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Volumn 86, Issue , 2017, Pages 27-68

Protein misfolding, amyloid formation, and human disease: A summary of progress over the last decade

Author keywords

Amyloidosis; Chaperones; Conformational diseases; Functional amyloid; Protein aggregation; Protein homeostasis; Quality control

Indexed keywords

ALPHA SYNUCLEIN; AMYLIN; AMYLOID; AMYLOID BETA PROTEIN; APOLIPOPROTEIN A2; APOLIPOPROTEIN A4; APOLIPOPROTEIN C2; CALCITONIN; HUNTINGTIN; LYSOZYME; MICROTUBULE ASSOCIATED PROTEIN; PREALBUMIN; PRION PROTEIN; PROLACTIN; SERUM AMYLOID A; TAU PROTEIN; CHAPERONE; NEW DRUG;

EID: 85020890340     PISSN: 00664154     EISSN: 15454509     Source Type: Book Series    
DOI: 10.1146/annurev-biochem-061516-045115     Document Type: Review
Times cited : (1925)

References (243)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM. (2006). Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75: 333-66
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 0033616575 scopus 로고    scopus 로고
    • Designing conditions for in vitro formation of amyloid protofilaments and fibrils
    • Chiti F, Webster P, Taddei N, Clark A, Stefani M, et al. (1999). Designing conditions for in vitro formation of amyloid protofilaments and fibrils. PNAS 96: 3590-94
    • (1999) PNAS , vol.96 , pp. 3590-3594
    • Chiti, F.1    Webster, P.2    Taddei, N.3    Clark, A.4    Stefani, M.5
  • 4
    • 0036845354 scopus 로고    scopus 로고
    • The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
    • Fändrich M, Dobson CM. (2002). The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBO J. 21: 5682-90
    • (2002) EMBO J. , vol.21 , pp. 5682-5690
    • Fändrich, M.1    Dobson, C.M.2
  • 5
    • 84864285157 scopus 로고    scopus 로고
    • Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria
    • Adler-Abramovich L, Vaks L, Carny O, Trudler D, Magno A, et al. (2012). Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria. Nat. Chem. Biol. 8: 701-6
    • (2012) Nat. Chem. Biol , vol.8 , pp. 701-706
    • Adler-Abramovich, L.1    Vaks, L.2    Carny, O.3    Trudler, D.4    Magno, A.5
  • 6
    • 37549063068 scopus 로고    scopus 로고
    • Role of intermolecular forces in defining material properties of protein nanofibrils
    • Knowles TP, Fitzpatrick AW, Meehan S, Mott HR, Vendruscolo M, et al. (2007). Role of intermolecular forces in defining material properties of protein nanofibrils. Science 318: 1900-3
    • (2007) Science , vol.318 , pp. 1900-1903
    • Knowles, T.P.1    Fitzpatrick, A.W.2    Meehan, S.3    Mott, H.R.4    Vendruscolo, M.5
  • 7
    • 47049100201 scopus 로고    scopus 로고
    • Amyloids: Not only pathological agents but also ordered nanomaterials
    • Cherny I, Gazit E. (2008). Amyloids: not only pathological agents but also ordered nanomaterials. Angew. Chem. Int. Ed. Engl. 47: 4062-69
    • (2008) Angew. Chem. Int. Ed. Engl , vol.47 , pp. 4062-4069
    • Cherny, I.1    Gazit, E.2
  • 9
    • 67650809307 scopus 로고    scopus 로고
    • Functional amyloids as natural storage of peptide hormones in pituitary secretory granules
    • Maji SK, Perrin MH, Sawaya MR, Jessberger S, Vadodaria K, et al. (2009). Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325: 328-32
    • (2009) Science , vol.325 , pp. 328-332
    • Maji, S.K.1    Perrin, M.H.2    Sawaya, M.R.3    Jessberger, S.4    Vadodaria, K.5
  • 10
    • 84864240409 scopus 로고    scopus 로고
    • The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis
    • Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, et al. (2012). The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. Cell 150: 339-50
    • (2012) Cell , vol.150 , pp. 339-350
    • Li, J.1    McQuade, T.2    Siemer, A.B.3    Napetschnig, J.4    Moriwaki, K.5
  • 11
    • 84876281768 scopus 로고    scopus 로고
    • Unusual biophysics of intrinsically disordered proteins
    • Uversky VN. (2013). Unusual biophysics of intrinsically disordered proteins. Biochim. Biophys. Acta 1834: 932-51
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 932-951
    • Uversky, V.N.1
  • 12
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson CM. (2003). Protein folding and misfolding. Nature 426: 884-90
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 13
    • 84860389674 scopus 로고    scopus 로고
    • Amyloid-β forms fibrils by nucleated conformational conversion of oligomers
    • Lee J, Culyba EK, Powers ET, Kelly JW. (2011). Amyloid-β forms fibrils by nucleated conformational conversion of oligomers. Nat. Chem. Biol. 7: 602-9
    • (2011) Nat. Chem. Biol , vol.7 , pp. 602-609
    • Lee, J.1    Culyba, E.K.2    Powers, E.T.3    Kelly, J.W.4
  • 14
    • 84861563520 scopus 로고    scopus 로고
    • Direct observation of the interconversion of normal and toxic forms of α-synuclein
    • Cremades N, Cohen SI, Deas E, Abramov AY, Chen AY, et al. (2012). Direct observation of the interconversion of normal and toxic forms of α-synuclein. Cell 149: 1048-59
    • (2012) Cell , vol.149 , pp. 1048-1059
    • Cremades, N.1    Cohen, S.I.2    Deas, E.3    Abramov, A.Y.4    Chen, A.Y.5
  • 15
    • 33644813233 scopus 로고    scopus 로고
    • A native to amyloidogenic transition regulated by a backbone trigger
    • Eakin CM, Berman AJ, Miranker AD. 2006.A native to amyloidogenic transition regulated by a backbone trigger. Nat. Struct. Mol. Biol. 13: 202-8
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 202-208
    • Eakin, C.M.1    Berman, A.J.2    Miranker, A.D.3
  • 16
    • 17044402604 scopus 로고    scopus 로고
    • The biological and chemical basis for tissue-selective amyloid disease
    • Sekijima Y, Wiseman RL, Matteson J, Hammarström P, Miller SR, et al. (2005). The biological and chemical basis for tissue-selective amyloid disease. Cell 121: 73-85
    • (2005) Cell , vol.121 , pp. 73-85
    • Sekijima, Y.1    Wiseman, R.L.2    Matteson, J.3    Hammarström, P.4    Miller, S.R.5
  • 17
    • 0033777523 scopus 로고    scopus 로고
    • Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
    • Bouchard M, Zurdo J, Nettleton EJ, Dobson CM, Robinson CV. (2000). Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy. Protein Sci. 9: 1960-67
    • (2000) Protein Sci , vol.9 , pp. 1960-1967
    • Bouchard, M.1    Zurdo, J.2    Nettleton, E.J.3    Dobson, C.M.4    Robinson, C.V.5
  • 18
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • Serio TR, Cashikar AG, Kowal AS, Sawicki GJ, Moslehi JJ, et al. (2000). Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 289: 1317-21
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.R.1    Cashikar, A.G.2    Kowal, A.S.3    Sawicki, G.J.4    Moslehi, J.J.5
  • 19
    • 0037422540 scopus 로고    scopus 로고
    • Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways
    • Bitan G, Kirkitadze MD, Lomakin A, Vollers SS, Benedek GB, Teplow DB. (2003). Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways. PNAS 100: 330-35
    • (2003) PNAS , vol.100 , pp. 330-335
    • Bitan, G.1    Kirkitadze, M.D.2    Lomakin, A.3    Vollers, S.S.4    Benedek, G.B.5    Teplow, D.B.6
  • 20
    • 0037255361 scopus 로고    scopus 로고
    • Assembly of amyloid protofibrils via critical oligomers-a novel pathway of amyloid formation
    • Modler AJ, Gast K, Lutsch G, Damaschun G. (2003). Assembly of amyloid protofibrils via critical oligomers-a novel pathway of amyloid formation. J. Mol. Biol. 325: 135-48
    • (2003) J. Mol. Biol , vol.325 , pp. 135-148
    • Modler, A.J.1    Gast, K.2    Lutsch, G.3    Damaschun, G.4
  • 21
    • 23444447864 scopus 로고    scopus 로고
    • Evidence for a mechanism of amyloid formation involvingmolecular reorganisation within native-like precursor aggregates
    • Plakoutsi G, Bemporad F, Calamai M, Taddei N, Dobson CM, Chiti F. (2005). Evidence for a mechanism of amyloid formation involvingmolecular reorganisation within native-like precursor aggregates. J. Mol. Biol. 351: 910-22
    • (2005) J. Mol. Biol , vol.351 , pp. 910-922
    • Plakoutsi, G.1    Bemporad, F.2    Calamai, M.3    Taddei, N.4    Dobson, C.M.5    Chiti, F.6
  • 22
    • 66049093067 scopus 로고    scopus 로고
    • Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation
    • Carulla N, Zhou M, Arimon M, Gairí M, Giralt E, et al. (2009). Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation. PNAS 106: 7828-33
    • (2009) PNAS , vol.106 , pp. 7828-7833
    • Carulla, N.1    Zhou, M.2    Arimon, M.3    Gairí, M.4    Giralt, E.5
  • 23
    • 79251631002 scopus 로고    scopus 로고
    • Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to β-sheet in amyloid fibril formation
    • Bleiholder C, Dupuis NF, Wyttenbach T, Bowers MT. (2011). Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to β-sheet in amyloid fibril formation. Nat Chem. 3: 172-77
    • (2011) Nat Chem , vol.3 , pp. 172-177
    • Bleiholder, C.1    Dupuis, N.F.2    Wyttenbach, T.3    Bowers, M.T.4
  • 24
    • 17144461932 scopus 로고
    • Intercapillary deposits of IgA-Ig G
    • Berger J, Hinglais N. (1968). Intercapillary deposits of IgA-Ig G. J. Urol. Nephrol. 74: 694-95
    • (1968) J. Urol. Nephrol , vol.74 , pp. 694-695
    • Berger, J.1    Hinglais, N.2
  • 25
    • 0015219685 scopus 로고
    • Amyloid fibril proteins: Proof of homology with immunoglobulin light chains by sequence analyses
    • Glenner GG, Terry W, Harada M, Isersky C, Page D. (1971). Amyloid fibril proteins: proof of homology with immunoglobulin light chains by sequence analyses. Science 172: 1150-51
    • (1971) Science , vol.172 , pp. 1150-1151
    • Glenner, G.G.1    Terry, W.2    Harada, M.3    Isersky, C.4    Page, D.5
  • 26
    • 84862896883 scopus 로고    scopus 로고
    • Light chain deposition disease: Novel biological insights and treatment advances
    • Jimenez-Zepeda VH. (2012). Light chain deposition disease: novel biological insights and treatment advances. Int. J. Lab. Hematol. 34: 347-55
    • (2012) Int. J. Lab. Hematol , vol.34 , pp. 347-355
    • Jimenez-Zepeda, V.H.1
  • 27
  • 31
    • 79251498807 scopus 로고    scopus 로고
    • Protein homeostasis and aging: The importance of exquisite quality control
    • Koga H, Kaushik S, Cuervo AM. (2011). Protein homeostasis and aging: the importance of exquisite quality control. Ageing Res. Rev. 10: 205-15
    • (2011) Ageing Res. Rev , vol.10 , pp. 205-215
    • Koga, H.1    Kaushik, S.2    Cuervo, A.M.3
  • 32
    • 84901355639 scopus 로고    scopus 로고
    • The amyloid state and its association with protein misfolding diseases
    • Knowles TP, Vendruscolo M, Dobson CM. (2014). The amyloid state and its association with protein misfolding diseases. Nat. Rev. Mol. Cell Biol. 15: 384-96
    • (2014) Nat. Rev. Mol. Cell Biol , vol.15 , pp. 384-396
    • Knowles, T.P.1    Vendruscolo, M.2    Dobson, C.M.3
  • 33
    • 0014021742 scopus 로고
    • Experimental transmission of a Kuru-like syndrome to chimpanzees
    • Gajdusek DC, Gibbs CJ, Alpers M. (1966). Experimental transmission of a Kuru-like syndrome to chimpanzees. Nature 209: 794-96
    • (1966) Nature , vol.209 , pp. 794-796
    • Gajdusek, D.C.1    Gibbs, C.J.2    Alpers, M.3
  • 34
    • 84857201877 scopus 로고    scopus 로고
    • An overview of human prion diseases
    • Imran M, Mahmood S. (2011). An overview of human prion diseases. Virol. J. 8: 559
    • (2011) Virol. J. , vol.8 , pp. 559
    • Imran, M.1    Mahmood, S.2
  • 36
    • 84888594143 scopus 로고    scopus 로고
    • Biology and genetics of prions causing neurodegeneration
    • Prusiner SB. (2013). Biology and genetics of prions causing neurodegeneration. Annu. Rev. Genet. 47: 601-23
    • (2013) Annu. Rev. Genet , vol.47 , pp. 601-623
    • Prusiner, S.B.1
  • 38
    • 84937392013 scopus 로고    scopus 로고
    • Neurodegenerative diseases: Expanding the prion concept
    • Walker LC, Jucker M. (2015). Neurodegenerative diseases: expanding the prion concept. Annu. Rev. Neurosci. 38: 87-103
    • (2015) Annu. Rev. Neurosci , vol.38 , pp. 87-103
    • Walker, L.C.1    Jucker, M.2
  • 39
    • 84955245033 scopus 로고    scopus 로고
    • Cell biology of prions and prionoids: A status report
    • Aguzzi A, Lakkaraju AK. (2016). Cell biology of prions and prionoids: a status report. Trends Cell Biol. 26: 40-51
    • (2016) Trends Cell Biol , vol.26 , pp. 40-51
    • Aguzzi, A.1    Lakkaraju, A.K.2
  • 40
    • 0036220131 scopus 로고    scopus 로고
    • Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme
    • Canet D, Last AM, Tito P, Sunde M, Spencer A, et al. (2002). Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme. Nat. Struct. Biol. 9: 308-15
    • (2002) Nat. Struct. Biol , vol.9 , pp. 308-315
    • Canet, D.1    Last, A.M.2    Tito, P.3    Sunde, M.4    Spencer, A.5
  • 41
    • 78649728415 scopus 로고    scopus 로고
    • Local cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution
    • Dhulesia A, Cremades N, Kumita JR, Hsu ST, Mossuto MF, et al. (2010). Local cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution. J. Am. Chem. Soc. 132: 15580-88
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 15580-15588
    • Dhulesia, A.1    Cremades, N.2    Kumita, J.R.3    Hsu, S.T.4    Mossuto, M.F.5
  • 42
    • 85002156858 scopus 로고    scopus 로고
    • The significance of the location of mutations for the native-state dynamics of human lysozyme
    • Ahn M, Hagan CL, Bernardo-Gancedo A, De Genst E, Newby FN, et al. (2016). The significance of the location of mutations for the native-state dynamics of human lysozyme. Biophys. J. 111: 2358-67
    • (2016) Biophys. J. , vol.111 , pp. 2358-2367
    • Ahn, M.1    Hagan, C.L.2    Bernardo-Gancedo, A.3    De Genst, E.4    Newby, F.N.5
  • 43
    • 79952451835 scopus 로고    scopus 로고
    • Effects of the known pathogenic mutations on the aggregation pathway of the amyloidogenic peptide of apolipoprotein A-I
    • Raimondi S, Guglielmi F, Giorgetti S, Di Gaetano S, Arciello A, et al. (2011). Effects of the known pathogenic mutations on the aggregation pathway of the amyloidogenic peptide of apolipoprotein A-I. J. Mol. Biol. 407: 465-76
    • (2011) J. Mol. Biol , vol.407 , pp. 465-476
    • Raimondi, S.1    Guglielmi, F.2    Giorgetti, S.3    Di Gaetano, S.4    Arciello, A.5
  • 44
    • 84856857216 scopus 로고    scopus 로고
    • The crystal structure of the C-terminal truncated apolipoprotein A-I sheds new light on amyloid formation by the N-terminal fragment
    • Gursky O, Mei X, Atkinson D. (2012). The crystal structure of the C-terminal truncated apolipoprotein A-I sheds new light on amyloid formation by the N-terminal fragment. Biochemistry 51: 10-18
    • (2012) Biochemistry , vol.51 , pp. 10-18
    • Gursky, O.1    Mei, X.2    Atkinson, D.3
  • 45
    • 0035890055 scopus 로고    scopus 로고
    • Furin initiates gelsolin familial amyloidosis in the Golgi through a defect in Ca2+ stabilization
    • Chen CD, Huff ME, Matteson J, Page L, Phillips R, et al. (2001). Furin initiates gelsolin familial amyloidosis in the Golgi through a defect in Ca2+ stabilization. EMBO J. 20: 6277-87
    • (2001) EMBO J. , vol.20 , pp. 6277-6287
    • Chen, C.D.1    Huff, M.E.2    Matteson, J.3    Page, L.4    Phillips, R.5
  • 46
    • 28644437423 scopus 로고    scopus 로고
    • Metalloendoprotease cleavage triggers gelsolin amyloidogenesis
    • Page LJ, Suk JY, Huff ME, Lim HJ, Venable J, et al. (2005). Metalloendoprotease cleavage triggers gelsolin amyloidogenesis. EMBO J. 24: 4124-32
    • (2005) EMBO J. , vol.24 , pp. 4124-4132
    • Page, L.J.1    Suk, J.Y.2    Huff, M.E.3    Lim, H.J.4    Venable, J.5
  • 47
    • 84860128609 scopus 로고    scopus 로고
    • Gelsolin amyloidosis: Genetics, biochemistry, pathology and possible strategies for therapeutic intervention
    • Solomon JP, Page LJ, Balch WE, Kelly JW. (2012). Gelsolin amyloidosis: genetics, biochemistry, pathology and possible strategies for therapeutic intervention. Crit. Rev. Biochem. Mol. Biol. 47: 282-96
    • (2012) Crit. Rev. Biochem. Mol. Biol , vol.47 , pp. 282-296
    • Solomon, J.P.1    Page, L.J.2    Balch, W.E.3    Kelly, J.W.4
  • 48
    • 84877906835 scopus 로고    scopus 로고
    • Tau pathology and neurodegeneration
    • Spillantini MG, Goedert M. (2013). Tau pathology and neurodegeneration. Lancet Neurol. 12: 609-22
    • (2013) Lancet Neurol , vol.12 , pp. 609-622
    • Spillantini, M.G.1    Goedert, M.2
  • 49
    • 84864390773 scopus 로고    scopus 로고
    • Tau alternative splicing in familial and sporadic tauopathies
    • Niblock M, Gallo JM. (2012). Tau alternative splicing in familial and sporadic tauopathies. Biochem. Soc. Trans. 40: 677-80
    • (2012) Biochem. Soc. Trans , vol.40 , pp. 677-680
    • Niblock, M.1    Gallo, J.M.2
  • 50
    • 0033616590 scopus 로고    scopus 로고
    • Unusual phenotypic alteration ofβ amyloid precursor protein (βAPP) maturation by a new Val-715 MetβAPP-770 mutation responsible for probable early-onset Alzheimer's disease
    • Ancolio K, Dumanchin C, Barelli H, Warter JM, Brice A, et al. (1999). Unusual phenotypic alteration ofâ amyloid precursor protein (âAPP) maturation by a new Val-715 MetβAPP-770 mutation responsible for probable early-onset Alzheimer's disease. PNAS 96: 4119-24
    • (1999) PNAS , vol.96 , pp. 4119-4124
    • Ancolio, K.1    Dumanchin, C.2    Barelli, H.3    Warter, J.M.4    Brice, A.5
  • 51
    • 0035421638 scopus 로고    scopus 로고
    • Pathogenic APP mutations near the γ-secretase cleavage site differentially affect Aβsecretion and APP C-terminal fragment stability
    • De Jonghe C, Esselens C, Kumar-Singh S, Craessaerts K, Serneels S, et al. (2001). Pathogenic APP mutations near the γ-secretase cleavage site differentially affect Aβsecretion and APP C-terminal fragment stability. Hum. Mol. Genet. 10: 1665-71
    • (2001) Hum. Mol. Genet , vol.10 , pp. 1665-1671
    • De Jonghe, C.1    Esselens, C.2    Kumar-Singh, S.3    Craessaerts, K.4    Serneels, S.5
  • 52
    • 0034662929 scopus 로고    scopus 로고
    • BACE2, aβ-secretase homolog, cleaves at the βsite and within the amyloid-βregion of the amyloid-βprecursor protein
    • Farzan M, Schnitzler CE, Vasilieva N, Leung D, Choe H. (2000). BACE2, aβ-secretase homolog, cleaves at the βsite and within the amyloid-βregion of the amyloid-βprecursor protein. PNAS 97: 9712-17
    • (2000) PNAS , vol.97 , pp. 9712-9717
    • Farzan, M.1    Schnitzler, C.E.2    Vasilieva, N.3    Leung, D.4    Choe, H.5
  • 53
    • 62449330486 scopus 로고    scopus 로고
    • A recessive mutation in the APP gene with dominant-negative effect on amyloidogenesis
    • Di Fede G, Catania M, Morbin M, Rossi G, Suardi S, et al. (2009). A recessive mutation in the APP gene with dominant-negative effect on amyloidogenesis. Science 323: 1473-77
    • (2009) Science , vol.323 , pp. 1473-1477
    • Di Fede, G.1    Catania, M.2    Morbin, M.3    Rossi, G.4    Suardi, S.5
  • 54
    • 17944368176 scopus 로고    scopus 로고
    • The ?Arctic? APP mutation (E693G) causes Alzheimer's disease by enhanced Aβprotofibril formation
    • Nilsberth C, Westlind-Danielsson A, Eckman CB, Condron MM, Axelman K, et al. (2001). The ?Arctic? APP mutation (E693G) causes Alzheimer's disease by enhanced Aβprotofibril formation. Nat. Neurosci. 4: 887-93
    • (2001) Nat. Neurosci , vol.4 , pp. 887-893
    • Nilsberth, C.1    Westlind-Danielsson, A.2    Eckman, C.B.3    Condron, M.M.4    Axelman, K.5
  • 55
    • 41749096713 scopus 로고    scopus 로고
    • A new amyloid β variant favoring oligomerization in Alzheimer's-type dementia
    • Tomiyama T, Nagata T, Shimada H, Teraoka R, Fukushima A, et al. (2008). A new amyloid â variant favoring oligomerization in Alzheimer's-type dementia. Ann. Neurol. 63: 377-87
    • (2008) Ann. Neurol , vol.63 , pp. 377-387
    • Tomiyama, T.1    Nagata, T.2    Shimada, H.3    Teraoka, R.4    Fukushima, A.5
  • 56
    • 0031742418 scopus 로고    scopus 로고
    • Flemish and Dutch mutations in amyloid βprecursor protein have different effects on amyloid βsecretion
    • De Jonghe C, Zehr C, Yager D, Prada CM, Younkin S, et al. (1998). Flemish and Dutch mutations in amyloid βprecursor protein have different effects on amyloid βsecretion. Neurobiol. Dis. 5: 281-86
    • (1998) Neurobiol. Dis , vol.5 , pp. 281-286
    • De Jonghe, C.1    Zehr, C.2    Yager, D.3    Prada, C.M.4    Younkin, S.5
  • 57
    • 5644300685 scopus 로고    scopus 로고
    • Familial Alzheimer disease associated with A713T mutation in APP
    • Armstrong J, Boada M, Rey MJ, Vidal N, Ferrer I. (2004). Familial Alzheimer disease associated with A713T mutation in APP. Neurosci. Lett. 370: 241-43
    • (2004) Neurosci. Lett , vol.370 , pp. 241-243
    • Armstrong, J.1    Boada, M.2    Rey, M.J.3    Vidal, N.4    Ferrer, I.5
  • 58
    • 0034282630 scopus 로고    scopus 로고
    • Substitutions at codon 22 of Alzheimer's Aβpeptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells
    • Miravalle L, Tokuda T, Chiarle R, Giaccone G, Bugiani O, et al. (2000). Substitutions at codon 22 of Alzheimer's Aβpeptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells. J. Biol. Chem. 275: 27110-16
    • (2000) J. Biol. Chem , vol.275 , pp. 27110-27116
    • Miravalle, L.1    Tokuda, T.2    Chiarle, R.3    Giaccone, G.4    Bugiani, O.5
  • 59
    • 79955602314 scopus 로고    scopus 로고
    • Amyloid precursor protein mutation E682K at the alternative β-secretase cleavage β-site increases Aβ generation
    • Zhou L, Brouwers N, Benilova I, Vandersteen A, Mercken M, et al. (2011). Amyloid precursor protein mutation E682K at the alternative β-secretase cleavage β-site increases Aβ generation. EMBO Mol. Med. 3: 291-302
    • (2011) EMBO Mol. Med , vol.3 , pp. 291-302
    • Zhou, L.1    Brouwers, N.2    Benilova, I.3    Vandersteen, A.4    Mercken, M.5
  • 60
    • 84908204323 scopus 로고    scopus 로고
    • The newly discovered Parkinson's disease associated Finnish mutation (A53E) attenuates α-synuclein aggregation and membrane binding
    • Ghosh D, Sahay S, Ranjan P, Salot S, Mohite GM, et al. (2014). The newly discovered Parkinson's disease associated Finnish mutation (A53E) attenuates α-synuclein aggregation and membrane binding. Biochemistry 53: 6419-21
    • (2014) Biochemistry , vol.53 , pp. 6419-6421
    • Ghosh, D.1    Sahay, S.2    Ranjan, P.3    Salot, S.4    Mohite, G.M.5
  • 61
    • 84987620704 scopus 로고    scopus 로고
    • Mutations associated with familial Parkinson's disease alter the initiation and amplification steps of α-synuclein aggregation
    • Flagmeier P, Meisl G, Vendruscolo M, Knowles TP, Dobson CM, et al. (2016). Mutations associated with familial Parkinson's disease alter the initiation and amplification steps of α-synuclein aggregation. PNAS 113: 10328-33
    • (2016) PNAS , vol.113 , pp. 10328-10333
    • Flagmeier, P.1    Meisl, G.2    Vendruscolo, M.3    Knowles, T.P.4    Dobson, C.M.5
  • 62
    • 77956635278 scopus 로고    scopus 로고
    • A new amyloidosis caused by fibrillar aggregates of mutated corneodesmosin
    • Caubet C, Bousset L, Clemmensen O, Sourigues Y, Bygum A, et al. (2010). A new amyloidosis caused by fibrillar aggregates of mutated corneodesmosin. FASEB J. 24: 3416-26
    • (2010) FASEB J. , vol.24 , pp. 3416-3426
    • Caubet, C.1    Bousset, L.2    Clemmensen, O.3    Sourigues, Y.4    Bygum, A.5
  • 63
    • 0347403723 scopus 로고    scopus 로고
    • Systemic amyloid deposits in familial British dementia
    • Vidal R, Frangione B, Rostagno A, Mead S, Révész T, et al. (1999). Systemic amyloid deposits in familial British dementia. Nature 399: 776-81
    • (1999) Nature , vol.399 , pp. 776-781
    • Vidal, R.1    Frangione, B.2    Rostagno, A.3    Mead, S.4    Révész, T.5
  • 64
    • 0034712749 scopus 로고    scopus 로고
    • A decamer duplication in the 3 region of the BRI gene originates an amyloid peptide that is associated with dementia in a Danish kindred
    • Vidal R, Révész T, Rostagno A, Kim E, Holton JL, et al. (2000). A decamer duplication in the 3 region of the BRI gene originates an amyloid peptide that is associated with dementia in a Danish kindred. PNAS 97: 4920-25
    • (2000) PNAS , vol.97 , pp. 4920-4925
    • Vidal, R.1    Révész, T.2    Rostagno, A.3    Kim, E.4    Holton, J.L.5
  • 65
    • 0035868431 scopus 로고    scopus 로고
    • A new human hereditary amyloidosis: The result of a stop-codon mutation in the apolipoprotein AII gene
    • Benson MD, Liepnieks JJ, Yazaki M, Yamashita T, Hamidi Asl K, et al. (2001). A new human hereditary amyloidosis: the result of a stop-codon mutation in the apolipoprotein AII gene. Genomics 72: 272-77
    • (2001) Genomics , vol.72 , pp. 272-277
    • Benson, M.D.1    Liepnieks, J.J.2    Yazaki, M.3    Yamashita, T.4    Hamidi Asl, K.5
  • 66
    • 33645554421 scopus 로고    scopus 로고
    • Hereditary renal amyloidosis associated with a novel mutation in the apolipoprotein AII gene
    • De Gracia R, Fernández EJ, Riñón C, Selgas R, Garcia-Bustos J. (2006). Hereditary renal amyloidosis associated with a novel mutation in the apolipoprotein AII gene. QJM 99: 274
    • (2006) QJM , vol.99 , pp. 274
    • De Gracia, R.1    Fernández, E.J.2    Riñón, C.3    Selgas, R.4    Garcia-Bustos, J.5
  • 67
    • 0142247606 scopus 로고    scopus 로고
    • PH-dependent amyloid and protofibril formation by the ABri peptide of familial British dementia
    • Srinivasan R, Jones EM, Liu K, Ghiso J, Marchant RE, Zagorski MG. (2003). pH-dependent amyloid and protofibril formation by the ABri peptide of familial British dementia. J. Mol. Biol. 333: 1003-23
    • (2003) J. Mol. Biol , vol.333 , pp. 1003-1023
    • Srinivasan, R.1    Jones, E.M.2    Liu, K.3    Ghiso, J.4    Marchant, R.E.5    Zagorski, M.G.6
  • 68
    • 84903975397 scopus 로고    scopus 로고
    • Pathology and function of nuclear amyloid protein homeostasis matters
    • Von Mikecz A. (2014). Pathology and function of nuclear amyloid. Protein homeostasis matters. Nucleus 5: 311-17
    • (2014) Nucleus , vol.5 , pp. 311-317
    • Von Mikecz, A.1
  • 69
    • 29444442794 scopus 로고    scopus 로고
    • APP locus duplication causes autosomal dominant early-onset Alzheimer disease with cerebral amyloid angiopathy
    • Rovelet-Lecrux A, Hannequin D, Raux G, LeMeur N, Laquerrière A, et al. (2006). APP locus duplication causes autosomal dominant early-onset Alzheimer disease with cerebral amyloid angiopathy. Nat. Genet. 38: 24-26
    • (2006) Nat. Genet , vol.38 , pp. 24-26
    • Rovelet-Lecrux, A.1    Hannequin, D.2    Raux, G.3    Le Meur, N.4    Laquerrière, A.5
  • 71
    • 4644290985 scopus 로고    scopus 로고
    • Α-Synuclein locus duplication as a cause of familial Parkinson's disease
    • Chartier-Harlin MC, Kachergus J, Roumier C, Mouroux V, Douay X, et al. (2004). á-Synuclein locus duplication as a cause of familial Parkinson's disease. Lancet 364: 1167-69
    • (2004) Lancet , vol.364 , pp. 1167-1169
    • Chartier-Harlin, M.C.1    Kachergus, J.2    Roumier, C.3    Mouroux, V.4    Douay, X.5
  • 72
    • 57449091884 scopus 로고    scopus 로고
    • Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils
    • Paravastu AK, Leapman RD, Yau WM, Tycko R. (2008). Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils. PNAS 105: 18349-54
    • (2008) PNAS , vol.105 , pp. 18349-18354
    • Paravastu, A.K.1    Leapman, R.D.2    Yau, W.M.3    Tycko, R.4
  • 73
    • 40849120669 scopus 로고    scopus 로고
    • Amyloid fibrils of the HET-s(218-289) prion form a βsolenoid with a triangular hydrophobic core
    • Wasmer C, Lange A, Van Melckebeke H, Siemer AB, Riek R, Meier BH. (2008). Amyloid fibrils of the HET-s(218-289) prion form a βsolenoid with a triangular hydrophobic core. Science 319: 1523-26
    • (2008) Science , vol.319 , pp. 1523-1526
    • Wasmer, C.1    Lange, A.2    Van Melckebeke, H.3    Siemer, A.B.4    Riek, R.5    Meier, B.H.6
  • 74
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • Sunde M, Blake C. (1997). The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv. Protein Chem. 50: 123-59
    • (1997) Adv. Protein Chem , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.2
  • 75
    • 9344243513 scopus 로고    scopus 로고
    • FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils
    • Zandomeneghi G, Krebs MR, McCammon MG, Fändrich M. (2004). FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils. Protein Sci. 13: 3314-21
    • (2004) Protein Sci , vol.13 , pp. 3314-3321
    • Zandomeneghi, G.1    Krebs, M.R.2    McCammon, M.G.3    Fändrich, M.4
  • 76
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of proteins in human diseases
    • Eisenberg D, Jucker M. (2012). The amyloid state of proteins in human diseases. Cell 148: 1188-203
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 77
    • 3343003514 scopus 로고    scopus 로고
    • Techniques to study amyloid fibril formation in vitro
    • Nilsson MR. (2004). Techniques to study amyloid fibril formation in vitro. Methods 34: 151-60
    • (2004) Methods , vol.34 , pp. 151-160
    • Nilsson, M.R.1
  • 78
    • 84869021291 scopus 로고    scopus 로고
    • Development of positron emission tomography β-amyloid plaque imaging agents
    • Mathis CA, Mason NS, Lopresti BJ, Klunk WE. (2012). Development of positron emission tomography β-amyloid plaque imaging agents. Semin. Nucl. Med. 42: 423-32
    • (2012) Semin. Nucl. Med , vol.42 , pp. 423-432
    • Mathis, C.A.1    Mason, N.S.2    Lopresti, B.J.3    Klunk, W.E.4
  • 79
    • 0037126833 scopus 로고    scopus 로고
    • The correctly folded state of proteins: Is it a metastable state?
    • Gazit E. (2002). The correctly folded state of proteins: Is it a metastable state? Angew. Chem. Int. Ed. Engl. 41: 257-69
    • (2002) Angew. Chem. Int. Ed. Engl , vol.41 , pp. 257-269
    • Gazit, E.1
  • 81
    • 84976889285 scopus 로고    scopus 로고
    • In vivo aspects of protein folding and quality control
    • aac4354
    • Balchin D, Hayer-Hartl M, Hartl FU. (2016). In vivo aspects of protein folding and quality control. Science 353: aac4354
    • (2016) Science , vol.353
    • Balchin, D.1    Hayer-Hartl, M.2    Hartl, F.U.3
  • 82
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils
    • Petkova AT, Yau WM, Tycko R. (2006). Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils. Biochemistry 45: 498-512
    • (2006) Biochemistry , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.M.2    Tycko, R.3
  • 84
    • 84884217594 scopus 로고    scopus 로고
    • Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue
    • Lu JX, Qiang W, Yau WM, Schwieters CD, Meredith SC, Tycko R. (2013). Molecular structure of â-amyloid fibrils in Alzheimer's disease brain tissue. Cell 154: 1257-68
    • (2013) Cell , vol.154 , pp. 1257-1268
    • Lu, J.X.1    Qiang, W.2    Yau, W.M.3    Schwieters, C.D.4    Meredith, S.C.5    Tycko, R.6
  • 85
    • 84982685920 scopus 로고    scopus 로고
    • Atomic resolution structure ofmonomorphic Aβ42 amyloid fibrils
    • Colvin MT, Silvers R, Ni QZ, Can TV, Sergeyev I, et al. (2016). Atomic resolution structure ofmonomorphic Aβ42 amyloid fibrils. J. Am. Chem. Soc. 138: 9663-74
    • (2016) J. Am. Chem. Soc , vol.138 , pp. 9663-9674
    • Colvin, M.T.1    Silvers, R.2    Ni, Q.Z.3    Can, T.V.4    Sergeyev, I.5
  • 86
    • 36749033116 scopus 로고    scopus 로고
    • Peptide conformation and supramolecular organization in amylin fibrils: Constraints from solid-state NMR
    • Luca S, Yau WM, Leapman R, Tycko R. (2007). Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR. Biochemistry 46: 13505-22
    • (2007) Biochemistry , vol.46 , pp. 13505-13522
    • Luca, S.1    Yau, W.M.2    Leapman, R.3    Tycko, R.4
  • 87
    • 84992125283 scopus 로고    scopus 로고
    • Structural characterization of fibrils from recombinant human islet amyloid polypeptide by solid-state NMR: The central FGAILS segment is part of the β-sheet core
    • Weirich F, Gremer L, Mirecka EA, Schiefer S, Hoyer W, Heise H. (2016). Structural characterization of fibrils from recombinant human islet amyloid polypeptide by solid-state NMR: The central FGAILS segment is part of the β-sheet core. PLOS ONE 11: e0161243
    • (2016) Plos One , vol.11 , pp. e0161243
    • Weirich, F.1    Gremer, L.2    Mirecka, E.A.3    Schiefer, S.4    Hoyer, W.5    Heise, H.6
  • 88
    • 84925337340 scopus 로고    scopus 로고
    • Comparisons with amyloid-β reveal an aspartate residue that stabilizes fibrils of the aortic amyloid peptide medin
    • Davies HA, Madine J, Middleton DA. (2015). Comparisons with amyloid-β reveal an aspartate residue that stabilizes fibrils of the aortic amyloid peptide medin. J. Biol. Chem. 290: 7791-803
    • (2015) J. Biol. Chem , vol.290 , pp. 7791-7803
    • Davies, H.A.1    Madine, J.2    Middleton, D.A.3
  • 89
    • 84957824317 scopus 로고    scopus 로고
    • Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core
    • Hoop CL, Lin HK, Kar K, Magyarfalvi G, Lamley JM, et al. (2016). Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core. PNAS 113: 1546-51
    • (2016) PNAS , vol.113 , pp. 1546-1551
    • Hoop, C.L.1    Lin, H.K.2    Kar, K.3    Magyarfalvi, G.4    Lamley, J.M.5
  • 90
    • 80052320137 scopus 로고    scopus 로고
    • Intermolecular alignment in Y145Stop human prion protein amyloid fibrils probed by solid-state NMR spectroscopy
    • Helmus JJ, Surewicz K, Apostol MI, Surewicz WK, Jaroniec CP. (2011). Intermolecular alignment in Y145Stop human prion protein amyloid fibrils probed by solid-state NMR spectroscopy. J. Am. Chem. Soc. 133: 13934-37
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 13934-13937
    • Helmus, J.J.1    Surewicz, K.2    Apostol, M.I.3    Surewicz, W.K.4    Jaroniec, C.P.5
  • 91
    • 84920755041 scopus 로고    scopus 로고
    • Progress towards structural understanding of infectious sheep PrP-amyloid
    • Müller H, Brener O, Andreoletti O, Piechatzek T, Willbold D, et al. (2014). Progress towards structural understanding of infectious sheep PrP-amyloid. Prion 8: 344-58
    • (2014) Prion , vol.8 , pp. 344-358
    • Müller, H.1    Brener, O.2    Andreoletti, O.3    Piechatzek, T.4    Willbold, D.5
  • 92
    • 77951214424 scopus 로고    scopus 로고
    • An Achilles? Heel in an amyloidogenic protein and its repair: Insulin fibrillation and therapeutic design
    • Yang Y, Petkova A, Huang K, Xu B, Hua QX, et al. (2010). An Achilles? heel in an amyloidogenic protein and its repair: insulin fibrillation and therapeutic design. J. Biol. Chem. 285: 10806-21
    • (2010) J. Biol. Chem , vol.285 , pp. 10806-10821
    • Yang, Y.1    Petkova, A.2    Huang, K.3    Xu, B.4    Hua, Q.X.5
  • 93
    • 81255200361 scopus 로고    scopus 로고
    • Experimentally derived structural constraints for amyloid fibrils of wild-type transthyretin
    • Bateman DA, Tycko R, Wickner RB. (2011). Experimentally derived structural constraints for amyloid fibrils of wild-type transthyretin. Biophys. J. 101: 2485-92
    • (2011) Biophys. J. , vol.101 , pp. 2485-2492
    • Bateman, D.A.1    Tycko, R.2    Wickner, R.B.3
  • 95
    • 84878090825 scopus 로고    scopus 로고
    • Role of aromatic residues in amyloid fibril formation of human calcitonin by solid-state 13CNMRandmolecular dynamics simulation
    • Itoh-Watanabe H, Kamihira-Ishijima M, Javkhlantugs N, Inoue R, Itoh Y, et al. (2013). Role of aromatic residues in amyloid fibril formation of human calcitonin by solid-state 13CNMRandmolecular dynamics simulation. Phys. Chem. Chem. Phys. 15: 8890-901
    • (2013) Phys. Chem. Chem. Phys , vol.15 , pp. 8890-8901
    • Itoh-Watanabe, H.1    Kamihira-Ishijima, M.2    Javkhlantugs, N.3    Inoue, R.4    Itoh, Y.5
  • 96
    • 84899766632 scopus 로고    scopus 로고
    • Secondary structure in the core of amyloid fibrils formed from human β2m and its truncated variant N6
    • Su Y, Sarell CJ, Eddy MT, Debelouchina GT, Andreas LB, et al. (2014). Secondary structure in the core of amyloid fibrils formed from human β2m and its truncated variant N6. J. Am. Chem. Soc. 136: 6313-25
    • (2014) J. Am. Chem. Soc , vol.136 , pp. 6313-6325
    • Su, Y.1    Sarell, C.J.2    Eddy, M.T.3    Debelouchina, G.T.4    Andreas, L.B.5
  • 97
    • 27644518721 scopus 로고    scopus 로고
    • Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR
    • Heise H, Hoyer W, Becker S, Andronesi OC, Riedel D, Baldus M. (2005). Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR. PNAS 102: 15871-76
    • (2005) PNAS , vol.102 , pp. 15871-15876
    • Heise, H.1    Hoyer, W.2    Becker, S.3    Andronesi, O.C.4    Riedel, D.5    Baldus, M.6
  • 99
    • 80051672851 scopus 로고    scopus 로고
    • Structured regions of α-synuclein fibrils include the early-onset Parkinson's disease mutation sites
    • Comellas G, Lemkau LR, Nieuwkoop AJ, Kloepper KD, Ladror DT, et al. (2011). Structured regions of á-synuclein fibrils include the early-onset Parkinson's disease mutation sites. J. Mol. Biol. 411: 881-95
    • (2011) J. Mol. Biol , vol.411 , pp. 881-895
    • Comellas, G.1    Lemkau, L.R.2    Nieuwkoop, A.J.3    Kloepper, K.D.4    Ladror, D.T.5
  • 100
    • 84897135636 scopus 로고    scopus 로고
    • Unlike twins: An NMR comparison of two α-synuclein polymorphs featuring different toxicity
    • Gath J, Bousset L, Habenstein B, Melki R, Böckmann A, Meier BH. (2014). Unlike twins: an NMR comparison of two α-synuclein polymorphs featuring different toxicity. PLOS ONE 9: e90659
    • (2014) Plos One , vol.9 , pp. e90659
    • Gath, J.1    Bousset, L.2    Habenstein, B.3    Melki, R.4    Böckmann, A.5    Meier, B.H.6
  • 103
    • 77957324146 scopus 로고    scopus 로고
    • Atomic-resolution threedimensional structure of HET-s 218-289) amyloid fibrils by solid-state NMR spectroscopy
    • Van Melckebeke H, Wasmer C, Lange A, Ab E, Loquet A, et al. (2010). Atomic-resolution threedimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy. J. Am. Chem. Soc. 132: 13765-75
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 13765-13775
    • Van Melckebeke, H.1    Wasmer, C.2    Lange, A.3    Ab, E.4    Loquet, A.5
  • 104
    • 84989868977 scopus 로고    scopus 로고
    • The structural architecture of an infectious mammalian prion using electron cryomicroscopy
    • Vázquez-Fernández E, Vos MR, Afanasyev P, Cebey L, Sevillano AM, et al. (2016). The structural architecture of an infectious mammalian prion using electron cryomicroscopy. PLOS Pathog. 12: e1005835
    • (2016) Plos Pathog , vol.12 , pp. e1005835
    • Vázquez-Fernández, E.1    Vos, M.R.2    Afanasyev, P.3    Cebey, L.4    Sevillano, A.M.5
  • 107
    • 14044278010 scopus 로고    scopus 로고
    • New model for crystalline polyglutamine assemblies and their connection with amyloid fibrils
    • Sikorski P, Atkins E. (2005). New model for crystalline polyglutamine assemblies and their connection with amyloid fibrils. Biomacromolecules 6: 425-32
    • (2005) Biomacromolecules , vol.6 , pp. 425-432
    • Sikorski, P.1    Atkins, E.2
  • 108
    • 84864575689 scopus 로고    scopus 로고
    • X-ray fibre diffraction studies of amyloid fibrils
    • Morris KL, Serpell LC. (2012). X-ray fibre diffraction studies of amyloid fibrils. MethodsMol. Biol. 849: 121-35
    • (2012) MethodsMol. Biol , vol.849 , pp. 121-135
    • Morris, K.L.1    Serpell, L.C.2
  • 109
    • 84942522975 scopus 로고    scopus 로고
    • Structure of the toxic core of α-synuclein from invisible crystals
    • Rodriguez JA, Ivanova MI, Sawaya MR, Cascio D, Reyes FE, et al. (2015). Structure of the toxic core of α-synuclein from invisible crystals. Nature 525: 486-90
    • (2015) Nature , vol.525 , pp. 486-490
    • Rodriguez, J.A.1    Ivanova, M.I.2    Sawaya, M.R.3    Cascio, D.4    Reyes, F.E.5
  • 111
    • 1242316998 scopus 로고    scopus 로고
    • Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy
    • Olofsson A, Ippel JH, Wijmenga SS, Lundgren E, Ohman A. (2004). Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy. J. Biol. Chem. 279: 5699-707
    • (2004) J. Biol. Chem , vol.279 , pp. 5699-5707
    • Olofsson, A.1    Ippel, J.H.2    Wijmenga, S.S.3    Lundgren, E.4    Ohman, A.5
  • 112
    • 84988557105 scopus 로고    scopus 로고
    • Solid-state NMR studies reveal native-like β-sheet structures in transthyretin amyloid
    • Lim KH, Dasari AK, Hung I, Gan Z, Kelly JW, et al. (2016). Solid-state NMR studies reveal native-like β-sheet structures in transthyretin amyloid. Biochemistry 55: 5272-78
    • (2016) Biochemistry , vol.55 , pp. 5272-5278
    • Lim, K.H.1    Dasari, A.K.2    Hung, I.3    Gan, Z.4    Kelly, J.W.5
  • 113
    • 0038442784 scopus 로고    scopus 로고
    • Amyloid-like filaments and waterfilled nanotubes formed by SOD1 mutant proteins linked to familial ALS
    • Elam JS, Taylor AB, Strange R, Antonyuk S, Doucette PA, et al. (2003). Amyloid-like filaments and waterfilled nanotubes formed by SOD1 mutant proteins linked to familial ALS. Nat. Struct. Biol. 10: 461-67
    • (2003) Nat. Struct. Biol , vol.10 , pp. 461-467
    • Elam, J.S.1    Taylor, A.B.2    Strange, R.3    Antonyuk, S.4    Doucette, P.A.5
  • 114
    • 27544500011 scopus 로고    scopus 로고
    • 3D domain-swapped human cystatin C with amyloidlike intermolecular β-sheets
    • Janowski R, Kozak M, Abrahamson M, Grubb A, Jaskolski M. (2005). 3D domain-swapped human cystatin C with amyloidlike intermolecular β-sheets. Proteins 61: 570-78
    • (2005) Proteins , vol.61 , pp. 570-578
    • Janowski, R.1    Kozak, M.2    Abrahamson, M.3    Grubb, A.4    Jaskolski, M.5
  • 115
    • 24644510813 scopus 로고    scopus 로고
    • Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure
    • Sambashivan S, Liu Y, Sawaya MR, Gingery M, Eisenberg D. (2005). Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure. Nature 437: 266-69
    • (2005) Nature , vol.437 , pp. 266-269
    • Sambashivan, S.1    Liu, Y.2    Sawaya, M.R.3    Gingery, M.4    Eisenberg, D.5
  • 116
    • 33744497267 scopus 로고    scopus 로고
    • Runaway domain swapping in amyloid-like fibrils of T7 endonuclease I
    • Guo Z, Eisenberg D. (2006). Runaway domain swapping in amyloid-like fibrils of T7 endonuclease I. PNAS 103: 8042-47
    • (2006) PNAS , vol.103 , pp. 8042-8047
    • Guo, Z.1    Eisenberg, D.2
  • 117
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecularlevel polymorphism in Alzheimer's β-amyloid fibrils
    • Petkova AT, Leapman RD, Guo Z, Yau WM, Mattson MP, Tycko R. (2005). Self-propagating, molecularlevel polymorphism in Alzheimer's β-amyloid fibrils. Science 307: 262-65
    • (2005) Science , vol.307 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.M.4    Mattson, M.P.5    Tycko, R.6
  • 118
    • 84870175936 scopus 로고    scopus 로고
    • Cross-seeding of fibrils from two types of insulin induces new amyloid strains
    • Surmacz-Chwedoruk W, Nieznánska H, Wójcik S, Dzwolak W. (2012). Cross-seeding of fibrils from two types of insulin induces new amyloid strains. Biochemistry 51: 9460-69
    • (2012) Biochemistry , vol.51 , pp. 9460-9469
    • Surmacz-Chwedoruk, W.1    Nieznánska, H.2    Wójcik, S.3    Dzwolak, W.4
  • 119
    • 84934983329 scopus 로고    scopus 로고
    • Α -Synuclein strains cause distinct synucleinopathies after local and systemic administration
    • Peelaerts W, Bousset L, Van der Perren A, Moskalyuk A, Pulizzi R, et al. 2015.α-Synuclein strains cause distinct synucleinopathies after local and systemic administration. Nature 522: 340-44
    • (2015) Nature , vol.522 , pp. 340-344
    • Peelaerts, W.1    Bousset, L.2    Van Der Perren, A.3    Moskalyuk, A.4    Pulizzi, R.5
  • 120
    • 36049020231 scopus 로고    scopus 로고
    • A general model of prion strains and their pathogenicity
    • Collinge J, Clarke AR. (2007). A general model of prion strains and their pathogenicity. Science 318: 930-36
    • (2007) Science , vol.318 , pp. 930-936
    • Collinge, J.1    Clarke, A.R.2
  • 121
    • 0037174998 scopus 로고    scopus 로고
    • Structural and dynamic features of Alzheimer's Aβpeptide in amyloid fibrils studied by site-directed spin labeling
    • Török M, Milton S, Kayed R, Wu P, McIntire T, et al. (2002). Structural and dynamic features of Alzheimer's Aβpeptide in amyloid fibrils studied by site-directed spin labeling. J. Biol. Chem. 277: 40810-15
    • (2002) J. Biol. Chem , vol.277 , pp. 40810-40815
    • Török, M.1    Milton, S.2    Kayed, R.3    Wu, P.4    McIntire, T.5
  • 122
    • 28444442999 scopus 로고    scopus 로고
    • 3D structure of Alzheimer's amyloid-β(1-42) fibrils
    • Lührs T, Ritter C, Adrian M, Riek-Loher D, Bohrmann B, et al. (2005). 3D structure of Alzheimer's amyloid-β(1-42) fibrils. PNAS 102: 17342-47
    • (2005) PNAS , vol.102 , pp. 17342-17347
    • Lührs, T.1    Ritter, C.2    Adrian, M.3    Riek-Loher, D.4    Bohrmann, B.5
  • 123
    • 0141733169 scopus 로고    scopus 로고
    • Structural organization ofα-synuclein fibrils studied by site-directed spin labeling
    • Der-Sarkissian A, Jao CC, Chen J, Langen R. (2003). Structural organization ofα-synuclein fibrils studied by site-directed spin labeling. J. Biol. Chem. 278: 37530-35
    • (2003) J. Biol. Chem , vol.278 , pp. 37530-37535
    • Der-Sarkissian, A.1    Jao, C.C.2    Chen, J.3    Langen, R.4
  • 124
    • 34548359337 scopus 로고    scopus 로고
    • Investigation of α-synuclein fibril structure by sitedirected spin labeling
    • Chen M, Margittai M, Chen J, Langen R. (2007). Investigation of α-synuclein fibril structure by sitedirected spin labeling. J. Biol. Chem. 282: 24970-79
    • (2007) J. Biol. Chem , vol.282 , pp. 24970-24979
    • Chen, M.1    Margittai, M.2    Chen, J.3    Langen, R.4
  • 125
    • 3142699791 scopus 로고    scopus 로고
    • Template-assisted filament growth by parallel stacking of tau
    • Margittai M, Langen R. (2004). Template-assisted filament growth by parallel stacking of tau. PNAS 101: 10278-83
    • (2004) PNAS , vol.101 , pp. 10278-10283
    • Margittai, M.1    Langen, R.2
  • 126
    • 84863116618 scopus 로고    scopus 로고
    • Fibril structure of human islet amyloid polypeptide
    • Bedrood S, Li Y, Isas JM, Hegde BG, Baxa U, et al. (2012). Fibril structure of human islet amyloid polypeptide. J. Biol. Chem. 287: 5235-41
    • (2012) J. Biol. Chem , vol.287 , pp. 5235-5241
    • Bedrood, S.1    Li, Y.2    Isas, J.M.3    Hegde, B.G.4    Baxa, U.5
  • 127
    • 77952759080 scopus 로고    scopus 로고
    • Stacked sets of parallel, in-register β-strands of β2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling
    • Ladner CL, Chen M, Smith DP, Platt GW, Radford SE, Langen R. (2010). Stacked sets of parallel, in-register β-strands of β2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling. J. Biol. Chem. 285: 17137-47
    • (2010) J. Biol. Chem , vol.285 , pp. 17137-17147
    • Ladner, C.L.1    Chen, M.2    Smith, D.P.3    Platt, G.W.4    Radford, S.E.5    Langen, R.6
  • 128
    • 78149307698 scopus 로고    scopus 로고
    • The α-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel β-sheet structure in PrP fibrils: Evidence from solid state nuclear magnetic resonance
    • Tycko R, Savtchenko R, Ostapchenko V, Makarava N, Baskakov I. (2010). The α-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel β-sheet structure in PrP fibrils: evidence from solid state nuclear magnetic resonance. Biochemistry 49: 9488-97
    • (2010) Biochemistry , vol.49 , pp. 9488-9497
    • Tycko, R.1    Savtchenko, R.2    Ostapchenko, V.3    Makarava, N.4    Baskakov, I.5
  • 129
    • 79952754330 scopus 로고    scopus 로고
    • Structural evolution of Iowa mutant β-amyloid fibrils from polymorphic to homogeneous states under repeated seeded growth
    • Qiang W, Yau WM, Tycko R. (2011). Structural evolution of Iowa mutant β-amyloid fibrils from polymorphic to homogeneous states under repeated seeded growth. J. Am. Chem. Soc. 133: 4018-29
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 4018-4029
    • Qiang, W.1    Yau, W.M.2    Tycko, R.3
  • 130
    • 79960005237 scopus 로고    scopus 로고
    • Prediction of amyloid aggregation in vivo
    • Belli M, Ramazzotti M, Chiti F. 2011 Prediction of amyloid aggregation in vivo. EMBO Rep. 12: 657-63
    • (2011) EMBO Rep , vol.12 , pp. 657-663
    • Belli, M.1    Ramazzotti, M.2    Chiti, F.3
  • 131
    • 20444403757 scopus 로고    scopus 로고
    • Prediction of aggregationprone and aggregation-susceptible regions in proteins associated with neurodegenerative diseases
    • Pawar AP, Dubay KF, Zurdo J, Chiti F, Vendruscolo M, Dobson CM. (2005). Prediction of aggregationprone and aggregation-susceptible regions in proteins associated with neurodegenerative diseases. J. Mol. Biol. 350: 379-92
    • (2005) J. Mol. Biol , vol.350 , pp. 379-392
    • Pawar, A.P.1    Dubay, K.F.2    Zurdo, J.3    Chiti, F.4    Vendruscolo, M.5    Dobson, C.M.6
  • 133
  • 134
    • 84885455505 scopus 로고    scopus 로고
    • Conformational features of tau fibrils from Alzheimer's disease brain are faithfully propagated by unmodified recombinant protein
    • Morozova OA, March ZM, Robinson AS, Colby DW. (2013). Conformational features of tau fibrils from Alzheimer's disease brain are faithfully propagated by unmodified recombinant protein. Biochemistry 52: 6960-67
    • (2013) Biochemistry , vol.52 , pp. 6960-6967
    • Morozova, O.A.1    March, Z.M.2    Robinson, A.S.3    Colby, D.W.4
  • 135
    • 72149118250 scopus 로고    scopus 로고
    • An analytical solution to the kinetics of breakable filament assembly
    • Knowles TP, Waudby CA, Devlin GL, Cohen SI, Aguzzi A, et al. (2009). An analytical solution to the kinetics of breakable filament assembly. Science 326: 1533-37
    • (2009) Science , vol.326 , pp. 1533-1537
    • Knowles, T.P.1    Waudby, C.A.2    Devlin, G.L.3    Cohen, S.I.4    Aguzzi, A.5
  • 136
    • 0027258525 scopus 로고
    • The carboxy terminus of theβamyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • Jarrett JT, Berger EP, Lansbury PTJr. (1993). The carboxy terminus of theâamyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32: 4693-97
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury, P.T.3
  • 137
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of protein aggregation kinetics
    • Ferrone F. (1999). Analysis of protein aggregation kinetics. Methods Enzymol. 309: 256-74
    • (1999) Methods Enzymol , vol.309 , pp. 256-274
    • Ferrone, F.1
  • 138
    • 59349083966 scopus 로고    scopus 로고
    • Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature
    • Morris AM, Watzky MA, Finke RG. (2009). Protein aggregation kinetics, mechanism, and curve-fitting: a review of the literature. Biochim. Biophys. Acta 1794: 375-97
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 375-397
    • Morris, A.M.1    Watzky, M.A.2    Finke, R.G.3
  • 140
    • 0037015081 scopus 로고    scopus 로고
    • Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation
    • Chen S, Ferrone FA, Wetzel R. (2002). Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation. PNAS 99: 11884-89
    • (2002) PNAS , vol.99 , pp. 11884-11889
    • Chen, S.1    Ferrone, F.A.2    Wetzel, R.3
  • 141
    • 84920773998 scopus 로고    scopus 로고
    • Assembly of Aβproceeds via monomeric nuclei
    • Ferrone FA. (2015). Assembly of Aβproceeds via monomeric nuclei. J. Mol. Biol. 427: 287-90
    • (2015) J. Mol. Biol , vol.427 , pp. 287-290
    • Ferrone, F.A.1
  • 142
    • 0032968132 scopus 로고    scopus 로고
    • Quantifying the kinetic parameters of prion replication
    • Masel J, Jansen VAA, Nowak MA. (1999). Quantifying the kinetic parameters of prion replication. Biophys. Chem. 77: 139-52
    • (1999) Biophys. Chem , vol.77 , pp. 139-152
    • Masel, J.1    Jansen, V.A.A.2    Nowak, M.A.3
  • 143
    • 0035815664 scopus 로고    scopus 로고
    • Evidence for a partially folded intermediate in α-synuclein fibril formation
    • Uversky VN, Li J, Fink AL. (2001). Evidence for a partially folded intermediate in α-synuclein fibril formation. J. Biol. Chem. 276: 10737-44
    • (2001) J. Biol. Chem , vol.276 , pp. 10737-10744
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 144
    • 27344435254 scopus 로고    scopus 로고
    • Polyglutamine aggregation nucleation: Thermodynamics of a highly unfavorable protein folding reaction
    • Bhattacharyya AM, Thakur AK, Wetzel R. (2005). Polyglutamine aggregation nucleation: thermodynamics of a highly unfavorable protein folding reaction. PNAS 102: 15400-5
    • (2005) PNAS , vol.102 , pp. 15400-15405
    • Bhattacharyya, A.M.1    Thakur, A.K.2    Wetzel, R.3
  • 145
    • 78650208860 scopus 로고    scopus 로고
    • Probing the nucleus model for oligomer formation during insulin amyloid fibrillogenesis
    • Pease LF 3rd, Sorci M, Guha S, Tsai DH, Zachariah MR, et al. (2010). Probing the nucleus model for oligomer formation during insulin amyloid fibrillogenesis. Biophys. J. 99: 3979-85
    • (2010) Biophys. J. , vol.99 , pp. 3979-3985
    • Pease, L.F.1    Sorci, M.2    Guha, S.3    Tsai, D.H.4    Zachariah, M.R.5
  • 146
    • 70449437082 scopus 로고    scopus 로고
    • Influence of aggregation propensity and stability on amyloid fibril formation as studied by Fourier transform infrared spectroscopy and two-dimensional COS analysis
    • Cerdà-Costa N, De la Arada I, Avilés FX, Arrondo JL, Villegas S. (2009). Influence of aggregation propensity and stability on amyloid fibril formation as studied by Fourier transform infrared spectroscopy and two-dimensional COS analysis. Biochemistry 48: 10582-90
    • (2009) Biochemistry , vol.48 , pp. 10582-10590
    • Cerdà-Costa, N.1    De La Arada, I.2    Avilés, F.X.3    Arrondo, J.L.4    Villegas, S.5
  • 147
    • 85046915636 scopus 로고    scopus 로고
    • Amyloid fibrils of human prion protein are spun and woven from morphologically disordered aggregates
    • Almstedt K, Nyström S, Nilsson KP, Hammarström P. (2009). Amyloid fibrils of human prion protein are spun and woven from morphologically disordered aggregates. Prion 3: 224-35
    • (2009) Prion , vol.3 , pp. 224-235
    • Almstedt, K.1    Nyström, S.2    Nilsson, K.P.3    Hammarström, P.4
  • 148
    • 64049119303 scopus 로고    scopus 로고
    • Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism
    • Thakur AK, Jayaraman M, Mishra R, Thakur M, Chellgren VM, et al. (2009). Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism. Nat. Struct. Mol. Biol. 16: 380-89
    • (2009) Nat. Struct. Mol. Biol , vol.16 , pp. 380-389
    • Thakur, A.K.1    Jayaraman, M.2    Mishra, R.3    Thakur, M.4    Chellgren, V.M.5
  • 149
    • 79953230499 scopus 로고    scopus 로고
    • The molecular basis of distinct aggregation pathways of islet amyloid polypeptide
    • Wei L, Jiang P, Xu W, Li H, Zhang H, et al. (2011). The molecular basis of distinct aggregation pathways of islet amyloid polypeptide. J. Biol. Chem. 286: 6291-300
    • (2011) J. Biol. Chem , vol.286 , pp. 6291-6300
    • Wei, L.1    Jiang, P.2    Xu, W.3    Li, H.4    Zhang, H.5
  • 150
    • 84906501636 scopus 로고    scopus 로고
    • New insight into amyloid fibril formation of hen egg white lysozyme using a two-step temperature-dependent FTIR approach
    • Zou Y, Hao W, Li H, Gao Y, Sun Y, Ma G. (2014). New insight into amyloid fibril formation of hen egg white lysozyme using a two-step temperature-dependent FTIR approach. J. Phys. Chem. B 118: 9834-43
    • (2014) J. Phys. Chem. B , vol.118 , pp. 9834-9843
    • Zou, Y.1    Hao, W.2    Li, H.3    Gao, Y.4    Sun, Y.5    Ma, G.6
  • 151
    • 57749098600 scopus 로고    scopus 로고
    • Amyloid formation by globular proteins under native conditions
    • Chiti F, Dobson CM. (2009). Amyloid formation by globular proteins under native conditions. Nat. Chem. Biol. 5: 15-22
    • (2009) Nat. Chem. Biol , vol.5 , pp. 15-22
    • Chiti, F.1    Dobson, C.M.2
  • 152
    • 27744607600 scopus 로고    scopus 로고
    • Fully metallated S134N Cu, Znsuperoxide dismutase displays abnormal mobility and intermolecular contacts in solution
    • Banci L, Bertini I, D'Amelio N, Gaggelli E, Libralesso E, et al. (2005). Fully metallated S134N Cu, Znsuperoxide dismutase displays abnormal mobility and intermolecular contacts in solution. J. Biol. Chem. 280: 35815-21
    • (2005) J. Biol. Chem , vol.280 , pp. 35815-35821
    • Banci, L.1    Bertini, I.2    D'Amelio, N.3    Gaggelli, E.4    Libralesso, E.5
  • 153
    • 68649095591 scopus 로고    scopus 로고
    • Native-like aggregation of the acylphosphatase from Sulfolobus solfataricus and its biological implications
    • Bemporad F, Chiti F. (2009). Native-like aggregation of the acylphosphatase from Sulfolobus solfataricus and its biological implications. FEBS Lett. 583: 2630-38
    • (2009) FEBS Lett , vol.583 , pp. 2630-2638
    • Bemporad, F.1    Chiti, F.2
  • 154
    • 28444464509 scopus 로고    scopus 로고
    • Amyloid formation of a protein in the absence of initial unfolding and destabilization of the native state
    • Soldi G, Bemporad F, Torrassa S, Relini A, Ramazzotti M, et al. (2005). Amyloid formation of a protein in the absence of initial unfolding and destabilization of the native state. Biophys. J. 89: 4234-44
    • (2005) Biophys. J. , vol.89 , pp. 4234-4244
    • Soldi, G.1    Bemporad, F.2    Torrassa, S.3    Relini, A.4    Ramazzotti, M.5
  • 155
    • 84860013075 scopus 로고    scopus 로고
    • Structure of an intermediate state in protein folding and aggregation
    • Neudecker P, Robustelli P, Cavalli A, Walsh P, Lundström P, et al. (2012). Structure of an intermediate state in protein folding and aggregation. Science 336: 362-66
    • (2012) Science , vol.336 , pp. 362-366
    • Neudecker, P.1    Robustelli, P.2    Cavalli, A.3    Walsh, P.4    Lundström, P.5
  • 156
    • 84917690463 scopus 로고    scopus 로고
    • Amyloid formation by human carboxypeptidase D transthyretin-like domain under physiological conditions
    • Garcia-Pardo J, Graña-Montes R, Fernandez-Mendez M, Ruyra A, Roher N, et al. (2014). Amyloid formation by human carboxypeptidase D transthyretin-like domain under physiological conditions. J. Biol. Chem. 289: 33783-96
    • (2014) J. Biol. Chem , vol.289 , pp. 33783-33796
    • Garcia-Pardo, J.1    Graña-Montes, R.2    Fernandez-Mendez, M.3    Ruyra, A.4    Roher, N.5
  • 157
    • 79251572023 scopus 로고    scopus 로고
    • Functional interactions as a survival strategy against abnormal aggregation
    • Masino L, Nicastro G, Calder L, Vendruscolo M, Pastore A. (2011). Functional interactions as a survival strategy against abnormal aggregation. FASEB J. 25: 45-54
    • (2011) FASEB J. , vol.25 , pp. 45-54
    • Masino, L.1    Nicastro, G.2    Calder, L.3    Vendruscolo, M.4    Pastore, A.5
  • 158
    • 84890546088 scopus 로고    scopus 로고
    • Delicate balance between functionally required flexibility and aggregation risk in a β-rich protein
    • Ferrolino MC, Zhuravleva A, Budyak IL, Krishnan B, Gierasch LM. (2013). Delicate balance between functionally required flexibility and aggregation risk in a β-rich protein. Biochemistry 52: 8843-54
    • (2013) Biochemistry , vol.52 , pp. 8843-8854
    • Ferrolino, M.C.1    Zhuravleva, A.2    Budyak, I.L.3    Krishnan, B.4    Gierasch, L.M.5
  • 159
    • 67650079178 scopus 로고    scopus 로고
    • Structurally distinct amyloid protofibrils form on separate pathways of aggregation of a small protein
    • Kumar S, Udgaonkar JB. (2009). Structurally distinct amyloid protofibrils form on separate pathways of aggregation of a small protein. Biochemistry 48: 6441-49
    • (2009) Biochemistry , vol.48 , pp. 6441-6449
    • Kumar, S.1    Udgaonkar, J.B.2
  • 160
    • 0009586942 scopus 로고    scopus 로고
    • Understanding protein folding via the free-energy surfaces from theory and experiment
    • Dinner AR, Šali A, Smith LJ, Dobson CM, Karplus M. (2000). Understanding protein folding via the free-energy surfaces from theory and experiment. Trends Biochem. Sci. 7: 331-39
    • (2000) Trends Biochem. Sci , vol.7 , pp. 331-339
    • Dinner, A.R.1    Šali, A.2    Smith, L.J.3    Dobson, C.M.4    Karplus, M.5
  • 161
    • 0037046151 scopus 로고    scopus 로고
    • Islet amyloid: Phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis
    • Padrick SB, Miranker AD. (2002). Islet amyloid: Phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis. Biochemistry 41: 4694-703
    • (2002) Biochemistry , vol.41 , pp. 4694-4703
    • Padrick, S.B.1    Miranker, A.D.2
  • 162
    • 84863983902 scopus 로고    scopus 로고
    • Evidence for the existence of a secondary pathway for fibril growth during the aggregation of tau
    • Ramachandran G, Udgaonkar JB. (2012). Evidence for the existence of a secondary pathway for fibril growth during the aggregation of tau. J. Mol. Biol. 421: 296-314
    • (2012) J. Mol. Biol , vol.421 , pp. 296-314
    • Ramachandran, G.1    Udgaonkar, J.B.2
  • 163
    • 84878994873 scopus 로고    scopus 로고
    • Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism
    • Cohen SI, Linse S, Luheshi LM, Hellstrand E, White DA, et al. (2013). Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism. PNAS 110: 9758-63
    • (2013) PNAS , vol.110 , pp. 9758-9763
    • Cohen, S.I.1    Linse, S.2    Luheshi, L.M.3    Hellstrand, E.4    White, D.A.5
  • 164
    • 84903696629 scopus 로고    scopus 로고
    • Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides
    • Meisl G, Yang X, Hellstrand E, Frohm B, Kirkegaard JB, et al. (2014). Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides. PNAS 111: 9384-89
    • (2014) PNAS , vol.111 , pp. 9384-9389
    • Meisl, G.1    Yang, X.2    Hellstrand, E.3    Frohm, B.4    Kirkegaard, J.B.5
  • 165
    • 84901660540 scopus 로고    scopus 로고
    • Solution conditions determine the relative importance of nucleation and growth processes inα-synuclein aggregation
    • Buell AK, Galvagnion C, Gaspar R, Sparr E, Vendruscolo M, et al. (2014). Solution conditions determine the relative importance of nucleation and growth processes inα-synuclein aggregation. PNAS 111: 7671-76
    • (2014) PNAS , vol.111 , pp. 7671-7676
    • Buell, A.K.1    Galvagnion, C.2    Gaspar, R.3    Sparr, E.4    Vendruscolo, M.5
  • 166
    • 84963566241 scopus 로고    scopus 로고
    • The S/T-rich motif in the DNAJB6 chaperone delays polyglutamine aggregation and the onset of disease in a mouse model
    • Kakkar V, Månsson C, de Mattos EP, Bergink S, van der Zwaag M, et al. (2016). The S/T-rich motif in the DNAJB6 chaperone delays polyglutamine aggregation and the onset of disease in a mouse model. Mol. Cell 62: 272-83
    • (2016) Mol. Cell , vol.62 , pp. 272-283
    • Kakkar, V.1    Månsson, C.2    De Mattos, E.P.3    Bergink, S.4    Van Der Zwaag, M.5
  • 167
    • 84875425248 scopus 로고    scopus 로고
    • Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2
    • Xu LQ, Wu S, Buell AK, Cohen SI, Chen LJ, et al. (2013). Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2. Philos. Trans. R. Soc. B. 368: 20110410
    • (2013) Philos. Trans. R. Soc. B. , vol.368 , pp. 20110410
    • Xu, L.Q.1    Wu, S.2    Buell, A.K.3    Cohen, S.I.4    Chen, L.J.5
  • 168
    • 84923362547 scopus 로고    scopus 로고
    • Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation
    • Galvagnion C, Buell AK, Meisl G, Michaels TC, Vendruscolo M, et al. (2015). Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation. Nat. Chem. Biol. 11: 229-34
    • (2015) Nat. Chem. Biol , vol.11 , pp. 229-234
    • Galvagnion, C.1    Buell, A.K.2    Meisl, G.3    Michaels, T.C.4    Vendruscolo, M.5
  • 169
    • 84961620982 scopus 로고    scopus 로고
    • Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation
    • Arosio P, Michaels TC, Linse S, Månsson C, Emanuelsson C, et al. (2016). Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation. Nat. Commun. 7: 10948
    • (2016) Nat. Commun , vol.7 , pp. 10948
    • Arosio, P.1    Michaels, T.C.2    Linse, S.3    Månsson, C.4    Emanuelsson, C.5
  • 170
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, et al. (2003). Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300: 486-89
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5
  • 171
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-βprotein assembly in the brain impairs memory
    • Lesné S, Koh MT, Kotilinek L, Kayed R, Glabe CG, et al. (2006). A specific amyloid-βprotein assembly in the brain impairs memory. Nature 440: 352-57
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesné, S.1    Koh, M.T.2    Kotilinek, L.3    Kayed, R.4    Glabe, C.G.5
  • 172
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins
    • Lambert MP, Barlow AK, Chromy BA, Edwards C, Freed R, et al. (1998). Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins. PNAS 95: 6448-53
    • (1998) PNAS , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3    Edwards, C.4    Freed, R.5
  • 173
    • 36749078121 scopus 로고    scopus 로고
    • Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers
    • Kayed R, Head E, Sarsoza F, Saing T, Cotman CW, et al. (2007). Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers. Mol. Neurodegener. 2: 18
    • (2007) Mol. Neurodegener , vol.2 , pp. 18
    • Kayed, R.1    Head, E.2    Sarsoza, F.3    Saing, T.4    Cotman, C.W.5
  • 174
    • 63249103989 scopus 로고    scopus 로고
    • Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer
    • Kayed R, Pensalfini A, Margol L, Sokolov Y, Sarsoza F, et al. (2009). Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer. J. Biol. Chem. 284: 4230-37
    • (2009) J. Biol. Chem , vol.284 , pp. 4230-4237
    • Kayed, R.1    Pensalfini, A.2    Margol, L.3    Sokolov, Y.4    Sarsoza, F.5
  • 175
    • 27644493692 scopus 로고    scopus 로고
    • Globular amyloidβ-peptide1-42 oligomer-a homogenous and stable neuropathological protein in Alzheimer's disease
    • Barghorn S, Nimmrich V, Striebinger A, Krantz C, Keller P, et al. (2005). Globular amyloidâ-peptide1-42 oligomer-a homogenous and stable neuropathological protein in Alzheimer's disease. J. Neurochem. 95: 834-47
    • (2005) J. Neurochem , vol.95 , pp. 834-847
    • Barghorn, S.1    Nimmrich, V.2    Striebinger, A.3    Krantz, C.4    Keller, P.5
  • 176
    • 0037975676 scopus 로고    scopus 로고
    • Spherical aggregates of β-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3β
    • Hoshi M, Sato M, Matsumoto S, Noguchi A, Yasutake K, et al. (2003). Spherical aggregates of β-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3β. PNAS 100: 6370-75
    • (2003) PNAS , vol.100 , pp. 6370-6375
    • Hoshi, M.1    Sato, M.2    Matsumoto, S.3    Noguchi, A.4    Yasutake, K.5
  • 177
    • 36849084640 scopus 로고    scopus 로고
    • Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate ofAlzheimer'sβ-amyloid
    • Chimon S, Shaibat MA, Jones CR, Calero DC, Aizezi B, Ishii Y. (2007). Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate ofAlzheimer'sβ-amyloid. Nat. Struct. Mol. Biol. 14: 1157-64
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 1157-1164
    • Chimon, S.1    Shaibat, M.A.2    Jones, C.R.3    Calero, D.C.4    Aizezi, B.5    Ishii, Y.6
  • 178
    • 77951975748 scopus 로고    scopus 로고
    • Structural conversion of neurotoxic amyloidbeta1-42 oligomers to fibrils
    • Ahmed M, Davis J, Aucoin D, Sato T, Ahuja S, et al. (2010). Structural conversion of neurotoxic amyloidbeta1-42 oligomers to fibrils. Nat. Struct. Mol. Biol. 17: 561-67
    • (2010) Nat. Struct. Mol. Biol , vol.17 , pp. 561-567
    • Ahmed, M.1    Davis, J.2    Aucoin, D.3    Sato, T.4    Ahuja, S.5
  • 179
    • 0028952749 scopus 로고
    • Aggregation of secreted amyloid β-protein into sodium dodecyl sulfate-stable oligomers in cell culture
    • Podlisny MB, Ostaszewski BL, Squazzo SL, Koo EH, Rydell RE, et al. (1995). Aggregation of secreted amyloid β-protein into sodium dodecyl sulfate-stable oligomers in cell culture. J. Biol. Chem. 270: 9564-70
    • (1995) J. Biol. Chem , vol.270 , pp. 9564-9570
    • Podlisny, M.B.1    Ostaszewski, B.L.2    Squazzo, S.L.3    Koo, E.H.4    Rydell, R.E.5
  • 180
    • 0030614627 scopus 로고    scopus 로고
    • Observation ofmetastable Aβamyloid protofibrils by atomic force microscopy
    • Harper JD, Wong SS, Lieber CM, Lansbury PT. (1997). Observation ofmetastable Aβamyloid protofibrils by atomic force microscopy. Chem. Biol. 4: 119-25
    • (1997) Chem. Biol , vol.4 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 181
    • 84861206757 scopus 로고    scopus 로고
    • Toxic fibrillar oligomers of amyloid-β have cross-β structure
    • Stroud JC, Liu C, Teng PK, Eisenberg D. (2012). Toxic fibrillar oligomers of amyloid-β have cross-β structure. PNAS 109: 7717-22
    • (2012) PNAS , vol.109 , pp. 7717-7722
    • Stroud, J.C.1    Liu, C.2    Teng, P.K.3    Eisenberg, D.4
  • 182
    • 84930205771 scopus 로고    scopus 로고
    • Structural insight into an Alzheimer's brain-derived spherical assembly of amyloid β by solid-state NMR
    • Parthasarathy S, Inoue M, Xiao Y, Matsumura Y, Nabeshima Y, et al. (2015). Structural insight into an Alzheimer's brain-derived spherical assembly of amyloid β by solid-state NMR. J. Am. Chem. Soc. 137: 6480-83
    • (2015) J. Am. Chem. Soc , vol.137 , pp. 6480-6483
    • Parthasarathy, S.1    Inoue, M.2    Xiao, Y.3    Matsumura, Y.4    Nabeshima, Y.5
  • 183
    • 78049326855 scopus 로고    scopus 로고
    • Amyloid β-protein dimers rapidly form stable synaptotoxic protofibrils
    • O'Nuallain B, Freir DB, Nicoll AJ, Risse E, Ferguson N, et al. (2010). Amyloid β-protein dimers rapidly form stable synaptotoxic protofibrils. J. Neurosci. 30: 14411-19
    • (2010) J. Neurosci , vol.30 , pp. 14411-14419
    • O'Nuallain, B.1    Freir, D.B.2    Nicoll, A.J.3    Risse, E.4    Ferguson, N.5
  • 184
    • 79953191504 scopus 로고    scopus 로고
    • Two distinct amyloid β-protein (Aβ) assembly pathways leading to oligomers and fibrils identified by combined fluorescence correlation spectroscopy, morphology, and toxicity analyses
    • Matsumura S, Shinoda K, Yamada M, Yokojima S, Inoue M, et al. (2011). Two distinct amyloid β-protein (Aβ) assembly pathways leading to oligomers and fibrils identified by combined fluorescence correlation spectroscopy, morphology, and toxicity analyses. J. Biol. Chem. 286: 11555-62
    • (2011) J. Biol. Chem , vol.286 , pp. 11555-11562
    • Matsumura, S.1    Shinoda, K.2    Yamada, M.3    Yokojima, S.4    Inoue, M.5
  • 186
    • 79959351077 scopus 로고    scopus 로고
    • Amyloid-β annular protofibrils evade fibrillar fate in Alzheimer disease brain
    • Lasagna-Reeves CA, Glabe CG, Kayed R. (2011). Amyloid-β annular protofibrils evade fibrillar fate in Alzheimer disease brain. J. Biol. Chem. 286: 22122-30
    • (2011) J. Biol. Chem , vol.286 , pp. 22122-22130
    • Lasagna-Reeves, C.A.1    Glabe, C.G.2    Kayed, R.3
  • 187
    • 84928170240 scopus 로고    scopus 로고
    • Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation
    • Chen SW, Drakulic S, Deas E, Ouberai M, Aprile FA, et al. (2015). Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation. PNAS 112: E1994-2003
    • (2015) PNAS , vol.112 , pp. E1994-2003
    • Chen, S.W.1    Drakulic, S.2    Deas, E.3    Ouberai, M.4    Aprile, F.A.5
  • 188
    • 84907571241 scopus 로고    scopus 로고
    • Structural insights into amyloid oligomers of the Parkinson disease-related protein α-synuclein
    • Gallea JI, Celej MS. (2014). Structural insights into amyloid oligomers of the Parkinson disease-related protein α-synuclein. J. Biol. Chem. 289: 26733-42
    • (2014) J. Biol. Chem , vol.289 , pp. 26733-26742
    • Gallea, J.I.1    Celej, M.S.2
  • 189
    • 84896265204 scopus 로고    scopus 로고
    • The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation
    • Lorenzen N, Nielsen SB, Buell AK, Kaspersen JD, Arosio P, et al. (2014). The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation. J. Am. Chem. Soc. 136: 3859-68
    • (2014) J. Am. Chem. Soc , vol.136 , pp. 3859-3868
    • Lorenzen, N.1    Nielsen, S.B.2    Buell, A.K.3    Kaspersen, J.D.4    Arosio, P.5
  • 190
    • 77952091224 scopus 로고    scopus 로고
    • Toxic oligomers and islet beta cell death: Guilty by association or convicted by circumstantial evidence?
    • Zraika S, Hull RL, Verchere CB, Clark A, Potter KJ, et al. (2010). Toxic oligomers and islet beta cell death: guilty by association or convicted by circumstantial evidence? Diabetologia 53: 1046-56
    • (2010) Diabetologia , vol.53 , pp. 1046-1056
    • Zraika, S.1    Hull, R.L.2    Verchere, C.B.3    Clark, A.4    Potter, K.J.5
  • 191
    • 84864931018 scopus 로고    scopus 로고
    • Clearance of extracellular misfolded proteins in systemic amyloidosis: Experience with transthyretin
    • Almeida MR, Saraiva MJ. (2012). Clearance of extracellular misfolded proteins in systemic amyloidosis: experience with transthyretin. FEBS Lett. 586: 2891-96
    • (2012) FEBS Lett , vol.586 , pp. 2891-2896
    • Almeida, M.R.1    Saraiva, M.J.2
  • 192
    • 84954025980 scopus 로고    scopus 로고
    • Recent advances in the management of AL amyloidosis
    • Kastritis E, Dimopoulos MA. (2016). Recent advances in the management of AL amyloidosis. Br. J. Haematol. 172: 170-86
    • (2016) Br. J. Haematol , vol.172 , pp. 170-186
    • Kastritis, E.1    Dimopoulos, M.A.2
  • 193
    • 85012093582 scopus 로고    scopus 로고
    • Seeking a mechanism for the toxicity of oligomeric α-synuclein
    • Roberts HL, Brown DR. (2015). Seeking a mechanism for the toxicity of oligomeric α-synuclein. Biomolecules 5: 282-305
    • (2015) Biomolecules , vol.5 , pp. 282-305
    • Roberts, H.L.1    Brown, D.R.2
  • 194
    • 84857642949 scopus 로고    scopus 로고
    • The toxic Aβoligomer and Alzheimer's disease: An emperor in need of clothes
    • Benilova I, Karran E, De Strooper B. (2012). The toxic Aβoligomer and Alzheimer's disease: an emperor in need of clothes. Nat. Neurosci. 15: 349-57
    • (2012) Nat. Neurosci , vol.15 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 196
    • 84930746830 scopus 로고    scopus 로고
    • The biology of proteostasis in aging and disease
    • Labbadia J, Morimoto RI. (2015). The biology of proteostasis in aging and disease. Annu. Rev. Biochem. 84: 435-64
    • (2015) Annu. Rev. Biochem , vol.84 , pp. 435-464
    • Labbadia, J.1    Morimoto, R.I.2
  • 197
    • 38049056730 scopus 로고    scopus 로고
    • Lipids revert inert Aβ amyloid fibrils to neurotoxic protofibrils that affect learning in mice
    • Martins IC, Kuperstein I, Wilkinson H, Maes E, Vanbrabant M, et al. (2008). Lipids revert inert Aβ amyloid fibrils to neurotoxic protofibrils that affect learning in mice. EMBO J. 27: 224-33
    • (2008) EMBO J. , vol.27 , pp. 224-233
    • Martins, I.C.1    Kuperstein, I.2    Wilkinson, H.3    Maes, E.4    Vanbrabant, M.5
  • 198
    • 62649174753 scopus 로고    scopus 로고
    • Oligomeric amyloid βassociates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques
    • Koffie RM, Meyer-Luehmann M, Hashimoto T, Adams KW, Mielke ML, et al. (2009). Oligomeric amyloid βassociates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques. PNAS 106: 4012-17
    • (2009) PNAS , vol.106 , pp. 4012-4017
    • Koffie, R.M.1    Meyer-Luehmann, M.2    Hashimoto, T.3    Adams, K.W.4    Mielke, M.L.5
  • 199
    • 75349097530 scopus 로고    scopus 로고
    • A causative link between the structure of aberrant protein oligomers and their toxicity
    • Campioni S, Mannini B, Zampagni M, Pensalfini A, Parrini C, et al. (2010). A causative link between the structure of aberrant protein oligomers and their toxicity. Nat. Chem. Biol. 6: 140-47
    • (2010) Nat. Chem. Biol , vol.6 , pp. 140-147
    • Campioni, S.1    Mannini, B.2    Zampagni, M.3    Pensalfini, A.4    Parrini, C.5
  • 200
    • 84863799510 scopus 로고    scopus 로고
    • Conformational differences between two amyloid βoligomers of similar size and dissimilar toxicity
    • Ladiwala AR, Litt J, Kane RS, Aucoin DS, Smith SO, et al. (2012). Conformational differences between two amyloid βoligomers of similar size and dissimilar toxicity. J. Biol. Chem. 287: 24765-73
    • (2012) J. Biol. Chem , vol.287 , pp. 24765-24773
    • Ladiwala, A.R.1    Litt, J.2    Kane, R.S.3    Aucoin, D.S.4    Smith, S.O.5
  • 201
    • 84863973455 scopus 로고    scopus 로고
    • Conserved features of intermediates in amyloid assembly determine their benign or toxic states
    • Krishnan R, Goodman JL, Mukhopadhyay S, Pacheco CD, Lemke EA, et al. (2012). Conserved features of intermediates in amyloid assembly determine their benign or toxic states. PNAS 109: 11172-77
    • (2012) PNAS , vol.109 , pp. 11172-11177
    • Krishnan, R.1    Goodman, J.L.2    Mukhopadhyay, S.3    Pacheco, C.D.4    Lemke, E.A.5
  • 203
    • 78650963274 scopus 로고    scopus 로고
    • Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions
    • Olzscha H, Schermann SM, Woerner AC, Pinkert S, Hecht MH, et al. (2011). Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell 144: 67-78
    • (2011) Cell , vol.144 , pp. 67-78
    • Olzscha, H.1    Schermann, S.M.2    Woerner, A.C.3    Pinkert, S.4    Hecht, M.H.5
  • 204
    • 0034740197 scopus 로고    scopus 로고
    • Vaccination with soluble Aβ oligomers generates toxicity-neutralizing antibodies
    • Lambert MP, Viola KL, Chromy BA, Chang L, Morgan TE, et al. (2001). Vaccination with soluble Aβ oligomers generates toxicity-neutralizing antibodies. J. Neurochem. 79: 595-605
    • (2001) J. Neurochem , vol.79 , pp. 595-605
    • Lambert, M.P.1    Viola, K.L.2    Chromy, B.A.3    Chang, L.4    Morgan, T.E.5
  • 205
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: Presence of oligomeric Aβligands (ADDLs) suggests a molecular basis for reversiblememory loss
    • Gong Y, Chang L, Viola KL, Lacor PN, Lambert MP, et al. (2003). Alzheimer's disease-affected brain: Presence of oligomeric Aβligands (ADDLs) suggests a molecular basis for reversiblememory loss. PNAS 100: 10417-22
    • (2003) PNAS , vol.100 , pp. 10417-10422
    • Gong, Y.1    Chang, L.2    Viola, K.L.3    Lacor, P.N.4    Lambert, M.P.5
  • 206
  • 207
    • 84864515731 scopus 로고    scopus 로고
    • Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers
    • Mannini B, Cascella R, Zampagni M, van Waarde-Verhagen M, Meehan S, et al. (2012). Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers. PNAS 109: 12479-84
    • (2012) PNAS , vol.109 , pp. 12479-12484
    • Mannini, B.1    Cascella, R.2    Zampagni, M.3    Van Waarde-Verhagen, M.4    Meehan, S.5
  • 208
    • 84885081944 scopus 로고    scopus 로고
    • Transthyretin suppresses the toxicity of oligomers formed by misfolded proteins in vitro
    • Cascella R, Conti S, Mannini B, Li X, Buxbaum JN, et al. (2013). Transthyretin suppresses the toxicity of oligomers formed by misfolded proteins in vitro. Biochim. Biophys. Acta 1832: 2302-14
    • (2013) Biochim. Biophys. Acta , vol.1832 , pp. 2302-2314
    • Cascella, R.1    Conti, S.2    Mannini, B.3    Li, X.4    Buxbaum, J.N.5
  • 209
    • 84908211476 scopus 로고    scopus 로고
    • Toxicity of protein oligomers is rationalized by a function combining size and surface hydrophobicity
    • Mannini B, Mulvihill E, Sgromo C, Cascella R, Khodarahmi R, et al. (2014). Toxicity of protein oligomers is rationalized by a function combining size and surface hydrophobicity. ACS Chem. Biol. 9: 2309-17
    • (2014) ACS Chem. Biol , vol.9 , pp. 2309-2317
    • Mannini, B.1    Mulvihill, E.2    Sgromo, C.3    Cascella, R.4    Khodarahmi, R.5
  • 210
    • 78650763561 scopus 로고    scopus 로고
    • Membrane permeabilization by oligomeric α-synuclein: In search of the mechanism
    • van Rooijen BD, Claessens MM, Subramaniam V. (2010). Membrane permeabilization by oligomeric α-synuclein: in search of the mechanism. PLOS ONE 5: e14292
    • (2010) Plos One , vol.5 , pp. e14292
    • Van Rooijen, B.D.1    Claessens, M.M.2    Subramaniam, V.3
  • 211
    • 84979948625 scopus 로고    scopus 로고
    • Interaction of toxic and nontoxic HypF-N oligomers with lipid bilayers investigated at high resolution with atomic force microscopy
    • Oropesa-Nuñez R, Seghezza S, Dante S, Diaspro A, Cascella R, et al. (2016). Interaction of toxic and nontoxic HypF-N oligomers with lipid bilayers investigated at high resolution with atomic force microscopy. Oncotarget 7: 44991-5004
    • (2016) Oncotarget , vol.7 , pp. 44991-45004
    • Oropesa-Nuñez, R.1    Seghezza, S.2    Dante, S.3    Diaspro, A.4    Cascella, R.5
  • 212
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is acommonconformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • Kayed R, Sokolov Y, Edmonds B, McIntire TM, Milton SC, et al. (2004). Permeabilization of lipid bilayers is acommonconformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J. Biol. Chem. 279: 46363-66
    • (2004) J. Biol. Chem , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3    McIntire, T.M.4    Milton, S.C.5
  • 214
    • 84876891740 scopus 로고    scopus 로고
    • Α-Synuclein oligomers: An amyloid pore? Insights into mechanisms of α-synuclein oligomer-lipid interactions
    • Stöckl MT, Zijlstra N, Subramaniam V. (2013). α-Synuclein oligomers: an amyloid pore? Insights into mechanisms of α-synuclein oligomer-lipid interactions. Mol. Neurobiol. 47: 613-21
    • (2013) Mol. Neurobiol , vol.47 , pp. 613-621
    • Stöckl, M.T.1    Zijlstra, N.2    Subramaniam, V.3
  • 215
    • 84919764653 scopus 로고    scopus 로고
    • A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease
    • Brehme M, Voisine C, Rolland T, Wachi S, Soper JH, et al. (2014). A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease. Cell Rep. 9: 1135-50
    • (2014) Cell Rep , vol.9 , pp. 1135-1150
    • Brehme, M.1    Voisine, C.2    Rolland, T.3    Wachi, S.4    Soper, J.H.5
  • 216
    • 84939559331 scopus 로고    scopus 로고
    • Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation
    • Nillegoda NB, Kirstein J, Szlachcic A, Berynskyy M, Stank A, et al. (2015). Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation. Nature 524: 247-51
    • (2015) Nature , vol.524 , pp. 247-251
    • Nillegoda, N.B.1    Kirstein, J.2    Szlachcic, A.3    Berynskyy, M.4    Stank, A.5
  • 217
    • 84964835117 scopus 로고    scopus 로고
    • Clusterin binds to Aβ1-42 oligomers with high affinity and interfereswith peptide aggregation by inhibiting primary and secondary nucleation
    • Beeg M, Stravalaci M, Romeo M, Carrá AD, Cagnotto A, et al. (2016). Clusterin binds to Aβ1-42 oligomers with high affinity and interfereswith peptide aggregation by inhibiting primary and secondary nucleation. J. Biol. Chem. 291: 6958-66
    • (2016) J. Biol. Chem , vol.291 , pp. 6958-6966
    • Beeg, M.1    Stravalaci, M.2    Romeo, M.3    Carrá, A.D.4    Cagnotto, A.5
  • 218
    • 84984674677 scopus 로고    scopus 로고
    • Holdase activity of secreted Hsp70 masks amyloid-β42 neurotoxicity in Drosophila
    • Fernandez-Funez P, Sanchez-Garcia J, de Mena L, Zhang Y, Levites Y, et al. (2016). Holdase activity of secreted Hsp70 masks amyloid-β42 neurotoxicity in Drosophila. PNAS 113: E5212-21
    • (2016) PNAS , vol.113 , pp. E5212-E5221
    • Fernandez-Funez, P.1    Sanchez-Garcia, J.2    De Mena, L.3    Zhang, Y.4    Levites, Y.5
  • 219
    • 34547631623 scopus 로고    scopus 로고
    • Prevention of amyloid-like aggregation as a driving force of protein evolution
    • Monsellier E, Chiti F. (2007). Prevention of amyloid-like aggregation as a driving force of protein evolution. EMBO Rep. 8: 737-42
    • (2007) EMBO Rep , vol.8 , pp. 737-742
    • Monsellier, E.1    Chiti, F.2
  • 220
    • 72949113219 scopus 로고    scopus 로고
    • Correlation between mRNA expression levels and protein aggregation propensities in subcellular localisations
    • Tartaglia GG, Vendruscolo M. (2009). Correlation between mRNA expression levels and protein aggregation propensities in subcellular localisations. Mol. Biosyst. 5: 1873-76
    • (2009) Mol. Biosyst , vol.5 , pp. 1873-1876
    • Tartaglia, G.G.1    Vendruscolo, M.2
  • 221
    • 79959837318 scopus 로고    scopus 로고
    • An evolutionary trade-off between protein turnover rate and protein aggregation favors a higher aggregation propensity in fast degrading proteins
    • De Baets G, Reumers J, Delgado Blanco J, Dopazo J, Schymkowitz J, Rousseau F. (2011). An evolutionary trade-off between protein turnover rate and protein aggregation favors a higher aggregation propensity in fast degrading proteins. PLOS Comput. Biol. 7: e1002090
    • (2011) Plos Comput. Biol , vol.7 , pp. e1002090
    • De Baets, G.1    Reumers, J.2    Delgado Blanco, J.3    Dopazo, J.4    Schymkowitz, J.5    Rousseau, F.6
  • 222
    • 84936757682 scopus 로고    scopus 로고
    • Role of cholesterol and phospholipids in amylin misfolding, aggregation and etiology of islet amyloidosis
    • Singh S, Trikha S, Bhowmick DC, Sarkar AA, Jeremic AM. (2015). Role of cholesterol and phospholipids in amylin misfolding, aggregation and etiology of islet amyloidosis. Adv. Exp. Med. Biol. 855: 95-116
    • (2015) Adv. Exp. Med. Biol , vol.855 , pp. 95-116
    • Singh, S.1    Trikha, S.2    Bhowmick, D.C.3    Sarkar, A.A.4    Jeremic, A.M.5
  • 223
  • 224
    • 0015141213 scopus 로고
    • Chemical classes of amyloid substance
    • Benditt EP, Eriksen N. (1971). Chemical classes of amyloid substance. Am. J. Pathol. 65: 231-52
    • (1971) Am. J. Pathol , vol.65 , pp. 231-252
    • Benditt, E.P.1    Eriksen, N.2
  • 225
    • 84912536138 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in neurodegeneration
    • McKinnon C, Tabrizi SJ. (2014). The ubiquitin-proteasome system in neurodegeneration. Antioxid. Redox Signal. 21: 2302-21
    • (2014) Antioxid. Redox Signal , vol.21 , pp. 2302-2321
    • McKinnon, C.1    Tabrizi, S.J.2
  • 227
    • 34247882072 scopus 로고    scopus 로고
    • Life on the edge: A link between gene expression levels and aggregation rates of human proteins
    • Tartaglia GG, Pechmann S, Dobson CM, Vendruscolo M. (2007). Life on the edge: a link between gene expression levels and aggregation rates of human proteins. Trends Biochem. Sci. 32: 204-6
    • (2007) Trends Biochem. Sci , vol.32 , pp. 204-206
    • Tartaglia, G.G.1    Pechmann, S.2    Dobson, C.M.3    Vendruscolo, M.4
  • 228
    • 84887606872 scopus 로고    scopus 로고
    • Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins
    • Ciryam P, Tartaglia GG, Morimoto RI, Dobson CM, Vendruscolo M. (2013). Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins. Cell Rep. 5: 781-90
    • (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
  • 229
    • 85019334475 scopus 로고    scopus 로고
    • A protein homeostasis signature in healthy brains recapitulates tissue vulnerability to Alzheimer's disease
    • Freer R, Sormanni P, Vecchi G, Ciryam P, Dobson CM, Vendruscolo M. (2016). A protein homeostasis signature in healthy brains recapitulates tissue vulnerability to Alzheimer's disease. Sci. Adv. 2: e1600947
    • (2016) Sci. Adv , vol.2 , pp. e1600947
    • Freer, R.1    Sormanni, P.2    Vecchi, G.3    Ciryam, P.4    Dobson, C.M.5    Vendruscolo, M.6
  • 230
    • 84964701731 scopus 로고    scopus 로고
    • A transcriptional signature of Alzheimer's disease is associated with a metastable subproteome at risk for aggregation
    • Ciryam P, Kundra R, Freer R, Morimoto RI, Dobson CM, Vendruscolo M. (2016). A transcriptional signature of Alzheimer's disease is associated with a metastable subproteome at risk for aggregation. PNAS 113: 4753-58
    • (2016) PNAS , vol.113 , pp. 4753-4758
    • Ciryam, P.1    Kundra, R.2    Freer, R.3    Morimoto, R.I.4    Dobson, C.M.5    Vendruscolo, M.6
  • 231
    • 85014070035 scopus 로고    scopus 로고
    • Drug treatments in Alzheimer's disease
    • Briggs R, Kennelly SP, O'Neill D. (2016). Drug treatments in Alzheimer's disease. Clin. Med. 16: 247-53
    • (2016) Clin. Med , vol.16 , pp. 247-253
    • Briggs, R.1    Kennelly, S.P.2    O'Neill, D.3
  • 232
    • 85027942434 scopus 로고    scopus 로고
    • Therapeutic approaches in Parkinson's disease and related disorders
    • Valera E, Masliah E. (2016). Therapeutic approaches in Parkinson's disease and related disorders. J. Neurochem. 139: 346-52
    • (2016) J. Neurochem , vol.139 , pp. 346-352
    • Valera, E.1    Masliah, E.2
  • 233
    • 85018747356 scopus 로고    scopus 로고
    • Systemic amyloidosis: Novel therapies and role of biomarkers
    • Nuvolone M, Merlini G. (2017). Systemic amyloidosis: novel therapies and role of biomarkers. Nephrol. Dial. Transplant. 32: 770-80
    • (2017) Nephrol. Dial. Transplant , vol.32 , pp. 770-780
    • Nuvolone, M.1    Merlini, G.2
  • 234
    • 85006228054 scopus 로고    scopus 로고
    • Mechanism of action and clinical application of tafamidis in hereditary transthyretin amyloidosis
    • Coelho T, Merlini G, Bulawa CE, Fleming JA, Judge DP, et al. (2016). Mechanism of action and clinical application of tafamidis in hereditary transthyretin amyloidosis. Neurol. Ther. 5: 1-25
    • (2016) Neurol. Ther , vol.5 , pp. 1-25
    • Coelho, T.1    Merlini, G.2    Bulawa, C.E.3    Fleming, J.A.4    Judge, D.P.5
  • 235
    • 85009348250 scopus 로고    scopus 로고
    • Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer's disease
    • Habchi J, Chia S, Limbocker R, Mannini B, Ahn M, et al. (2017). Systematic development of small molecules to inhibit specific microscopic steps of Aâ42 aggregation in Alzheimer's disease. PNAS 114: E200-8
    • (2017) PNAS , vol.114 , pp. E200-E208
    • Habchi, J.1    Chia, S.2    Limbocker, R.3    Mannini, B.4    Ahn, M.5
  • 237
    • 0037174998 scopus 로고    scopus 로고
    • Structural and dynamic features of Alzheimer's Aβpeptide in amyloid fibrils studied by site-directed spin labeling
    • Török M, Milton S, Kayed R, Wu P, McIntire T, et al. (2002). Structural and dynamic features of Alzheimer's Aβpeptide in amyloid fibrils studied by site-directed spin labeling. J. Biol. Chem. 277: 40810-15
    • (2002) J. Biol. Chem , vol.277 , pp. 40810-40815
    • Török, M.1    Milton, S.2    Kayed, R.3    Wu, P.4    McIntire, T.5
  • 238
    • 28444442999 scopus 로고    scopus 로고
    • 3D structure of Alzheimer's amyloid-β(1-42) fibrils
    • Lührs T, Ritter C, Adrian M, Riek-Loher D, Bohrmann B, et al. (2005). 3D structure of Alzheimer's amyloid-β(1-42) fibrils. PNAS 102: 17342-47
    • (2005) PNAS , vol.102 , pp. 17342-17347
    • Lührs, T.1    Ritter, C.2    Adrian, M.3    Riek-Loher, D.4    Bohrmann, B.5
  • 239
    • 33746781304 scopus 로고    scopus 로고
    • Structural differences in Aβamyloid protofibrils and fibrils mapped by hydrogen exchange-mass spectrometry with on-line proteolytic fragmentation
    • Kheterpal I, Chen M, Cook KD, Wetzel R. (2006). Structural differences in Aβamyloid protofibrils and fibrils mapped by hydrogen exchange-mass spectrometry with on-line proteolytic fragmentation. J. Mol. Biol. 361: 785-95
    • (2006) J. Mol. Biol , vol.361 , pp. 785-795
    • Kheterpal, I.1    Chen, M.2    Cook, K.D.3    Wetzel, R.4
  • 240
    • 0037166267 scopus 로고    scopus 로고
    • Biochemical characterization of the core structure of α-synuclein filaments
    • Miake H, Mizusawa H, Iwatsubo T, Hasegawa M. (2002). Biochemical characterization of the core structure of α-synuclein filaments. J. Biol. Chem. 277: 19213-19
    • (2002) J. Biol. Chem , vol.277 , pp. 19213-19219
    • Miake, H.1    Mizusawa, H.2    Iwatsubo, T.3    Hasegawa, M.4
  • 241
    • 27344436619 scopus 로고    scopus 로고
    • Structure and properties of α-synuclein and other amyloids determined at the amino acid level
    • DelMar C, Greenbaum EA, Mayne L, Englander SW, Woods VL Jr. (2005). Structure and properties of α-synuclein and other amyloids determined at the amino acid level. PNAS 102: 15477-82
    • (2005) PNAS , vol.102 , pp. 15477-15482
    • Del Mar, C.1    Greenbaum, E.A.2    Mayne, L.3    Englander, S.W.4    Woods, V.L.5
  • 242
    • 16244376187 scopus 로고    scopus 로고
    • The parallel superpleated β-structure as a model for amyloid fibrils of human amylin
    • Kajava AV, Aebi U, Steven AC. (2005). The parallel superpleated β-structure as a model for amyloid fibrils of human amylin. J. Mol. Biol. 348: 247-52
    • (2005) J. Mol. Biol , vol.348 , pp. 247-252
    • Kajava, A.V.1    Aebi, U.2    Steven, A.C.3
  • 243
    • 84874037807 scopus 로고    scopus 로고
    • Amide proton solvent protection in amylin fibrils probed by quenched hydrogen exchange NMR
    • Alexandrescu AT. (2013). Amide proton solvent protection in amylin fibrils probed by quenched hydrogen exchange NMR. PLOS ONE 8: e56467
    • (2013) Plos One , vol.8 , pp. e56467
    • Alexandrescu, A.T.1


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