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Volumn , Issue , 2011, Pages 301-324

HspB1 and HspB8 mutations in neuropathies

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EID: 84895308310     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (2)

References (100)
  • 1
    • 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. (2006). 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., 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
  • 2
    • 0029043135 scopus 로고
    • Effects of the overexpression of the small heat shock protein, HSP27, on the sensitivity of human fibroblast cells exposed to oxidative stress
    • Arata, S., Hamaguchi, S. & Nose, K. (1995). Effects of the overexpression of the small heat shock protein, HSP27, on the sensitivity of human fibroblast cells exposed to oxidative stress. Cell Physiol., 163, 458-465.
    • (1995) Cell Physiol , vol.163 , pp. 458-465
    • Arata, S.1    Hamaguchi, S.2    Nose, K.3
  • 3
    • 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. (2007). The cellular "networking" of mammalian Hsp27 and its functions in the control of protein folding, redox state and apoptosis. Adv. Exp. Med. Biol., 594, 14-26.
    • (2007) Adv. Exp. Med. Biol. , vol.594 , pp. 14-26
    • Arrigo, A.-P.1
  • 4
    • 0036186869 scopus 로고    scopus 로고
    • Hsp27: novel regulator of intracellular redox state
    • Arrigo, A.-P. (2001). Hsp27: novel regulator of intracellular redox state. IUBMB Life, 52, 303-307.
    • (2001) IUBMB Life , vol.52 , pp. 303-307
    • Arrigo, A.-P.1
  • 8
    • 2642575701 scopus 로고    scopus 로고
    • Shocking Degeneration
    • Benndorf, R. & Welsh, M.J. (2004). Shocking Degeneration. Nat. Genet., 36, 547-548.
    • (2004) Nat. Genet. , vol.36 , pp. 547-548
    • Benndorf, R.1    Welsh, M.J.2
  • 9
    • 42449091462 scopus 로고    scopus 로고
    • Small heat shock proteins Hsp27 or αB-crystallin and the protein components of neurofibrillary tangles: tau and neurofilaments
    • Björkdahl, C., Sjögren, M.J., Zhou, X., Concha, H., Avila, J., Winblad, B. & Pei, J.J. (2008). Small heat shock proteins Hsp27 or αB-crystallin and the protein components of neurofibrillary tangles: tau and neurofilaments. J. Neurosci. Res., 86, 1343-1352.
    • (2008) J. Neurosci. Res. , vol.86 , pp. 1343-1352
    • Björkdahl, C.1    Sjögren, M.J.2    Zhou, X.3    Concha, H.4    Avila, J.5    Winblad, B.6    Pei, J.J.7
  • 11
    • 33845655395 scopus 로고    scopus 로고
    • Recruitment of phosphorylated small heat shock protein Hsp27 to nuclear speckles without stress
    • Bryantsev, A.L., Chechenova, M.B. & Shelden, E.A. (2007). Recruitment of phosphorylated small heat shock protein Hsp27 to nuclear speckles without stress. Exp. Cell Res., 313, 195-209.
    • (2007) Exp. Cell Res. , vol.313 , pp. 195-209
    • Bryantsev, A.L.1    Chechenova, M.B.2    Shelden, E.A.3
  • 12
    • 65549101724 scopus 로고    scopus 로고
    • HSPB8 participates in protein quality control by a non chaperone-like mechanism that requires eIF2α phosphorylation
    • Carra, S., Brunsting, J.F., Lambert, H., Landry, J. & Kampinga, H.H. (2009) HSPB8 participates in protein quality control by a non chaperone-like mechanism that requires eIF2α phosphorylation. J. Biol. Chem., 284, 5523-5532.
    • (2009) J. Biol. Chem. , vol.284 , pp. 5523-5532
    • Carra, S.1    Brunsting, J.F.2    Lambert, H.3    Landry, J.4    Kampinga, H.H.5
  • 13
    • 38349105324 scopus 로고    scopus 로고
    • HspB8 chaperone activity toward poly(Q)-containing proteins depends on its association with Bag3, a stimulator of macroautophagy
    • Carra, S., Seguin, S.J., Lambert, H. & Landry, J. (2008). HspB8 chaperone activity toward poly(Q)-containing proteins depends on its association with Bag3, a stimulator of macroautophagy. J. Biol. Chem., 283, 1437-1444.
    • (2008) J. Biol. Chem. , vol.283 , pp. 1437-1444
    • Carra, S.1    Seguin, S.J.2    Lambert, H.3    Landry, J.4
  • 14
    • 21744448008 scopus 로고    scopus 로고
    • Structural instability caused by a mutation at a conserved arginine in the α-crystallin domain of Chinese hamster heat shock protein 27
    • Chávez-Zobel, A.T., Lambert, H., Thériault, J.R. & Landry, J. (2005). Structural instability caused by a mutation at a conserved arginine in the α-crystallin domain of Chinese hamster heat shock protein 27. Cell Stress Chaperones, 10, 157-166.
    • (2005) Cell Stress Chaperones , vol.10 , pp. 157-166
    • Chávez-Zobel, A.T.1    Lambert, H.2    Thériault, J.R.3    Landry, J.4
  • 15
    • 0038104369 scopus 로고    scopus 로고
    • Distinct chaperone mechanisms can delay the formation of aggresomes by the myopathy-causing R120G αB-crystallin mutant
    • Chávez-Zobel, A.T., Loranger, A., Marceau, N., Thériault, J. R., Lambert H. & Landry, J. (2003). Distinct chaperone mechanisms can delay the formation of aggresomes by the myopathy-causing R120G αB-crystallin mutant. Hum. Mol. Genet., 12, 1609-1620.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1609-1620
    • Chávez-Zobel, A.T.1    Loranger, A.2    Marceau, N.3    Thériault, J.R.4    Lambert, H.5    Landry, J.6
  • 17
    • 3242776825 scopus 로고    scopus 로고
    • Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity
    • Chowdary, T.K., Raman, B., Ramakrishna, T. & Rao, C.M. (2004). Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity. Biochem. J., 381, 379-87.
    • (2004) Biochem. J. , vol.381 , pp. 379-387
    • Chowdary, T.K.1    Raman, B.2    Ramakrishna, T.3    Rao, C.M.4
  • 19
    • 27744461695 scopus 로고    scopus 로고
    • Nuclear import of B-crystallin is phosphorylation-dependent and hampered by hyperphosphorylation of the myopathy-related mutant R120G
    • den Engelsman, J., Gerrits, D., de Jong, W.W., Robbins, J., Kato, K. & Boelens, W.C. (2005). Nuclear import of B-crystallin is phosphorylation-dependent and hampered by hyperphosphorylation of the myopathy-related mutant R120G. J. Biol. Chem., 280, 37139-37148.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37139-37148
    • Den Engelsman, J.1    Gerrits, D.2    de Jong, W.W.3    Robbins, J.4    Kato, K.5    Boelens, W.C.6
  • 22
    • 26944453184 scopus 로고    scopus 로고
    • Small heat shock proteins in inherited peripheral neuropathies
    • Dierick, I., Irobi, J., De Jonghe, P. & Timmerman, V. (2005). Small heat shock proteins in inherited peripheral neuropathies. Ann. Med., 37, 413-422.
    • (2005) Ann. Med. , vol.37 , pp. 413-422
    • Dierick, I.1    Irobi, J.2    De Jonghe, P.3    Timmerman, V.4
  • 26
    • 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. (2006). Abnormal small heat shock protein interactions involving neuropathy-associated HSP22 (HSPB8) mutants. FASEB J., 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
  • 27
    • 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. (2003). The sperm outer dense fiber protein is the 10th member of the superfamily of mammalian small stress proteins. Cell Stress Chaperones, 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
  • 29
    • 3242756684 scopus 로고    scopus 로고
    • Correspondence regarding M.V. Kim et al. "Some properties of human small heat shock protein Hsp22 (H11 or HspB8)"
    • Gober, M.D., Depre, C. & Aurelian L. (2004) Correspondence regarding M.V. Kim et al. "Some properties of human small heat shock protein Hsp22 (H11 or HspB8)". Biochem. Biophys. Res. Commun., 321, 267-268.
    • (2004) Biochem. Biophys. Res. Commun. , vol.321 , pp. 267-268
    • Gober, M.D.1    Depre, C.2    Aurelian, L.3
  • 30
    • 0141844530 scopus 로고    scopus 로고
    • Forced expression of the H11 heat shock protein can be regulated by DNA methylation and trigger apoptosis in human cells
    • Gober, M.D., Smith, C.C., Ueda, K., Toretsky, J.A. & Aurelian L. (2003). Forced expression of the H11 heat shock protein can be regulated by DNA methylation and trigger apoptosis in human cells. J. Biol. Chem., 278, 37600-37609.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37600-37609
    • Gober, M.D.1    Smith, C.C.2    Ueda, K.3    Toretsky, J.A.4    Aurelian, L.5
  • 33
    • 20544446917 scopus 로고    scopus 로고
    • H11 has dose-dependent and dual hypertrophic and proapoptotic functions in cardiac myocytes
    • Hase, M., Depre, C., Vatner, S.F. & Sadoshima, J. (2005). H11 has dose-dependent and dual hypertrophic and proapoptotic functions in cardiac myocytes. Biochem J., 388, 475-483.
    • (2005) Biochem J , vol.388 , pp. 475-483
    • Hase, M.1    Depre, C.2    Vatner, S.F.3    Sadoshima, J.4
  • 34
    • 0033853066 scopus 로고    scopus 로고
    • Small heat shock proteins, the cytoskeleton, and inclusion body formation
    • Head, M. W. & Goldman, J.E. (2000). Small heat shock proteins, the cytoskeleton, and inclusion body formation. Neuropathol. Appl. Neurobiol., 26, 304-312.
    • (2000) Neuropathol. Appl. Neurobiol. , vol.26 , pp. 304-312
    • Head, M.W.1    Goldman, J.E.2
  • 35
  • 36
    • 77957219328 scopus 로고
    • Sequence and organization of genes encoding the human 27 kDa heat shock protein
    • Erratum in: Nucleic Acids Res., 14, 8230 (1986)
    • Hickey, E., Brandon, S.E., Potter, R., Stein, G., Stein, J. & Weber, L.A. (1986). Sequence and organization of genes encoding the human 27 kDa heat shock protein. Nucleic Acids Res. 14, 4127-4145. Erratum in: Nucleic Acids Res., 14, 8230 (1986).
    • (1986) Nucleic Acids Res , vol.14 , pp. 4127-4145
    • Hickey, E.1    Brandon, S.E.2    Potter, R.3    Stein, G.4    Stein, J.5    Weber, L.A.6
  • 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. (2008). Mutations in the HSP27 (HSPB1) gene cause dominant, recessive, and sporadic distal HMN/CMT type 2. Neurology, 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
  • 38
    • 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. (2007). Insights into function and regulation of small heat shock protein 25 (HSPB1) in a mouse model with targeted gene disruption. Genesis, 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
  • 39
    • 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. (2009). A clinical phenotype of distal hereditary motor neuronopathy type II with a novel HSPB1 mutation. J. Neurol. Sci., 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
  • 41
    • 0029004307 scopus 로고
    • Induction of the synthesis of hsp27 and αB-crystallin in tissues of heat-stressed rats and its suppression by ethanol or an alpha 1-adrenergic antagonist
    • Inaguma, Y., Hasegawa, K., Goto, S., Ito, H. & Kato, K. (1995). Induction of the synthesis of hsp27 and αB-crystallin in tissues of heat-stressed rats and its suppression by ethanol or an alpha 1-adrenergic antagonist. J. Biochem (Tokyo), 117, 1238-1243.
    • (1995) J. Biochem (Tokyo) , vol.117 , pp. 1238-1243
    • Inaguma, Y.1    Hasegawa, K.2    Goto, S.3    Ito, H.4    Kato, K.5
  • 43
    • 5444229769 scopus 로고    scopus 로고
    • Molecular genetics of distal hereditary motor neuropathies
    • Irobi, J., De Jonghe, P. & Timmerman, V. (2004). Molecular genetics of distal hereditary motor neuropathies. Hum. Mol. Genet., 13 (Suppl. 2), R195-R202.
    • (2004) Hum. Mol. Genet. , vol.13 , Issue.SUPPL. 2
    • Irobi, J.1    De Jonghe, P.2    Timmerman, V.3
  • 44
    • 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. (2008). Asymmetrical late onset motor neuropathy associated with a novel mutation in the small heat shock protein HSPB1 (HSP27). J. Neurol. Neurosurg. Psychiatry, 79, 461-463.
    • (2008) J. Neurol. Neurosurg. Psychiatry , vol.79 , pp. 461-463
    • James, P.A.1    Rankin, J.2    Talbot, K.3
  • 45
    • 15344340688 scopus 로고    scopus 로고
    • Polymorphisms affecting gene regulation and mRNA processing: broad implications for pharmacogenetics
    • Johnson, A.D., Wang, D. & Sadee, W. (2005). Polymorphisms affecting gene regulation and mRNA processing: broad implications for pharmacogenetics. Pharmacol. Ther., 106, 19-38.
    • (2005) Pharmacol. Ther. , vol.106 , pp. 19-38
    • Johnson, A.D.1    Wang, D.2    Sadee, W.3
  • 47
    • 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. (2007). Effect of mutations in the beta5-beta7 loop on the structure and properties of human small heat shock protein HSP22 (HspB8, H11). FEBS J. 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
  • 48
    • 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. (2005). Small heat shock protein 27 mutation in a Japanese patient with distal hereditary motor neuropathy. J. Hum. Genet., 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
  • 49
    • 33748892808 scopus 로고    scopus 로고
    • Structure and properties of K141E mutant of small heat shock protein HSP22 (HspB8, H11) that is expressed in human neuromuscular disorders
    • Kim, M.V., Kasakov, A.S., Seit-Nebi, A.S., Marston, S.B. & Gusev, N.B. (2006). Structure and properties of K141E mutant of small heat shock protein HSP22 (HspB8, H11) that is expressed in human neuromuscular disorders. Arch. Biochem. Biophys. 454, 32-41.
    • (2006) Arch. Biochem. Biophys. , vol.454 , pp. 32-41
    • Kim, M.V.1    Kasakov, A.S.2    Seit-Nebi, A.S.3    Marston, S.B.4    Gusev, N.B.5
  • 51
    • 8444231226 scopus 로고    scopus 로고
    • The problem of protein kinase activity of small heat shock protein Hsp22 (H11 or HspB8)
    • Kim, M,V, Seit-Nebi, A.S. & Gusev, N.B. (2004). The problem of protein kinase activity of small heat shock protein Hsp22 (H11 or HspB8). Biochem. Biophys. Res. Commun, 325, 649-652.
    • (2004) Biochem. Biophys. Res. Commun , vol.325 , pp. 649-652
    • Kim, M.V.1    Seit-Nebi, A.S.2    Gusev, N.B.3
  • 54
    • 0034077529 scopus 로고    scopus 로고
    • Regulation of cyclooxygenase 2 mRNA stability by the mitogen-activated protein kinase p38 signaling cascade
    • Lasa, M., Mahtani, K.R., Finch, A., Brewer, G., Saklatvala, J. and Clark, A.R. (2000). Regulation of cyclooxygenase 2 mRNA stability by the mitogen-activated protein kinase p38 signaling cascade. Mol. Cell. Biol., 20, 4265-4274.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4265-4274
    • Lasa, M.1    Mahtani, K.R.2    Finch, A.3    Brewer, G.4    Saklatvala, J.5    Clark, A.R.6
  • 55
    • 0036372750 scopus 로고    scopus 로고
    • Protection of neuronal and cardiac cells by HSP27
    • Arrigo, A.-P. & Müller W.E.G. (eds), Springer-Verlag Berlin
    • Latchman, D.S. Protection of neuronal and cardiac cells by HSP27. in: Arrigo, A.-P. & Müller W.E.G. (eds), Small Stress Proteins, Springer-Verlag Berlin. 2002, pp. 253-265.
    • (2002) Small Stress Proteins , pp. 253-265
    • Latchman, D.S.1
  • 58
    • 0033664329 scopus 로고    scopus 로고
    • The distribution of heat shock proteins in the nervous system of the unstressed mouse embryo suggests a role in neuronal and non-neuronal differentiation
    • Loones, M.T., Chang, Y., Morange, M. (2000). The distribution of heat shock proteins in the nervous system of the unstressed mouse embryo suggests a role in neuronal and non-neuronal differentiation. Cell Stress Chaperones, 5, 291-305.
    • (2000) Cell Stress Chaperones , vol.5 , pp. 291-305
    • Loones, M.T.1    Chang, Y.2    Morange, M.3
  • 59
    • 0031795906 scopus 로고    scopus 로고
    • Expression of HSP27 results in increased sensitivity to tumor necrosis factor, etoposide, and H2O2 in an oxidative stress-resistant cell line
    • Mairesse, N., Bernaert, D., Del Bino, G., Horman, S., Mosselmans, R., Robaye, B. & Galand P. (1998). Expression of HSP27 results in increased sensitivity to tumor necrosis factor, etoposide, and H2O2 in an oxidative stress-resistant cell line. J. Cell. Physiol., 177, 606-617.
    • (1998) J. Cell. Physiol. , vol.177 , pp. 606-617
    • Mairesse, N.1    Bernaert, D.2    Del Bino, G.3    Horman, S.4    Mosselmans, R.5    Robaye, B.6    Galand, P.7
  • 61
    • 31944446927 scopus 로고    scopus 로고
    • Hsp27 enhances recovery of splicing as well as rephosphorylation of SRp38 after heat shock
    • Marin-Vinader, L., Shin, C., Onnekink, C., Manley, J.L. & Lubsen, N.H. (2006). Hsp27 enhances recovery of splicing as well as rephosphorylation of SRp38 after heat shock. Mol. Biol. Cell, 17, 886-894.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 886-894
    • Marin-Vinader, L.1    Shin, C.2    Onnekink, C.3    Manley, J.L.4    Lubsen, N.H.5
  • 62
    • 59849129128 scopus 로고    scopus 로고
    • Abnormal assemblies and subunit exchange of αB-crystallin R120 mutants could be associated with destabilization of the dimeric substructure
    • Michiel, M., Skouri-Panet, F., Duprat, E., Simon, S., Férard, C., Tardieu, A. & Finet, S. (2009). Abnormal assemblies and subunit exchange of αB-crystallin R120 mutants could be associated with destabilization of the dimeric substructure. Biochemistry, 48, 442-453.
    • (2009) Biochemistry , vol.48 , pp. 442-453
    • Michiel, M.1    Skouri-Panet, F.2    Duprat, E.3    Simon, S.4    Férard, C.5    Tardieu, A.6    Finet, S.7
  • 63
    • 33745268197 scopus 로고    scopus 로고
    • Pathomechanisms of mutant proteins in Charcot-Marie-Tooth disease
    • Niemann, A., Berger, P. & Suter, U. (2006). Pathomechanisms of mutant proteins in Charcot-Marie-Tooth disease. Neuromolecular Med., 8, 217-242.
    • (2006) Neuromolecular Med , vol.8 , pp. 217-242
    • Niemann, A.1    Berger, P.2    Suter, U.3
  • 64
    • 0020826867 scopus 로고
    • Formation of cytoplasmic heat shock granules in tomato cell cultures and leaves
    • Nover, L., Scharf, K.D. & Neumann, D. (1989). Formation of cytoplasmic heat shock granules in tomato cell cultures and leaves. Mol. Cell. Biol., 3, 1648-1655.
    • (1989) Mol. Cell. Biol. , vol.3 , pp. 1648-1655
    • Nover, L.1    Scharf, K.D.2    Neumann, D.3
  • 67
    • 0000843475 scopus 로고    scopus 로고
    • The cardiomyopathy and lens cataract mutation in αB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro
    • Perng, M.D., Muchowski, P.J., van Den Ijssel, P., Wu, G.J., Hutcheson, A.M., Clark, J.I. & Quinlan, R.A.(1999). The cardiomyopathy and lens cataract mutation in αB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro. J. Biol. Chem., 274, 33235-33243.
    • (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.4    Hutcheson, A.M.5    Clark, J.I.6    Quinlan, R.A.7
  • 69
    • 33745365549 scopus 로고    scopus 로고
    • αB-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. (2006). αB-crystallin mutation in dilated cardiomyopathies: low prevalence in a consecutive series of 200 unrelated probands. Biochem. Biophys. Res. Commun., 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
  • 70
    • 42749092501 scopus 로고    scopus 로고
    • Expression of the small heat shock protein family in the mouse CNS: Differential anatomical and biochemical compartmentalization
    • Quraishe, S., Asuni, A., Boelens, W.C., O'Connor, V. & Wyttenbach, A. (2008). Expression of the small heat shock protein family in the mouse CNS: Differential anatomical and biochemical compartmentalization. Neuroscience, 153, 483-491.
    • (2008) Neuroscience , vol.153 , pp. 483-491
    • Quraishe, S.1    Asuni, A.2    Boelens, W.C.3    O'Connor, V.4    Wyttenbach, A.5
  • 75
    • 0344664368 scopus 로고    scopus 로고
    • Myofibrillar myopathy caused by novel dominant negative αB-crystallin mutations
    • Selcen, D. & Engel, A.G. (2003). Myofibrillar myopathy caused by novel dominant negative αB-crystallin mutations. Ann. Neurol., 54, 804-810.
    • (2003) Ann. Neurol. , vol.54 , pp. 804-810
    • Selcen, D.1    Engel, A.G.2
  • 76
    • 38849180142 scopus 로고    scopus 로고
    • Structure, properties, and functions of the human small heat-shock protein HSP22 (HspB8, H11, E2IG1): a critical review
    • Shemetov, A.A., Seit-Nebi, A.S. &, Gusev, N.B. (2008) Structure, properties, and functions of the human small heat-shock protein HSP22 (HspB8, H11, E2IG1): a critical review. J. Neurosci. Res., 86, 264-269.
    • (2008) J. Neurosci. Res. , vol.86 , pp. 264-269
    • Shemetov, A.A.1    Seit-Nebi, A.S.2    Gusev, N.B.3
  • 77
    • 0037033055 scopus 로고    scopus 로고
    • Cell death inhibiting RNA (CDIR) derived from a 3'-untranslated region binds AUF1 and heat shock protein 27
    • Shchors, K., Yehiely, F. & Deiss, L.P. (2002). Cell death inhibiting RNA (CDIR) derived from a 3'-untranslated region binds AUF1 and heat shock protein 27. J. Biol. Chem., 277, 47061-47072.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47061-47072
    • Shchors, K.1    Yehiely, F.2    Deiss, L.P.3
  • 78
    • 6944246275 scopus 로고    scopus 로고
    • Charcot-Marie-Tooth disease: an update
    • Shy, M.E. (2004). Charcot-Marie-Tooth disease: an update. Curr. Opin. Neurol., 17, 579-585.
    • (2004) Curr. Opin. Neurol. , vol.17 , pp. 579-585
    • Shy, M.E.1
  • 79
    • 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. (2007). Myopathy-associated αB-crystallin mutants: abnormal phosphorylation, intracellular location, and interactions with other small heat shock proteins. J. Biol. Chem., 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
  • 80
    • 0034682806 scopus 로고    scopus 로고
    • A novel gene homologous to PK coding domain of the large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10) codes for a serine-threonine PK and is expressed in melanoma cells
    • Smith, C.C., Yu, Y.X., Kulka, M. & Aurelian, L. (2000). A novel gene homologous to PK coding domain of the large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10) codes for a serine-threonine PK and is expressed in melanoma cells. J. Biol. Chem., 275, 25690-25699.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25690-25699
    • Smith, C.C.1    Yu, Y.X.2    Kulka, M.3    Aurelian, L.4
  • 81
    • 27744592137 scopus 로고    scopus 로고
    • The c-Yes 3'-UTR contains adenine/uridine-rich elements that bind AUF1 and HuR involved in mRNA decay in breast cancer cells
    • Sommer, S., Cui, Y., Brewer, G. & Fuqua, S.A. (2005). The c-Yes 3'-UTR contains adenine/uridine-rich elements that bind AUF1 and HuR involved in mRNA decay in breast cancer cells. J. Steroid. Biochem. Mol. Biol., 97, 219-229.
    • (2005) J. Steroid. Biochem. Mol. Biol. , vol.97 , pp. 219-229
    • Sommer, S.1    Cui, Y.2    Brewer, G.3    Fuqua, S.A.4
  • 82
    • 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. (2003). Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol Med., 81, 678-699.
    • (2003) J. Mol Med. , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 88
    • 2542451125 scopus 로고    scopus 로고
    • Essential role of the NH2-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27
    • Thériault, J.R., Lambert, H., Chávez-Zobel, A.T., Charest, G., Lavigne, P. & Landry, J. (2004). Essential role of the NH2-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27. J. Biol. Chem., 279, 23463-23471.
    • (2004) J. Biol. Chem. , vol.279 , pp. 23463-23471
    • Thériault, J.R.1    Lambert, H.2    Chávez-Zobel, A.T.3    Charest, G.4    Lavigne, P.5    Landry, J.6
  • 89
    • 0043205911 scopus 로고    scopus 로고
    • Nuclear speckle localisation of the small heat shock protein αB-crystallin and its inhibition by the R120G cardiomyopathy-linked mutation
    • van den Ijssel, P., Wheelock, R., Prescott, A., Russell, P. & Quinlan, R.A. (2003). Nuclear speckle localisation of the small heat shock protein αB-crystallin and its inhibition by the R120G cardiomyopathy-linked mutation. Exp. Cell Res., 287, 249-261.
    • (2003) Exp. Cell Res. , vol.287 , pp. 249-261
    • van Den Ijssel, P.1    Wheelock, R.2    Prescott, A.3    Russell, P.4    Quinlan, R.A.5
  • 90
    • 0242407366 scopus 로고    scopus 로고
    • Expression of small heat shock proteins HspB2, HspB8, Hsp20 and cvHsp in different tissues of the perinatal developing pig
    • Verschuure, P., Tatard, C., Boelens, W.C., Grongnet, J.F. & David, J.C. (2003). Expression of small heat shock proteins HspB2, HspB8, Hsp20 and cvHsp in different tissues of the perinatal developing pig. Eur. J. Cell Biol., 82, 523-530.
    • (2003) Eur. J. Cell Biol. , vol.82 , pp. 523-530
    • Verschuure, P.1    Tatard, C.2    Boelens, W.C.3    Grongnet, J.F.4    David, J.C.5
  • 92
    • 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. (2008). Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families. Biochemistry, 47, 7001-7011.
    • (2008) Biochemistry , vol.47 , pp. 7001-7011
    • Vos, M.J.1    Hageman, J.2    Carra, S.3    Kampinga, H.H.4
  • 93
    • 0035816115 scopus 로고    scopus 로고
    • Expression of R120G-αB-crystallin causes aberrant desmin and αB-crystallin aggregation and cardiomyopathy in mice
    • Wang, X., Osinska, H., Klevitsky, R., Gerdes, A.M., Nieman, M., Lorenz, J., Hewett, T. & Robbins, J. (2001). Expression of R120G-αB-crystallin causes aberrant desmin and αB-crystallin aggregation and cardiomyopathy in mice. Circ. Res., 89, 84-91.
    • (2001) Circ. Res. , vol.89 , pp. 84-91
    • Wang, X.1    Osinska, H.2    Klevitsky, R.3    Gerdes, A.M.4    Nieman, M.5    Lorenz, J.6    Hewett, T.7    Robbins, J.8
  • 94
    • 33646857038 scopus 로고    scopus 로고
    • Small heat shock proteins inhibit amyloid-beta protein aggregation and cerebrovascular amyloid-beta protein toxicity
    • Wilhelmus, M.M., Boelens, W.C., Otte-Höller, I., Kamps, B., de Waal, R.M., Verbeek, M.M. (2006). Small heat shock proteins inhibit amyloid-beta protein aggregation and cerebrovascular amyloid-beta protein toxicity. Brain Res., 17, 1089, 67-78.
    • (2006) Brain Res , vol.17 , Issue.1089 , pp. 67-78
    • Wilhelmus, M.M.1    Boelens, W.C.2    Otte-Höller, I.3    Kamps, B.4    de Waal, R.M.5    Verbeek, M.M.6
  • 95
    • 0028014337 scopus 로고
    • The molecular basis of genetic dominance
    • Wilkie, A.O.M. (1994). The molecular basis of genetic dominance. J. Med. Genet., 31, 89-98.
    • (1994) J. Med. Genet. , vol.31 , pp. 89-98
    • Wilkie, A.O.M.1
  • 96
    • 33748560874 scopus 로고    scopus 로고
    • Heat shock protein 27 is involved in neurite extension and branching of dorsal root ganglion neurons in vitro
    • Williams, K.L., Rahimtula, M. & Mearow, K.M. (2006) Heat shock protein 27 is involved in neurite extension and branching of dorsal root ganglion neurons in vitro. J. Neurosci. Res., 84, 716-723.
    • (2006) J. Neurosci. Res. , vol.84 , pp. 716-723
    • Williams, K.L.1    Rahimtula, M.2    Mearow, K.M.3
  • 97
    • 41749089797 scopus 로고    scopus 로고
    • Reprogramming mRNA translation during stress
    • Yamasaki, S. & Anderson, P. (2008). Reprogramming mRNA translation during stress. Curr. Opin. Cell Biol., 20, 222-226.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 222-226
    • Yamasaki, S.1    Anderson, P.2
  • 98
    • 51649098097 scopus 로고    scopus 로고
    • α-crystallin protected axons from optic nerve degeneration after crushing in rats
    • Ying, X., Zhang, J., Wang, Y., Wu, N., Wang, Y. & Yew, D.T. (2008). α-crystallin protected axons from optic nerve degeneration after crushing in rats. J. Mol. Neurosci., 35, 253-258.
    • (2008) J. Mol. Neurosci. , vol.35 , pp. 253-258
    • Ying, X.1    Zhang, J.2    Wang, Y.3    Wu, N.4    Wang, Y.5    Yew, D.T.6
  • 99
    • 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. (2007). 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., 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
  • 100
    • 33745261763 scopus 로고    scopus 로고
    • Molecular genetics of autosomal-dominant axonal Charcot-Marie-Tooth disease
    • Züchner, S. & Vance, J.M. (2006). Molecular genetics of autosomal-dominant axonal Charcot-Marie-Tooth disease. Neuromolecular Med., 8, 63-74.
    • (2006) Neuromolecular Med , vol.8 , pp. 63-74
    • Züchner, S.1    Vance, J.M.2


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