메뉴 건너뛰기




Volumn 1848, Issue 9, 2015, Pages 1897-1907

Interactions between misfolded protein oligomers and membranes: A central topic in neurodegenerative diseases?

Author keywords

Alpha synuclein; Amyloid; Anionic lipids; Fasciclin domain; Membrane destabilization; Protein oligomer

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; DRONABINOL; EPIGALLOCATECHIN GALLATE; FASCICLIN I; MONOMER; OLIGOMER; PEPTIDOMIMETIC AGENT; PROTEIN FAS1-4; TRANSFORMING GROWTH FACTOR BETA; TRANSFORMING GROWTH FACTOR BETA INDUCED PROTEIN; UNCLASSIFIED DRUG; MEMBRANE LIPID; MEMBRANE PROTEIN; PROTEIN BINDING;

EID: 84936892251     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2015.01.018     Document Type: Review
Times cited : (93)

References (140)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 11144221004 scopus 로고    scopus 로고
    • Amyloid accomplices and enforcers
    • A.T. Alexandrescu Amyloid accomplices and enforcers Protein Sci. 14 1 2005 1 12
    • (2005) Protein Sci. , vol.14 , Issue.1 , pp. 1-12
    • Alexandrescu, A.T.1
  • 4
    • 10644225416 scopus 로고    scopus 로고
    • Protein misfolding and aggregation: New examples in medicine and biology of the dark side of the protein world
    • M. Stefani Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world Biochim. Biophys. Acta 1739 1 2004 5 25
    • (2004) Biochim. Biophys. Acta , vol.1739 , Issue.1 , pp. 5-25
    • Stefani, M.1
  • 5
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • M. Stefani, and C.M. Dobson Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution J. Mol. Med. (Berl) 81 11 2003 678 699
    • (2003) J. Mol. Med. (Berl) , vol.81 , Issue.11 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 6
    • 33645521792 scopus 로고    scopus 로고
    • Protein aggregation and its consequences for human disease
    • C.M. Dobson Protein aggregation and its consequences for human disease Protein Pept. Lett. 13 3 2006 219 227
    • (2006) Protein Pept. Lett. , vol.13 , Issue.3 , pp. 219-227
    • Dobson, C.M.1
  • 7
    • 0014351967 scopus 로고
    • X-ray diffraction studies on amyloid filaments
    • E.D. Eanes, and G.G. Glenner X-ray diffraction studies on amyloid filaments J. Histochem. Cytochem. 16 11 1968 673 677
    • (1968) J. Histochem. Cytochem. , vol.16 , Issue.11 , pp. 673-677
    • Eanes, E.D.1    Glenner, G.G.2
  • 8
    • 0032879438 scopus 로고    scopus 로고
    • X-ray fiber diffraction of amyloid fibrils
    • L.C. Serpell, P.E. Fraser, and M. Sunde X-ray fiber diffraction of amyloid fibrils Methods Enzymol. 309 1999 526 536
    • (1999) Methods Enzymol. , vol.309 , pp. 526-536
    • Serpell, L.C.1    Fraser, P.E.2    Sunde, M.3
  • 9
    • 33845652277 scopus 로고    scopus 로고
    • Structural models of amyloid-like fibrils
    • R. Nelson, and D. Eisenberg Structural models of amyloid-like fibrils Adv. Protein Chem. 73 2006 235 282
    • (2006) Adv. Protein Chem. , vol.73 , pp. 235-282
    • Nelson, R.1    Eisenberg, D.2
  • 10
    • 0033849738 scopus 로고    scopus 로고
    • Review: History of the amyloid fibril
    • J.D. Sipe, and A.S. Cohen Review: history of the amyloid fibril J. Struct. Biol. 130 2-3 2000 88 98
    • (2000) J. Struct. Biol. , vol.130 , Issue.2-3 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.S.2
  • 11
    • 33745045946 scopus 로고    scopus 로고
    • Spatial persistence of angular correlations in amyloid fibrils
    • T.P.J. Knowles Spatial persistence of angular correlations in amyloid fibrils Phys. Rev. Lett. 96 2006 238301
    • (2006) Phys. Rev. Lett. , vol.96 , pp. 238301
    • Knowles, T.P.J.1
  • 12
    • 0034725535 scopus 로고    scopus 로고
    • The protofilament substructure of amyloid fibrils
    • L.C. Serpell The protofilament substructure of amyloid fibrils J. Mol. Biol. 300 5 2000 1033 1039
    • (2000) J. Mol. Biol. , vol.300 , Issue.5 , pp. 1033-1039
    • Serpell, L.C.1
  • 13
    • 84884217594 scopus 로고    scopus 로고
    • Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue
    • J.-X. Lu Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue Cell 154 6 2013 1257 1268
    • (2013) Cell , vol.154 , Issue.6 , pp. 1257-1268
    • Lu, J.-X.1
  • 14
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • C.M. Dobson Protein misfolding, evolution and disease Trends Biochem. Sci. 24 9 1999 329 332
    • (1999) Trends Biochem. Sci. , vol.24 , Issue.9 , pp. 329-332
    • Dobson, C.M.1
  • 15
    • 3242785264 scopus 로고    scopus 로고
    • Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains
    • K.F. DuBay Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains J. Mol. Biol. 341 5 2004 1317 1326
    • (2004) J. Mol. Biol. , vol.341 , Issue.5 , pp. 1317-1326
    • Dubay, K.F.1
  • 16
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • F. Chiti Rationalization of the effects of mutations on peptide and protein aggregation rates Nature 424 6950 2003 805 808
    • (2003) Nature , vol.424 , Issue.6950 , pp. 805-808
    • Chiti, F.1
  • 17
    • 67650809307 scopus 로고    scopus 로고
    • Functional amyloids as natural storage of peptide hormones in pituitary secretory granules
    • S.K. Maji Functional amyloids as natural storage of peptide hormones in pituitary secretory granules Science 325 5938 2009 328 332
    • (2009) Science , vol.325 , Issue.5938 , pp. 328-332
    • Maji, S.K.1
  • 18
    • 0037986392 scopus 로고    scopus 로고
    • Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis
    • J.F. Berson Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis J. Cell Biol. 161 3 2003 521 533
    • (2003) J. Cell Biol. , vol.161 , Issue.3 , pp. 521-533
    • Berson, J.F.1
  • 19
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • J.A. Hardy, and G.A. Higgins Alzheimer's disease: the amyloid cascade hypothesis Science 256 5054 1992 184 185
    • (1992) Science , vol.256 , Issue.5054 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 20
    • 0026512066 scopus 로고
    • Identification of normal and pathological aging in prospectively studied nondemented elderly humans
    • D.W. Dickson Identification of normal and pathological aging in prospectively studied nondemented elderly humans Neurobiol. Aging 13 1 1992 179 189
    • (1992) Neurobiol. Aging , vol.13 , Issue.1 , pp. 179-189
    • Dickson, D.W.1
  • 21
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
    • R.D. Terry Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment Ann. Neurol. 30 4 1991 572 580
    • (1991) Ann. Neurol. , vol.30 , Issue.4 , pp. 572-580
    • Terry, R.D.1
  • 22
    • 0030007964 scopus 로고    scopus 로고
    • Sequence of deposition of heterogeneous amyloid beta-peptides and APO e in Down syndrome: Implications for initial events in amyloid plaque formation
    • C.A. Lemere Sequence of deposition of heterogeneous amyloid beta-peptides and APO E in Down syndrome: implications for initial events in amyloid plaque formation Neurobiol. Dis. 3 1 1996 16 32
    • (1996) Neurobiol. Dis. , vol.3 , Issue.1 , pp. 16-32
    • Lemere, C.A.1
  • 23
    • 0029078972 scopus 로고
    • Correlations of synaptic and pathological markers with cognition of the elderly
    • (discussion 298-304)
    • D.W. Dickson Correlations of synaptic and pathological markers with cognition of the elderly Neurobiol. Aging 16 3 1995 285 298 (discussion 298-304)
    • (1995) Neurobiol. Aging , vol.16 , Issue.3 , pp. 285-298
    • Dickson, D.W.1
  • 24
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • B. Caughey, and P.T. Lansbury Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders Annu. Rev. Neurosci. 26 2003 267 298
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 25
    • 0038386274 scopus 로고    scopus 로고
    • Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease
    • M.J. Volles, and P.T. Lansbury Jr. Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease Biochemistry 42 26 2003 7871 7878
    • (2003) Biochemistry , vol.42 , Issue.26 , pp. 7871-7878
    • Volles, M.J.1    Lansbury, Jr.P.T.2
  • 26
    • 65249162241 scopus 로고    scopus 로고
    • Detection of elevated levels of soluble alpha-synuclein oligomers in post-mortem brain extracts from patients with dementia with Lewy bodies
    • K.E. Paleologou Detection of elevated levels of soluble alpha-synuclein oligomers in post-mortem brain extracts from patients with dementia with Lewy bodies Brain 132 Pt 4 2009 1093 1101
    • (2009) Brain , vol.132 , pp. 1093-1101
    • Paleologou, K.E.1
  • 27
    • 78649990079 scopus 로고    scopus 로고
    • Detection of elevated levels of alpha-synuclein oligomers in CSF from patients with Parkinson disease
    • T. Tokuda Detection of elevated levels of alpha-synuclein oligomers in CSF from patients with Parkinson disease Neurology 75 20 2010 1766 1772
    • (2010) Neurology , vol.75 , Issue.20 , pp. 1766-1772
    • Tokuda, T.1
  • 28
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • M. Bucciantini Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases Nature 416 6880 2002 507 511
    • (2002) Nature , vol.416 , Issue.6880 , pp. 507-511
    • Bucciantini, M.1
  • 29
    • 1842529223 scopus 로고    scopus 로고
    • Fibrillogenesis and cytotoxic activity of the amyloid-forming apomyoglobin mutant W7FW14F
    • I. Sirangelo Fibrillogenesis and cytotoxic activity of the amyloid-forming apomyoglobin mutant W7FW14F J. Biol. Chem. 279 13 2004 13183 13189
    • (2004) J. Biol. Chem. , vol.279 , Issue.13 , pp. 13183-13189
    • Sirangelo, I.1
  • 30
    • 84907854533 scopus 로고    scopus 로고
    • High stability and cooperative unfolding of alpha-synuclein oligomers
    • W. Paslawski High stability and cooperative unfolding of alpha-synuclein oligomers Biochemistry 53 39 2014 6252 6263
    • (2014) Biochemistry , vol.53 , Issue.39 , pp. 6252-6263
    • Paslawski, W.1
  • 31
    • 23044449398 scopus 로고    scopus 로고
    • Amyloid ion channels: A common structural link for protein-misfolding disease
    • A. Quist Amyloid ion channels: a common structural link for protein-misfolding disease Proc. Natl. Acad. Sci. U. S. A. 102 30 2005 10427 10432
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , Issue.30 , pp. 10427-10432
    • Quist, A.1
  • 32
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • R. Kayed Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis Science 300 5618 2003 486 489
    • (2003) Science , vol.300 , Issue.5618 , pp. 486-489
    • Kayed, R.1
  • 33
    • 84896265204 scopus 로고    scopus 로고
    • The role of stable alpha-synuclein oligomers in the molecular events underlying amyloid formation
    • N. Lorenzen The role of stable alpha-synuclein oligomers in the molecular events underlying amyloid formation J. Am. Chem. Soc. 136 10 2014 3859 3868
    • (2014) J. Am. Chem. Soc. , vol.136 , Issue.10 , pp. 3859-3868
    • Lorenzen, N.1
  • 34
    • 84904515491 scopus 로고    scopus 로고
    • Co-existence of two different alpha-synuclein oligomers with different core structures determined by hydrogen/deuterium exchange mass spectrometry
    • W. Paslawski Co-existence of two different alpha-synuclein oligomers with different core structures determined by hydrogen/deuterium exchange mass spectrometry Angew. Chem. Int. Ed. Engl. 53 29 2014 7560 7563
    • (2014) Angew. Chem. Int. Ed. Engl. , vol.53 , Issue.29 , pp. 7560-7563
    • Paslawski, W.1
  • 35
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils
    • A.T. Petkova Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils Science 307 5707 2005 262 265
    • (2005) Science , vol.307 , Issue.5707 , pp. 262-265
    • Petkova, A.T.1
  • 36
    • 24644447303 scopus 로고    scopus 로고
    • Seeding-dependent propagation and maturation of amyloid fibril conformation
    • K. Yamaguchi Seeding-dependent propagation and maturation of amyloid fibril conformation J. Mol. Biol. 352 4 2005 952 960
    • (2005) J. Mol. Biol. , vol.352 , Issue.4 , pp. 952-960
    • Yamaguchi, K.1
  • 37
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • C.J. Cummings Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1 Nat. Genet. 19 2 1998 148 154
    • (1998) Nat. Genet. , vol.19 , Issue.2 , pp. 148-154
    • Cummings, C.J.1
  • 38
    • 0030830270 scopus 로고    scopus 로고
    • Immunocytochemical co-localization of the proteasome in ubiquitinated structures in neurodegenerative diseases and the elderly
    • K. Ii Immunocytochemical co-localization of the proteasome in ubiquitinated structures in neurodegenerative diseases and the elderly J. Neuropathol. Exp. Neurol. 56 2 1997 125 131
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , Issue.2 , pp. 125-131
    • Ii, K.1
  • 39
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • C. Soto Unfolding the role of protein misfolding in neurodegenerative diseases Nat. Rev. Neurosci. 4 1 2003 49 60
    • (2003) Nat. Rev. Neurosci. , vol.4 , Issue.1 , pp. 49-60
    • Soto, C.1
  • 40
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • C. Behl Hydrogen peroxide mediates amyloid beta protein toxicity Cell 77 6 1994 817 827
    • (1994) Cell , vol.77 , Issue.6 , pp. 817-827
    • Behl, C.1
  • 41
    • 0033890821 scopus 로고    scopus 로고
    • Alpha-synuclein promotes mitochondrial deficit and oxidative stress
    • L.J. Hsu Alpha-synuclein promotes mitochondrial deficit and oxidative stress Am. J. Pathol. 157 2 2000 401 410
    • (2000) Am. J. Pathol. , vol.157 , Issue.2 , pp. 401-410
    • Hsu, L.J.1
  • 42
    • 0031687793 scopus 로고    scopus 로고
    • Understanding cell death in Parkinson's disease
    • P. Jenner, and C.W. Olanow Understanding cell death in Parkinson's disease Ann. Neurol. 44 3 Suppl 1 1998 S72 S84
    • (1998) Ann. Neurol. , vol.44 , Issue.3 , pp. S72-S84
    • Jenner, P.1    Olanow, C.W.2
  • 43
    • 0037378026 scopus 로고    scopus 로고
    • Oxidative stress in Parkinson's disease
    • (discussion S36-8)
    • P. Jenner Oxidative stress in Parkinson's disease Ann. Neurol. 53 Suppl. 3 2003 S26 S36 (discussion S36-8)
    • (2003) Ann. Neurol. , vol.53 , pp. S26-S36
    • Jenner, P.1
  • 44
    • 0035753031 scopus 로고    scopus 로고
    • Production of reactive oxygen species from aggregating proteins implicated in Alzheimer's disease, Parkinson's disease and other neurodegenerative diseases
    • B.J. Tabner Production of reactive oxygen species from aggregating proteins implicated in Alzheimer's disease, Parkinson's disease and other neurodegenerative diseases Curr. Top. Med. Chem. 1 6 2001 507 517
    • (2001) Curr. Top. Med. Chem. , vol.1 , Issue.6 , pp. 507-517
    • Tabner, B.J.1
  • 45
    • 68949151944 scopus 로고    scopus 로고
    • Alpha-synuclein overexpression and aggregation exacerbates impairment of mitochondrial functions by augmenting oxidative stress in human neuroblastoma cells
    • M.S. Parihar Alpha-synuclein overexpression and aggregation exacerbates impairment of mitochondrial functions by augmenting oxidative stress in human neuroblastoma cells Int. J. Biochem. Cell Biol. 41 10 2009 2015 2024
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , Issue.10 , pp. 2015-2024
    • Parihar, M.S.1
  • 46
    • 84892794505 scopus 로고    scopus 로고
    • The N-terminus of alpha-synuclein is essential for both monomeric and oligomeric interactions with membranes
    • N. Lorenzen The N-terminus of alpha-synuclein is essential for both monomeric and oligomeric interactions with membranes FEBS Lett. 588 3 2014 497 502
    • (2014) FEBS Lett. , vol.588 , Issue.3 , pp. 497-502
    • Lorenzen, N.1
  • 47
    • 84905376066 scopus 로고    scopus 로고
    • How epigallocatechin gallate can inhibit alpha-synuclein oligomer toxicity in vitro
    • N. Lorenzen How epigallocatechin gallate can inhibit alpha-synuclein oligomer toxicity in vitro J. Biol. Chem. 289 31 2014 21299 21310
    • (2014) J. Biol. Chem. , vol.289 , Issue.31 , pp. 21299-21310
    • Lorenzen, N.1
  • 48
    • 84902668958 scopus 로고    scopus 로고
    • Alpha-synuclein oligomers distinctively permeabilize complex model membranes
    • A.N. Stefanovic Alpha-synuclein oligomers distinctively permeabilize complex model membranes FEBS J. 281 12 2014 2838 2850
    • (2014) FEBS J. , vol.281 , Issue.12 , pp. 2838-2850
    • Stefanovic, A.N.1
  • 49
    • 78650763561 scopus 로고    scopus 로고
    • Membrane permeabilization by oligomeric α-synuclein: In search of the mechanism
    • C.M. van Rooijen BD, and V. Subramaniam Membrane permeabilization by oligomeric α-synuclein: in search of the mechanism PLoS ONE 5 2010
    • (2010) PLoS ONE , vol.5
    • Van Rooijen Bd, C.M.1    Subramaniam, V.2
  • 50
    • 33846817163 scopus 로고    scopus 로고
    • Relationships between the sequence of alpha-synuclein and its membrane affinity, fibrillization propensity, and yeast toxicity
    • M.J. Volles, and P.T. Lansbury Jr. Relationships between the sequence of alpha-synuclein and its membrane affinity, fibrillization propensity, and yeast toxicity J. Mol. Biol. 366 5 2007 1510 1522
    • (2007) J. Mol. Biol. , vol.366 , Issue.5 , pp. 1510-1522
    • Volles, M.J.1    Lansbury, Jr.P.T.2
  • 51
    • 70449626845 scopus 로고    scopus 로고
    • Tryptophan fluorescence reveals structural features of alpha-synuclein oligomers
    • B.D. van Rooijen Tryptophan fluorescence reveals structural features of alpha-synuclein oligomers J. Mol. Biol. 394 5 2009 826 833
    • (2009) J. Mol. Biol. , vol.394 , Issue.5 , pp. 826-833
    • Van Rooijen, B.D.1
  • 52
    • 0035800097 scopus 로고    scopus 로고
    • Vesicle Permeabilization by Protofibrillar α-Synuclein: Implications for the Pathogenesis and Treatment of Parkinson's Disease
    • M.J. Volles, S.-J. Lee, J.-C. Rochet, M.D. Shtilerman, T.T. Ding, J.C. Kessler, and P.T. Lansbury Vesicle Permeabilization by Protofibrillar α-Synuclein: Implications for the Pathogenesis and Treatment of Parkinson's Disease Biochemistry 40 26 2001 7812 7819
    • (2001) Biochemistry , vol.40 , Issue.26 , pp. 7812-7819
    • Volles, M.J.1    Lee, S.-J.2    Rochet, J.-C.3    Shtilerman, M.D.4    Ding, T.T.5    Kessler, J.C.6    Lansbury, P.T.7
  • 53
    • 82655175456 scopus 로고    scopus 로고
    • Kinetic measurements give new insights into lipid membrane permeabilization by alpha-synuclein oligomers
    • M. Stockl, M.M. Claessens, and V. Subramaniam Kinetic measurements give new insights into lipid membrane permeabilization by alpha-synuclein oligomers Mol. BioSyst. 8 1 2012 338 345
    • (2012) Mol. BioSyst. , vol.8 , Issue.1 , pp. 338-345
    • Stockl, M.1    Claessens, M.M.2    Subramaniam, V.3
  • 54
    • 65549114936 scopus 로고    scopus 로고
    • Lipid bilayer disruption by oligomeric alpha-synuclein depends on bilayer charge and accessibility of the hydrophobic core
    • B.D. van Rooijen, M.M. Claessens, and V. Subramaniam Lipid bilayer disruption by oligomeric alpha-synuclein depends on bilayer charge and accessibility of the hydrophobic core Biochim. Biophys. Acta 1788 6 2009 1271 1278
    • (2009) Biochim. Biophys. Acta , vol.1788 , Issue.6 , pp. 1271-1278
    • Van Rooijen, B.D.1    Claessens, M.M.2    Subramaniam, V.3
  • 55
    • 7544245555 scopus 로고    scopus 로고
    • Islet amyloid polypeptide-induced membrane leakage involves uptake of lipids by forming amyloid fibers
    • E. Sparr Islet amyloid polypeptide-induced membrane leakage involves uptake of lipids by forming amyloid fibers FEBS Lett. 577 1-2 2004 117 120
    • (2004) FEBS Lett. , vol.577 , Issue.1-2 , pp. 117-120
    • Sparr, E.1
  • 56
    • 0027508926 scopus 로고
    • Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: Blockade by tromethamine and aluminum
    • N. Arispe, E. Rojas, and H.B. Pollard Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum Proc. Natl. Acad. Sci. 90 2 1993 567
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , Issue.2 , pp. 567
    • Arispe, N.1    Rojas, E.2    Pollard, H.B.3
  • 57
    • 0031024927 scopus 로고    scopus 로고
    • Channel formation by a neurotoxic prion protein fragment
    • M.C. Lin, T. Mirzabekov, and B.L. Kagan Channel formation by a neurotoxic prion protein fragment J. Biol. Chem. 272 1 1997 44 47
    • (1997) J. Biol. Chem. , vol.272 , Issue.1 , pp. 44-47
    • Lin, M.C.1    Mirzabekov, T.2    Kagan, B.L.3
  • 58
    • 0030044018 scopus 로고    scopus 로고
    • Pore formation by the cytotoxic islet amyloid peptide amylin
    • T.A. Mirzabekov, M. Lin, and B.L. Kagan Pore formation by the cytotoxic islet amyloid peptide amylin J. Biol. Chem. 271 4 1996 1988
    • (1996) J. Biol. Chem. , vol.271 , Issue.4 , pp. 1988
    • Mirzabekov, T.A.1    Lin, M.2    Kagan, B.L.3
  • 59
    • 84867260559 scopus 로고    scopus 로고
    • Polymorphic fibrillation of the destabilized fourth fasciclin-1 domain mutant A546T of the transforming growth factor-β-induced protein (TGFBIp) occurs through multiple pathways with different oligomeric intermediates
    • M. Andreasen Polymorphic fibrillation of the destabilized fourth fasciclin-1 domain mutant A546T of the transforming growth factor-β-induced protein (TGFBIp) occurs through multiple pathways with different oligomeric intermediates J. Biol. Chem. 287 41 2012 34730 34742
    • (2012) J. Biol. Chem. , vol.287 , Issue.41 , pp. 34730-34742
    • Andreasen, M.1
  • 60
    • 33744961740 scopus 로고    scopus 로고
    • The yeast prion Ure2p native-like assemblies are toxic to mammalian cells regardless of their aggregation state
    • L. Pieri The yeast prion Ure2p native-like assemblies are toxic to mammalian cells regardless of their aggregation state J. Biol. Chem. 281 22 2006 15337 15344
    • (2006) J. Biol. Chem. , vol.281 , Issue.22 , pp. 15337-15344
    • Pieri, L.1
  • 61
    • 75349097530 scopus 로고    scopus 로고
    • A causative link between the structure of aberrant protein oligomers and their toxicity
    • S. Campioni A causative link between the structure of aberrant protein oligomers and their toxicity Nat. Chem. Biol. 6 2 2010 140 147
    • (2010) Nat. Chem. Biol. , vol.6 , Issue.2 , pp. 140-147
    • Campioni, S.1
  • 62
    • 34548726211 scopus 로고    scopus 로고
    • Generic cell dysfunction in neurodegenerative disorders: Role of surfaces in early protein misfolding, aggregation, and aggregate cytotoxicity
    • M. Stefani Generic cell dysfunction in neurodegenerative disorders: role of surfaces in early protein misfolding, aggregation, and aggregate cytotoxicity Neuroscientist 13 5 2007 519 531
    • (2007) Neuroscientist , vol.13 , Issue.5 , pp. 519-531
    • Stefani, M.1
  • 63
    • 33749838193 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange mass spectrometry - A window into amyloid structure
    • I. Kheterpal, and R. Wetzel Hydrogen/deuterium exchange mass spectrometry - a window into amyloid structure Acc. Chem. Res. 39 9 2006 584 593
    • (2006) Acc. Chem. Res. , vol.39 , Issue.9 , pp. 584-593
    • Kheterpal, I.1    Wetzel, R.2
  • 64
    • 84861563520 scopus 로고    scopus 로고
    • Direct observation of the interconversion of normal and toxic forms of alpha-synuclein
    • N. Cremades Direct observation of the interconversion of normal and toxic forms of alpha-synuclein Cell 149 5 2012 1048 1059
    • (2012) Cell , vol.149 , Issue.5 , pp. 1048-1059
    • Cremades, N.1
  • 65
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the alpha-synuclein gene identified in families with Parkinson's disease
    • M.H. Polymeropoulos Mutation in the alpha-synuclein gene identified in families with Parkinson's disease Science 276 5321 1997 2045 2047
    • (1997) Science , vol.276 , Issue.5321 , pp. 2045-2047
    • Polymeropoulos, M.H.1
  • 66
    • 0030882856 scopus 로고    scopus 로고
    • Alpha-synuclein in Lewy bodies
    • M.G. Spillantini Alpha-synuclein in Lewy bodies Nature 388 6645 1997 839 840
    • (1997) Nature , vol.388 , Issue.6645 , pp. 839-840
    • Spillantini, M.G.1
  • 67
    • 12944304172 scopus 로고    scopus 로고
    • Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations
    • M.M. Dedmon Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations J. Am. Chem. Soc. 127 2 2005 476 477
    • (2005) J. Am. Chem. Soc. , vol.127 , Issue.2 , pp. 476-477
    • Dedmon, M.M.1
  • 68
    • 73249124356 scopus 로고    scopus 로고
    • Determination of the free energy landscape of alpha-synuclein using spin label nuclear magnetic resonance measurements
    • J.R. Allison Determination of the free energy landscape of alpha-synuclein using spin label nuclear magnetic resonance measurements J. Am. Chem. Soc. 131 51 2009 18314 18326
    • (2009) J. Am. Chem. Soc. , vol.131 , Issue.51 , pp. 18314-18326
    • Allison, J.R.1
  • 69
    • 27344436619 scopus 로고    scopus 로고
    • Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level
    • C. Del Mar Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level Proc. Natl. Acad. Sci. U. S. A. 102 43 2005 15477 15482
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , Issue.43 , pp. 15477-15482
    • Del Mar, C.1
  • 70
    • 84895775448 scopus 로고    scopus 로고
    • Characterizing the dynamics of alpha-synuclein oligomers using hydrogen/deuterium exchange monitored by mass spectrometry
    • S. Mysling Characterizing the dynamics of alpha-synuclein oligomers using hydrogen/deuterium exchange monitored by mass spectrometry Biochemistry 52 51 2013 9097 9103
    • (2013) Biochemistry , vol.52 , Issue.51 , pp. 9097-9103
    • Mysling, S.1
  • 71
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes
    • W.S. Davidson Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes J. Biol. Chem. 273 16 1998 9443 9449
    • (1998) J. Biol. Chem. , vol.273 , Issue.16 , pp. 9443-9449
    • Davidson, W.S.1
  • 72
    • 15744362063 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound human alpha-synuclein
    • T.S. Ulmer Structure and dynamics of micelle-bound human alpha-synuclein J. Biol. Chem. 280 10 2005 9595 9603
    • (2005) J. Biol. Chem. , vol.280 , Issue.10 , pp. 9595-9603
    • Ulmer, T.S.1
  • 73
    • 75749093356 scopus 로고    scopus 로고
    • Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy
    • C.R. Bodner Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy Biochemistry 49 5 2010 862 871
    • (2010) Biochemistry , vol.49 , Issue.5 , pp. 862-871
    • Bodner, C.R.1
  • 74
    • 77958482255 scopus 로고    scopus 로고
    • The N-terminus of the intrinsically disordered protein alpha-synuclein triggers membrane binding and helix folding
    • T. Bartels The N-terminus of the intrinsically disordered protein alpha-synuclein triggers membrane binding and helix folding Biophys. J. 99 7 2010 2116 2124
    • (2010) Biophys. J. , vol.99 , Issue.7 , pp. 2116-2124
    • Bartels, T.1
  • 75
    • 84901812732 scopus 로고    scopus 로고
    • Direct observation of the three regions in alpha-synuclein that determine its membrane-bound behaviour
    • G. Fusco Direct observation of the three regions in alpha-synuclein that determine its membrane-bound behaviour Nat. Commun. 5 2014 3827
    • (2014) Nat. Commun. , vol.5 , pp. 3827
    • Fusco, G.1
  • 76
    • 77957775523 scopus 로고    scopus 로고
    • Membrane curvature induction and tubulation are common features of synucleins and apolipoproteins
    • J. Varkey Membrane curvature induction and tubulation are common features of synucleins and apolipoproteins J. Biol. Chem. 285 42 2010 32486 32493
    • (2010) J. Biol. Chem. , vol.285 , Issue.42 , pp. 32486-32493
    • Varkey, J.1
  • 77
    • 82755176258 scopus 로고    scopus 로고
    • Membrane curvature sensing by amphipathic helices: A single liposome study using alpha-synuclein and annexin B12
    • M.B. Jensen Membrane curvature sensing by amphipathic helices: a single liposome study using alpha-synuclein and annexin B12 J. Biol. Chem. 286 49 2011 42603 42614
    • (2011) J. Biol. Chem. , vol.286 , Issue.49 , pp. 42603-42614
    • Jensen, M.B.1
  • 78
    • 84880521916 scopus 로고    scopus 로고
    • Alpha-synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling
    • M.M. Ouberai Alpha-synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling J. Biol. Chem. 288 29 2013 20883 20895
    • (2013) J. Biol. Chem. , vol.288 , Issue.29 , pp. 20883-20895
    • Ouberai, M.M.1
  • 79
    • 0037046163 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism
    • M.J. Volles, and P.T. Lansbury Jr. Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism Biochemistry 41 14 2002 4595 4602
    • (2002) Biochemistry , vol.41 , Issue.14 , pp. 4595-4602
    • Volles, M.J.1    Lansbury, Jr.P.T.2
  • 80
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • H.A. Lashuel Neurodegenerative disease: amyloid pores from pathogenic mutations Nature 418 6895 2002 291
    • (2002) Nature , vol.418 , Issue.6895 , pp. 291
    • Lashuel, H.A.1
  • 81
    • 84865426796 scopus 로고    scopus 로고
    • Molecular composition of sub-stoichiometrically labeled alpha-synuclein oligomers determined by single-molecule photobleaching
    • N. Zijlstra Molecular composition of sub-stoichiometrically labeled alpha-synuclein oligomers determined by single-molecule photobleaching Angew. Chem. Int. Ed. Engl. 51 35 2012 8821 8824
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.51 , Issue.35 , pp. 8821-8824
    • Zijlstra, N.1
  • 82
    • 79952748803 scopus 로고    scopus 로고
    • Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation
    • L. Giehm, S.D., D.E. Otzen, and B. Vestergaard Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation Proc. Natl. Acad. Sci. U. S. A. 108 8 2011 3246 3251
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , Issue.8 , pp. 3246-3251
    • Giehm, L.1    Otzen, D.E.2    Vestergaard, B.3
  • 83
    • 84907571241 scopus 로고    scopus 로고
    • Structural insights into amyloid oligomers of the Parkinson disease-related protein alpha-synuclein
    • J.I. Gallea, and M.S. Celej Structural insights into amyloid oligomers of the Parkinson disease-related protein alpha-synuclein J. Biol. Chem. 289 39 2014 26733 26742
    • (2014) J. Biol. Chem. , vol.289 , Issue.39 , pp. 26733-26742
    • Gallea, J.I.1    Celej, M.S.2
  • 84
    • 84860110592 scopus 로고    scopus 로고
    • Toxic prefibrillar alpha-synuclein amyloid oligomers adopt a distinctive antiparallel beta-sheet structure
    • M.S. Celej Toxic prefibrillar alpha-synuclein amyloid oligomers adopt a distinctive antiparallel beta-sheet structure Biochem. J. 443 3 2012 719 726
    • (2012) Biochem. J. , vol.443 , Issue.3 , pp. 719-726
    • Celej, M.S.1
  • 85
    • 84936892181 scopus 로고    scopus 로고
    • Formation and characterization of α-synuclein oligomers
    • (in press)
    • W. Paslawski, N. Lorenzen, and D.E. Otzen Formation and characterization of α-synuclein oligomers Methods Mol. Biol. 2015 (in press)
    • (2015) Methods Mol. Biol.
    • Paslawski, W.1    Lorenzen, N.2    Otzen, D.E.3
  • 86
    • 67649344732 scopus 로고    scopus 로고
    • The influence of vesicle size and composition on alpha-synuclein structure and stability
    • L. Kjaer The influence of vesicle size and composition on alpha-synuclein structure and stability Biophys. J. 96 7 2009 2857 2870
    • (2009) Biophys. J. , vol.96 , Issue.7 , pp. 2857-2870
    • Kjaer, L.1
  • 87
    • 54849417407 scopus 로고    scopus 로고
    • Membrane binding of oligomeric alpha-synuclein depends on bilayer charge and packing
    • B.D. van Rooijen, M.M. Claessens, and V. Subramaniam Membrane binding of oligomeric alpha-synuclein depends on bilayer charge and packing FEBS Lett. 582 27 2008 3788 3792
    • (2008) FEBS Lett. , vol.582 , Issue.27 , pp. 3788-3792
    • Van Rooijen, B.D.1    Claessens, M.M.2    Subramaniam, V.3
  • 88
    • 77955881152 scopus 로고    scopus 로고
    • ANS binding reveals common features of cytotoxic amyloid species
    • B. Bolognesi ANS binding reveals common features of cytotoxic amyloid species ACS Chem. Biol. 5 8 2010 735 740
    • (2010) ACS Chem. Biol. , vol.5 , Issue.8 , pp. 735-740
    • Bolognesi, B.1
  • 89
    • 65549107985 scopus 로고    scopus 로고
    • The first N-terminal amino acids of α-synuclein are essential for α-helical structure formation in vitro and membrane binding in yeast
    • K. Vamcava, M.J. Volles, and P.T. Lansbury The first N-terminal amino acids of α-synuclein are essential for α-helical structure formation in vitro and membrane binding in yeast J. Mol. Biol. 389 4755 2009 413 424
    • (2009) J. Mol. Biol. , vol.389 , Issue.4755 , pp. 413-424
    • Vamcava, K.1    Volles, M.J.2    Lansbury, P.T.3
  • 90
    • 79953155808 scopus 로고    scopus 로고
    • Human phenotypically distinct TGFBI corneal dystrophies are linked to the stability of the fourth FAS1 domain of TGFBIp
    • K. Runager Human phenotypically distinct TGFBI corneal dystrophies are linked to the stability of the fourth FAS1 domain of TGFBIp J. Biol. Chem. 286 7 2011 4951 4958
    • (2011) J. Biol. Chem. , vol.286 , Issue.7 , pp. 4951-4958
    • Runager, K.1
  • 91
    • 0031020733 scopus 로고    scopus 로고
    • Kerato-epithelin mutations in four 5q31-linked corneal dystrophies
    • F.L. Munier Kerato-epithelin mutations in four 5q31-linked corneal dystrophies Nat. Genet. 15 3 1997 247 251
    • (1997) Nat. Genet. , vol.15 , Issue.3 , pp. 247-251
    • Munier, F.L.1
  • 92
    • 33745728355 scopus 로고    scopus 로고
    • TGFBI gene mutations in corneal dystrophies
    • C. Kannabiran, and G.K. Klintworth TGFBI gene mutations in corneal dystrophies Hum. Mutat. 27 7 2006 615 625
    • (2006) Hum. Mutat. , vol.27 , Issue.7 , pp. 615-625
    • Kannabiran, C.1    Klintworth, G.K.2
  • 93
    • 0347581233 scopus 로고    scopus 로고
    • The molecular genetics of the corneal dystrophies - Current status
    • G.K. Klintworth The molecular genetics of the corneal dystrophies - current status Front. Biosci. 8 2003 d687 d713
    • (2003) Front. Biosci. , vol.8 , pp. d687-d713
    • Klintworth, G.K.1
  • 94
    • 0026783009 scopus 로고
    • CDNA cloning and sequence analysis of beta ig-h3, a novel gene induced in a human adenocarcinoma cell line after treatment with transforming growth factor-beta
    • J. Skonier cDNA cloning and sequence analysis of beta ig-h3, a novel gene induced in a human adenocarcinoma cell line after treatment with transforming growth factor-beta DNA Cell Biol. 11 7 1992 511 522
    • (1992) DNA Cell Biol. , vol.11 , Issue.7 , pp. 511-522
    • Skonier, J.1
  • 95
    • 0032902822 scopus 로고    scopus 로고
    • Immunolocalization of beta ig-h3 protein in 5q31-linked corneal dystrophies and normal corneas
    • B.W. Streeten Immunolocalization of beta ig-h3 protein in 5q31-linked corneal dystrophies and normal corneas Arch. Ophthalmol. 117 1 1999 67 75
    • (1999) Arch. Ophthalmol. , vol.117 , Issue.1 , pp. 67-75
    • Streeten, B.W.1
  • 96
    • 0034646599 scopus 로고    scopus 로고
    • Amyloid and non-amyloid forms of 5q31-linked corneal dystrophy resulting from kerato-epithelin mutations at Arg-124 are associated with abnormal turnover of the protein
    • E. Korvatska Amyloid and non-amyloid forms of 5q31-linked corneal dystrophy resulting from kerato-epithelin mutations at Arg-124 are associated with abnormal turnover of the protein J. Biol. Chem. 275 15 2000 11465 11469
    • (2000) J. Biol. Chem. , vol.275 , Issue.15 , pp. 11465-11469
    • Korvatska, E.1
  • 97
    • 17344365347 scopus 로고    scopus 로고
    • Mutation hot spots in 5q31-linked corneal dystrophies
    • E. Korvatska Mutation hot spots in 5q31-linked corneal dystrophies Am. J. Hum. Genet. 62 2 1998 320 324
    • (1998) Am. J. Hum. Genet. , vol.62 , Issue.2 , pp. 320-324
    • Korvatska, E.1
  • 98
    • 0033983763 scopus 로고    scopus 로고
    • A new mutation (A546T) of the betaig-h3 gene responsible for a French lattice corneal dystrophy type IIIA
    • P. Dighiero A new mutation (A546T) of the betaig-h3 gene responsible for a French lattice corneal dystrophy type IIIA Am J. Ophthalmol. 129 2 2000 248 251
    • (2000) Am J. Ophthalmol. , vol.129 , Issue.2 , pp. 248-251
    • Dighiero, P.1
  • 99
    • 79953836704 scopus 로고    scopus 로고
    • SAXS models of TGFBIp reveal a trimeric structure and show that the overall shape is not affected by the Arg124His mutation
    • R.V. Basaiawmoit SAXS models of TGFBIp reveal a trimeric structure and show that the overall shape is not affected by the Arg124His mutation J. Mol. Biol. 408 3 2011 503 513
    • (2011) J. Mol. Biol. , vol.408 , Issue.3 , pp. 503-513
    • Basaiawmoit, R.V.1
  • 100
    • 39149129078 scopus 로고    scopus 로고
    • Maintaining transparency: A review of the developmental physiology and pathophysiology of two avascular tissues
    • D.C. Beebe Maintaining transparency: a review of the developmental physiology and pathophysiology of two avascular tissues Semin. Cell Dev. Biol. 19 2 2008 125 133
    • (2008) Semin. Cell Dev. Biol. , vol.19 , Issue.2 , pp. 125-133
    • Beebe, D.C.1
  • 101
    • 84857801063 scopus 로고    scopus 로고
    • Composition and proteolytic processing of corneal deposits associated with mutations in the TGFBI gene
    • H. Karring Composition and proteolytic processing of corneal deposits associated with mutations in the TGFBI gene Exp. Eye Res. 96 1 2012 163 170
    • (2012) Exp. Eye Res. , vol.96 , Issue.1 , pp. 163-170
    • Karring, H.1
  • 102
    • 11044229726 scopus 로고    scopus 로고
    • Purification and structural characterization of transforming growth factor beta induced protein (TGFBIp) from porcine and human corneas
    • R.B. Andersen Purification and structural characterization of transforming growth factor beta induced protein (TGFBIp) from porcine and human corneas Biochemistry 43 51 2004 16374 16384
    • (2004) Biochemistry , vol.43 , Issue.51 , pp. 16374-16384
    • Andersen, R.B.1
  • 103
    • 0030971789 scopus 로고    scopus 로고
    • Disaggregation of Alzheimer beta-amyloid by site-directed mAb
    • B. Solomon Disaggregation of Alzheimer beta-amyloid by site-directed mAb Proc. Natl. Acad. Sci. U. S. A. 94 8 1997 4109 4112
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , Issue.8 , pp. 4109-4112
    • Solomon, B.1
  • 104
    • 0034700471 scopus 로고    scopus 로고
    • A beta peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease
    • C. Janus A beta peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease Nature 408 6815 2000 979 982
    • (2000) Nature , vol.408 , Issue.6815 , pp. 979-982
    • Janus, C.1
  • 105
    • 74549169940 scopus 로고    scopus 로고
    • Small molecule beta-amyloid inhibitors that stabilize protofibrillar structures in vitro improve cognition and pathology in a mouse model of Alzheimer's disease
    • C.A. Hawkes Small molecule beta-amyloid inhibitors that stabilize protofibrillar structures in vitro improve cognition and pathology in a mouse model of Alzheimer's disease Eur. J. Neurosci. 31 2 2010 203 213
    • (2010) Eur. J. Neurosci. , vol.31 , Issue.2 , pp. 203-213
    • Hawkes, C.A.1
  • 106
    • 78149282151 scopus 로고    scopus 로고
    • Antibodies to human serum amyloid P component eliminate visceral amyloid deposits
    • K. Bodin Antibodies to human serum amyloid P component eliminate visceral amyloid deposits Nature 468 7320 2010 93 97
    • (2010) Nature , vol.468 , Issue.7320 , pp. 93-97
    • Bodin, K.1
  • 107
    • 0030757182 scopus 로고    scopus 로고
    • Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene
    • M. Botto Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene Nat. Med. 3 8 1997 855 859
    • (1997) Nat. Med. , vol.3 , Issue.8 , pp. 855-859
    • Botto, M.1
  • 108
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red
    • A. Lorenzo, and B.A. Yankner Beta-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red Proc. Natl. Acad. Sci. U. S. A. 91 25 1994 12243 12247
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , Issue.25 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 109
    • 0034612220 scopus 로고    scopus 로고
    • Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: Implications for Huntington's disease therapy
    • V. Heiser Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: implications for Huntington's disease therapy Proc. Natl. Acad. Sci. U. S. A. 97 12 2000 6739 6744
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , Issue.12 , pp. 6739-6744
    • Heiser, V.1
  • 110
    • 0032500717 scopus 로고    scopus 로고
    • Chrysamine-G, a lipophilic analogue of Congo red, inhibits A beta-induced toxicity in PC12 cells
    • W.E. Klunk Chrysamine-G, a lipophilic analogue of Congo red, inhibits A beta-induced toxicity in PC12 cells Life Sci. 63 20 1998 1807 1814
    • (1998) Life Sci. , vol.63 , Issue.20 , pp. 1807-1814
    • Klunk, W.E.1
  • 111
    • 20044370990 scopus 로고    scopus 로고
    • Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo
    • F. Yang Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo J. Biol. Chem. 280 7 2005 5892 5901
    • (2005) J. Biol. Chem. , vol.280 , Issue.7 , pp. 5892-5901
    • Yang, F.1
  • 112
    • 54849423681 scopus 로고    scopus 로고
    • Inhibition of alpha-synuclein fibrillization by dopamine is mediated by interactions with five C-terminal residues and with E83 in the NAC region
    • F.E. Herrera Inhibition of alpha-synuclein fibrillization by dopamine is mediated by interactions with five C-terminal residues and with E83 in the NAC region PLoS ONE 3 10 2008 e3394
    • (2008) PLoS ONE , vol.3 , Issue.10 , pp. e3394
    • Herrera, F.E.1
  • 113
    • 20444401187 scopus 로고    scopus 로고
    • Reversible inhibition of alpha-synuclein fibrillization by dopaminochrome-mediated conformational alterations
    • E.H. Norris Reversible inhibition of alpha-synuclein fibrillization by dopaminochrome-mediated conformational alterations J. Biol. Chem. 280 22 2005 21212 21219
    • (2005) J. Biol. Chem. , vol.280 , Issue.22 , pp. 21212-21219
    • Norris, E.H.1
  • 114
    • 4344650564 scopus 로고    scopus 로고
    • Dopamine and L-dopa disaggregate amyloid fibrils: Implications for Parkinson's and Alzheimer's disease
    • J. Li Dopamine and L-dopa disaggregate amyloid fibrils: implications for Parkinson's and Alzheimer's disease FASEB J. 18 9 2004 962 964
    • (2004) FASEB J. , vol.18 , Issue.9 , pp. 962-964
    • Li, J.1
  • 115
    • 62049085927 scopus 로고    scopus 로고
    • Formation of dopamine-mediated alpha-synuclein-soluble oligomers requires methionine oxidation
    • S.L. Leong Formation of dopamine-mediated alpha-synuclein-soluble oligomers requires methionine oxidation Free Radic. Biol. Med. 46 10 2009 1328 1337
    • (2009) Free Radic. Biol. Med. , vol.46 , Issue.10 , pp. 1328-1337
    • Leong, S.L.1
  • 116
    • 44849087785 scopus 로고    scopus 로고
    • EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers
    • D.E. Ehrnhoefer EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers Nat. Struct. Mol. Biol. 15 6 2008 558 566
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , Issue.6 , pp. 558-566
    • Ehrnhoefer, D.E.1
  • 117
    • 77952346781 scopus 로고    scopus 로고
    • EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity
    • J. Bieschke EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity Proc. Natl. Acad. Sci. U. S. A. 107 17 2010 7710 7715
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , Issue.17 , pp. 7710-7715
    • Bieschke, J.1
  • 118
    • 84907146173 scopus 로고    scopus 로고
    • The potential therapeutic effects of THC on Alzheimer's disease
    • C. Cao The potential therapeutic effects of THC on Alzheimer's disease J. Alzheimers Dis. 42 3 2014 973 984
    • (2014) J. Alzheimers Dis. , vol.42 , Issue.3 , pp. 973-984
    • Cao, C.1
  • 119
    • 9444229299 scopus 로고    scopus 로고
    • A strategy for designing inhibitors of alpha-synuclein aggregation and toxicity as a novel treatment for Parkinson's disease and related disorders
    • O.M. El-Agnaf A strategy for designing inhibitors of alpha-synuclein aggregation and toxicity as a novel treatment for Parkinson's disease and related disorders FASEB J. 18 11 2004 1315 1317
    • (2004) FASEB J. , vol.18 , Issue.11 , pp. 1315-1317
    • El-Agnaf, O.M.1
  • 120
    • 75749130652 scopus 로고    scopus 로고
    • Design and study of peptide-based inhibitors of amylin cytotoxicity
    • K. Muthusamy Design and study of peptide-based inhibitors of amylin cytotoxicity Bioorg. Med. Chem. Lett. 20 4 2010 1360 1362
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , Issue.4 , pp. 1360-1362
    • Muthusamy, K.1
  • 121
    • 78649757873 scopus 로고    scopus 로고
    • Inhibiting alpha-synuclein oligomerization by stable cell-penetrating beta-synuclein fragments recovers phenotype of Parkinson's disease model flies
    • R. Shaltiel-Karyo Inhibiting alpha-synuclein oligomerization by stable cell-penetrating beta-synuclein fragments recovers phenotype of Parkinson's disease model flies PLoS ONE 5 11 2010 e13863
    • (2010) PLoS ONE , vol.5 , Issue.11 , pp. e13863
    • Shaltiel-Karyo, R.1
  • 122
    • 1842608890 scopus 로고    scopus 로고
    • Inhibition of fibril formation and toxicity of a fragment of alpha-synuclein by an N-methylated peptide analogue
    • A.M. Bodles Inhibition of fibril formation and toxicity of a fragment of alpha-synuclein by an N-methylated peptide analogue Neurosci. Lett. 359 1-2 2004 89 93
    • (2004) Neurosci. Lett. , vol.359 , Issue.1-2 , pp. 89-93
    • Bodles, A.M.1
  • 123
    • 39649124929 scopus 로고    scopus 로고
    • Designing peptide inhibitors for oligomerization and toxicity of Alzheimer's beta-amyloid peptide
    • B.M. Austen Designing peptide inhibitors for oligomerization and toxicity of Alzheimer's beta-amyloid peptide Biochemistry 47 7 2008 1984 1992
    • (2008) Biochemistry , vol.47 , Issue.7 , pp. 1984-1992
    • Austen, B.M.1
  • 124
    • 0030600371 scopus 로고    scopus 로고
    • Inhibition of Alzheimer's amyloidosis by peptides that prevent beta-sheet conformation
    • C. Soto Inhibition of Alzheimer's amyloidosis by peptides that prevent beta-sheet conformation Biochem. Biophys. Res. Commun. 226 3 1996 672 680
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , Issue.3 , pp. 672-680
    • Soto, C.1
  • 125
    • 79955404847 scopus 로고    scopus 로고
    • A cyclic undecamer peptide mimics a turn in folded Alzheimer amyloid beta and elicits antibodies against oligomeric and fibrillar amyloid and plaques
    • P. Hoogerhout A cyclic undecamer peptide mimics a turn in folded Alzheimer amyloid beta and elicits antibodies against oligomeric and fibrillar amyloid and plaques PLoS ONE 6 4 2011 e19110
    • (2011) PLoS ONE , vol.6 , Issue.4 , pp. e19110
    • Hoogerhout, P.1
  • 126
    • 78650257792 scopus 로고    scopus 로고
    • Chemical probes that selectively recognize the earliest Abeta oligomers in complex mixtures
    • A.A. Reinke Chemical probes that selectively recognize the earliest Abeta oligomers in complex mixtures J. Am. Chem. Soc. 132 50 2010 17655 17657
    • (2010) J. Am. Chem. Soc. , vol.132 , Issue.50 , pp. 17655-17657
    • Reinke, A.A.1
  • 127
    • 18844427273 scopus 로고    scopus 로고
    • Structural properties of Abeta protofibrils stabilized by a small molecule
    • A.D. Williams Structural properties of Abeta protofibrils stabilized by a small molecule Proc. Natl. Acad. Sci. U. S. A. 102 20 2005 7115 7120
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , Issue.20 , pp. 7115-7120
    • Williams, A.D.1
  • 128
    • 83655184703 scopus 로고    scopus 로고
    • Small-molecule conversion of toxic oligomers to nontoxic beta-sheet-rich amyloid fibrils
    • J. Bieschke Small-molecule conversion of toxic oligomers to nontoxic beta-sheet-rich amyloid fibrils Nat. Chem. Biol. 8 1 2012 93 101
    • (2012) Nat. Chem. Biol. , vol.8 , Issue.1 , pp. 93-101
    • Bieschke, J.1
  • 129
    • 84892150877 scopus 로고    scopus 로고
    • Structural and functional characterization of two alpha-synuclein strains
    • L. Bousset Structural and functional characterization of two alpha-synuclein strains Nat. Commun. 4 2013
    • (2013) Nat. Commun. , vol.4
    • Bousset, L.1
  • 130
    • 84856545963 scopus 로고    scopus 로고
    • Toxic effects of amyloid fibrils on cell membranes: The importance of ganglioside GM1
    • M. Bucciantini Toxic effects of amyloid fibrils on cell membranes: the importance of ganglioside GM1 FASEB J. 26 2 2012 818 831
    • (2012) FASEB J. , vol.26 , Issue.2 , pp. 818-831
    • Bucciantini, M.1
  • 131
    • 4143094106 scopus 로고    scopus 로고
    • Phospholipid catalysis of diabetic amyloid assembly
    • J.D. Knight, and A.D. Miranker Phospholipid catalysis of diabetic amyloid assembly J. Mol. Biol. 341 5 2004 1175 1187
    • (2004) J. Mol. Biol. , vol.341 , Issue.5 , pp. 1175-1187
    • Knight, J.D.1    Miranker, A.D.2
  • 132
    • 84905457722 scopus 로고    scopus 로고
    • 2m-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH
    • 2m-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH PLoS ONE 9 8 2014
    • (2014) PLoS ONE , vol.9 , Issue.8
    • Goodchild, S.C.1
  • 133
    • 84870947924 scopus 로고    scopus 로고
    • Direct three-dimensional visualization of membrane disruption by amyloid fibrils
    • L. Milanesi Direct three-dimensional visualization of membrane disruption by amyloid fibrils Proc. Natl. Acad. Sci. U. S. A. 109 50 2012 20455 20460
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , Issue.50 , pp. 20455-20460
    • Milanesi, L.1
  • 134
    • 4043100348 scopus 로고    scopus 로고
    • Formation of amyloid fibers triggered by phosphatidylserine-containing membranes
    • H. Zhao, E.K.J. Tuominen, and P.K.J. Kinnunen Formation of amyloid fibers triggered by phosphatidylserine-containing membranes Biochemistry 43 3610 2004 10302 10307
    • (2004) Biochemistry , vol.43 , Issue.3610 , pp. 10302-10307
    • Zhao, H.1    Tuominen, E.K.J.2    Kinnunen, P.K.J.3
  • 135
    • 31344478495 scopus 로고    scopus 로고
    • Islet amyloid polypeptide inserts into phospholipid monolayers as monomer
    • M.F. Engel Islet amyloid polypeptide inserts into phospholipid monolayers as monomer J. Mol. Biol. 356 3 2006 783 789
    • (2006) J. Mol. Biol. , vol.356 , Issue.3 , pp. 783-789
    • Engel, M.F.1
  • 136
    • 84865388990 scopus 로고    scopus 로고
    • Two-step mechanism of membrane disruption by Abeta through membrane fragmentation and pore formation
    • M.F. Sciacca Two-step mechanism of membrane disruption by Abeta through membrane fragmentation and pore formation Biophys. J. 103 4 2012 702 710
    • (2012) Biophys. J. , vol.103 , Issue.4 , pp. 702-710
    • Sciacca, M.F.1
  • 137
    • 43149118349 scopus 로고    scopus 로고
    • Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane
    • M.F. Engel Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane Proc. Natl. Acad. Sci. U. S. A. 105 16 2008 6033 6038
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , Issue.16 , pp. 6033-6038
    • Engel, M.F.1
  • 138
    • 4143094106 scopus 로고    scopus 로고
    • Phospholipid catalysis of diabetic amyloid assembly
    • J.D. Knight, and A.D. Miranker Phospholipid catalysis of diabetic amyloid assembly J. Mol. Biol. 341 2004 1175 1187
    • (2004) J. Mol. Biol. , vol.341 , pp. 1175-1187
    • Knight, J.D.1    Miranker, A.D.2
  • 139
    • 84902995340 scopus 로고    scopus 로고
    • Amyloids of alpha-synuclein affect the structure and dynamics of supported lipid bilayers
    • A. Iyer Amyloids of alpha-synuclein affect the structure and dynamics of supported lipid bilayers Biophys. J. 106 12 2014 2585 2594
    • (2014) Biophys. J. , vol.106 , Issue.12 , pp. 2585-2594
    • Iyer, A.1
  • 140
    • 84910664562 scopus 로고    scopus 로고
    • Membrane interactions and fibrillization of alpha-synuclein play an essential role in membrane disruption
    • H. Chaudhary Membrane interactions and fibrillization of alpha-synuclein play an essential role in membrane disruption FEBS Lett. 588 23 2014 4457 4463
    • (2014) FEBS Lett. , vol.588 , Issue.23 , pp. 4457-4463
    • Chaudhary, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.