메뉴 건너뛰기




Volumn 15, Issue 6, 2014, Pages 384-396

The amyloid state and its association with protein misfolding diseases

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; OLIGOMER; PEPTIDES AND PROTEINS; SYNUCLEIN;

EID: 84901355639     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm3810     Document Type: Review
Times cited : (1856)

References (180)
  • 1
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • DOI 10.1038/nature02261
    • Dobson, C. M. Protein folding and misfolding. Nature 426, 884-890 (2003). (Pubitemid 38056880)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 884-890
    • Dobson, C.M.1
  • 2
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy, J. & Selkoe, D. J. Medicine - the amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356 (2002). (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 3
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • DOI 10.1126/science.1141448
    • Balch, W. E., Morimoto, R. I., Dillin, A. & Kelly, J. W. Adapting proteostasis for disease intervention. Science 319, 916-919 (2008). (Pubitemid 351263754)
    • (2008) Science , vol.319 , Issue.5865 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 4
    • 33746698975 scopus 로고    scopus 로고
    • The physical basis of how prion conformations determine strain phenotypes
    • DOI 10.1038/nature04922, PII NATURE04922
    • Tanaka, M., Collins, S. R., Toyama, B. H. & Weissman, J. S. The physical basis of how prion conformations determine strain phenotypes. Nature 442, 585-589 (2006). (Pubitemid 44167919)
    • (2006) Nature , vol.442 , Issue.7102 , pp. 585-589
    • Tanaka, M.1    Collins, S.R.2    Toyama, B.H.3    Weissman, J.S.4
  • 5
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • Chiti, F. & Dobson, C. M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Bioch. 75, 333-366 (2006). (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 6
    • 79961211353 scopus 로고    scopus 로고
    • Nanomechanics of functional and pathological amyloid materials
    • Knowles, T. P. J. & Buehler, M. J. Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469-479 (2011).
    • (2011) Nature Nanotech. , vol.6 , pp. 469-479
    • Knowles, T.P.J.1    Buehler, M.J.2
  • 7
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • DOI 10.1038/nrm2101, PII NRM2101
    • Haass, C. & Selkoe, D. J. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nature Rev. Mol. Cell. Biol. 8, 101-112 (2007). (Pubitemid 46432529)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 8
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of proteins in human diseases
    • Eisenberg, D. & Jucker, M. The amyloid state of proteins in human diseases. Cell 148, 1188-1203 (2012).
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 9
    • 79952747862 scopus 로고    scopus 로고
    • Alzheimer's disease
    • Ballard, C. et al. Alzheimer's disease. Lancet 377, 1019-1031 (2011).
    • (2011) Lancet , vol.377 , pp. 1019-1031
    • Ballard, C.1
  • 10
    • 75449102536 scopus 로고    scopus 로고
    • Mechanisms of disease Alzheimer's disease
    • Querfurth, H. W. & LaFerla, F. M. Mechanisms of disease Alzheimer's disease. N. Engl. J. Med. 362, 329-344 (2010).
    • (2010) N. Engl. J. Med. , vol.362 , pp. 329-344
    • Querfurth, H.W.1    Laferla, F.M.2
  • 12
    • 78951482115 scopus 로고    scopus 로고
    • Alzheimer's disease international
    • Alzheimer's disease international. World Alzheimer report (2010).
    • (2010) World Alzheimer Report
  • 15
    • 84879852246 scopus 로고    scopus 로고
    • Alzheimer's disease: Facts and figures
    • Alzheimer's disease: Facts and figures. Alzheimer's association (2012).
    • (2012) Alzheimer's Association
  • 17
    • 84861563520 scopus 로고    scopus 로고
    • Direct observation of the interconversion of normal and toxic forms of α-synuclein
    • Cremades, N. et al. Direct observation of the interconversion of normal and toxic forms of α-synuclein. Cell 149, 1048-1059 (2012).
    • (2012) Cell , vol.149 , pp. 1048-1059
    • Cremades, N.1
  • 18
    • 84878994873 scopus 로고    scopus 로고
    • Proliferation of amyloid-β 42 aggregates occurs through a secondary nucleation mechanism
    • Cohen, S. I. A. et al. Proliferation of amyloid-β 42 aggregates occurs through a secondary nucleation mechanism. Proc. Natl Acad. Sci. USA 110, 9758-9763 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 9758-9763
    • Cohen, S.I.A.1
  • 19
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-β protein assembly in the brain impairs memory
    • Lesne, S. et al. A specific amyloid-β protein assembly in the brain impairs memory. Nature 440, 352-357 (2006).
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesne, S.1
  • 20
    • 75349097530 scopus 로고    scopus 로고
    • A causative link between the structure of aberrant protein oligomers and their toxicity
    • Campioni, S. et al. A causative link between the structure of aberrant protein oligomers and their toxicity. Nature Chem. Biol. 6, 140-147 (2010).
    • (2010) Nature Chem. Biol. , vol.6 , pp. 140-147
    • Campioni, S.1
  • 22
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • DOI 10.1146/annurev.neuro.26.010302.081142
    • Caughey, B. & Lansbury, P. T. Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26, 267-298 (2003). (Pubitemid 37064935)
    • (2003) Annual Review of Neuroscience , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury Jr., P.T.2
  • 23
    • 14644442872 scopus 로고    scopus 로고
    • Intraneuronal Aβ causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice
    • DOI 10.1016/j.neuron.2005.01.040
    • Billings, L. M., Oddo, S., Green, K. N., McGaugh, J. L. & La Ferla, F. M. Intraneuronal a β causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice. Neuron 45, 675-688 (2005). (Pubitemid 40320703)
    • (2005) Neuron , vol.45 , Issue.5 , pp. 675-688
    • Billings, L.M.1    Oddo, S.2    Green, K.N.3    McGaugh, J.L.4    LaFerla, F.M.5
  • 24
    • 79952742454 scopus 로고    scopus 로고
    • In vivo demonstration that α-synuclein oligomers are toxic
    • Winner, B. et al. In vivo demonstration that α-synuclein oligomers are toxic. Proc. Natl Acad. Sci. USA 108, 4194-4199 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 4194-4199
    • Winner, B.1
  • 25
    • 62649174753 scopus 로고    scopus 로고
    • Oligomeric amyloid β associates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques
    • Koffie, R. M. et al. Oligomeric amyloid β associates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques. Proc. Natl Acad. Sci. USA 106, 4012-4017 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 4012-4017
    • Koffie, R.M.1
  • 26
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • DOI 10.1016/S0968-0004(99)01445-0, PII S0968000499014450
    • Dobson, C. M. Protein misfolding, evolution and disease. Trends Bioch. Sci. 24, 329-332 (1999). (Pubitemid 29421804)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.9 , pp. 329-332
    • Dobson, C.M.1
  • 27
    • 84864288105 scopus 로고    scopus 로고
    • On the possible amyloid origin of protein folds
    • Greenwald, J. & Riek, R. On the possible amyloid origin of protein folds. J. Mol. Biol. 421, 417-426 (2012).
    • (2012) J. Mol. Biol. , vol.421 , pp. 417-426
    • Greenwald, J.1    Riek, R.2
  • 28
    • 21744439797 scopus 로고    scopus 로고
    • A model for the role of short self-assembled peptides in the very early stages of the origin of life
    • DOI 10.1096/fj.04-3256hyp
    • Carny, O. & Gazit, E. A model for the role of short self-assembled peptides in the very early stages of the origin of life. FASEB J. 19, 1051-1055 (2005). (Pubitemid 40946429)
    • (2005) FASEB Journal , vol.19 , Issue.9 , pp. 1051-1055
    • Carny, O.1    Gazit, E.2
  • 29
    • 84870755228 scopus 로고    scopus 로고
    • Microbial manipulation of the amyloid fold
    • De Pas, W. H. & Chapman, M. R. Microbial manipulation of the amyloid fold. Res. Microbiol. 163, 592-606 (2012).
    • (2012) Res. Microbiol. , vol.163 , pp. 592-606
    • De Pas, W.H.1    Chapman, M.R.2
  • 30
    • 34247899121 scopus 로고    scopus 로고
    • Functional amyloid - from bacteria to humans
    • DOI 10.1016/j.tibs.2007.03.003, PII S096800040700059X
    • Fowler, D. M., Koulov, A. V., Balch, W. E. & Kelly, J. W. Functional amyloid - from bacteria to humans. Trends Bioch. Sci. 32, 217-224 (2007). (Pubitemid 46694328)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.5 , pp. 217-224
    • Fowler, D.M.1    Koulov, A.V.2    Balch, W.E.3    Kelly, J.W.4
  • 31
    • 0036845354 scopus 로고    scopus 로고
    • The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
    • DOI 10.1093/emboj/cdf573
    • Fandrich, M. & Dobson, C. M. The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBO J. 21, 5682-5690 (2002). (Pubitemid 35315268)
    • (2002) EMBO Journal , vol.21 , Issue.21 , pp. 5682-5690
    • Fandrich, M.1    Dobson, C.M.2
  • 32
    • 80052607718 scopus 로고    scopus 로고
    • Observation of spatial propagation of amyloid assembly from single nuclei
    • Knowles, T. P. J. et al. Observation of spatial propagation of amyloid assembly from single nuclei. Proc. Natl Acad. Sci. USA 108, 14746-14751 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 14746-14751
    • Knowles, T.P.J.1
  • 33
    • 0001419932 scopus 로고
    • The X-ray interpretation of denaturation and the structure of the seed globulins
    • Astbury, W. T., Dickinson, S. & Bailey, K. The X-ray interpretation of denaturation and the structure of the seed globulins. Biochem. J. 29, 2351-2360 (1935).
    • (1935) Biochem. J. , vol.29 , pp. 2351-2360
    • Astbury, W.T.1    Dickinson, S.2    Bailey, K.3
  • 34
    • 0001266102 scopus 로고
    • 3-dimensional model of the myoglobin molecule obtained by X-ray analysis
    • Kendrew, J. C. et al. 3-dimensional model of the myoglobin molecule obtained by X-ray analysis. Nature 181, 662-666 (1958).
    • (1958) Nature , vol.181 , pp. 662-666
    • Kendrew, J.C.1
  • 36
    • 66249144426 scopus 로고    scopus 로고
    • The structure and function of g-protein-coupled receptors
    • Rosenbaum, D. M., Rasmussen, S. G. F. & Kobilka, B. K. The structure and function of g-protein-coupled receptors. Nature 459, 356-363 (2009).
    • (2009) Nature , vol.459 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.F.2    Kobilka, B.K.3
  • 37
    • 0015859467 scopus 로고
    • Principles that govern folding of protein chains
    • Anfinsen, C. B. Principles that govern folding of protein chains. Science 181, 223-230 (1973).
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 38
    • 1842298212 scopus 로고    scopus 로고
    • From levinthal to pathways to funnels
    • DOI 10.1038/nsb0197-10
    • Dill, K. A. & Chan, H. S. From Levinthal to pathways to funnels. Nature Struct. Biol. 4, 10-19 (1997). (Pubitemid 27020916)
    • (1997) Nature Structural Biology , vol.4 , Issue.1 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 40
    • 0344301982 scopus 로고    scopus 로고
    • Protein folding: A perspective from theory and experiment
    • DOI 10.1002/(SICI)1521-3773(19980420)37:7<868::AID-ANIE868>3.0. CO;2-H
    • Dobson, C. M., Sali, A. & Karplus, M. Protein folding: a perspective from theory and experiment. Angew. Chem. Int. Ed. 37, 868-893 (1998). (Pubitemid 28228882)
    • (1998) Angewandte Chemie - International Edition , vol.37 , Issue.7 , pp. 868-893
    • Dobson, C.M.1    Sali, A.2    Karplus, M.3
  • 41
    • 80052555139 scopus 로고    scopus 로고
    • Metastability of native proteins and the phenomenon of amyloid formation
    • Baldwin, A. J. et al. Metastability of native proteins and the phenomenon of amyloid formation. J. Am. Chem. Soc. 133, 14160-14163 (2011).
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 14160-14163
    • Baldwin, A.J.1
  • 42
    • 0037126833 scopus 로고    scopus 로고
    • The "correctly folded" state of proteins: Is it a metastable state?
    • DOI 10.1002/1521-3773(20020118)41:2<257::AID-ANIE257>3.0.CO;2-M
    • Gazit, E. The "correctly folded" state of proteins: is it a metastable state. Angew. Chem. Int. Ed. 41, 257-259 (2002). (Pubitemid 34118066)
    • (2002) Angewandte Chemie - International Edition , vol.41 , Issue.2 , pp. 257-259
    • Gazit, E.1
  • 43
    • 84863958621 scopus 로고    scopus 로고
    • Protein solubility and protein homeostasis: A generic view of protein misfolding disorders
    • Vendruscolo, M., Knowles, T. P. J. & Dobson, C. M. Protein solubility and protein homeostasis: A generic view of protein misfolding disorders. Cold Spring Harb. Perspect. Biol. 3, a010454 (2011).
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3
    • Vendruscolo, M.1    Knowles, T.P.J.2    Dobson, C.M.3
  • 44
    • 84897129156 scopus 로고    scopus 로고
    • Differential scales of protein quality control
    • Wolff, S., Weissman, J. S. & Dillin, A. Differential scales of protein quality control. Cell 157, 52-64 (2014).
    • (2014) Cell , vol.157 , pp. 52-64
    • Wolff, S.1    Weissman, J.S.2    Dillin, A.3
  • 45
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • DOI 10.1038/nrm1589
    • Dyson, H. J. & Wright, P. E. Intrinsically unstructured proteins and their functions. Nature Rev. Mol. Cell Biol. 6, 197-208 (2005). (Pubitemid 40314921)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 46
    • 77949916296 scopus 로고    scopus 로고
    • Understanding protein non-folding
    • Uversky, V. N. & Dunker, A. K. Understanding protein non-folding. Biochim. Biophys. Acta 1804, 1231-1264 (2010).
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 1231-1264
    • Uversky, V.N.1    Dunker, A.K.2
  • 48
    • 10744219665 scopus 로고    scopus 로고
    • Solution NMR studies of the Aβ(1-40) and Aβ(1-42) peptides establish that the Met35 oxidation state affects the mechanism of amyloid formation
    • Hou, L. M. et al. Solution NMR studies of the Aβ(1-40) and Aβ(1-42) peptides establish that the Met35 oxidation state affects the mechanism of amyloid formation. J. Am. Chem. Soc. 126, 1992-2005 (2004).
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 1992-2005
    • Hou, L.M.1
  • 49
    • 84891810469 scopus 로고    scopus 로고
    • PE-DB: A database of structural ensembles of intrinsically disordered and of unfolded proteins
    • Varadi, M. et al. pE-DB: A database of structural ensembles of intrinsically disordered and of unfolded proteins. Nucl. Acids Res. 42, D326-D335 (2014).
    • (2014) Nucl. Acids Res. , vol.42
    • Varadi, M.1
  • 50
    • 44949219079 scopus 로고    scopus 로고
    • Prediction of aggregation-prone regions in structured proteins
    • Tartaglia, G. G. et al. Prediction of aggregation-prone regions in structured proteins. J. Mol. Biol. 380, 425-436 (2008).
    • (2008) J. Mol. Biol. , vol.380 , pp. 425-436
    • Tartaglia, G.G.1
  • 52
    • 0030882856 scopus 로고    scopus 로고
    • α-synuclein in Lewy bodies
    • Spillantini, M. G. et al. α-synuclein in Lewy bodies. Nature 388, 839-840 (1997).
    • (1997) Nature , vol.388 , pp. 839-840
    • Spillantini, M.G.1
  • 53
    • 0023192941 scopus 로고
    • Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells
    • DOI 10.1073/pnas.84.11.3881
    • Westermark, P. et al. Amyloid fibrils in human insulinoma and islets of langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells. Proc. Natl Acad. Sci. USA 84, 3881-3885 (1987). (Pubitemid 17088383)
    • (1987) Proceedings of the National Academy of Sciences of the United States of America , vol.84 , Issue.11 , pp. 3881-3885
    • Westermark, P.1    Wernstedt, C.2    Wilander, E.3
  • 55
    • 57749098600 scopus 로고    scopus 로고
    • Amyloid formation by globular proteins under native conditions
    • Chiti, F. & Dobson, C. M. Amyloid formation by globular proteins under native conditions. Nature Chem. Biol. 5, 15-22 (2009).
    • (2009) Nature Chem. Biol. , vol.5 , pp. 15-22
    • Chiti, F.1    Dobson, C.M.2
  • 56
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • DOI 10.1016/S0959-440X(98)80016-X
    • Kelly, J. W. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 8, 101-106 (1998). (Pubitemid 28107921)
    • (1998) Current Opinion in Structural Biology , vol.8 , Issue.1 , pp. 101-106
    • Kelly, J.W.1
  • 57
    • 84875470470 scopus 로고    scopus 로고
    • Structural biology: Protein self-assembly intermediates
    • Vendruscolo, M. & Dobson, C. M. Structural biology: protein self-assembly intermediates. Nature Chem. Biol. 9, 216-217 (2013).
    • (2013) Nature Chem. Biol. , vol.9 , pp. 216-217
    • Vendruscolo, M.1    Dobson, C.M.2
  • 58
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert, W. & Herrmann, J. M. Translocation of proteins into mitochondria. Annu. Rev. Bioch. 76, 723-749 (2007).
    • (2007) Annu. Rev. Bioch. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 59
    • 68749112707 scopus 로고    scopus 로고
    • Importing mitochondrial proteins: Machineries and mechanisms
    • Chacinska, A., Koehler, C. M., Milenkovic, D., Lithgow, T. & Pfanner, N. Importing mitochondrial proteins: machineries and mechanisms. Cell 138, 628-644 (2009).
    • (2009) Cell , vol.138 , pp. 628-644
    • Chacinska, A.1    Koehler, C.M.2    Milenkovic, D.3    Lithgow, T.4    Pfanner, N.5
  • 60
    • 79959846745 scopus 로고    scopus 로고
    • Long unfolded linkers facilitate membrane protein import through the nuclear pore complex
    • Meinema, A. C. et al. Long unfolded linkers facilitate membrane protein import through the nuclear pore complex. Science 333, 90-93 (2011).
    • (2011) Science , vol.333 , pp. 90-93
    • Meinema, A.C.1
  • 61
    • 84879920420 scopus 로고    scopus 로고
    • PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone
    • Park, S. H. et al. PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone. Cell 154, 134-145 (2013).
    • (2013) Cell , vol.154 , pp. 134-145
    • Park, S.H.1
  • 62
    • 75749107907 scopus 로고    scopus 로고
    • Cell mechanics and the cytoskeleton
    • Fletcher, D. A. & Mullins, D. Cell mechanics and the cytoskeleton. Nature 463, 485-492 (2010).
    • (2010) Nature , vol.463 , pp. 485-492
    • Fletcher, D.A.1    Mullins, D.2
  • 63
    • 77955111796 scopus 로고    scopus 로고
    • New opportunities for an ancient material
    • Omenetto, F. G. & Kaplan, D. L. New opportunities for an ancient material. Science 329, 528-531 (2010).
    • (2010) Science , vol.329 , pp. 528-531
    • Omenetto, F.G.1    Kaplan, D.L.2
  • 64
    • 0037171856 scopus 로고    scopus 로고
    • Insights into phase transition kinetics from colloid science
    • DOI 10.1038/416811a
    • Anderson, V. J. & Lekkerkerker, H. N. W. Insights into phase transition kinetics from colloid science. Nature 416, 811-815 (2002). (Pubitemid 34453731)
    • (2002) Nature , vol.416 , Issue.6883 , pp. 811-815
    • Anderson, V.J.1    Lekkerkerker, H.N.W.2
  • 67
    • 0033849738 scopus 로고    scopus 로고
    • Review: History of the amyloid fibril
    • Sipe, J. D. & Cohen, A. S. Review: History of the amyloid fibril. J. Struct. Biol. 130, 88-98 (2000).
    • (2000) J. Struct. Biol. , vol.130 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.S.2
  • 68
    • 84863988708 scopus 로고    scopus 로고
    • A molecular history of the amyloidoses
    • Buxbaum, J. N. & Linke, R. P. A molecular history of the amyloidoses. J. Mol. Biol. 421, 142-159 (2012).
    • (2012) J. Mol. Biol. , vol.421 , pp. 142-159
    • Buxbaum, J.N.1    Linke, R.P.2
  • 69
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • DOI 10.1007/s00109-003-0464-5
    • Stefani, M. & Dobson, C. M. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 81, 678-699 (2003). (Pubitemid 37491594)
    • (2003) Journal of Molecular Medicine , vol.81 , Issue.11 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 71
    • 18144406844 scopus 로고    scopus 로고
    • Proteomic analysis of neurofibrillary tangles in Alzheimer disease identifies GAPDH as a detergent-insoluble paired helical filament tau binding protein
    • DOI 10.1096/fj.04-3210fje
    • Wang, Q. et al. Proteomic analysis of neurofibrillary tangles in Alzheimer disease identifies GAPDH as a detergent-insoluble paired helical filament tau binding protein. FASEB J. 19, 869-871 (2005). (Pubitemid 40617412)
    • (2005) FASEB Journal , vol.19 , Issue.7 , pp. 869-871
    • Wang, Q.1    Woltjer, R.L.2    Cimino, P.J.3    Pan, C.4    Montine, K.S.5    Zhang, J.6    Montine, T.J.7
  • 75
    • 84875871051 scopus 로고    scopus 로고
    • Atomic structure and hierarchical assembly of a cross-β amyloid fibril
    • Fitzpatrick, A. W. P. et al. Atomic structure and hierarchical assembly of a cross-β amyloid fibril. Proc. Natl Acad. Sci. USA 110, 5468-5473 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 5468-5473
    • Fitzpatrick, A.W.P.1
  • 77
    • 40849120669 scopus 로고    scopus 로고
    • Amyloid fibrils of the HET-s(218-289) prion form a β solenoid with a triangular hydrophobic core
    • DOI 10.1126/science.1151839
    • Wasmer, C. et al. Amyloid fibrils of the HET-s(218-289) prion form a β solenoid with a triangular hydrophobic core. Science 319, 1523-1526 (2008). (Pubitemid 351398180)
    • (2008) Science , vol.319 , Issue.5869 , pp. 1523-1526
    • Wasmer, C.1    Lange, A.2    Van Melckebeke, H.3    Siemer, A.B.4    Riek, R.5    Meier, B.H.6
  • 78
    • 28444442999 scopus 로고    scopus 로고
    • 3D structure of Alzheimer's amyloid-β(1-42) fibrils
    • Luhrs, T. et al. 3D structure of Alzheimer's amyloid-β(1-42) fibrils. Proc. Natl Acad. Sci. USA 102, 17342-17347 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 17342-17347
    • Luhrs, T.1
  • 82
    • 57149102288 scopus 로고    scopus 로고
    • A generic mechanism of emergence of amyloid protofilaments from disordered oligomeric aggregates
    • Auer, S., Meersman, F., Dobson, C. M. & Vendruscolo, M. A generic mechanism of emergence of amyloid protofilaments from disordered oligomeric aggregates. PLoS Comp. Biol. 4, e1000222 (2008).
    • (2008) PLoS Comp. Biol. , vol.4
    • Auer, S.1    Meersman, F.2    Dobson, C.M.3    Vendruscolo, M.4
  • 83
    • 79953765150 scopus 로고    scopus 로고
    • Solid-state NMR studies of amyloid fibril structure
    • Tycko, R. Solid-state NMR studies of amyloid fibril structure. Annu. Rev. Phys. Chem. 62, 279-299 (2011).
    • (2011) Annu. Rev. Phys. Chem. , vol.62 , pp. 279-299
    • Tycko, R.1
  • 86
    • 37549063068 scopus 로고    scopus 로고
    • Role of intermolecular forces in defining material properties of protein nanofibrils
    • Knowles, T. P. et al. Role of intermolecular forces in defining material properties of protein nanofibrils. Science 318, 1900-1903 (2007).
    • (2007) Science , vol.318 , pp. 1900-1903
    • Knowles, T.P.1
  • 87
    • 20444474976 scopus 로고    scopus 로고
    • Structural insights into a yeast prion illuminate nucleation and strain diversity
    • DOI 10.1038/nature03679
    • Krishnan, R. & Lindquist, S. L. Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 435, 765-772 (2005). (Pubitemid 40839721)
    • (2005) Nature , vol.435 , Issue.7043 , pp. 765-772
    • Krishnan, R.1    Lindquist, S.L.2
  • 88
    • 36049020231 scopus 로고    scopus 로고
    • A general model of prion strains and their pathogenicity
    • DOI 10.1126/science.1138718
    • Collinge, J. & Clarke, A. R. A general model of prion strains and their pathogenicity. Science 318, 930-936 (2007). (Pubitemid 350098981)
    • (2007) Science , vol.318 , Issue.5852 , pp. 930-936
    • Collinge, J.1    Clarke, A.R.2
  • 89
    • 77249122579 scopus 로고    scopus 로고
    • Prions, protein homeostasis, and phenotypic diversity
    • Halfmann, R., Alberti, S. & Lindquist, S. Prions, protein homeostasis, and phenotypic diversity. Trends Cell Biol. 20, 125-133 (2010).
    • (2010) Trends Cell Biol. , vol.20 , pp. 125-133
    • Halfmann, R.1    Alberti, S.2    Lindquist, S.3
  • 90
    • 28644437048 scopus 로고    scopus 로고
    • The importance of sequence diversity in the aggregation and evolution of proteins
    • DOI 10.1038/nature04195
    • Wright, C. F., Teichmann, S. A., Clarke, J. & Dobson, C. M. The importance of sequence diversity in the aggregation and evolution of proteins. Nature 438, 878-881 (2005). (Pubitemid 41753072)
    • (2005) Nature , vol.438 , Issue.7069 , pp. 878-881
    • Wright, C.F.1    Teichmann, S.A.2    Clarke, J.3    Dobson, C.M.4
  • 91
    • 84867320649 scopus 로고    scopus 로고
    • Twisting transition between crystalline and fibrillar phases of aggregated peptides
    • Knowles, T. P. J. et al. Twisting transition between crystalline and fibrillar phases of aggregated peptides. Phys. Rev. Lett. 109, 158101 (2012).
    • (2012) Phys. Rev. Lett. , vol.109 , pp. 158101
    • Knowles, T.P.J.1
  • 93
    • 34247882072 scopus 로고    scopus 로고
    • Life on the edge: A link between gene expression levels and aggregation rates of human proteins
    • DOI 10.1016/j.tibs.2007.03.005, PII S0968000407000618
    • Tartaglia, G. G., Pechmann, S., Dobson, C. M. & Vendruscolo, M. Life on the edge: a link between gene expression levels and aggregation rates of human proteins. Trends Bioch. Sci. 32, 204-206 (2007). (Pubitemid 46694330)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.5 , pp. 204-206
    • Tartaglia, G.G.1    Pechmann, S.2    Dobson, C.M.3    Vendruscolo, M.4
  • 94
    • 28844441969 scopus 로고    scopus 로고
    • Secondary structure of α-synuclein oligomers: Characterization by Raman and atomic force microscopy
    • DOI 10.1016/j.jmb.2005.10.071, PII S0022283605013318
    • Apetri, M. M., Maiti, N. C., Zagorski, M. G., Carey, P. R. & Anderson, V. E. Secondary structure of α -synuclein oligomers: characterization by Raman and atomic force microscopy. J. Mol. Biol. 355, 63-71 (2006). (Pubitemid 41774139)
    • (2006) Journal of Molecular Biology , vol.355 , Issue.1 , pp. 63-71
    • Apetri, M.M.1    Maiti, N.C.2    Zagorski, M.G.3    Carey, P.R.4    Anderson, V.E.5
  • 95
    • 0033869084 scopus 로고    scopus 로고
    • Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry
    • Nettleton, E. J. et al. Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry. Bioph. J. 79, 1053-1065 (2000). (Pubitemid 30626196)
    • (2000) Biophysical Journal , vol.79 , Issue.2 , pp. 1053-1065
    • Nettleton, E.J.1    Tito, P.2    Sunde, M.3    Bouchard, M.4    Dobson, C.M.5    Robinson, C.V.6
  • 96
    • 77951081386 scopus 로고    scopus 로고
    • 2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry
    • 2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry. Proc. Natl Acad. Sci. USA 107, 6794-6798 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 6794-6798
    • Smith, D.P.1    Radford, S.E.2    Ashcroft, A.E.3
  • 97
    • 67849106670 scopus 로고    scopus 로고
    • Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease
    • Bernstein, S. L. et al. Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease. Nature Chem. 1, 326-331 (2009).
    • (2009) Nature Chem. , vol.1 , pp. 326-331
    • Bernstein, S.L.1
  • 99
    • 84863981137 scopus 로고    scopus 로고
    • From macroscopic measurements to microscopic mechanisms of protein aggregation
    • Cohen, S. I. A., Vendruscolo, M., Dobson, C. M. & Knowles, T. P. J. From macroscopic measurements to microscopic mechanisms of protein aggregation. J. Mol. Biol. 421, 160-171 (2012).
    • (2012) J. Mol. Biol. , vol.421 , pp. 160-171
    • Cohen, S.I.A.1    Vendruscolo, M.2    Dobson, C.M.3    Knowles, T.P.J.4
  • 100
    • 72149118250 scopus 로고    scopus 로고
    • An analytical solution to the kinetics of breakable filament assembly
    • Knowles, T. P. J. et al. An analytical solution to the kinetics of breakable filament assembly. Science 326, 1533-1537 (2009).
    • (2009) Science , vol.326 , pp. 1533-1537
    • Knowles, T.P.J.1
  • 101
    • 0030806177 scopus 로고    scopus 로고
    • Enhancement of protein crystal nucleation by critical density fluctuations
    • DOI 10.1126/science.277.5334.1975
    • ten Wolde, P.R. & Frenkel, D. Enhancement of protein crystal nucleation by critical density fluctuations. Science 277, 1975-1978 (1997). (Pubitemid 27449135)
    • (1997) Science , vol.277 , Issue.5334 , pp. 1975-1978
    • Ten Wolde, P.R.1    Frenkel, D.2
  • 103
    • 80054024011 scopus 로고    scopus 로고
    • Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders
    • Jucker, M. & Walker, L. C. Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders. Ann. Neurol. 70, 532-540 (2011).
    • (2011) Ann. Neurol. , vol.70 , pp. 532-540
    • Jucker, M.1    Walker, L.C.2
  • 104
    • 33846005437 scopus 로고    scopus 로고
    • Absolute Correlation between Lag Time and Growth Rate in the Spontaneous Formation of Several Amyloid-like Aggregates and Fibrils
    • DOI 10.1016/j.jmb.2006.11.009, PII S0022283606015385
    • Fandrich, M. Absolute correlation between lag time and growth rate in the spontaneous formation of several amyloid-like aggregates and fibrils. J. Mol. Biol. 365, 1266-1270 (2007). (Pubitemid 46048846)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.5 , pp. 1266-1270
    • Fandrich, M.1
  • 105
    • 8844247180 scopus 로고    scopus 로고
    • Mechanism of prion propagation: Amyloid growth occurs by monomer addition
    • Collins, S. R., Douglass, A., Vale, R. D. & Weissman, J. S. Mechanism of prion propagation: amyloid growth occurs by monomer addition. PLoS Biol. 2, 1582-1590 (2004).
    • (2004) PLoS Biol. , vol.2 , pp. 1582-1590
    • Collins, S.R.1    Douglass, A.2    Vale, R.D.3    Weissman, J.S.4
  • 106
    • 84896689644 scopus 로고    scopus 로고
    • Single point mutations induce a switch in the molecular mechanism of the aggregation of the Alzheimer's disease associated Aβ42 peptide
    • Bolognesi, B. et al. Single point mutations induce a switch in the molecular mechanism of the aggregation of the Alzheimer's disease associated Aβ42 peptide. ACS Chem. Biol. 9, 378-382 (2013).
    • (2013) ACS Chem. Biol. , vol.9 , pp. 378-382
    • Bolognesi, B.1
  • 107
    • 77955566477 scopus 로고    scopus 로고
    • Plug-based microfluidics with defined surface chemistry to miniaturize and control aggregation of amyloidogenic peptides
    • Meier, M. et al. Plug-based microfluidics with defined surface chemistry to miniaturize and control aggregation of amyloidogenic peptides. Angew. Chem. Int. Ed. 121, 1515-1517 (2009).
    • (2009) Angew. Chem. Int. Ed. , vol.121 , pp. 1515-1517
    • Meier, M.1
  • 109
    • 80155157847 scopus 로고    scopus 로고
    • The seeds of neurodegeneration: Prion-like spreading in als
    • Polymenidou, M. & Cleveland, D. W. The seeds of neurodegeneration: prion-like spreading in als. Cell 147, 498-508 (2011).
    • (2011) Cell , vol.147 , pp. 498-508
    • Polymenidou, M.1    Cleveland, D.W.2
  • 110
    • 84896377600 scopus 로고    scopus 로고
    • Spatial propagation of protein polymerization
    • Cohen, S. et al. Spatial propagation of protein polymerization. Phys. Rev. Lett. 112, 098101 (2014).
    • (2014) Phys. Rev. Lett. , vol.112 , pp. 098101
    • Cohen, S.1
  • 111
    • 67649286622 scopus 로고    scopus 로고
    • Cell biology: Beyond the prion principle
    • Aguzzi, A. Cell biology: Beyond the prion principle. Nature 459, 924-925 (2009).
    • (2009) Nature , vol.459 , pp. 924-925
    • Aguzzi, A.1
  • 112
    • 72149125838 scopus 로고    scopus 로고
    • The transcellular spread of cytosolic amyloids, prions, and prionoids
    • Aguzzi, A. & Rajendran, L. The transcellular spread of cytosolic amyloids, prions, and prionoids. Neuron 64, 783-790 (2009).
    • (2009) Neuron , vol.64 , pp. 783-790
    • Aguzzi, A.1    Rajendran, L.2
  • 113
    • 84883688262 scopus 로고    scopus 로고
    • Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
    • Jucker, M. & Walker, L. C. Self-propagation of pathogenic protein aggregates in neurodegenerative diseases. Nature 501, 45-51 (2013).
    • (2013) Nature , vol.501 , pp. 45-51
    • Jucker, M.1    Walker, L.C.2
  • 114
    • 84874853965 scopus 로고    scopus 로고
    • Mechanisms of protein seeding in neurodegenerative diseases
    • Walker, L. C., Diamond, M. I., Duff, K. E. & Hyman, B. T. Mechanisms of protein seeding in neurodegenerative diseases. JAMA Neurol. 70, 304-310 (2013).
    • (2013) JAMA Neurol. , vol.70 , pp. 304-310
    • Walker, L.C.1    Diamond, M.I.2    Duff, K.E.3    Hyman, B.T.4
  • 115
    • 67650809307 scopus 로고    scopus 로고
    • Functional amyloids as natural storage of peptide hormones in pituitary secretory granules
    • Maji, S. K. et al. Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325, 328-332 (2009).
    • (2009) Science , vol.325 , pp. 328-332
    • Maji, S.K.1
  • 116
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • DOI 10.1038/nature01891
    • Chiti, F., Stefani, M., Taddei, N., Ramponi, G. & Dobson, C. M. Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424, 805-808 (2003). (Pubitemid 37021713)
    • (2003) Nature , vol.424 , Issue.6950 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddel, N.3    Ramponi, G.4    Dobson, C.M.5
  • 117
    • 3242785264 scopus 로고    scopus 로고
    • Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains
    • Dubay, K. F. et al. Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains. J. Mol. Biol. 341, 1317-1326 (2004).
    • (2004) J. Mol. Biol. , vol.341 , pp. 1317-1326
    • Dubay, K.F.1
  • 118
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • DOI 10.1038/nbt1012
    • Fernandez-Escamilla, A. M., Rousseau, F., Schymkowitz, J. & Serrano, L. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nature Biotech. 22, 1302-1306 (2004). (Pubitemid 39336784)
    • (2004) Nature Biotechnology , vol.22 , Issue.10 , pp. 1302-1306
    • Fernandez-Escamilla, A.-M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 119
    • 20444403757 scopus 로고    scopus 로고
    • Prediction of "aggregation-prone" and "aggregation- susceptible" regions in proteins associated with neurodegenerative diseases
    • DOI 10.1016/j.jmb.2005.04.016, PII S0022283605004262
    • Pawar, A. P. et al. Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. J. Mol. Biol. 350, 379-392 (2005). (Pubitemid 40805470)
    • (2005) Journal of Molecular Biology , vol.350 , Issue.2 , pp. 379-392
    • Pawar, A.P.1    DuBay, K.F.2    Zurdo, J.3    Chiti, F.4    Vendruscolo, M.5    Dobson, C.M.6
  • 120
    • 84860013075 scopus 로고    scopus 로고
    • Structure of an intermediate state in protein folding and aggregation
    • Neudecker, P. et al. Structure of an intermediate state in protein folding and aggregation. Science 336, 362-366 (2012).
    • (2012) Science , vol.336 , pp. 362-366
    • Neudecker, P.1
  • 121
    • 0034598954 scopus 로고    scopus 로고
    • Nature disfavors sequences of alternating polar and non-polar amino acids: Implications for amyloidogenesis
    • Broome, B. M. & Hecht, M. H. Nature disfavors sequences of alternating polar and non-polar amino acids: Implications for amyloidogenesis. J. Mol. Biol. 296, 961-968 (2000).
    • (2000) J. Mol. Biol. , vol.296 , pp. 961-968
    • Broome, B.M.1    Hecht, M.H.2
  • 124
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • Kaganovich, D., Kopito, R. & Frydman, J. Misfolded proteins partition between two distinct quality control compartments. Nature 454, 1088-1095 (2008).
    • (2008) Nature , vol.454 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 125
    • 77958487260 scopus 로고    scopus 로고
    • Cellular strategies for controlling protein aggregation
    • Tyedmers, J., Mogk, A. & Bukau, B. Cellular strategies for controlling protein aggregation. Nature Rev. Mol. Cell. Biol. 11, 777-788 (2010).
    • (2010) Nature Rev. Mol. Cell. Biol. , vol.11 , pp. 777-788
    • Tyedmers, J.1    Mogk, A.2    Bukau, B.3
  • 126
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • DOI 10.1126/science.292.5521.1552
    • Bence, N. F., Sampat, R. M. & Kopito, R. R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292, 1552-1555 (2001). (Pubitemid 32493425)
    • (2001) Science , vol.292 , Issue.5521 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 127
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • DOI 10.1038/nm1066
    • Ross, C. A. & Poirier, M. A. Protein aggregation and neurodegenerative disease. Nature Med. 10, S10-S17 (2004). (Pubitemid 38901862)
    • (2004) Nature Medicine , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 128
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman, M. H. & Ciechanover, A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82, 373-428 (2002). (Pubitemid 34654457)
    • (2002) Physiological Reviews , vol.82 , Issue.2 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 129
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • DOI 10.1038/nature05291, PII NATURE05291
    • Rubinsztein, D. C. The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 443, 780-786 (2006). (Pubitemid 44622682)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 780-786
    • Rubinsztein, D.C.1
  • 131
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • DOI 10.1038/nature06639, PII NATURE06639
    • Mizushima, N., Levine, B., Cuervo, A. M. & Klionsky, D. J. Autophagy fights disease through cellular self-digestion. Nature 451, 1069-1075 (2008). (Pubitemid 351317450)
    • (2008) Nature , vol.451 , Issue.7182 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 132
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones, and negative regulators
    • Morimoto, R. I. Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev. 12, 3788-3796 (1998). (Pubitemid 29024840)
    • (1998) Genes and Development , vol.12 , Issue.24 , pp. 3788-3796
    • Morimoto, R.I.1
  • 133
    • 44649197748 scopus 로고    scopus 로고
    • ApoE promotes the proteolytic degradation of Aβ
    • Jiang, Q. et al. ApoE promotes the proteolytic degradation of Aβ. Neuron 58, 681-693 (2008).
    • (2008) Neuron , vol.58 , pp. 681-693
    • Jiang, Q.1
  • 135
    • 84875425248 scopus 로고    scopus 로고
    • Influence of specific Hsp70 domains on fibril formation of the yeast prion protein Ure2
    • Xu, L. Q. et al. Influence of specific Hsp70 domains on fibril formation of the yeast prion protein Ure2. Philos. Trans. R. Soc. B 368, 20110410 (2013).
    • (2013) Philos. Trans. R. Soc. B , vol.368 , pp. 20110410
    • Xu, L.Q.1
  • 136
    • 0034161616 scopus 로고    scopus 로고
    • Clusterin is a secreted mammalian chaperone
    • DOI 10.1016/S0968-0004(99)01534-0, PII S0968000499015340
    • Wilson, M. R. & Easterbrook-Smith, S. B. Clusterin is a secreted mammalian chaperone. Trends Bioch. Sci. 25, 95-98 (2000). (Pubitemid 30122416)
    • (2000) Trends in Biochemical Sciences , vol.25 , Issue.3 , pp. 95-98
    • Wilson, M.R.1    Easterbrook-Smith, S.B.2
  • 137
    • 70349558522 scopus 로고    scopus 로고
    • Genome-wide association study identifies variants at CLU and PICALM associated with Alzheimer's disease
    • Harold, D. et al. Genome-wide association study identifies variants at CLU and PICALM associated with Alzheimer's disease. Nature Genet. 41, 1088-1093 (2009).
    • (2009) Nature Genet. , vol.41 , pp. 1088-1093
    • Harold, D.1
  • 138
    • 84888317489 scopus 로고    scopus 로고
    • Meta-analysis of 74,046 individuals identifies 11 new susceptibility loci for Alzheimer's disease
    • Lambert, J.-C. et al. Meta-analysis of 74,046 individuals identifies 11 new susceptibility loci for Alzheimer's disease. Nature Genet. 45, 1452-1458 (2013).
    • (2013) Nature Genet. , vol.45 , pp. 1452-1458
    • Lambert, J.-C.1
  • 139
    • 78549264026 scopus 로고    scopus 로고
    • Genome-wide association study identifies variants at CLU and CR1 associated with Alzheimer's disease
    • Lambert, J. C. et al. Genome-wide association study identifies variants at CLU and CR1 associated with Alzheimer's disease. Nature Genet. 41, 1094-1099 (2009).
    • (2009) Nature Genet. , vol.41 , pp. 1094-1099
    • Lambert, J.C.1
  • 140
    • 68149162581 scopus 로고    scopus 로고
    • Soluble fibrillar oligomer levels are elevated in Alzheimer's disease brain and correlate with cognitive dysfunction
    • Tomic, J. L., Pensalfini, A., Head, E. & Glabe, C. G. Soluble fibrillar oligomer levels are elevated in Alzheimer's disease brain and correlate with cognitive dysfunction. Neurobiol. Dis. 35, 352-358 (2009).
    • (2009) Neurobiol. Dis. , vol.35 , pp. 352-358
    • Tomic, J.L.1    Pensalfini, A.2    Head, E.3    Glabe, C.G.4
  • 141
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid-β protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • DOI 10.1523/JNEUROSCI.4970-06.2007
    • Shankar, G. M. et al. Natural oligomers of the Alzheimer amyloid-β protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J. Neurosci. 27, 2866-2875 (2007). (Pubitemid 46438992)
    • (2007) Journal of Neuroscience , vol.27 , Issue.11 , pp. 2866-2875
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.L.6
  • 142
    • 77954132249 scopus 로고    scopus 로고
    • Amyloid-β-induced neuronal dysfunction in Alzheimer's disease: From synapses toward neural networks
    • Palop, J. J. & Mucke, L. Amyloid-β-induced neuronal dysfunction in Alzheimer's disease: from synapses toward neural networks. Nature Neurosci. 13, 812-818 (2010).
    • (2010) Nature Neurosci. , vol.13 , pp. 812-818
    • Palop, J.J.1    Mucke, L.2
  • 143
    • 0034704752 scopus 로고    scopus 로고
    • A Drosophila model of Parkinson's disease
    • DOI 10.1038/35006074
    • Feany, M. B. & Bender, W. W. A Drosophila model of Parkinson's disease. Nature 404, 394-398 (2000). (Pubitemid 30164341)
    • (2000) Nature , vol.404 , Issue.6776 , pp. 394-398
    • Feany, M.B.1    Bender, W.W.2
  • 144
    • 46549084254 scopus 로고    scopus 로고
    • Protein misfolding and disease: From the test tube to the organism
    • Luheshi, L. M., Crowther, D. C. & Dobson, C. M. Protein misfolding and disease: from the test tube to the organism. Curr. Opin. Chem. Biol. 12, 25-31 (2008).
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 25-31
    • Luheshi, L.M.1    Crowther, D.C.2    Dobson, C.M.3
  • 145
    • 29444455075 scopus 로고    scopus 로고
    • Drosophila as a model for human neurodegenerative disease
    • DOI 10.1146/annurev.genet.39.110304.095804
    • Bilen, J. & Bonini, N. M. Drosophila as a model for human neurodegenerative disease. Annu. Rev. Genet. 39, 153-171 (2005). (Pubitemid 43011111)
    • (2005) Annual Review of Genetics , vol.39 , pp. 153-171
    • Bilen, J.1    Bonini, N.M.2
  • 146
    • 70349266064 scopus 로고    scopus 로고
    • Collapse of proteostasis represents an early molecular event in caenorhabditis elegans aging
    • Ben-Zvi, A., Miller, E. A. & Morimoto, R. I. Collapse of proteostasis represents an early molecular event in caenorhabditis elegans aging. Proc. Natl Acad. Sci. USA 106, 14914-14919 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 14914-14919
    • Ben-Zvi, A.1    Miller, E.A.2    Morimoto, R.I.3
  • 147
    • 80051760335 scopus 로고    scopus 로고
    • In situ measurements of the formation and morphology of intracellular β-amyloid fibrils by super-resolution fluorescence imaging
    • Kaminksi Schierle, G. S. et al. In situ measurements of the formation and morphology of intracellular β-amyloid fibrils by super-resolution fluorescence imaging. J. Am. Chem. Soc. 133, 12902-12905 (2011).
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 12902-12905
    • Kaminksi Schierle, G.S.1
  • 148
    • 84862863296 scopus 로고    scopus 로고
    • Selenium-enhanced electron microscopic imaging of different aggregate forms of a segment of the amyloid beta peptide in cells
    • McGuire, E. K. et al. Selenium-enhanced electron microscopic imaging of different aggregate forms of a segment of the amyloid beta peptide in cells. ACS Nano 6, 4740-4747 (2012).
    • (2012) ACS Nano , vol.6 , pp. 4740-4747
    • McGuire, E.K.1
  • 149
    • 84880382398 scopus 로고    scopus 로고
    • Superresolution imaging of amyloid fibrils with binding-activated probes
    • Ries, J. et al. Superresolution imaging of amyloid fibrils with binding-activated probes. ACS Chem. Neurosci. 4, 1057-1061 (2013).
    • (2013) ACS Chem. Neurosci. , vol.4 , pp. 1057-1061
    • Ries, J.1
  • 150
    • 33750361540 scopus 로고    scopus 로고
    • A century-old debate on protein aggregation and neurodegeneration enters the clinic
    • DOI 10.1038/nature05290, PII NATURE05290
    • Lansbury, P. T. & Lashuel, H. A. A century-old debate on protein aggregation and neurodegeneration enters the clinic. Nature 443, 774-779 (2006). (Pubitemid 44622681)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 774-779
    • Lansbury, P.T.1    Lashuel, H.A.2
  • 151
    • 80052266213 scopus 로고    scopus 로고
    • The amyloid cascade hypothesis for Alzheimer's disease: An appraisal for the development of therapeutics
    • Karran, E., Mercken, M. & De Strooper, B. The amyloid cascade hypothesis for Alzheimer's disease: an appraisal for the development of therapeutics. Nature Rev. Drug Discov. 10, 698-712 (2011).
    • (2011) Nature Rev. Drug Discov. , vol.10 , pp. 698-712
    • Karran, E.1    Mercken, M.2    De Strooper, B.3
  • 152
    • 0032888131 scopus 로고    scopus 로고
    • Soluble amyloid β peptide concentration as a predictor of synaptic change in Alzheimer's disease
    • Lue, L. F. et al. Soluble amyloid β peptide concentration as a predictor of synaptic change in Alzheimer's disease. Am. J. Pathol. 155, 853-862 (1999).
    • (1999) Am. J. Pathol. , vol.155 , pp. 853-862
    • Lue, L.F.1
  • 155
    • 77955881152 scopus 로고    scopus 로고
    • ANS binding reveals common features of cytotoxic amyloid species
    • Bolognesi, B. et al. ANS binding reveals common features of cytotoxic amyloid species. ACS Chem. Biol. 5, 735-740 (2010).
    • (2010) ACS Chem. Biol. , vol.5 , pp. 735-740
    • Bolognesi, B.1
  • 156
    • 78650963274 scopus 로고    scopus 로고
    • Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions
    • Olzscha, H. et al. Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell 144, 67-78 (2011).
    • (2011) Cell , vol.144 , pp. 67-78
    • Olzscha, H.1
  • 157
    • 84873809834 scopus 로고    scopus 로고
    • Single molecule characterization of the interactions between amyloid-β peptides and the membranes of hippocampal cells
    • Narayan, P. et al. Single molecule characterization of the interactions between amyloid-β peptides and the membranes of hippocampal cells. J. Am. Chem. Soc. 135, 1491-1498 (2013).
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 1491-1498
    • Narayan, P.1
  • 158
    • 84887606872 scopus 로고    scopus 로고
    • Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins
    • Ciryam, P., Tartaglia, G. G., Morimoto, R. I., Dobson, C. M. & Vendruscolo, M. Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins. Cell Rep. 5, 781-790 (2013).
    • (2013) Cell Rep. , vol.5 , pp. 781-790
    • Ciryam, P.1    Tartaglia, G.G.2    Morimoto, R.I.3    Dobson, C.M.4    Vendruscolo, M.5
  • 159
    • 77956795163 scopus 로고    scopus 로고
    • Widespread protein aggregation as an inherent part of aging in C. Elegans
    • David, D. C. et al. Widespread protein aggregation as an inherent part of aging in C. elegans. PLoS Biol. 8, e1000450 (2010).
    • (2010) PLoS Biol. , vol.8
    • David, D.C.1
  • 160
    • 33644850056 scopus 로고    scopus 로고
    • Progressive disruption of cellular protein folding in models of polyglutamine diseases
    • DOI 10.1126/science.1124514
    • Gidalevitz, T., Ben-Zvi, A., Ho, K. H., Brignull, H. R. & Morimoto, R. I. Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science 311, 1471-1474 (2006). (Pubitemid 43376703)
    • (2006) Science , vol.311 , Issue.5766 , pp. 1471-1474
    • Gidalevitz, T.1    Ben-Zvi, A.2    Ho, K.H.3    Brignull, H.R.4    Morimoto, R.I.5
  • 161
    • 79251498807 scopus 로고    scopus 로고
    • Protein homeostasis and aging: The importance of exquisite quality control
    • Koga, H., Kaushik, S. & Cuervo, A. M. Protein homeostasis and aging: the importance of exquisite quality control. Ageing Res. Rev. 10, 205-215 (2011).
    • (2011) Ageing Res. Rev. , vol.10 , pp. 205-215
    • Koga, H.1    Kaushik, S.2    Cuervo, A.M.3
  • 162
    • 84855823950 scopus 로고    scopus 로고
    • Proteomic analysis of age-dependent changes in protein solubility identifies genes that modulate lifespan
    • Reis-Rodrigues, P. et al. Proteomic analysis of age-dependent changes in protein solubility identifies genes that modulate lifespan. Aging Cell 11, 120-127 (2012).
    • (2012) Aging Cell , vol.11 , pp. 120-127
    • Reis-Rodrigues, P.1
  • 163
    • 84866062627 scopus 로고    scopus 로고
    • Gene expression profiling in human neurodegenerative disease
    • Cooper-Knock, J. et al. Gene expression profiling in human neurodegenerative disease. Nature Rev. Neurol. 8, 518-530 (2012).
    • (2012) Nature Rev. Neurol. , vol.8 , pp. 518-530
    • Cooper-Knock, J.1
  • 166
    • 2542530161 scopus 로고    scopus 로고
    • In the footsteps of alchemists
    • DOI 10.1126/science.1093078
    • Dobson, C. M. In the footsteps of alchemists. Science 304, 1259-1262 (2004). (Pubitemid 38697410)
    • (2004) Science , vol.304 , Issue.5675 , pp. 1259-1262
    • Dobson, C.M.1
  • 167
    • 28244502156 scopus 로고    scopus 로고
    • Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: A focus on the transthyretin amyloidoses
    • Johnson, S. M. et al. Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: a focus on the transthyretin amyloidoses. Acc. Chem. Res. 38, 911-921 (2005).
    • (2005) Acc. Chem. Res. , vol.38 , pp. 911-921
    • Johnson, S.M.1
  • 169
    • 84862234023 scopus 로고    scopus 로고
    • Tafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascade
    • Bulawa, C. E. et al. Tafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascade. Proc. Natl Acad. Sci. USA 109, 9629-9634 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 9629-9634
    • Bulawa, C.E.1
  • 170
    • 84861512163 scopus 로고    scopus 로고
    • Intrinsically disordered proteins and novel strategies for drug discovery
    • Uversky, V. N. Intrinsically disordered proteins and novel strategies for drug discovery. Expert Opin. Drug Discov. 7, 475-488 (2012).
    • (2012) Expert Opin. Drug Discov. , vol.7 , pp. 475-488
    • Uversky, V.N.1
  • 171
    • 84895866256 scopus 로고    scopus 로고
    • Targeting the intrinsically disordered structural ensemble of α-synuclein by small molecules as a potential therapeutic strategy for Parkinson's disease
    • Tóth, G. et al. Targeting the intrinsically disordered structural ensemble of α-synuclein by small molecules as a potential therapeutic strategy for Parkinson's disease. PLoS ONE 9, e87133 (2014).
    • (2014) PLoS ONE , vol.9
    • Tóth, G.1
  • 172
    • 84896695581 scopus 로고    scopus 로고
    • Chemical kinetics for drug discovery to combat protein aggregation diseases
    • Arosio, P., Vendruscolo, M., Dobson, C. M. & Knowles, T. P. Chemical kinetics for drug discovery to combat protein aggregation diseases. Trends Pharmacol. Sci. 35, 127-135 (2014).
    • (2014) Trends Pharmacol. Sci. , vol.35 , pp. 127-135
    • Arosio, P.1    Vendruscolo, M.2    Dobson, C.M.3    Knowles, T.P.4
  • 173
    • 26244432388 scopus 로고    scopus 로고
    • Efficacy and safety of cholesterol-lowering treatment: Prospective meta-analysis of data from 90,056 participants in 14 randomised trials of statins
    • Baigent, C. et al. Efficacy and safety of cholesterol-lowering treatment: prospective meta-analysis of data from 90,056 participants in 14 randomised trials of statins. Lancet 366, 1267-1278 (2005).
    • (2005) Lancet , vol.366 , pp. 1267-1278
    • Baigent, C.1
  • 175
    • 76849086405 scopus 로고    scopus 로고
    • The secretases: Enzymes with therapeutic potential in Alzheimer disease
    • De Strooper, B., Vassar, R. & Golde, T. The secretases: enzymes with therapeutic potential in Alzheimer disease. Nature Rev. Neurol. 6, 99-107 (2010).
    • (2010) Nature Rev. Neurol. , vol.6 , pp. 99-107
    • De Strooper, B.1    Vassar, R.2    Golde, T.3
  • 176
    • 8844257296 scopus 로고    scopus 로고
    • Probing the origins, diagnosis and treatment of amyloid diseases using antibodies
    • DOI 10.1016/j.biochi.2004.09.012, PII S0300908404001592
    • Dumoulin, M. & Dobson, C. M. Probing the origins, diagnosis and treatment of amyloid diseases using antibodies. Biochimie 86, 589-600 (2004). (Pubitemid 39535630)
    • (2004) Biochimie , vol.86 , Issue.9-10 , pp. 589-600
    • Dumoulin, M.1    Dobson, C.M.2
  • 177
    • 84863987464 scopus 로고    scopus 로고
    • Inhibition of amyloid formation
    • Hard, T. & Lendel, C. Inhibition of amyloid formation. J. Mol. Biol. 421, 441-465 (2012).
    • (2012) J. Mol. Biol. , vol.421 , pp. 441-465
    • Hard, T.1    Lendel, C.2
  • 178
    • 77950579610 scopus 로고    scopus 로고
    • Sequestration of the Aβ peptide prevents toxicity and promotes degradation in vivo
    • Luheshi, L. M. et al. Sequestration of the Aβ peptide prevents toxicity and promotes degradation in vivo. PLoS Biol. 8, e1000334 (2010).
    • (2010) PLoS Biol. , vol.8
    • Luheshi, L.M.1
  • 179
    • 0036780877 scopus 로고    scopus 로고
    • Amyloid-β immunotherapy for Alzheimer's disease: The end of the beginning
    • DOI 10.1038/nrn938
    • Schenk, D. Amyloid-β immunotherapy for Alzheimer's disease: The end of the beginning. Nature Rev. Neurosci. 3, 824-828 (2002). (Pubitemid 135706694)
    • (2002) Nature Reviews Neuroscience , vol.3 , Issue.10 , pp. 824-828
    • Schenk, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.