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Structures of α-synuclein filaments from human brains with Lewy pathology
Yang Yang, Yang Shi, Manuel Schweighauser and 17 more
Nature · 2022
doi:10.1038/s41586-022-05319-3
References 66
- 1.
- 2.
Goedert M, Spillantini MG, Del Tredici K, Braak H. 100 years of Lewy pathology. Nature Rev Neurol. 2013;9:13-24.
Not in our library10.1038/nrneurol.2012.242
- 3.
Aarsland D, Andersen K, Larsen JP, Lolk A, Kragh-Sørensen P. Prevalence and characteristics of dementia in Parkinson disease: an 8-year prospective study. Arch Neurol. 2003;60:387-392.
Not in our library10.1001/archneur.60.3.387
- 4.
- 5.
Fanciulli A, Wenning GK. Multiple system atrophy. N Engl J Med. 2015;372:249-263.
Not in our library10.1056/nejmra1311488
- 6.
Schweighauser M, et al. Structures of α-synuclein filaments from multiple system atrophy. Nature. 2020;585:464-469.
Not in our library10.1038/s41586-020-2317-6
- 7.
Polymeropoulos MH, et al. Mutation in the α-synuclein gene identified in families with Parkinson’s disease. Science. 1997;276:2045-2047.
Not in our library10.1126/science.276.5321.2045
- 8.
Singleton AB, et al. α-Synuclein locus triplication causes Parkinson’s disease. Science. 2003;302:841.
Not in our library10.1126/science.1090278
- 9.
Zarranz JJ, et al. The new mutation, E46K, of alpha-synuclein causes Parkinson’s disease and Lewy body dementia. Ann Neurol. 2004;55:164-173.
Not in our library10.1002/ana.10795
- 10.
Nalls MA, et al. Large-scale meta-analysis of genome-wide association data identifies six new risk loci for Parkinson’s disease. Nature Genet. 2014;46:989-993.
Not in our library10.1038/ng.3043
- 11.
Davidson WS, Jonas A, Clayton DF, George JM. Stabilization of α-synuclein secondary structure upon binding to synthetic membranes. J Biol Chem. 1998;273:9443-9449.
Not in our library10.1074/jbc.273.16.9443
- 12.
Ueda K, et al. Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease. Proc Natl Acad Sci USA. 1993;90:11282-11286.
Not in our library10.1073/pnas.90.23.11282
- 13.
Li HT, Du HN, Tang L, Hu J, Hu HY. Structural transformation and aggregation of human α-synuclein in trifluoroethanol: non-amyloid component sequence is essential and β-sheet formation is prerequisite to aggregation. Biopolymers. 2002;64:221-226.
Not in our library10.1002/bip.10179
- 14.
Crowther RA, Jakes R, Spillantini MG, Goedert M. Synthetic filaments assembled from C-terminally truncated α-synuclein. FEBS Lett. 1998;436:309-312.
Not in our library10.1016/s0014-5793(98)01146-6
- 15.
Conway KA, Harper JD, Lansbury PT. Fibrils formed in vitro from α-synuclein and two mutant forms linked to Parkinson’s disease are typical amyloid. Biochemistry. 2000;39:2525-2563.
Not in our library10.1021/bi991447r
- 16.
Serpell LC, Berriman J, Jakes R, Goedert M, Crowther RA. Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-ß conformation. Proc Natl Acad Sci USA. 2000;97:4897-4902.
Not in our library10.1073/pnas.97.9.4897
- 17.
Miake H, Mizusawa H, Iwatsubo T, Hasegawa M. Biochemical characterization of the core structure of α-synuclein filaments. J Biol Chem. 2002;277:19213-19219.
Not in our library10.1074/jbc.m110551200
- 18.
Mougenot AL, et al. Prion-like acceleration of a synucleinopathy in a transgenic mouse model. Neurobiol Aging. 2012;33:2225-2228.
Not in our library10.1016/j.neurobiolaging.2011.06.022
- 19.
Luk KC, et al. Pathological α-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice. Science. 2012;338:949-953.
Not in our library10.1126/science.1227157
- 20.
Masuda-Suzukake M, et al. Prion-like spreading of pathological α-synuclein in brain. Brain. 2013;136:1128-1138.
Not in our library10.1093/brain/awt037
- 21.
Osterberg VR, et al. Progressive aggregation of α-synuclein and selective degeneration of Lewy inclusion-bearing neurons in a mouse model of parkinsonism. Cell Rep. 2015;10:1252-1260.
Not in our library10.1016/j.celrep.2015.01.060
- 22.
Peelaerts W, et al. α-Synuclein strains cause distinct synucleinopathies after local and systemic administration. Nature. 2015;522:340-344.
Not in our library10.1038/nature14547
- 23.
Peng C, et al. Cellular milieu imparts pathological α-synuclein strains in α-synucleinopathies. Nature. 2018;557:558-563.
Not in our library10.1038/s41586-018-0104-4
- 24.
Prusiner SB, et al. Evidence for α-synuclein prions causing multiple system atrophy in humans with parkinsonism. Proc Natl Acad Sci USA. 2015;112:E5308-E5317.
Not in our library10.1073/pnas.1514475112
- 25.
Tarutani A, Arai T, Murayama S, Hisanaga SI, Hasegawa M. Potent prion-like behaviors of pathogenic α-synuclein and evaluation of inactivation methods. Acta Neuropathol Commun. 2018;6:29.
Not in our library10.1186/s40478-018-0532-2
- 26.
- 27.
- 28.
Klingstedt T, et al. Luminescent conjugated oligothiophenes distinguish between α-synuclein assemblies of Parkinson’s disease and multiple system atrophy. Acta Neuropathol Commun. 2019;7:193.
Not in our library10.1186/s40478-019-0840-1
- 29.
- 30.
Lau A, et al. α-Synuclein strains target distinct brain regions and cell types. Nature Neurosci. 2020;23:21-31.
Not in our library10.1038/s41593-019-0541-x
- 31.
Shahnawaz M, et al. Discriminating α-synuclein strains in Parkinson’s disease and multiple system atrophy. Nature. 2020;578:273-277.
Not in our library10.1038/s41586-020-1984-7
- 32.
Ayers JI, et al. Different α-synuclein prion strains cause dementia with Lewy bodies and multiple system atrophy. Proc Natl Acad Sci USA. 2022;119:e2113489119.
Not in our library10.1073/pnas.2113489119
- 33.
Spillantini MG, Crowther RA, Jakes R, Hasegawa M, Goedert M. α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with Lewy bodies. Proc Natl Acad Sci USA. 1998;95:6469-6473.
Not in our library10.1073/pnas.95.11.6469
- 34.
Crowther RA, Daniel SE, Goedert M. Characterisation of isolated α-synuclein filaments from substantia nigra of Parkinson’s disease brain. Neurosci Lett. 2000;292:128-130.
Not in our library10.1016/s0304-3940(00)01440-3
- 35.
Holec SAM, Liu SL, Woerman AL. Consequences of variability in α-synuclein fibril structure on strain biology. Acta Neuropathol. 2022;143:311-330.
Not in our library10.1007/s00401-022-02403-w
- 36.
Zhao K, et al. Parkinson’s disease-related phosphorylation at Tyr39 rearranges α-synuclein amyloid fibril structure revealed by cryo-EM. Proc Natl Acad Sci USA. 2020;117:20305-20315.
Not in our library10.1073/pnas.1922741117
- 37.
McGlinchey RP, Ni X, Shadish JA, Jiang J, Lee JC. The N-terminus of α-synuclein dictates fibril formation. Proc Natl Acad Sci USA. 2021;118:e2023487118.
Not in our library10.1073/pnas.2023487118
- 38.
- 39.
Shi Y, et al. Structure-based classification of tauopathies. Nature. 2021;598:359-363.
Not in our library10.1038/s41586-021-03911-7
- 40.
Tsuboi Y, Dickson DW. Dementia with Lewy bodies and Parkinson’s disease with dementia: Are they different? Parkinsonism Relat. Disord. 2005;11:S47-S51.
Not in our library10.1016/j.parkreldis.2004.10.014
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