godet-Guillain J., Tome F.M., Collin H., Gardeau S., Boffety C., Vernant P. Une nouvelle affection musculaire familiale, definie par l'accumulation intra-sarco-plasmique d'un materiel granulo-filamentaire dense en microscopie electronique. Rev. Neurol. (Paris) 1978, 134:411-425.
    • (1978) Rev. Neurol. (Paris) , vol.134 , pp. 411-425
    • Fardeau, M.1    Godet-Guillain, J.2    Tome, F.M.3    Collin, H.4    Gardeau, S.5    Boffety, C.6    Vernant, P.7
  • 56
    • 33745365549 scopus 로고    scopus 로고
    • AlphaB-crystallin mutation in dilated cardiomyopathies: low prevalence in a consecutive series of 200 unrelated probands
    • Pilotto A., Marziliano N., Pasotti M., Grasso M., Costante A.M., Arbustini E. alphaB-crystallin mutation in dilated cardiomyopathies: low prevalence in a consecutive series of 200 unrelated probands. Biochem. Biophys. Res. Commun. 2006, 346:1115-1117.
    • (2006) Biochem. Biophys. Res. Commun. , vol.346 , pp. 1115-1117
    • Pilotto, A.1    Marziliano, N.2    Pasotti, M.3    Grasso, M.4    Costante, A.M.5    Arbustini, E.6
  • 63
    • 0344664368 scopus 로고    scopus 로고
    • Myofibrillar myopathy caused by novel dominant negative alpha B-crystallin mutations
    • Selcen D., Engel A.G. Myofibrillar myopathy caused by novel dominant negative alpha B-crystallin mutations. Ann. Neurol. 2003, 54:804-810.
    • (2003) Ann. Neurol. , vol.54 , pp. 804-810
    • Selcen, D.1    Engel, A.G.2
  • 65
    • 15344340688 scopus 로고    scopus 로고
    • Polymorphisms affecting gene regulation and mRNA processing: broad implications for pharmacogenetics
    • Johnson A.D., Wang D., Sadee W. Polymorphisms affecting gene regulation and mRNA processing: broad implications for pharmacogenetics. Pharmacol. Ther. 2005, 106:19-38.
    • (2005) Pharmacol. Ther. , vol.106 , pp. 19-38
    • Johnson, A.D.1    Wang, D.2    Sadee, W.3
  • 66
    • 0028014337 scopus 로고
    • The molecular basis of genetic dominance
    • Wilkie A.O.M. The molecular basis of genetic dominance. J. Med. Genet. 1994, 31:89-98.
    • (1994) J. Med. Genet. , vol.31 , pp. 89-98
    • Wilkie, A.O.M.1
  • 67
    • 52149093002 scopus 로고    scopus 로고
    • The flux-summation theorem and the 'evolution of dominance'
    • Agutter P.S. The flux-summation theorem and the 'evolution of dominance'. J. Theor. Biol. 2008, 254:821-825.
    • (2008) J. Theor. Biol. , vol.254 , pp. 821-825
    • Agutter, P.S.1
  • 69
    • 78650395329 scopus 로고    scopus 로고
    • The role played by natural selection on Mendelian traits in humans
    • Quintana-Murci L., Barreiro L.B. The role played by natural selection on Mendelian traits in humans. Ann. N. Y. Acad. Sci. 2010, 1214:1-17.
    • (2010) Ann. N. Y. Acad. Sci. , vol.1214 , pp. 1-17
    • Quintana-Murci, L.1    Barreiro, L.B.2
  • 71
    • 33746443339 scopus 로고    scopus 로고
    • Unresolved boundaries of evolutionary theory and the question of how inheritance systems evolve: 75 years of debate on the evolution of dominance
    • Bagheri H.C. Unresolved boundaries of evolutionary theory and the question of how inheritance systems evolve: 75 years of debate on the evolution of dominance. J. Exp. Zool. B Mol. Dev. Evol. 2006, 306:329-359.
    • (2006) J. Exp. Zool. B Mol. Dev. Evol. , vol.306 , pp. 329-359
    • Bagheri, H.C.1
  • 72
    • 77951640530 scopus 로고    scopus 로고
    • A generalized model of gene dosage and dominant negative effects in macromolecular complexes
    • Veitia R.A. A generalized model of gene dosage and dominant negative effects in macromolecular complexes. FASEB J. 2010, 24:994-1002.
    • (2010) FASEB J. , vol.24 , pp. 994-1002
    • Veitia, R.A.1
  • 73
    • 73949089947 scopus 로고    scopus 로고
    • Dominance and gene dosage balance in health and disease: why levels matter!
    • Veitia R.A., Birchler J.A. Dominance and gene dosage balance in health and disease: why levels matter!. J. Pathol. 2010, 220:174-185.
    • (2010) J. Pathol. , vol.220 , pp. 174-185
    • Veitia, R.A.1    Birchler, J.A.2
  • 74
    • 33644681986 scopus 로고    scopus 로고
    • The advantages and disadvantages of being polyploid
    • Comai L. The advantages and disadvantages of being polyploid. Nat. Rev. Genet. 2005, 6:836-846.
    • (2005) Nat. Rev. Genet. , vol.6 , pp. 836-846
    • Comai, L.1
  • 75
    • 84862848512 scopus 로고    scopus 로고
    • Heterooligomeric complexes of human small heat shock proteins
    • Mymrikov E.V., Seit-Nebi A.S., Gusev N.B. Heterooligomeric complexes of human small heat shock proteins. Cell Stress Chaperones 2012, 17:157-169.
    • (2012) Cell Stress Chaperones , vol.17 , pp. 157-169
    • Mymrikov, E.V.1    Seit-Nebi, A.S.2    Gusev, N.B.3
  • 76
    • 33845600705 scopus 로고    scopus 로고
    • Abnormal small heat shock protein interactions involving neuropathy-associated HSP22 (HSPB8) mutants
    • Fontaine J.-M., Sun X., Hoppe A.D., Simon S., Vicart P., Welsh M.J., Benndorf R. Abnormal small heat shock protein interactions involving neuropathy-associated HSP22 (HSPB8) mutants. FASEB J. 2006, 20:2168-2170.
    • (2006) FASEB J. , vol.20 , pp. 2168-2170
    • Fontaine, J.-M.1    Sun, X.2    Hoppe, A.D.3    Simon, S.4    Vicart, P.5    Welsh, M.J.6    Benndorf, R.7
  • 77
    • 36348957457 scopus 로고    scopus 로고
    • Myopathy-associated αB-crystallin mutants: abnormal phosphorylation, intracellular location, and interactions with other small heat shock proteins
    • Simon S., Fontaine J.-M., Martin J.L., Sun X., Hoppe A.D., Welsh M.J., Benndorf R., Vicart P. Myopathy-associated αB-crystallin mutants: abnormal phosphorylation, intracellular location, and interactions with other small heat shock proteins. J. Biol. Chem. 2007, 282:34276-34287.
    • (2007) J. Biol. Chem. , vol.282 , pp. 34276-34287
    • Simon, S.1    Fontaine, J.-M.2    Martin, J.L.3    Sun, X.4    Hoppe, A.D.5    Welsh, M.J.6    Benndorf, R.7    Vicart, P.8
  • 79
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito R.R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 2000, 10:524-530.
    • (2000) Trends Cell Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 80
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution
    • Stefani M., Dobson C.M. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 2003, 81:678-699.
    • (2003) J. Mol. Med. , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 81
    • 81455138093 scopus 로고    scopus 로고
    • Molecular mechanisms of α-crystallinopathy and its therapeutic strategy
    • Sanbe A. Molecular mechanisms of α-crystallinopathy and its therapeutic strategy. Biol. Pharm. Bull. 2011, 34:1653-1658.
    • (2011) Biol. Pharm. Bull. , vol.34 , pp. 1653-1658
    • Sanbe, A.1
  • 82
    • 84895392709 scopus 로고    scopus 로고
    • The two-faced nature of small heat shock proteins: Amyloid fibril assembly and the inhibition of fibril formation. Relevance to disease states
    • Nova Science Publishers, New York, S. Simon, A.-P. Arrigo (Eds.)
    • Ecroyd H., Meehan S., Carver J.A. The two-faced nature of small heat shock proteins: Amyloid fibril assembly and the inhibition of fibril formation. Relevance to disease states. Small Stress Proteins and Human Diseases 2012, 189-211. Nova Science Publishers, New York. S. Simon, A.-P. Arrigo (Eds.).
    • (2012) Small Stress Proteins and Human Diseases , pp. 189-211
    • Ecroyd, H.1    Meehan, S.2    Carver, J.A.3
  • 83
    • 84857219453 scopus 로고    scopus 로고
    • Protein localization in disease and therapy
    • Hung M.C., Link W. Protein localization in disease and therapy. J. Cell Sci. 2011, 124:3381-3392.
    • (2011) J. Cell Sci. , vol.124 , pp. 3381-3392
    • Hung, M.C.1    Link, W.2
  • 84
    • 84860668972 scopus 로고    scopus 로고
    • Alteration of protein folding and degradation in motor neuron diseases: implications and protective functions of small heat shock proteins
    • Carra S., Crippa V., Rusmini P., Boncoraglio A., Minoia M., Giorgetti E., Kampinga H.H., Poletti A. Alteration of protein folding and degradation in motor neuron diseases: implications and protective functions of small heat shock proteins. Prog. Neurobiol. 2012, 97:83-100.
    • (2012) Prog. Neurobiol. , vol.97 , pp. 83-100
    • Carra, S.1    Crippa, V.2    Rusmini, P.3    Boncoraglio, A.4    Minoia, M.5    Giorgetti, E.6    Kampinga, H.H.7    Poletti, A.8
  • 85
    • 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
    • Ackerley S., James P.A., Kalli A., French S., Davies K.E., 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, 15:347-354.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 347-354
    • Ackerley, S.1    James, P.A.2    Kalli, A.3    French, S.4    Davies, K.E.5    Talbot, K.6
  • 86
    • 36248947271 scopus 로고    scopus 로고
    • Disruption of neurofilament network with aggregation of light neurofilament protein: a common pathway leading to motor neuron degeneration due to Charcot-Marie-Tooth disease-linked mutations in NFL and HSPB1
    • Zhai J., Lin H., Julien J.P., Schlaepfer W.W. Disruption of neurofilament network with aggregation of light neurofilament protein: a common pathway leading to motor neuron degeneration due to Charcot-Marie-Tooth disease-linked mutations in NFL and HSPB1. Hum. Mol. Genet. 2007, 16:3103-3116.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 3103-3116
    • Zhai, J.1    Lin, H.2    Julien, J.P.3    Schlaepfer, W.W.4
  • 87
    • 33644874959 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and apoptosis underlie the pathogenic process in alpha-B-crystallin desmin-related cardiomyopathy
    • Maloyan A., Sanbe A., Osinska H., Westfall M., Robinson D., Imahashi K., Murphy E., Robbins J. Mitochondrial dysfunction and apoptosis underlie the pathogenic process in alpha-B-crystallin desmin-related cardiomyopathy. Circulation 2005, 112:3451-4361.
    • (2005) Circulation , vol.112 , pp. 3451-4361
    • Maloyan, A.1    Sanbe, A.2    Osinska, H.3    Westfall, M.4    Robinson, D.5    Imahashi, K.6    Murphy, E.7    Robbins, J.8
  • 89
    • 5444229769 scopus 로고    scopus 로고
    • Molecular genetics of distal hereditary motor neuropathies
    • Irobi J., De Jonghe P., Timmerman V. Molecular genetics of distal hereditary motor neuropathies. Hum. Mol. Genet. 2004, 13(Suppl. 2):Rl95-R202.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. Rl95-R202
    • Irobi, J.1    De Jonghe, P.2    Timmerman, V.3
  • 90
    • 6944246275 scopus 로고    scopus 로고
    • Charcot-Marie-Tooth disease: an update
    • Shy M.E. Charcot-Marie-Tooth disease: an update. Curr. Opin. Neural. 2004, 17:579-585.
    • (2004) Curr. Opin. Neural. , vol.17 , pp. 579-585
    • Shy, M.E.1
  • 96
    • 35348844114 scopus 로고    scopus 로고
    • Insights into function and regulation of small heat shock protein 25 (HSPB1) in a mouse model with targeted gene disruption
    • Huang L., Min J.N., Masters S., Mivechi N.F., Moskophidis D. Insights into function and regulation of small heat shock protein 25 (HSPB1) in a mouse model with targeted gene disruption. Genesis 2007, 45:487-501.
    • (2007) Genesis , vol.45 , pp. 487-501
    • Huang, L.1    Min, J.N.2    Masters, S.3    Mivechi, N.F.4    Moskophidis, D.5
  • 98
    • 84895379683 scopus 로고    scopus 로고
    • Beneficial and deleterious, the dual role of small stress proteins in human disease: implications for the therapeutic strategies
    • Nova Science Publishers, New York, S. Simon, A.-P. Arrigo (Eds.)
    • Simon S., Arrigo A.-P. Beneficial and deleterious, the dual role of small stress proteins in human disease: implications for the therapeutic strategies. Small Stress Proteins and Human Diseases 2012, 457-476. Nova Science Publishers, New York. S. Simon, A.-P. Arrigo (Eds.).
    • (2012) Small Stress Proteins and Human Diseases , pp. 457-476
    • Simon, S.1    Arrigo, A.-P.2
  • 100
    • 0029120317 scopus 로고
    • Effect of tauroursodeoxycholic and ursodeoxycholic acid on ethanol-induced cell injuries in the human Hep G2 cell line
    • Neuman M.G., Cameron R.G., Shear N.H., Bellentani S., Tiribelli C. Effect of tauroursodeoxycholic and ursodeoxycholic acid on ethanol-induced cell injuries in the human Hep G2 cell line. Gastroenterology 1995, 109:555-563.
    • (1995) Gastroenterology , vol.109 , pp. 555-563
    • Neuman, M.G.1    Cameron, R.G.2    Shear, N.H.3    Bellentani, S.4    Tiribelli, C.5
  • 101
    • 38849146956 scopus 로고    scopus 로고
    • ER and oxidative stresses are common mediators of apoptosis in both neurodegenerative and non-neurodegenerative lysosomal storage disorders and are alleviated by chemical chaperones
    • Wei H., Kim S.J., Zhang Z., Tsai P.C., Wisniewski K.E., Mukherjee A.B. ER and oxidative stresses are common mediators of apoptosis in both neurodegenerative and non-neurodegenerative lysosomal storage disorders and are alleviated by chemical chaperones. Hum. Mol. Genet. 2008, 17:469-477.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 469-477
    • Wei, H.1    Kim, S.J.2    Zhang, Z.3    Tsai, P.C.4    Wisniewski, K.E.5    Mukherjee, A.B.6
  • 106
    • 84882386037 scopus 로고    scopus 로고
    • Heat shock response activation exacerbates inclusion body formation in a cellular model of huntington disease
    • Bersuker K., Hipp M.S., Calamini B., Morimoto R.I., Kopito R.R. Heat shock response activation exacerbates inclusion body formation in a cellular model of huntington disease. J. Biol. Chem. 2013, 288:23633-23638.
    • (2013) J. Biol. Chem. , vol.288 , pp. 23633-23638
    • Bersuker, K.1    Hipp, M.S.2    Calamini, B.3    Morimoto, R.I.4    Kopito, R.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.