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Volumn 81, Issue 1, 2010, Pages 12-24

Conformational diseases: Looking into the eyes

Author keywords

Age related macula degeneration; Cataract; Lens; Protein aggregation; Retina; Rhodopsin

Indexed keywords

4 PHENYLBUTYRIC ACID; AMYLOID; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN ANTIBODY; ANSAMYCIN DERIVATIVE; BETA SHEET BREAKER; CHAPERONE; CRYSTALLIN; GELDANAMYCIN; LENS PROTEIN; NONSTEROID ANTIINFLAMMATORY AGENT; PRION PROTEIN; PROTEASOME INHIBITOR; RADICICOL; RHODOPSIN; SALICYLATE SODIUM; TANESPIMYCIN; UNCLASSIFIED DRUG;

EID: 71349083669     PISSN: 03619230     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.brainresbull.2009.09.015     Document Type: Review
Times cited : (96)

References (159)
  • 1
    • 0027976996 scopus 로고
    • Increased body temperature accelerates aggregation of the Leu-68-->Gln mutant cystatin C, the amyloid-forming protein in hereditary cystatin C amyloid angiopathy
    • Abrahamson M., and Grubb A. Increased body temperature accelerates aggregation of the Leu-68-->Gln mutant cystatin C, the amyloid-forming protein in hereditary cystatin C amyloid angiopathy. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 1416-1420
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 1416-1420
    • Abrahamson, M.1    Grubb, A.2
  • 2
    • 0345760069 scopus 로고    scopus 로고
    • Characterization of β-amyloid assemblies in druzen: the deposits associated with aging and aged-related macular degeneration
    • Anderson D.H., Talaga K.C., Rivest A.J., Barron E., Hageman G.S., and Johnson L.V. Characterization of β-amyloid assemblies in druzen: the deposits associated with aging and aged-related macular degeneration. Exp. Eye Res. 78 (2004) 243-256
    • (2004) Exp. Eye Res. , vol.78 , pp. 243-256
    • Anderson, D.H.1    Talaga, K.C.2    Rivest, A.J.3    Barron, E.4    Hageman, G.S.5    Johnson, L.V.6
  • 3
    • 0015361994 scopus 로고
    • The formation and stabilization of protein structure. The sixth jubilee lecture
    • Anfinsen C.B. The formation and stabilization of protein structure. The sixth jubilee lecture. Biochem. J. 128 (1972) 737-749
    • (1972) Biochem. J. , vol.128 , pp. 737-749
    • Anfinsen, C.B.1
  • 4
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen C.B. Principles that govern the folding of protein chains. Science 181 (1973) 223-230
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 6
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • Balch W.E., Morimoto R.I., Dillin A., and Kelly J.W. Adapting proteostasis for disease intervention. Science 319 (2008) 916-919
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 7
    • 1042288284 scopus 로고    scopus 로고
    • Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on beta-structure in the core domain
    • Barghorn S., Davies P., and Mandelkow E. Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on beta-structure in the core domain. Biochemistry 43 (2004) 1694-1703
    • (2004) Biochemistry , vol.43 , pp. 1694-1703
    • Barghorn, S.1    Davies, P.2    Mandelkow, E.3
  • 8
    • 0346093906 scopus 로고    scopus 로고
    • Isolated vitreoretinal amyloidosis in the absence of transthyretin mutations
    • Barouch F.C., Benson M.D., and Mukai S. Isolated vitreoretinal amyloidosis in the absence of transthyretin mutations. Arch. Ophthalmol. 122 (2004) 123-125
    • (2004) Arch. Ophthalmol. , vol.122 , pp. 123-125
    • Barouch, F.C.1    Benson, M.D.2    Mukai, S.3
  • 10
    • 0348240034 scopus 로고    scopus 로고
    • Vitreous amyloidosis
    • Albert D.M., and Jakobiec F.A. (Eds), WB Saunders, Philadelphia, PA
    • Bhisitkul R.B., and Mukai S. Vitreous amyloidosis. In: Albert D.M., and Jakobiec F.A. (Eds). Principles and Practice of Ophthalmology. 2nd ed. (2000), WB Saunders, Philadelphia, PA 2530-2539
    • (2000) Principles and Practice of Ophthalmology. 2nd ed. , pp. 2530-2539
    • Bhisitkul, R.B.1    Mukai, S.2
  • 12
    • 59549086901 scopus 로고    scopus 로고
    • A dominant vimentin mutant upregulates Hsp70 and the activity of the ubiquitin-proteasome system, and causes posterior cataracts in transgenic mice
    • Bornheim R., Müller M., Reuter U., Herrmann H., Büssow H., and Magin T.M. A dominant vimentin mutant upregulates Hsp70 and the activity of the ubiquitin-proteasome system, and causes posterior cataracts in transgenic mice. J. Cell Sci. 121 (2008) 3737-3746
    • (2008) J. Cell Sci. , vol.121 , pp. 3737-3746
    • Bornheim, R.1    Müller, M.2    Reuter, U.3    Herrmann, H.4    Büssow, H.5    Magin, T.M.6
  • 13
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau B., Weissman J., and Horwich A. Molecular chaperones and protein quality control. Cell 125 (2006) 443-451
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 14
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • Carrell R.W., and Lomas D.A. Conformational disease. Lancet 350 (1997) 134-138
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 15
    • 0038819926 scopus 로고    scopus 로고
    • The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation
    • Chapple J.P., and Cheetham M.E. The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation. J. Biol. Chem. 278 (2003) 19087-19094
    • (2003) J. Biol. Chem. , vol.278 , pp. 19087-19094
    • Chapple, J.P.1    Cheetham, M.E.2
  • 18
    • 0031464278 scopus 로고    scopus 로고
    • Molecular evidence for the involvement of alpha crystallin in the coloration/crosslinking of crystallins in age related nuclear cataract
    • Chen Y.C., Reid G.E., Simpson R.J., and Truscott R.J. Molecular evidence for the involvement of alpha crystallin in the coloration/crosslinking of crystallins in age related nuclear cataract. Exp. Eye Res. 65 (1997) 835-840
    • (1997) Exp. Eye Res. , vol.65 , pp. 835-840
    • Chen, Y.C.1    Reid, G.E.2    Simpson, R.J.3    Truscott, R.J.4
  • 19
    • 30344461634 scopus 로고    scopus 로고
    • Scrapie pathogenesis in brain and retina: effects of prion protein expression in neurons and astrocytes
    • Chesebro B., Race R., and Kercher L. Scrapie pathogenesis in brain and retina: effects of prion protein expression in neurons and astrocytes. J. Neurovirol. 11 (2005) 476-480
    • (2005) J. Neurovirol. , vol.11 , pp. 476-480
    • Chesebro, B.1    Race, R.2    Kercher, L.3
  • 20
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F., and Dobson C.M. Protein misfolding, functional amyloid, and human disease. Ann. Rev. Biochem. 75 (2006) 333-366
    • (2006) Ann. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 21
    • 0346670134 scopus 로고    scopus 로고
    • A model of FAS1 domain 4 of the corneal protein βig-h3 gives a clearer view on corneal dystrophies
    • Clout N.J., and Hohenester E. A model of FAS1 domain 4 of the corneal protein βig-h3 gives a clearer view on corneal dystrophies. Mol. Vis. 9 (2003) 440-448
    • (2003) Mol. Vis. , vol.9 , pp. 440-448
    • Clout, N.J.1    Hohenester, E.2
  • 23
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of α-synuclein secondary structure upon binding to synthetic membranes
    • Davidson W.S., Jonas A., Clayton D.F., and George J.M. Stabilization of α-synuclein secondary structure upon binding to synthetic membranes. J. Biol. Chem. 273 (1998) 9443-9449
    • (1998) J. Biol. Chem. , vol.273 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 24
    • 1842482905 scopus 로고    scopus 로고
    • Pharmaceutical strategies against amyloidosis: old and new drugs in targeting a protein misfolding disease
    • DeLorenzi E., Giorgetti S., Grossi S., Merlini G., Caccialanza G., and Belotti V. Pharmaceutical strategies against amyloidosis: old and new drugs in targeting a protein misfolding disease. Curr. Med. Chem. 204 (2004) 1065-1084
    • (2004) Curr. Med. Chem. , vol.204 , pp. 1065-1084
    • DeLorenzi, E.1    Giorgetti, S.2    Grossi, S.3    Merlini, G.4    Caccialanza, G.5    Belotti, V.6
  • 25
    • 0037096983 scopus 로고    scopus 로고
    • Effects of modifications of α-crystallin on its chaperone and other properties
    • Derham B.K., and Harding J.J. Effects of modifications of α-crystallin on its chaperone and other properties. Biochem. J. 364 (2002) 711-717
    • (2002) Biochem. J. , vol.364 , pp. 711-717
    • Derham, B.K.1    Harding, J.J.2
  • 26
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill K.A., and Chan H.S. From Levinthal to pathways to funnels. Nat. Struct. Biol. 4 (1997) 10-19
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 27
    • 38749112528 scopus 로고    scopus 로고
    • Targeting age-related macular degeneration with AD based immunotherapies: anti-amyloid-β antibody attenuates pathologies in an age-related macular degeneration mouse model
    • Ding J., Lin J., Mace B.E., Herrmann R., Sullivan P., and Rickman C.B. Targeting age-related macular degeneration with AD based immunotherapies: anti-amyloid-β antibody attenuates pathologies in an age-related macular degeneration mouse model. Vision Res. 48 (2008) 339-345
    • (2008) Vision Res. , vol.48 , pp. 339-345
    • Ding, J.1    Lin, J.2    Mace, B.E.3    Herrmann, R.4    Sullivan, P.5    Rickman, C.B.6
  • 28
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson C.M. Protein misfolding, evolution and disease. TIBS 24 (1999) 329-332
    • (1999) TIBS , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 29
    • 0035961329 scopus 로고    scopus 로고
    • The structural basis of protein folding and its links with human disease
    • Dobson C.M. The structural basis of protein folding and its links with human disease. Philos. Trans. R. Soc. Lond. B: Biol. Sci. 356 (2001) 133-145
    • (2001) Philos. Trans. R. Soc. Lond. B: Biol. Sci. , vol.356 , pp. 133-145
    • Dobson, C.M.1
  • 30
    • 0037102362 scopus 로고    scopus 로고
    • Protein-misfolding diseases: getting out of shape
    • Dobson C.M. Protein-misfolding diseases: getting out of shape. Nature 418 (2002) 729-730
    • (2002) Nature , vol.418 , pp. 729-730
    • Dobson, C.M.1
  • 31
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson C.M. Protein folding and misfolding. Nature 426 (2003) 884-890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 32
    • 71349087420 scopus 로고    scopus 로고
    • The generic nature of protein folding and misfolding
    • Atassi M.Z. (Ed), Springer
    • Dobson C.M. The generic nature of protein folding and misfolding. In: Atassi M.Z. (Ed). Protein Reviews (2006), Springer 21-41
    • (2006) Protein Reviews , pp. 21-41
    • Dobson, C.M.1
  • 36
    • 58149506229 scopus 로고    scopus 로고
    • Crystallin proteins and amyloid fibrils
    • Ecroyd H., and Carver J.A. Crystallin proteins and amyloid fibrils. Cell. Mol. Life Sci. 66 (2009) 62-81
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 62-81
    • Ecroyd, H.1    Carver, J.A.2
  • 37
    • 0035846548 scopus 로고    scopus 로고
    • Molecular chaperones: inside and outside the Anfinsen cage
    • Ellis R.J. Molecular chaperones: inside and outside the Anfinsen cage. Curr. Biol. 11 (2001) R1038-R1040
    • (2001) Curr. Biol. , vol.11
    • Ellis, R.J.1
  • 38
    • 0035253217 scopus 로고    scopus 로고
    • Macromolecular crowding: an important but neglected aspect of the intracellular environment
    • Ellis R.J. Macromolecular crowding: an important but neglected aspect of the intracellular environment. Curr. Opin. Struct. Biol. 11 (2001) 114-119
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 114-119
    • Ellis, R.J.1
  • 39
    • 0041822089 scopus 로고    scopus 로고
    • Join the crowd
    • Ellis R.J., and Minton A.P. Join the crowd. Nature 425 (2003) 27-28
    • (2003) Nature , vol.425 , pp. 27-28
    • Ellis, R.J.1    Minton, A.P.2
  • 40
    • 33947535828 scopus 로고    scopus 로고
    • Mechanisms involved in the protection of UV-induced protein inactivation by the corneal crystallin ALDH3A1
    • Estey T., Cantore M., Weston P.A., Carpenter J.F., Petrash J.M., and Vasiliou V. Mechanisms involved in the protection of UV-induced protein inactivation by the corneal crystallin ALDH3A1. J. Biol. Chem. 282 (2007) 4382-4392
    • (2007) J. Biol. Chem. , vol.282 , pp. 4382-4392
    • Estey, T.1    Cantore, M.2    Weston, P.A.3    Carpenter, J.F.4    Petrash, J.M.5    Vasiliou, V.6
  • 41
    • 68549104191 scopus 로고    scopus 로고
    • Nanotechnologies and controlled release systems for the delivery of antisense oligonucleotides and small interfering RNA
    • Fattal E., and Barratt G. Nanotechnologies and controlled release systems for the delivery of antisense oligonucleotides and small interfering RNA. Br. J. Pharmacol. 157 (2009) 179-194
    • (2009) Br. J. Pharmacol. , vol.157 , pp. 179-194
    • Fattal, E.1    Barratt, G.2
  • 42
    • 0034704752 scopus 로고    scopus 로고
    • A Drosophila model of Parkinson's disease
    • Feany M.B., and Bender W.W. A Drosophila model of Parkinson's disease. Nature 404 (2000) 394-398
    • (2000) Nature , vol.404 , pp. 394-398
    • Feany, M.B.1    Bender, W.W.2
  • 43
    • 0028889120 scopus 로고
    • Contribution of cotranslational folding to the rate of formation of native protein structure
    • Fedorov N., and Baldwin T.O. Contribution of cotranslational folding to the rate of formation of native protein structure. Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 1227-1231
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 1227-1231
    • Fedorov, N.1    Baldwin, T.O.2
  • 45
    • 34548812551 scopus 로고    scopus 로고
    • The role of amyloid beta peptide 42 in Alzheimer's disease
    • Findeis M.A. The role of amyloid beta peptide 42 in Alzheimer's disease. Pharmacol. Ther. 116 (2007) 266-286
    • (2007) Pharmacol. Ther. , vol.116 , pp. 266-286
    • Findeis, M.A.1
  • 47
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins
    • Fink A.L. Natively unfolded proteins. Curr. Opin. Struct. Biol. 15 (2005) 35-41
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 35-41
    • Fink, A.L.1
  • 48
    • 33749841522 scopus 로고    scopus 로고
    • The aggregation and fibrillation of alpha-synuclein
    • Fink A.L. The aggregation and fibrillation of alpha-synuclein. Acc. Chem. Res. 39 (2006) 628-634
    • (2006) Acc. Chem. Res. , vol.39 , pp. 628-634
    • Fink, A.L.1
  • 49
    • 14144250992 scopus 로고    scopus 로고
    • Contributions of hydrophobic domain interface interactions to the folding and stability of human gammaD-crystallin
    • Flaugh S.L., Kosinski-Collins M.S., and King J. Contributions of hydrophobic domain interface interactions to the folding and stability of human gammaD-crystallin. Protein Sci. 14 (2005) 569-581
    • (2005) Protein Sci. , vol.14 , pp. 569-581
    • Flaugh, S.L.1    Kosinski-Collins, M.S.2    King, J.3
  • 51
    • 65649111138 scopus 로고    scopus 로고
    • Liquid nitrogen cryotherapy for conjunctival amyloidosis
    • Fraunfelder F.W. Liquid nitrogen cryotherapy for conjunctival amyloidosis. Arch. Ophalmol. 127 (2009) 645-648
    • (2009) Arch. Ophalmol. , vol.127 , pp. 645-648
    • Fraunfelder, F.W.1
  • 52
    • 0029985732 scopus 로고    scopus 로고
    • Oxidative stress increases production of beta-amyloid precursor protein and beta-amyloid (Abeta) in mammalian lenses, and Abeta has toxic effects on lens epithelial cells
    • Frederikse P.H., Garland D., Zigler Jr. J.S., and Piatigorsky J. Oxidative stress increases production of beta-amyloid precursor protein and beta-amyloid (Abeta) in mammalian lenses, and Abeta has toxic effects on lens epithelial cells. J. Biol. Chem. 271 (1996) 10169-10174
    • (1996) J. Biol. Chem. , vol.271 , pp. 10169-10174
    • Frederikse, P.H.1    Garland, D.2    Zigler Jr., J.S.3    Piatigorsky, J.4
  • 54
    • 54449101793 scopus 로고    scopus 로고
    • Heat shock transcription factor 1-activating compounds suppress polyglutamine-induced neurodegeneration through induction of multiple molecular chaperones
    • Fujikake N., Nagai Y., Popiel H.A., Okamoto Y., Yamaguchi M., and Toda T. Heat shock transcription factor 1-activating compounds suppress polyglutamine-induced neurodegeneration through induction of multiple molecular chaperones. J. Biol. Chem. 283 (2008) 26188-26197
    • (2008) J. Biol. Chem. , vol.283 , pp. 26188-26197
    • Fujikake, N.1    Nagai, Y.2    Popiel, H.A.3    Okamoto, Y.4    Yamaguchi, M.5    Toda, T.6
  • 56
    • 0035504258 scopus 로고    scopus 로고
    • Unfolding and refolding of a quinone oxidoreductase: α-crystallin, a molecular chaperone, assists its reactivation
    • Goenka S., Raman B., Ramakrishna T., and Rao C.M. Unfolding and refolding of a quinone oxidoreductase: α-crystallin, a molecular chaperone, assists its reactivation. Biochem. J. 359 (2001) 547-556
    • (2001) Biochem. J. , vol.359 , pp. 547-556
    • Goenka, S.1    Raman, B.2    Ramakrishna, T.3    Rao, C.M.4
  • 57
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg A.L. Protein degradation and protection against misfolded or damaged proteins. Nature 426 (2003) 895-899
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 59
    • 0032941652 scopus 로고    scopus 로고
    • Cataract mutations and lens development
    • Graw J. Cataract mutations and lens development. Prog. Retin. Eye Res. 18 (1999) 235-267
    • (1999) Prog. Retin. Eye Res. , vol.18 , pp. 235-267
    • Graw, J.1
  • 60
    • 11144298645 scopus 로고    scopus 로고
    • Congenital hereditary cataracts
    • Graw J. Congenital hereditary cataracts. Int. J. Dev. Biol. 48 (2004) 1031-1044
    • (2004) Int. J. Dev. Biol. , vol.48 , pp. 1031-1044
    • Graw, J.1
  • 61
    • 61849122908 scopus 로고    scopus 로고
    • Genetics of crystallins: cataract and beyond
    • Graw J. Genetics of crystallins: cataract and beyond. Exp. Eye Res. 88 (2009) 173-189
    • (2009) Exp. Eye Res. , vol.88 , pp. 173-189
    • Graw, J.1
  • 62
    • 33748593902 scopus 로고    scopus 로고
    • Abnormal prion accumulation associated with retinal pathology in experimentally inoculated scrapie-affected sheep
    • Greenlee J.J., Hamir A.N., and West Greenlee M.H. Abnormal prion accumulation associated with retinal pathology in experimentally inoculated scrapie-affected sheep. Vet. Pathol. 43 (2006) 733-739
    • (2006) Vet. Pathol. , vol.43 , pp. 733-739
    • Greenlee, J.J.1    Hamir, A.N.2    West Greenlee, M.H.3
  • 66
    • 0015376691 scopus 로고
    • Conformational changes in human lens proteins in cataract
    • Harding J.J. Conformational changes in human lens proteins in cataract. Biochem. J. 129 (1972) 97-100
    • (1972) Biochem. J. , vol.129 , pp. 97-100
    • Harding, J.J.1
  • 67
    • 0036597985 scopus 로고    scopus 로고
    • Viewing molecular mechanisms of ageing through a lens
    • Harding J.J. Viewing molecular mechanisms of ageing through a lens. Ageing Res. Rev. 1 (2002) 465-479
    • (2002) Ageing Res. Rev. , vol.1 , pp. 465-479
    • Harding, J.J.1
  • 69
    • 0035823499 scopus 로고    scopus 로고
    • The molecular chaperone α-crystallin, inhibits amyloid formation by apolipoprotein C-II
    • Hatters D.M., Lindner R.A., Carver J.A., and Howlett G.J. The molecular chaperone α-crystallin, inhibits amyloid formation by apolipoprotein C-II. J. Biol. Chem. 276 (2001) 33755-33761
    • (2001) J. Biol. Chem. , vol.276 , pp. 33755-33761
    • Hatters, D.M.1    Lindner, R.A.2    Carver, J.A.3    Howlett, G.J.4
  • 71
    • 24044500298 scopus 로고    scopus 로고
    • Abnormal prion protein in the retina of the most commonly occurring subtype of sporadic Creutzfeldt-Jakob disease
    • Head M.W., Peden A.H., Yull H.M., Ritchie D.L., Bonshek R.E., Tullo A.B., and Ironside J.W. Abnormal prion protein in the retina of the most commonly occurring subtype of sporadic Creutzfeldt-Jakob disease. Br. J. Ophthalmol. 89 (2005) 1131-1133
    • (2005) Br. J. Ophthalmol. , vol.89 , pp. 1131-1133
    • Head, M.W.1    Peden, A.H.2    Yull, H.M.3    Ritchie, D.L.4    Bonshek, R.E.5    Tullo, A.B.6    Ironside, J.W.7
  • 72
    • 0019351880 scopus 로고
    • Progressive retinal degeneration in scrapie-infected hamsters: a light and electron microscopic analysis
    • Hogan R.N., Baringer J.R., and Prusiner S.B. Progressive retinal degeneration in scrapie-infected hamsters: a light and electron microscopic analysis. Lab. Invest. 44 (1981) 34-42
    • (1981) Lab. Invest. , vol.44 , pp. 34-42
    • Hogan, R.N.1    Baringer, J.R.2    Prusiner, S.B.3
  • 73
    • 52149087029 scopus 로고    scopus 로고
    • Identification and localization of α-synuclein in human cornea
    • Hong S., Lee H.K., Kim C.Y., and Seong G.J. Identification and localization of α-synuclein in human cornea. Korean J. Ophthalmol. 22 (2008) 145-146
    • (2008) Korean J. Ophthalmol. , vol.22 , pp. 145-146
    • Hong, S.1    Lee, H.K.2    Kim, C.Y.3    Seong, G.J.4
  • 74
    • 48649101750 scopus 로고    scopus 로고
    • Suppression of keratoepithelin and myocilin by small interfering RNA
    • Huang A.J.W. Suppression of keratoepithelin and myocilin by small interfering RNA. Trans. Am. Ophthalmol. Soc. 105 (2007) 365-378
    • (2007) Trans. Am. Ophthalmol. Soc. , vol.105 , pp. 365-378
    • Huang, A.J.W.1
  • 75
    • 0028305304 scopus 로고
    • A role for destabilizing amino acid replacements in light-chain amyloidosis
    • Hurle M.R., Helms L.R., Li L., Chan W., and Wetzel R. A role for destabilizing amino acid replacements in light-chain amyloidosis. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 5446-5450
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 5446-5450
    • Hurle, M.R.1    Helms, L.R.2    Li, L.3    Chan, W.4    Wetzel, R.5
  • 76
    • 0037072934 scopus 로고    scopus 로고
    • A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system
    • Illing M.E., Rajan R.S., Bence N.F., and Kopito R.R. A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system. J. Biol. Chem. 277 (2002) 34150-34160
    • (2002) J. Biol. Chem. , vol.277 , pp. 34150-34160
    • Illing, M.E.1    Rajan, R.S.2    Bence, N.F.3    Kopito, R.R.4
  • 78
    • 0035167113 scopus 로고    scopus 로고
    • Lens crystallins and their microbial homologs: structure, stability and function
    • Jaenicke R., and Slingsby C. Lens crystallins and their microbial homologs: structure, stability and function. Crit. Rev. Biochem. Mol. Biol. 36 (2001) 435-499
    • (2001) Crit. Rev. Biochem. Mol. Biol. , vol.36 , pp. 435-499
    • Jaenicke, R.1    Slingsby, C.2
  • 79
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: a cellular response to misfolded proteins
    • Johnston J.A., Ward C.L., and Kopito R.R. Aggresomes: a cellular response to misfolded proteins. J. Cell Biol. 143 (1998) 1883-1898
    • (1998) J. Cell Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 80
    • 65249160170 scopus 로고    scopus 로고
    • The structure of the cataract-causing P23T mutant of human gammaD-crystallin exhibits distinctive local conformational and dynamic changes
    • Jung J., Byeon I.J., Wang Y., King J., and Gronenborn A.M. The structure of the cataract-causing P23T mutant of human gammaD-crystallin exhibits distinctive local conformational and dynamic changes. Biochemistry 48 (2009) 2597-2609
    • (2009) Biochemistry , vol.48 , pp. 2597-2609
    • Jung, J.1    Byeon, I.J.2    Wang, Y.3    King, J.4    Gronenborn, A.M.5
  • 81
    • 4043144280 scopus 로고    scopus 로고
    • Proteomic analysis of the soluble fraction from human corneal fibroblasts with reference to ocular transparency
    • Karring H., Thøgersen I.B., Klintworth G.K., Enghild J.J., and Møller-Pedersen T. Proteomic analysis of the soluble fraction from human corneal fibroblasts with reference to ocular transparency. Mol. Cell. Proteomics 3 (2004) 660-674
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 660-674
    • Karring, H.1    Thøgersen, I.B.2    Klintworth, G.K.3    Enghild, J.J.4    Møller-Pedersen, T.5
  • 82
    • 0028287273 scopus 로고
    • Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmentosa
    • Kaushal S., and Khorana H.G. Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmentosa. Biochemistry 33 (1994) 6121-6128
    • (1994) Biochemistry , vol.33 , pp. 6121-6128
    • Kaushal, S.1    Khorana, H.G.2
  • 83
    • 12244256129 scopus 로고    scopus 로고
    • A case of vitreous amyloidosis without systemic symptoms in familial amyloidotic polyneuropathy
    • Kawaji T., Ando Y., Ando E., Nakamura M., Hirata A., and Tanihara H.H. A case of vitreous amyloidosis without systemic symptoms in familial amyloidotic polyneuropathy. Amyloid 11 (2004) 257-259
    • (2004) Amyloid , vol.11 , pp. 257-259
    • Kawaji, T.1    Ando, Y.2    Ando, E.3    Nakamura, M.4    Hirata, A.5    Tanihara, H.H.6
  • 84
    • 0033106510 scopus 로고    scopus 로고
    • Amyloid and Pro501 Thr-mutated (beta)ig-h3 gene product colocalize in lattice corneal dystrophy type III
    • Kawasaki S., Nishida K., Quantock A.J., Dota A., Bennett K., and Kinoshita S. Amyloid and Pro501 Thr-mutated (beta)ig-h3 gene product colocalize in lattice corneal dystrophy type III. Am. J. Ophthalmol. 127 (1999) 456-458
    • (1999) Am. J. Ophthalmol. , vol.127 , pp. 456-458
    • Kawasaki, S.1    Nishida, K.2    Quantock, A.J.3    Dota, A.4    Bennett, K.5    Kinoshita, S.6
  • 85
    • 36348929457 scopus 로고    scopus 로고
    • Orally administered amyloidophilic compound is effective in prolonging the incubation periods of animals cerebrally infected with prion diseases in a prion strain-dependent manner
    • Kawasaki Y., Kawagoe K., Chen C., Teruya K., Sakasegawa Y., and Doh-ura K. Orally administered amyloidophilic compound is effective in prolonging the incubation periods of animals cerebrally infected with prion diseases in a prion strain-dependent manner. J. Virol. 81 (2007) 12889-12898
    • (2007) J. Virol. , vol.81 , pp. 12889-12898
    • Kawasaki, Y.1    Kawagoe, K.2    Chen, C.3    Teruya, K.4    Sakasegawa, Y.5    Doh-ura, K.6
  • 86
    • 34648834051 scopus 로고    scopus 로고
    • Prion protein expression differences in microglia and astroglia influence scrapie-induced neurodegeneration in the retina and brain of transgenic mice
    • Kercher L., Favara C., Striebel J.F., LaCasse R., and Chesebro B. Prion protein expression differences in microglia and astroglia influence scrapie-induced neurodegeneration in the retina and brain of transgenic mice. J. Virol. 81 (2007) 10340-10351
    • (2007) J. Virol. , vol.81 , pp. 10340-10351
    • Kercher, L.1    Favara, C.2    Striebel, J.F.3    LaCasse, R.4    Chesebro, B.5
  • 87
    • 0028053692 scopus 로고
    • Ocular amyloid deposition in familial amyloidosis finnish: an analysis of native and variant gelsolin in Meretoja's syndrome
    • Kivelä T., Tarkkanen A., Frangione B., Ghiso J., and Haltia M. Ocular amyloid deposition in familial amyloidosis finnish: an analysis of native and variant gelsolin in Meretoja's syndrome. Invest. Ophthalmol. Vis. Sci. 35 (1994) 3759-3769
    • (1994) Invest. Ophthalmol. Vis. Sci. , vol.35 , pp. 3759-3769
    • Kivelä, T.1    Tarkkanen, A.2    Frangione, B.3    Ghiso, J.4    Haltia, M.5
  • 88
    • 68149124522 scopus 로고    scopus 로고
    • Chaperone-like antibodies in neurodegenerative tauopathies: implication for immunotherapy
    • Kontsekova E., Ivanovova N., Handzusova M., and Novak M. Chaperone-like antibodies in neurodegenerative tauopathies: implication for immunotherapy. Cell. Mol. Neurobiol. 29 (2009) 793-798
    • (2009) Cell. Mol. Neurobiol. , vol.29 , pp. 793-798
    • Kontsekova, E.1    Ivanovova, N.2    Handzusova, M.3    Novak, M.4
  • 89
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito R.R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell. Biol. 10 (2000) 524-530
    • (2000) Trends Cell. Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 93
    • 0037372175 scopus 로고    scopus 로고
    • In vitro unfolding, refolding, and polymerization of human γD crystallin, a protein involved in cataract formation
    • Kosinski-Collins M.S., and King J. In vitro unfolding, refolding, and polymerization of human γD crystallin, a protein involved in cataract formation. Protein Sci. 12 (2003) 12480-12490
    • (2003) Protein Sci. , vol.12 , pp. 12480-12490
    • Kosinski-Collins, M.S.1    King, J.2
  • 94
    • 0026047846 scopus 로고
    • Nonuniform size distribution of nascent globin peptides, evidence for pause localization sites, and a cotranslational protein-folding model
    • Krasheninnikov I.A., Komar A.A., and Adzhubei I.A. Nonuniform size distribution of nascent globin peptides, evidence for pause localization sites, and a cotranslational protein-folding model. J. Protein Chem. 10 (1991) 445-453
    • (1991) J. Protein Chem. , vol.10 , pp. 445-453
    • Krasheninnikov, I.A.1    Komar, A.A.2    Adzhubei, I.A.3
  • 96
    • 69949084211 scopus 로고    scopus 로고
    • Protein aggregation as a paradigm of ageing
    • 10.1016/j.bbagen.2009.06.005
    • Lindner A.B., and Demarez A. Protein aggregation as a paradigm of ageing. Biochim. Biophys. Acta (2009) 10.1016/j.bbagen.2009.06.005
    • (2009) Biochim. Biophys. Acta
    • Lindner, A.B.1    Demarez, A.2
  • 97
    • 32444450909 scopus 로고    scopus 로고
    • Drusen deposits associated with aging and age-related macular degeneration contain nonfibrillar amyloid oligomers
    • Luibl V., Isas J.M., Kayed R., Glabe C.G., Langen R., and Chen J. Drusen deposits associated with aging and age-related macular degeneration contain nonfibrillar amyloid oligomers. J. Clin. Invest. 116 (2006) 378-385
    • (2006) J. Clin. Invest. , vol.116 , pp. 378-385
    • Luibl, V.1    Isas, J.M.2    Kayed, R.3    Glabe, C.G.4    Langen, R.5    Chen, J.6
  • 98
    • 2942718944 scopus 로고    scopus 로고
    • Reversal of mutant myocilin non-secretion and cell killing: implications for glaucoma
    • Liu Y., and Vollrath D. Reversal of mutant myocilin non-secretion and cell killing: implications for glaucoma. Hum. Mol. Genet. 13 (2004) 1193-1204
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1193-1204
    • Liu, Y.1    Vollrath, D.2
  • 100
    • 0028839438 scopus 로고
    • Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease
    • McCutchen S.L., Lai Z., Miroi G.J., Kelly J.W., and Colon W. Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease. Biochemistry 34 (1995) 13527-13536
    • (1995) Biochemistry , vol.34 , pp. 13527-13536
    • McCutchen, S.L.1    Lai, Z.2    Miroi, G.J.3    Kelly, J.W.4    Colon, W.5
  • 102
    • 0942276377 scopus 로고    scopus 로고
    • Amyloid fibril formation by lens crystallin proteins and its implications for cataract formation
    • Meehan S., Berry Y., Luisi B., Dobson C.M., Carver J.A., and MacPhee C.E. Amyloid fibril formation by lens crystallin proteins and its implications for cataract formation. J. Biol. Chem. 279 (2004) 3413-3419
    • (2004) J. Biol. Chem. , vol.279 , pp. 3413-3419
    • Meehan, S.1    Berry, Y.2    Luisi, B.3    Dobson, C.M.4    Carver, J.A.5    MacPhee, C.E.6
  • 103
    • 17044363529 scopus 로고    scopus 로고
    • Mechanisms of cell death in rhodopsin retinitis pigmentosa: implications for therapy
    • Mendes H.F., van der Spuy J., Chapple J.P., and Cheetham M.E. Mechanisms of cell death in rhodopsin retinitis pigmentosa: implications for therapy. Trends Mol. Med. 11 (2005) 177-185
    • (2005) Trends Mol. Med. , vol.11 , pp. 177-185
    • Mendes, H.F.1    van der Spuy, J.2    Chapple, J.P.3    Cheetham, M.E.4
  • 104
    • 0023657520 scopus 로고
    • Quasi-irreversibility in the unfolding-refolding transition of phosphoglycerate kinase induced by guanidine hydrochloride
    • Mitraki A., Betton J.M., Desmadril M., and Yon J.M. Quasi-irreversibility in the unfolding-refolding transition of phosphoglycerate kinase induced by guanidine hydrochloride. Eur. J. Biochem. 163 (1987) 29-34
    • (1987) Eur. J. Biochem. , vol.163 , pp. 29-34
    • Mitraki, A.1    Betton, J.M.2    Desmadril, M.3    Yon, J.M.4
  • 107
    • 67650620091 scopus 로고    scopus 로고
    • Amyloidosis-associated neurotrophic keratopathy precipitated by overcorrected blepharoptosis
    • Nguyen V.T., Hwang T.N., Shamie N., Chuck R.S., and McCulley T.J. Amyloidosis-associated neurotrophic keratopathy precipitated by overcorrected blepharoptosis. Cornea 28 (2009) 575-576
    • (2009) Cornea , vol.28 , pp. 575-576
    • Nguyen, V.T.1    Hwang, T.N.2    Shamie, N.3    Chuck, R.S.4    McCulley, T.J.5
  • 108
    • 36749045270 scopus 로고    scopus 로고
    • Early onset vitreous amyloidosis in familial amyloidotic polyneuropathy with a transthyretin Glu54Gly mutation is associated with elevated vitreous VEGF
    • O'Hearn T.M., Fawzi A., He S., Rao N.A., and Lim J.I. Early onset vitreous amyloidosis in familial amyloidotic polyneuropathy with a transthyretin Glu54Gly mutation is associated with elevated vitreous VEGF. Br. J. Ophthalmol. 91 (2007) 1607-1609
    • (2007) Br. J. Ophthalmol. , vol.91 , pp. 1607-1609
    • O'Hearn, T.M.1    Fawzi, A.2    He, S.3    Rao, N.A.4    Lim, J.I.5
  • 110
    • 20444403757 scopus 로고    scopus 로고
    • Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases
    • Pawar A.P., Dubay K.F., Zurdo J., Chiti F., Vendruscolo M., and Dobson C.M. Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. J. Mol. Biol. 350 (2005) 379-392
    • (2005) J. Mol. Biol. , vol.350 , pp. 379-392
    • Pawar, A.P.1    Dubay, K.F.2    Zurdo, J.3    Chiti, F.4    Vendruscolo, M.5    Dobson, C.M.6
  • 111
    • 34249663915 scopus 로고    scopus 로고
    • Insights into the beaded filament of the eye lens
    • Perng M.D., Zhang Q., and Quinlan R.A. Insights into the beaded filament of the eye lens. Exp. Cell Res. 313 (2007) 2180-2188
    • (2007) Exp. Cell Res. , vol.313 , pp. 2180-2188
    • Perng, M.D.1    Zhang, Q.2    Quinlan, R.A.3
  • 112
    • 0034602271 scopus 로고    scopus 로고
    • Interaction of human α-synuclein and Parkinson's disease variants with phospholipids: Structural analysis using site-directed mutagenesis
    • Perrin R.J., Woods W.S., Clayton D.F., and George J.M. Interaction of human α-synuclein and Parkinson's disease variants with phospholipids: Structural analysis using site-directed mutagenesis. J. Biol. Chem. 275 (2000) 34393-34398
    • (2000) J. Biol. Chem. , vol.275 , pp. 34393-34398
    • Perrin, R.J.1    Woods, W.S.2    Clayton, D.F.3    George, J.M.4
  • 114
    • 0023063602 scopus 로고
    • Prions causing degenerative neurological diseases
    • Prusiner S.B. Prions causing degenerative neurological diseases. Annu. Rev. Med. 38 (1987) 381-398
    • (1987) Annu. Rev. Med. , vol.38 , pp. 381-398
    • Prusiner, S.B.1
  • 115
    • 66049133683 scopus 로고    scopus 로고
    • Aging: central role for autophagy and the lysosomal degradative system
    • Rajawat Y.S., Hilioti Z., and Bossis I. Aging: central role for autophagy and the lysosomal degradative system. Ageing Res. Rev. 8 (2009) 199-213
    • (2009) Ageing Res. Rev. , vol.8 , pp. 199-213
    • Rajawat, Y.S.1    Hilioti, Z.2    Bossis, I.3
  • 116
    • 69949175897 scopus 로고    scopus 로고
    • Autophagy in neurodegeneration: fire-fighter and/or incendiarist?
    • Rami A. Autophagy in neurodegeneration: fire-fighter and/or incendiarist?. Neuropathol. Appl. Neurobiol. (2009)
    • (2009) Neuropathol. Appl. Neurobiol.
    • Rami, A.1
  • 118
    • 33645669165 scopus 로고    scopus 로고
    • Prediction of nucleating sequences from amyloidogenic propensities of tau-related peptides
    • Rojas Quijano F.A., Morrow D., Wise B.M., Brancia F.L., and Goux W.J. Prediction of nucleating sequences from amyloidogenic propensities of tau-related peptides. Biochemistry 45 (2006) 4638-4652
    • (2006) Biochemistry , vol.45 , pp. 4638-4652
    • Rojas Quijano, F.A.1    Morrow, D.2    Wise, B.M.3    Brancia, F.L.4    Goux, W.J.5
  • 119
    • 0028110523 scopus 로고    scopus 로고
    • Rhodopsin accumulation at abnormal sites in retinas of mice with a human P23H rhodopsin transgene
    • Roof D.J., Adamian M., and Hayes A. Rhodopsin accumulation at abnormal sites in retinas of mice with a human P23H rhodopsin transgene. Invest. Ophthalmol. Vis. Sci. 35 (1996) 4049-4062
    • (1996) Invest. Ophthalmol. Vis. Sci. , vol.35 , pp. 4049-4062
    • Roof, D.J.1    Adamian, M.2    Hayes, A.3
  • 120
    • 58049214009 scopus 로고    scopus 로고
    • Tau oligomerization: a role for tau aggregation intermediates linked to neurodegeneration
    • Sahara N., Maeda S., and Takashima A. Tau oligomerization: a role for tau aggregation intermediates linked to neurodegeneration. Curr. Alzheimer Res. 5 (2008) 591-598
    • (2008) Curr. Alzheimer Res. , vol.5 , pp. 591-598
    • Sahara, N.1    Maeda, S.2    Takashima, A.3
  • 121
    • 0037099080 scopus 로고    scopus 로고
    • The cellular fate of mutant rhodopsin: quality control, degradation and aggresome formation
    • Saliba R.S., Munro P.N., Luthert P.J., and Cheetham M.E. The cellular fate of mutant rhodopsin: quality control, degradation and aggresome formation. J. Cell. Sci. 115 (2002) 2907-2918
    • (2002) J. Cell. Sci. , vol.115 , pp. 2907-2918
    • Saliba, R.S.1    Munro, P.N.2    Luthert, P.J.3    Cheetham, M.E.4
  • 123
    • 9444229933 scopus 로고    scopus 로고
    • Inhibition of amyloid fibrillogenesis and toxicity by a peptide chaperone
    • Santhoshkumar P., and Sharma K.K. Inhibition of amyloid fibrillogenesis and toxicity by a peptide chaperone. Mol. Cell. Biochem. 267 (2004) 147-155
    • (2004) Mol. Cell. Biochem. , vol.267 , pp. 147-155
    • Santhoshkumar, P.1    Sharma, K.K.2
  • 124
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe D.J. Folding proteins in fatal ways. Nature 426 (2003) 900-904
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 125
    • 0034769477 scopus 로고    scopus 로고
    • Removal of oxidatively damaged proteins from lens cells by the ubiquitin-proteasome pathway
    • Shang F., Nowell Jr. T.R., and Taylor A. Removal of oxidatively damaged proteins from lens cells by the ubiquitin-proteasome pathway. Exp. Eye Res. 73 (2001) 229-238
    • (2001) Exp. Eye Res. , vol.73 , pp. 229-238
    • Shang, F.1    Nowell Jr., T.R.2    Taylor, A.3
  • 126
    • 37349075401 scopus 로고    scopus 로고
    • Silencing gene therapy for mutant membrane, secretory, and lipid proteins in retinitis pigmentosa (RP)
    • Shinohara T., Mulhern M.L., and Madson C.J. Silencing gene therapy for mutant membrane, secretory, and lipid proteins in retinitis pigmentosa (RP). Med. Hypotheses 70 (2008) 378-380
    • (2008) Med. Hypotheses , vol.70 , pp. 378-380
    • Shinohara, T.1    Mulhern, M.L.2    Madson, C.J.3
  • 127
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • Sitia R., and Braakman I. Quality control in the endoplasmic reticulum protein factory. Nature 426 (2003) 891-894
    • (2003) Nature , vol.426 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 128
    • 0035827318 scopus 로고    scopus 로고
    • Protein misfolding and disease; protein refolding and therapy
    • Soto C. Protein misfolding and disease; protein refolding and therapy. FEBS Lett. 498 (2001) 204-207
    • (2001) FEBS Lett. , vol.498 , pp. 204-207
    • Soto, C.1
  • 129
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto C. Unfolding the role of protein misfolding in neurodegenerative diseases. Nat. Rev. Neurosci. 4 (2003) 49-60
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 49-60
    • Soto, C.1
  • 130
    • 67651030654 scopus 로고    scopus 로고
    • Influence of conformational antibodies on dissociation of fibrillar amyloid beta (A beta 1-42) in vitro
    • Subramanian S., Madhavadas S., and Balasubramanian P. Influence of conformational antibodies on dissociation of fibrillar amyloid beta (A beta 1-42) in vitro. Indian J. Exp. Biol. 47 (2009) 309-313
    • (2009) Indian J. Exp. Biol. , vol.47 , pp. 309-313
    • Subramanian, S.1    Madhavadas, S.2    Balasubramanian, P.3
  • 132
    • 0027452148 scopus 로고
    • Rhodopsin mutations responsible for autosomal dominant retinitis pigmentosa clustering of functional classes along the polypeptide chain
    • Sung C.H., Davenport C.M., and Nathans J. Rhodopsin mutations responsible for autosomal dominant retinitis pigmentosa clustering of functional classes along the polypeptide chain. J. Biol. Chem. 268 (1993) 26645-26649
    • (1993) J. Biol. Chem. , vol.268 , pp. 26645-26649
    • Sung, C.H.1    Davenport, C.M.2    Nathans, J.3
  • 133
    • 0036221254 scopus 로고    scopus 로고
    • Synucleins in glaucoma: implication of γ-synuclein in glaucomatous alterations in the optic nerve
    • Surgucheva I., McMahan B., Ahmed F., Tomarev S., Wax M.B., and Surguchov A. Synucleins in glaucoma: implication of γ-synuclein in glaucomatous alterations in the optic nerve. J. Neurosci. Res. 68 (2002) 97-106
    • (2002) J. Neurosci. Res. , vol.68 , pp. 97-106
    • Surgucheva, I.1    McMahan, B.2    Ahmed, F.3    Tomarev, S.4    Wax, M.B.5    Surguchov, A.6
  • 135
    • 31544462086 scopus 로고    scopus 로고
    • Interaction of myocilin with gamma-synuclein affects its secretion and aggregation
    • Surgucheva I., Park B.C., Yue B.Y., Tomarev S., and Surguchov A. Interaction of myocilin with gamma-synuclein affects its secretion and aggregation. Cell. Mol. Neurobiol. 25 (2005) 1009-1033
    • (2005) Cell. Mol. Neurobiol. , vol.25 , pp. 1009-1033
    • Surgucheva, I.1    Park, B.C.2    Yue, B.Y.3    Tomarev, S.4    Surguchov, A.5
  • 136
    • 57149084065 scopus 로고    scopus 로고
    • Molecular and cellular biology of synucleins
    • Surguchov A. Molecular and cellular biology of synucleins. Int. Rev. Cytol. Cell Biol. 270 (2008) 225-317
    • (2008) Int. Rev. Cytol. Cell Biol. , vol.270 , pp. 225-317
    • Surguchov, A.1
  • 139
    • 0042819915 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins evolve by repeat expansion
    • Tompa P. Intrinsically unstructured proteins evolve by repeat expansion. BioEssays 25 (2003) 847-855
    • (2003) BioEssays , vol.25 , pp. 847-855
    • Tompa, P.1
  • 140
    • 0026625426 scopus 로고
    • Complete rescue of photoreceptor dysplasia and degeneration in transgenic retinal degeneration slow (rds) mice
    • Travis G.H., Groshan K.R., Lloyd M., and Bok D. Complete rescue of photoreceptor dysplasia and degeneration in transgenic retinal degeneration slow (rds) mice. Neuron 9 (1992) 113-119
    • (1992) Neuron , vol.9 , pp. 113-119
    • Travis, G.H.1    Groshan, K.R.2    Lloyd, M.3    Bok, D.4
  • 142
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: a point where biology waits for physics
    • Uversky V.N. Natively unfolded proteins: a point where biology waits for physics. Protein Sci. 11 (2002) 739-756
    • (2002) Protein Sci. , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 143
    • 0141861067 scopus 로고    scopus 로고
    • Protein folding revisited A polypeptided chain at the folding-misfolding-non-folding cross-roads: which way to go?
    • Uversky V.N. Protein folding revisited A polypeptided chain at the folding-misfolding-non-folding cross-roads: which way to go?. Cell. Mol. Life Sci. 60 (2003) 1852-1871
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1852-1871
    • Uversky, V.N.1
  • 144
    • 45449091418 scopus 로고    scopus 로고
    • Amyloidogenesis of naturally unfolded proteins
    • Uversky V.N. Amyloidogenesis of naturally unfolded proteins. Curr. Alzheimer's Res. 5 (2008) 260-267
    • (2008) Curr. Alzheimer's Res. , vol.5 , pp. 260-267
    • Uversky, V.N.1
  • 145
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: the importance of being unfolded
    • Uversky V.N., and Fink A.L. Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim. Biophys. Acta 1698 (2004) 131-153
    • (2004) Biochim. Biophys. Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 146
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky V.N., Gillespie J.R., and Fink A.L. Why are "natively unfolded" proteins unstructured under physiologic conditions?. Proteins 41 (2000) 415-427
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 147
    • 0035816404 scopus 로고    scopus 로고
    • Pesticides directly accelerate the rate of alpha synuclein fibril formation: a possible factor in Parkinson's disease
    • Uversky V.N., Li J., and Fink A.L. Pesticides directly accelerate the rate of alpha synuclein fibril formation: a possible factor in Parkinson's disease. FEBS Lett. 500 (2001) 105-108
    • (2001) FEBS Lett. , vol.500 , pp. 105-108
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 149
    • 0036195521 scopus 로고    scopus 로고
    • Subepithelial corneal amyloid deposits in a case of congenital glaucoma
    • Vemuganti G.K., and Mandal A.K. Subepithelial corneal amyloid deposits in a case of congenital glaucoma. Cornea 21 (2002) 315-317
    • (2002) Cornea , vol.21 , pp. 315-317
    • Vemuganti, G.K.1    Mandal, A.K.2
  • 150
    • 0034458454 scopus 로고    scopus 로고
    • The cerebral proteopathies: neurodegenerative disorders of protein conformation and assembly
    • Walker L.C., and LeVine H. The cerebral proteopathies: neurodegenerative disorders of protein conformation and assembly. Mol. Neurobiol. 21 (2000) 83-95
    • (2000) Mol. Neurobiol. , vol.21 , pp. 83-95
    • Walker, L.C.1    LeVine, H.2
  • 152
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward C.L., Omura S., and Kopito R.R. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83 (1995) 121-127
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 154
    • 57449087203 scopus 로고    scopus 로고
    • Preventing β-amyloid fibrillization and deposition: β-sheet breakers and pathological chaperone inhibitors
    • Wisniewski T., and Sadowski M. Preventing β-amyloid fibrillization and deposition: β-sheet breakers and pathological chaperone inhibitors. BMC Neurosci. 9 Suppl. 2 (2008) S5
    • (2008) BMC Neurosci. , vol.9 , Issue.SUPPL. 2
    • Wisniewski, T.1    Sadowski, M.2
  • 155
    • 34248376062 scopus 로고    scopus 로고
    • Sodium 4-phenylbutyrate acts as a chemical chaperone on misfolded myocilin to rescue cells from endoplasmic reticulum stress and apoptosis
    • Yam G.H., Gaplovska-Kysela K., Zuber C., and Roth J. Sodium 4-phenylbutyrate acts as a chemical chaperone on misfolded myocilin to rescue cells from endoplasmic reticulum stress and apoptosis. Invest. Ophthalmol. Vis. Sci. 48 (2007) 1683-1690
    • (2007) Invest. Ophthalmol. Vis. Sci. , vol.48 , pp. 1683-1690
    • Yam, G.H.1    Gaplovska-Kysela, K.2    Zuber, C.3    Roth, J.4
  • 156
    • 18044398967 scopus 로고    scopus 로고
    • Vitreous fluid levels of beta-amyloid (1-42) and tau in patients with retinal diseases
    • Yoneda S., Hara H., Hirata A., Fukushima M., Inomata Y., and Tanihara H. Vitreous fluid levels of beta-amyloid (1-42) and tau in patients with retinal diseases. Jpn. J. Ophthalmol. 492 (2005) 106-108
    • (2005) Jpn. J. Ophthalmol. , vol.492 , pp. 106-108
    • Yoneda, S.1    Hara, H.2    Hirata, A.3    Fukushima, M.4    Inomata, Y.5    Tanihara, H.6
  • 158
    • 57649131080 scopus 로고    scopus 로고
    • Identification of the primary targets of carbamylation in bovine lens proteins by mass spectrometry
    • Zhang J., Yan H., Harding J.J., Liu Z.X., Wang X., and Ruan Y.S. Identification of the primary targets of carbamylation in bovine lens proteins by mass spectrometry. Curr. Eye Res. 33 (2008) 963-976
    • (2008) Curr. Eye Res. , vol.33 , pp. 963-976
    • Zhang, J.1    Yan, H.2    Harding, J.J.3    Liu, Z.X.4    Wang, X.5    Ruan, Y.S.6
  • 159
    • 0032013091 scopus 로고    scopus 로고
    • Transthyretin mutation (serine 84) associated with familial amyloid polyneuropathy in a Hungarian family
    • Zólyomi Z., Benson M.D., Halász K., Uemichi T., and Fekete G. Transthyretin mutation (serine 84) associated with familial amyloid polyneuropathy in a Hungarian family. Amyloid 5 (1998) 30-34
    • (1998) Amyloid , vol.5 , pp. 30-34
    • Zólyomi, Z.1    Benson, M.D.2    Halász, K.3    Uemichi, T.4    Fekete, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.