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Volumn 61, Issue 2, 2011, Pages 237-250

Defective Protein Folding and Aggregation as the Basis of Neurodegenerative Diseases: The Darker Aspect of Proteins

Author keywords

Aggregation; Conformational diseases; Molecular chaperones; Protein misfolding

Indexed keywords

PROTEIN;

EID: 80955166037     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12013-011-9200-x     Document Type: Review
Times cited : (60)

References (138)
  • 2
    • 0015361994 scopus 로고
    • The formation and stabilization of protein structure
    • Anfinsen, C. (1972). The formation and stabilization of protein structure. Biochemistry Journal, 128, 737-749.
    • (1972) Biochemistry Journal , vol.128 , pp. 737-749
    • Anfinsen, C.1
  • 4
    • 0028235775 scopus 로고
    • Molecular mechanisms of acid denaturation The role of histidine residues in the partial unfolding of apomyoglobin
    • Barrick, D., Hughson, F. M., & Baldwin, R. L. (1994). Molecular mechanisms of acid denaturation The role of histidine residues in the partial unfolding of apomyoglobin. Journal of Molecular Biology, 237, 588-601.
    • (1994) Journal of Molecular Biology , vol.237 , pp. 588-601
    • Barrick, D.1    Hughson, F.M.2    Baldwin, R.L.3
  • 5
    • 0025876740 scopus 로고
    • Protein folding: Local structure, domains, subunits, and assemblies
    • Jaenicke, R. (1991). Protein folding: Local structure, domains, subunits, and assemblies. Biochemistry, 30, 3147-3161.
    • (1991) Biochemistry , vol.30 , pp. 3147-3161
    • Jaenicke, R.1
  • 6
    • 18844438057 scopus 로고    scopus 로고
    • Partially folded intermediate state of concanavalin A retains its carbohydrate specificity
    • Naeem, A., Khan, A., & Khan, R. H. (2005). Partially folded intermediate state of concanavalin A retains its carbohydrate specificity. Biochemistry and Biophysics Research Communications, 331, 1284-1294.
    • (2005) Biochemistry and Biophysics Research Communications , vol.331 , pp. 1284-1294
    • Naeem, A.1    Khan, A.2    Khan, R.H.3
  • 7
    • 0027391299 scopus 로고
    • Characterization of an intermediate in the folding pathway of phosphoglycerate kinase: Chemical reactivity of genetically introduced cysteinyl residues during the folding process
    • Ballery, N., Desmadril, M., Minard, P., & Yon, J. M. (1993). Characterization of an intermediate in the folding pathway of phosphoglycerate kinase: Chemical reactivity of genetically introduced cysteinyl residues during the folding process. Biochemistry, 32, 708-714.
    • (1993) Biochemistry , vol.32 , pp. 708-714
    • Ballery, N.1    Desmadril, M.2    Minard, P.3    Yon, J.M.4
  • 8
    • 0026524680 scopus 로고
    • The folding of an enzyme IV Structure of an intermediate in the refolding of barnase analyzed by a protein engineering procedure
    • Matousschek, A., Serrano, L., Meiering, E. M., Bycroft, M., & Ferscht, A. R. (1992). The folding of an enzyme IV Structure of an intermediate in the refolding of barnase analyzed by a protein engineering procedure. Journal of Molecular Biology, 224, 837-845.
    • (1992) Journal of Molecular Biology , vol.224 , pp. 837-845
    • Matousschek, A.1    Serrano, L.2    Meiering, E.M.3    Bycroft, M.4    Ferscht, A.R.5
  • 9
    • 7044228278 scopus 로고    scopus 로고
    • Characterization of a partially folded intermediate of papain induced by fluorinated alcohols at low pH
    • Naeem, A., Khan, K. A., & Khan, R. H. (2004). Characterization of a partially folded intermediate of papain induced by fluorinated alcohols at low pH. Archives of Biochemistry and Biophysics, 432, 79-87.
    • (2004) Archives of Biochemistry and Biophysics , vol.432 , pp. 79-87
    • Naeem, A.1    Khan, K.A.2    Khan, R.H.3
  • 10
    • 0026351184 scopus 로고
    • Role of electrostatic repulsion in the acidic molten globule of cytochrome c
    • Goto, Y., & Nishikiori, S. J. (1991). Role of electrostatic repulsion in the acidic molten globule of cytochrome c. Journal of Molecular Biology, 222, 679-686.
    • (1991) Journal of Molecular Biology , vol.222 , pp. 679-686
    • Goto, Y.1    Nishikiori, S.J.2
  • 12
    • 0023655983 scopus 로고
    • Conformational changes induced in lens alpha-and gamma crystallins by modification with glucose 6-phosphate Implications for cataract
    • Beswick, H. T., & Harding, J. J. (1987). Conformational changes induced in lens alpha-and gamma crystallins by modification with glucose 6-phosphate Implications for cataract. Biochemistry Journal, 246, 761-769.
    • (1987) Biochemistry Journal , vol.246 , pp. 761-769
    • Beswick, H.T.1    Harding, J.J.2
  • 13
    • 0028272883 scopus 로고
    • Pathogenic effects of advanced glycosylation: Biochemical, biologic, and clinical implications for diabetes and aging
    • Vlassara, H., Bucala, R., & Striker, L. (1994). Pathogenic effects of advanced glycosylation: Biochemical, biologic, and clinical implications for diabetes and aging. Laboratory Investigation, 70, 138-151.
    • (1994) Laboratory Investigation , vol.70 , pp. 138-151
    • Vlassara, H.1    Bucala, R.2    Striker, L.3
  • 14
    • 0021782568 scopus 로고
    • Non enzymatic covalent post translational modification of proteins in vivo
    • Harding, J. J. (1985). Non enzymatic covalent post translational modification of proteins in vivo. Advances in Protein Chemistry, 37, 247-334.
    • (1985) Advances in Protein Chemistry , vol.37 , pp. 247-334
    • Harding, J.J.1
  • 16
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau, B., & Horwich, A. L. (1998). The Hsp70 and Hsp60 chaperone machines. Cell, 92, 351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 17
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F. U., & Hayer-Hartl, M. (2002). Molecular chaperones in the cytosol: From nascent chain to folded protein. Science, 295, 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 19
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M. (2003). Protein folding and misfolding. Nature, 426, 884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 21
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn, O. B. (1995). Molten globule and protein folding. Advances in Protein Chemistry, 47, 83-87.
    • (1995) Advances in Protein Chemistry , vol.47 , pp. 83-87
    • Ptitsyn, O.B.1
  • 23
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto, C. (2003). Unfolding the role of protein misfolding in neurodegenerative diseases. Nature Reviews Neuroscience, 4, 49-60.
    • (2003) Nature Reviews Neuroscience , vol.4 , pp. 49-60
    • Soto, C.1
  • 24
    • 0037159944 scopus 로고    scopus 로고
    • Determination of the structures of distinct transition state ensembles for a β-sheet peptide with parallel folding pathways
    • Davis, R., Dobson, C. M., & Vendruscolo, M. (2002). Determination of the structures of distinct transition state ensembles for a β-sheet peptide with parallel folding pathways. Journal of Chemical Physics, 117, 9510-9517.
    • (2002) Journal of Chemical Physics , vol.117 , pp. 9510-9517
    • Davis, R.1    Dobson, C.M.2    Vendruscolo, M.3
  • 25
    • 0026059137 scopus 로고
    • Peptide-binding specificity of the molecular chaperone BiP
    • Flynn, G. C., Pohl, J., Flocco, MT., & Rothman, J. E. (1991). Peptide-binding specificity of the molecular chaperone BiP. Nature, 353, 726-730.
    • (1991) Nature , vol.353 , pp. 726-730
    • Flynn, G.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 26
    • 0026595140 scopus 로고
    • Different conformations for the same polypeptide bound to chaperones DnaK and GroEL
    • Landry, S. J., Jordan, R., McMacken, R., & Gierasch, L. M. (1992). Different conformations for the same polypeptide bound to chaperones DnaK and GroEL. Nature, 355, 455-457.
    • (1992) Nature , vol.355 , pp. 455-457
    • Landry, S.J.1    Jordan, R.2    McMacken, R.3    Gierasch, L.M.4
  • 27
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M. J., & Sambrook, J. (1992). Protein folding in the cell. Nature, 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 29
  • 31
    • 0032006678 scopus 로고    scopus 로고
    • Alternative conformation of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly, J. (1998). Alternative conformation of amyloidogenic proteins and their multi-step assembly pathways. Current Opinion in Structural Biology, 8, 101-106.
    • (1998) Current Opinion in Structural Biology , vol.8 , pp. 101-106
    • Kelly, J.1
  • 32
    • 0035961329 scopus 로고    scopus 로고
    • The structural basis of protein folding and its links with human disease
    • Dobson, C. M. (2001). The structural basis of protein folding and its links with human disease. Philosophical Transactions of the Royal Society London B, 356, 133-145.
    • (2001) Philosophical Transactions of the Royal Society London B , vol.356 , pp. 133-145
    • Dobson, C.M.1
  • 33
    • 0031056829 scopus 로고    scopus 로고
    • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
    • Booth, D. R., Sunde, M., Bellotti, V., Robinson, C. V., Hutchinson, W. L., et al. (1997). Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature, 385, 78-793.
    • (1997) Nature , vol.385 , pp. 78-793
    • Booth, D.R.1    Sunde, M.2    Bellotti, V.3    Robinson, C.V.4    Hutchinson, W.L.5
  • 35
    • 70049090962 scopus 로고    scopus 로고
    • Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases
    • Castillo, V., & Ventura, S. (2009). Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases. PLoS Computational Biology, 5, 1-16.
    • (2009) PLoS Computational Biology , vol.5 , pp. 1-16
    • Castillo, V.1    Ventura, S.2
  • 36
    • 2942580461 scopus 로고    scopus 로고
    • CFTR and chaperones processing and degradation
    • Amaral, M. D. (2004). CFTR and chaperones processing and degradation. Journal of Molecular Neuroscience, 23, 41-48.
    • (2004) Journal of Molecular Neuroscience , vol.23 , pp. 41-48
    • Amaral, M.D.1
  • 37
    • 58149316598 scopus 로고    scopus 로고
    • Early stages of β2-microglobulin aggregation and the inhibiting action of αB-crystallin
    • Pullara, F., & Emanuele, A. (2008). Early stages of β2-microglobulin aggregation and the inhibiting action of αB-crystallin. Proteins, 73, 1037-1046.
    • (2008) Proteins , vol.73 , pp. 1037-1046
    • Pullara, F.1    Emanuele, A.2
  • 38
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • Sherman, M. Y., & Goldberg, A. L. (2001). Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases. Neuron, 29, 15-32.
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 39
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanisms of pathogenesis
    • Kayed, R., Head, E., Thompson, J. L., et al. (2003). Common structure of soluble amyloid oligomers implies common mechanisms of pathogenesis. Science, 300, 486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3
  • 40
    • 0036845354 scopus 로고    scopus 로고
    • The behaviour of poly amino acids reveals an inverse side chain effect in amyloid structure formation
    • Fandrich, M., & Dobson, C. M. (2002). The behaviour of poly amino acids reveals an inverse side chain effect in amyloid structure formation. EMBO Journal, 21, 5682-5690.
    • (2002) EMBO Journal , vol.21 , pp. 5682-5690
    • Fandrich, M.1    Dobson, C.M.2
  • 43
    • 0037465708 scopus 로고    scopus 로고
    • Insights into the amyloid folding problem from solid-state NMR
    • Tycko, R. (2003). Insights into the amyloid folding problem from solid-state NMR. Biochemistry, 42, 3151-3159.
    • (2003) Biochemistry , vol.42 , pp. 3151-3159
    • Tycko, R.1
  • 44
    • 0037174998 scopus 로고    scopus 로고
    • Structural and dynamic features of Alzheimer's Aβ peptide in amyloid fibrils studied by site-directed spin labelling
    • Torok, M., Milton, S., Kayed, R., et al. (2002). Structural and dynamic features of Alzheimer's Aβ peptide in amyloid fibrils studied by site-directed spin labelling. Journal of Biological Chemistry, 277, 40810-40815.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 40810-40815
    • Torok, M.1    Milton, S.2    Kayed, R.3
  • 45
    • 0033534397 scopus 로고    scopus 로고
    • Watching amyloid fibrils grow by time-lapse atomic force microscopy
    • Goldsbury, C., Kistler, J., Aebi, U., et al. (1999). Watching amyloid fibrils grow by time-lapse atomic force microscopy. Journal of Molecular Biology, 285, 33-39.
    • (1999) Journal of Molecular Biology , vol.285 , pp. 33-39
    • Goldsbury, C.1    Kistler, J.2    Aebi, U.3
  • 46
    • 0034725535 scopus 로고    scopus 로고
    • The protofilament substructure of amyloid fibrils
    • Serpell, L., Sunde, M., Benson, M., et al. (2000). The protofilament substructure of amyloid fibrils. Journal of Molecular Biology, 300, 1033-1039.
    • (2000) Journal of Molecular Biology , vol.300 , pp. 1033-1039
    • Serpell, L.1    Sunde, M.2    Benson, M.3
  • 47
    • 0042847751 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
    • Jimenez, J. L., Guijarro, J. I., Orlova, E., et al. (1999). Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO Journal, 18, 815-821.
    • (1999) EMBO Journal , vol.18 , pp. 815-821
    • Jimenez, J.L.1    Guijarro, J.I.2    Orlova, E.3
  • 48
    • 0035839046 scopus 로고    scopus 로고
    • Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy
    • Jimenez, J. L., Tennent, G., Pepys, M. B., et al. (2001). Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy. Journal of Molecular Biology, 311, 241-247.
    • (2001) Journal of Molecular Biology , vol.311 , pp. 241-247
    • Jimenez, J.L.1    Tennent, G.2    Pepys, M.B.3
  • 51
    • 0031825554 scopus 로고    scopus 로고
    • From the globular to the fibrous state: Protein structure and structural conversion in amyloid formation
    • Sunde, M., & Blake, C. C. (1998). From the globular to the fibrous state: Protein structure and structural conversion in amyloid formation. Quarterly Review of Biophysics, 31, 1-39.
    • (1998) Quarterly Review of Biophysics , vol.31 , pp. 1-39
    • Sunde, M.1    Blake, C.C.2
  • 55
    • 69149103558 scopus 로고    scopus 로고
    • Intrinsic disorder in proteins associated with neurodegenerative diseases
    • Uversky, V. N. (2009). Intrinsic disorder in proteins associated with neurodegenerative diseases. Frontier Bioscience, 14, 5188-5238.
    • (2009) Frontier Bioscience , vol.14 , pp. 5188-5238
    • Uversky, V.N.1
  • 56
    • 3542995049 scopus 로고    scopus 로고
    • Stress-inducible responses and heat shock proteins: New pharmacologic targets for cytoprotection
    • Morimoto, R. I., & Santoro, M. G. (1998). Stress-inducible responses and heat shock proteins: New pharmacologic targets for cytoprotection. Nature Biotechnology, 16, 833-838.
    • (1998) Nature Biotechnology , vol.16 , pp. 833-838
    • Morimoto, R.I.1    Santoro, M.G.2
  • 57
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau, B., Weissmanand, J., & Horwich, A. (2006). Molecular chaperones and protein quality control. Cell, 125, 445-451.
    • (2006) Cell , vol.125 , pp. 445-451
    • Bukau, B.1    Weissmanand, J.2    Horwich, A.3
  • 58
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease
    • Auluck, P. K., Chan, H. Y., Trojanowsk, J. Q., Lee, V. M., & Bonini, N. M. (2002). Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease. Science, 295, 865-868.
    • (2002) Science , vol.295 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.2    Trojanowsk, J.Q.3    Lee, V.M.4    Bonini, N.M.5
  • 62
    • 0024997813 scopus 로고
    • Tissue-specific expression of the heat shock protein HSP27 during Drosophila melanogaster development
    • Pauli, D., Tonka, C. H., Tissieres, A., & Arrigo, A. P. (1990). Tissue-specific expression of the heat shock protein HSP27 during Drosophila melanogaster development. Journal of Cell Biology, 111, 817-828.
    • (1990) Journal of Cell Biology , vol.111 , pp. 817-828
    • Pauli, D.1    Tonka, C.H.2    Tissieres, A.3    Arrigo, A.P.4
  • 64
    • 0032572603 scopus 로고    scopus 로고
    • Stress (heat shock) proteins: Molecular chaperones in cardiovascular biology and disease
    • Benjamin, I. J., & McMillan, D. R. (1998). Stress (heat shock) proteins: Molecular chaperones in cardiovascular biology and disease. Circulation Research, 83, 117-132.
    • (1998) Circulation Research , vol.83 , pp. 117-132
    • Benjamin, I.J.1    McMillan, D.R.2
  • 67
    • 0036566675 scopus 로고    scopus 로고
    • Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntington
    • Wyttenbach, A., Sauvageot, O., Carmichael, J., Diaz-Latoud, C., Arrigo, A. P., & Rubinsztein, D. C. (2002). Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntington. Human Molecular Genetics, 11, 1137-1151.
    • (2002) Human Molecular Genetics , vol.11 , pp. 1137-1151
    • Wyttenbach, A.1    Sauvageot, O.2    Carmichael, J.3    Diaz-Latoud, C.4    Arrigo, A.P.5    Rubinsztein, D.C.6
  • 68
    • 1642356755 scopus 로고    scopus 로고
    • HSP27 but not HSP70 has a potent protective effect against alpha-synuclein-induced cell death in mammalian neuronal cells
    • Zourlidou, A., Payne Smith, M. D., & Latchman, D. S. (2004). HSP27 but not HSP70 has a potent protective effect against alpha-synuclein-induced cell death in mammalian neuronal cells. Journal of Neurochemistry, 88, 1439-1448.
    • (2004) Journal of Neurochemistry , vol.88 , pp. 1439-1448
    • Zourlidou, A.1    Payne Smith, M.D.2    Latchman, D.S.3
  • 70
    • 33750363298 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Rubinsztein, D. C. (2006). Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature, 443, 780-786.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 71
    • 34250183177 scopus 로고    scopus 로고
    • HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS
    • Pandey, U. B., Nie, Z., Batlevi, Y., et al. (2007). HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS. Nature, 447, 859-863.
    • (2007) Nature , vol.447 , pp. 859-863
    • Pandey, U.B.1    Nie, Z.2    Batlevi, Y.3
  • 72
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required for autophagic degradation of aggregated Huntington
    • Iwata, A., Riley, B. E., Johnston, J. A., & Kopito, R. R. (2005). HDAC6 and microtubules are required for autophagic degradation of aggregated Huntington. Journal of Biological Chemistry, 280, 40282-40292.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 40282-40292
    • Iwata, A.1    Riley, B.E.2    Johnston, J.A.3    Kopito, R.R.4
  • 73
    • 22244442489 scopus 로고    scopus 로고
    • The biochemistry of Parkinson's disease
    • Cookson, M. R. (2005). The biochemistry of Parkinson's disease. Annual Review of Biochemistry, 74, 29-52.
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 29-52
    • Cookson, M.R.1
  • 74
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parldn gene cause autosomal recessive juvenile parkinsonism
    • Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., & Minoshima, S. (1998). Mutations in the parldn gene cause autosomal recessive juvenile parkinsonism. Nature, 392, 605-608.
    • (1998) Nature , vol.392 , pp. 605-608
    • Kitada, T.1    Asakawa, S.2    Hattori, N.3    Matsumine, H.4    Yamamura, Y.5    Minoshima, S.6
  • 75
    • 0033933048 scopus 로고    scopus 로고
    • Familial Parkinson's disease gene product, parkin, is an ubiquitin-protein ligase
    • Shimura, H., Hattori, N., Kubo, S., Yoshikuni, K., Mizuno, Y., et al. (2000). Familial Parkinson's disease gene product, parkin, is an ubiquitin-protein ligase. Nature Genetics, 25, 302-305.
    • (2000) Nature Genetics , vol.25 , pp. 302-305
    • Shimura, H.1    Hattori, N.2    Kubo, S.3    Yoshikuni, K.4    Mizuno, Y.5
  • 77
    • 33745280651 scopus 로고    scopus 로고
    • Biochemical analysis of Parkinson's disease-causing variants of Parkin, an E3 ubiquitin-protein ligase with monoubiquitylation capacity
    • Hampe, C., Ardila-Osorio, H., Fournier, M., Alexis, B., & Olga, C. (2006). Biochemical analysis of Parkinson's disease-causing variants of Parkin, an E3 ubiquitin-protein ligase with monoubiquitylation capacity. Human Molecular Genetics, 15, 2059-2207.
    • (2006) Human Molecular Genetics , vol.15 , pp. 2059-2207
    • Hampe, C.1    Ardila-Osorio, H.2    Fournier, M.3    Alexis, B.4    Olga, C.5
  • 78
    • 33645635706 scopus 로고    scopus 로고
    • Diverse effects pathogenic mutations of Parkin that catalyze multiple monoub- iquitylation in vitro
    • Matsuda, N., Kitami, T., Suzuki, T., Mizuno, Y., Hattori, N., & Tanaka, K. (2006). Diverse effects pathogenic mutations of Parkin that catalyze multiple monoub- iquitylation in vitro. Journal of Biological Chemistry, 281, 3204-3209.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 3204-3209
    • Matsuda, N.1    Kitami, T.2    Suzuki, T.3    Mizuno, Y.4    Hattori, N.5    Tanaka, K.6
  • 79
    • 80955167092 scopus 로고    scopus 로고
    • Parkin mediates non-classical, proteasomal-independent ubiquitination of synphilin-466
    • Lim, K. L., Chew, K. C., & Tan, J. M. (2009). Parkin mediates non-classical, proteasomal-independent ubiquitination of synphilin-466. Apoptosis, 14, 455-468.
    • (2009) Apoptosis , vol.14 , pp. 455-468
    • Lim, K.L.1    Chew, K.C.2    Tan, J.M.3
  • 80
    • 33344456519 scopus 로고    scopus 로고
    • Parkin- mediated lysine 63-linked polyubiquitination: A link to Lewy Body formation
    • Lim, K. L., Dawson, V. L., & Dawson, T. M. (2006). Parkin- mediated lysine 63-linked polyubiquitination: A link to Lewy Body formation. Neurobiology of Aging, 27, 524-529.
    • (2006) Neurobiology of Aging , vol.27 , pp. 524-529
    • Lim, K.L.1    Dawson, V.L.2    Dawson, T.M.3
  • 81
    • 0026649584 scopus 로고
    • The cystic fibrosis transmembrane conductance regulatoreffects of the most common cystic fibrosis-causing mutation on the secondary structure and stability of a synthetic peptide
    • Thomas, P. J., Shenbagamurthi, P., Sondek, J., Hullihen, J. M., & Pedersen, P. L. (1992). The cystic fibrosis transmembrane conductance regulatoreffects of the most common cystic fibrosis-causing mutation on the secondary structure and stability of a synthetic peptide. Journal of Biological Chemistry, 267, 5727-5730.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 5727-5730
    • Thomas, P.J.1    Shenbagamurthi, P.2    Sondek, J.3    Hullihen, J.M.4    Pedersen, P.L.5
  • 82
    • 77954681706 scopus 로고    scopus 로고
    • The missing zinc: p53 misfolding and cancer
    • Stewart Loh, N. (2010). The missing zinc: p53 misfolding and cancer. Metallomics, 2, 442-449.
    • (2010) Metallomics , vol.2 , pp. 442-449
    • Stewart Loh, N.1
  • 83
    • 63749109353 scopus 로고    scopus 로고
    • Hereditary pancreatitis caused by mutation-induced misfolding of human cationic trypsinogen: A novel disease mechanism
    • Kereszturi, E., Szmola, R., Kukor, Z., et al. (2009). Hereditary pancreatitis caused by mutation-induced misfolding of human cationic trypsinogen: A novel disease mechanism. Human Mutation, 30, 575-582.
    • (2009) Human Mutation , vol.30 , pp. 575-582
    • Kereszturi, E.1    Szmola, R.2    Kukor, Z.3
  • 84
    • 0024296032 scopus 로고
    • Endothelium derived relaxing factor release on activation of NMDA receptors suggests role as intracellular messenger in the brain
    • Garthwaite, J., Charles, S. L., & Chess-Williams, R. (1988). Endothelium derived relaxing factor release on activation of NMDA receptors suggests role as intracellular messenger in the brain. Nature, 336, 385-388.
    • (1988) Nature , vol.336 , pp. 385-388
    • Garthwaite, J.1    Charles, S.L.2    Chess-Williams, R.3
  • 85
    • 0025802065 scopus 로고
    • Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase
    • Bredt, D. S., Hwang, P. M., Glatt, C. E., Lowenstein, C., Reed, R. R., & snyder, S. H. (1991). Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase. Nature, 351, 714-718.
    • (1991) Nature , vol.351 , pp. 714-718
    • Bredt, D.S.1    Hwang, P.M.2    Glatt, C.E.3    Lowenstein, C.4    Reed, R.R.5    Snyder, S.H.6
  • 86
    • 33745315287 scopus 로고    scopus 로고
    • S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration
    • Uehara, T., Nakamura, T., Yao, D., Shi, Z. Q., et al. (2006). S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration. Nature, 441, 513-517.
    • (2006) Nature , vol.441 , pp. 513-517
    • Uehara, T.1    Nakamura, T.2    Yao, D.3    Shi, Z.Q.4
  • 88
    • 34447131004 scopus 로고    scopus 로고
    • Molecular mechanisms of nitrosative stress-mediated protein misfolding in neurodegenerative diseases
    • Nakamura, T., & Lipton, S. A. (2007). Molecular mechanisms of nitrosative stress-mediated protein misfolding in neurodegenerative diseases. Cellular and Molecular Life Sciences, 64, 1609-1620.
    • (2007) Cellular and Molecular Life Sciences , vol.64 , pp. 1609-1620
    • Nakamura, T.1    Lipton, S.A.2
  • 90
    • 19944432234 scopus 로고    scopus 로고
    • Argpyrimidine, a methylglyoxal-derived advanced glycation end-product in familial amyloidotic polyneuropathy
    • Gomes, R., Sousasilva, M., Quintas, A., Cordeiro, C., et al. (2005). Argpyrimidine, a methylglyoxal-derived advanced glycation end-product in familial amyloidotic polyneuropathy. Biochemical Journal, 385, 339-345.
    • (2005) Biochemical Journal , vol.385 , pp. 339-345
    • Gomes, R.1    Sousasilva, M.2    Quintas, A.3    Cordeiro, C.4
  • 93
    • 0019796775 scopus 로고
    • Kinetic analysis of the non enzymatic glycosylation of hemoglobin
    • Bunn, H. F., & Higgins, P. J. (1981). Kinetic analysis of the non enzymatic glycosylation of hemoglobin. Journal of Biological Chemistry, 213, 222-224.
    • (1981) Journal of Biological Chemistry , vol.213 , pp. 222-224
    • Bunn, H.F.1    Higgins, P.J.2
  • 94
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F., & Dobson, C. M. (2006). Protein misfolding, functional amyloid, and human disease. Annual Review of Biochemistry, 75, 333-366.
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 95
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe, D. J. (2002). Alzheimer's disease is a synaptic failure. Science, 298, 789-791.
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 96
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J., & Selkoe, D. J. (2002). The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science, 297, 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 97
    • 0034716942 scopus 로고    scopus 로고
    • Direct visualisation of the beta-sheet structure of synthetic Alzheimer's amyloid
    • Serpell, L. C., & Smith, J. M. (2000). Direct visualisation of the beta-sheet structure of synthetic Alzheimer's amyloid. Journal of Molecular Biology, 299, 225-231.
    • (2000) Journal of Molecular Biology , vol.299 , pp. 225-231
    • Serpell, L.C.1    Smith, J.M.2
  • 98
    • 0035943345 scopus 로고    scopus 로고
    • A portrait of Alzheimer secretases-new features and familiar faces
    • Esler, W. P., & Wolfe, M. S. (2001). A portrait of Alzheimer secretases-new features and familiar faces. Science, 293, 1449-1454.
    • (2001) Science , vol.293 , pp. 1449-1454
    • Esler, W.P.1    Wolfe, M.S.2
  • 99
    • 0036828769 scopus 로고    scopus 로고
    • Alzheimer's disease: Treatments in discovery and development
    • Citron, M. (2002). Alzheimer's disease: Treatments in discovery and development. Nature Neuroscience, 5, 1055-1057.
    • (2002) Nature Neuroscience , vol.5 , pp. 1055-1057
    • Citron, M.1
  • 101
    • 0025733411 scopus 로고
    • In vitro aging of beta-amyloid protein causes peptide aggregation and neurotoxicity
    • Pike, C., Walencewicz, A., Glabe, C., & Cotman, C. (1991). In vitro aging of beta-amyloid protein causes peptide aggregation and neurotoxicity. European Journal of Pharmacology, 207, 367-368.
    • (1991) European Journal of Pharmacology , vol.207 , pp. 367-368
    • Pike, C.1    Walencewicz, A.2    Glabe, C.3    Cotman, C.4
  • 102
    • 0027447286 scopus 로고
    • Neurodegeneration induced by beta-amyloid peptides in vitro: The role of peptide assembly state
    • Pike, C., Burdick, D., Walencewicz, A., Glabe, C., & Cotman, C. (1993). Neurodegeneration induced by beta-amyloid peptides in vitro: The role of peptide assembly state. Journal of Neuroscience, 13, 1676-1687.
    • (1993) Journal of Neuroscience , vol.13 , pp. 1676-1687
    • Pike, C.1    Burdick, D.2    Walencewicz, A.3    Glabe, C.4    Cotman, C.5
  • 104
    • 0031990490 scopus 로고    scopus 로고
    • Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease
    • Kruger, R., Kuhn, W., Muller, T., et al. (1998). Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease. Nature Genetics, 18, 106-108.
    • (1998) Nature Genetics , vol.18 , pp. 106-108
    • Kruger, R.1    Kuhn, W.2    Muller, T.3
  • 105
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the alpha-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos, M. H., et al. (1997). Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science, 276, 2045-2047.
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1
  • 107
    • 0031910093 scopus 로고    scopus 로고
    • Aggregation of neurofilament and alpha-synuclein proteins in Lewy bodies: Implications for the pathogenesis of Parkinson disease and Lewy body dementia
    • Trojanowski, J., & Lee, V. (1998). Aggregation of neurofilament and alpha-synuclein proteins in Lewy bodies: Implications for the pathogenesis of Parkinson disease and Lewy body dementia. Archives of Neurology, 55, 151-152.
    • (1998) Archives of Neurology , vol.55 , pp. 151-152
    • Trojanowski, J.1    Lee, V.2
  • 108
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative diseases
    • Ross, R. A., & Poirier, M. A. (2004). Protein aggregation and neurodegenerative diseases. Nature Medicine, 10, S10-S17.
    • (2004) Nature Medicine , vol.10
    • Ross, R.A.1    Poirier, M.A.2
  • 109
    • 0035115942 scopus 로고    scopus 로고
    • Progression of symptoms in the early and middle stages of Huntington disease
    • Kirkwood, S. C., Su, J. L., Conneally, P., & Foroud, T. (2001). Progression of symptoms in the early and middle stages of Huntington disease. Archives of Neurology, 58, 273-278.
    • (2001) Archives of Neurology , vol.58 , pp. 273-278
    • Kirkwood, S.C.1    Su, J.L.2    Conneally, P.3    Foroud, T.4
  • 110
    • 18544410106 scopus 로고    scopus 로고
    • Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation
    • Davies, S. W., Turmaine, M., Cozens, B. A., et al. (1997). Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell, 90, 537-548.
    • (1997) Cell , vol.90 , pp. 537-548
    • Davies, S.W.1    Turmaine, M.2    Cozens, B.A.3
  • 112
    • 0035997016 scopus 로고    scopus 로고
    • Protein aggregation in Huntington's disease
    • Hoffner, G., & Djian, P. (2002). Protein aggregation in Huntington's disease. Biochimie, 84, 273-278.
    • (2002) Biochimie , vol.84 , pp. 273-278
    • Hoffner, G.1    Djian, P.2
  • 113
    • 0032450856 scopus 로고    scopus 로고
    • Amyloid formation by mutant huntingtin: Threshold, progressivity and recruitment of normal polyglutamine proteins
    • Huang, C. C., Faber, P. W., Persichetti, F., et al. (1998). Amyloid formation by mutant huntingtin: Threshold, progressivity and recruitment of normal polyglutamine proteins. Somatic Cell and Molecular Genetics, 24, 217-233.
    • (1998) Somatic Cell and Molecular Genetics , vol.24 , pp. 217-233
    • Huang, C.C.1    Faber, P.W.2    Persichetti, F.3
  • 116
    • 0019850528 scopus 로고
    • Amyotrophic lateral sclerosis and its association with dementia, Parkinsonism and other neurological disorders: A review
    • Hudson, A. J. (1981). Amyotrophic lateral sclerosis and its association with dementia, Parkinsonism and other neurological disorders: A review. Brain, 104, 217-247.
    • (1981) Brain , vol.104 , pp. 217-247
    • Hudson, A.J.1
  • 117
    • 34249751076 scopus 로고    scopus 로고
    • TDP43 is a human low molecular weight neurofilament (hNFL) mRNAbinding protein
    • Strong, M. J., Volkening, K., Hammond, R., et al. (2007). TDP43 is a human low molecular weight neurofilament (hNFL) mRNAbinding protein. Molecular and Cellular Neuroscience, 35, 320-327.
    • (2007) Molecular and Cellular Neuroscience , vol.35 , pp. 320-327
    • Strong, M.J.1    Volkening, K.2    Hammond, R.3
  • 118
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in fronto temporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann, M., Sampathu, D. M., Kwong, L. K., et al. (2006). Ubiquitinated TDP-43 in fronto temporal lobar degeneration and amyotrophic lateral sclerosis. Science, 314, 130-133.
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1    Sampathu, D.M.2    Kwong, L.K.3
  • 119
    • 33750716074 scopus 로고    scopus 로고
    • TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Arai, T., Hasegawa, M., Akiyama, H., et al. (2006). TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochemical and Biophysical Research Communications, 351, 602-611.
    • (2006) Biochemical and Biophysical Research Communications , vol.351 , pp. 602-611
    • Arai, T.1    Hasegawa, M.2    Akiyama, H.3
  • 120
    • 34249946466 scopus 로고    scopus 로고
    • Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations
    • Mackenzie, I. R., Bigio, E. H., Ince, P. G., et al. (2007). Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations. Annals of Neurology, 61, 427-434.
    • (2007) Annals of Neurology , vol.61 , pp. 427-434
    • Mackenzie, I.R.1    Bigio, E.H.2    Ince, P.G.3
  • 121
    • 0032199307 scopus 로고    scopus 로고
    • Cataract as a conformational disease: The Maillard reaction, alpha-crystallin and chemotherapy
    • Crabbe, M. J. (1998). Cataract as a conformational disease: The Maillard reaction, alpha-crystallin and chemotherapy. Cellular and Molecular Biology, 44, 1047-1050.
    • (1998) Cellular and Molecular Biology , vol.44 , pp. 1047-1050
    • Crabbe, M.J.1
  • 122
    • 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., & Truscott, R. J. (1997). Molecular evidence for the involvement of alpha crystallin in the coloration/crosslinking of crystallins in age related nuclear cataract. Experimental Eye Research, 65, 835-840.
    • (1997) Experimental Eye Research , vol.65 , pp. 835-840
    • Chen, Y.C.1    Reid, G.E.2    Simpson, R.J.3    Truscott, R.J.4
  • 124
  • 125
    • 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., & Ruan, Y. S. (2008). Identification of the primary targets of carbamylation in bovine lens proteins by mass spectrometry. Current Eye Research, 33, 963-976.
    • (2008) Current Eye Research , 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
  • 126
    • 0032941652 scopus 로고    scopus 로고
    • Cataract mutations and lens development
    • Graw, J. (1999). Cataract mutations and lens development. Progress in Retinal and Eye Research, 18, 235-267.
    • (1999) Progress in Retinal and Eye Research , vol.18 , pp. 235-267
    • Graw, J.1
  • 127
    • 61849122908 scopus 로고    scopus 로고
    • Genetics of crystallins: Cataract and beyond
    • Graw, J. (2009). Genetics of crystallins: Cataract and beyond. Experimental Eye Research, 88, 173-189.
    • (2009) Experimental Eye Research , vol.88 , pp. 173-189
    • Graw, J.1
  • 128
    • 65249160170 scopus 로고    scopus 로고
    • The structure of the cataract-causing P23T mutant of human gamma d-crystallin exhibits distinctive local conformational and dynamic changes
    • Jung, J., Byeon, I. J., Wang, Y., King, J., & Gronenborn, A. M. (2009). The structure of the cataract-causing P23T mutant of human gamma d-crystallin exhibits distinctive local conformational and dynamic changes. Biochemistry, 48, 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
  • 129
    • 18744404774 scopus 로고    scopus 로고
    • Altered aggregation properties of mutant g-crystallins cause inherited cataract
    • Sandilands, A., Hutcheson, A. M., Long, H. A., et al. (2002). Altered aggregation properties of mutant g-crystallins cause inherited cataract. EMBO Journal, 21, 6005-6014.
    • (2002) EMBO Journal , vol.21 , pp. 6005-6014
    • Sandilands, A.1    Hutcheson, A.M.2    Long, H.A.3
  • 131
    • 0029870085 scopus 로고    scopus 로고
    • Cystic fibrosis airway epithelia fail to kill bacteria because of abnormal airway surface fluid
    • Smith, J. J., Travis, S. M., Greenberg, E. P., & Welsh, M. J. (1996). Cystic fibrosis airway epithelia fail to kill bacteria because of abnormal airway surface fluid. Cell, 85, 229-236.
    • (1996) Cell , vol.85 , pp. 229-236
    • Smith, J.J.1    Travis, S.M.2    Greenberg, E.P.3    Welsh, M.J.4
  • 133
    • 0025349031 scopus 로고
    • Cystic fibrosis: A disease in electrolyte transport
    • Quinton, P. M. (1990). Cystic fibrosis: A disease in electrolyte transport. FASEB Journal, 4, 2709-2717.
    • (1990) FASEB Journal , vol.4 , pp. 2709-2717
    • Quinton, P.M.1
  • 134
    • 0026649584 scopus 로고
    • The cystic fibrosis transmembrane conductance regulator
    • Thomas, P. J., et al. (1992). The cystic fibrosis transmembrane conductance regulator. Journal of Biological Chemistry, 267, 5727-5730.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 5727-5730
    • Thomas, P.J.1
  • 136
    • 0035349804 scopus 로고    scopus 로고
    • Inhibition of Alzheimer's disease-amyloid aggregation, neurotoxicity, and in vivo deposition by nitrophenols: Implications for Alzheimer's therapy
    • De Felice, F., Houzel, J. C., Garcia-Abreu, J., Louzada, P., Afonso, R. C., & Meirelles, M. N. (2001). Inhibition of Alzheimer's disease-amyloid aggregation, neurotoxicity, and in vivo deposition by nitrophenols: Implications for Alzheimer's therapy. FASEB Journal, 15, 1297-1299.
    • (2001) FASEB Journal , vol.15 , pp. 1297-1299
    • de Felice, F.1    Houzel, J.C.2    Garcia-Abreu, J.3    Louzada, P.4    Afonso, R.C.5    Meirelles, M.N.6
  • 137
    • 0036544598 scopus 로고    scopus 로고
    • Inhibition of transthyretin amyloid fibril formation by 2,4-dinitrophenol through tetramer stabilization
    • Raghu, P., Reddy, G. B., & Sivakumar, B. (2002). Inhibition of transthyretin amyloid fibril formation by 2, 4-dinitrophenol through tetramer stabilization. Archives of Biochemistry and Biophysics, 400, 43-47.
    • (2002) Archives of Biochemistry and Biophysics , vol.400 , pp. 43-47
    • Raghu, P.1    Reddy, G.B.2    Sivakumar, B.3


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