Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel
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D. Eisenberg | Z. Zhou | M. Sawaya | P. Ge | D. Boyer | Binsen Li | K. Murray | Lin Jiang | G. Nair | P. Sheth | Meng Zhang | W. Shin | S. Ye | L. Jiang | Lin Jiang
[1] Paul D. Williams. Entry , 2018, Definitions.
[2] John L. Robinson,et al. Cellular Milieu Imparts Distinct Pathological α-Synuclein Strains in α-Synucleinopathies , 2018, Nature.
[3] E. L. Guenther,et al. Atomic-level evidence for packing and positional amyloid polymorphism by segment from TDP-43 RRM2 , 2018, Nature Structural & Molecular Biology.
[4] R. Riek,et al. Cryo-EM structure of alpha-synuclein fibrils , 2018, bioRxiv.
[5] G. Schröder,et al. Fibril structure of amyloid-β(1–42) by cryo–electron microscopy , 2017, Science.
[6] V. Sossi,et al. Homozygous alpha-synuclein p.A53V in familial Parkinson's disease , 2017, Neurobiology of Aging.
[7] A. Murzin,et al. Cryo-EM structures of Tau filaments from Alzheimer’s disease brain , 2017, Nature.
[8] Charles D. Schwieters,et al. Solid-State NMR Structure of a Pathogenic Fibril of Full-Length Human α-Synuclein , 2016, Nature Structural &Molecular Biology.
[9] M. Diamond,et al. Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry. , 2015, Journal of visualized experiments : JoVE.
[10] N. Grigorieff,et al. CTFFIND4: Fast and accurate defocus estimation from electron micrographs , 2015, bioRxiv.
[11] Nicholas K. Sauter,et al. Structure of the toxic core of α-synuclein from invisible crystals , 2015, Nature.
[12] D. Geschwind,et al. Evidence for α-synuclein prions causing multiple system atrophy in humans with parkinsonism , 2015, Proceedings of the National Academy of Sciences.
[13] M. Giugliano,et al. α-Synuclein strains cause distinct synucleinopathies after local and systemic administration , 2015, Nature.
[14] Nigel J. Cairns,et al. Proteopathic tau seeding predicts tauopathy in vivo , 2014, Proceedings of the National Academy of Sciences.
[15] A. Paetau,et al. A novel α-synuclein mutation A53E associated with atypical multiple system atrophy and Parkinson's disease-type pathology , 2014, Neurobiology of Aging.
[16] B. Meier,et al. Structural and functional characterization of two alpha-synuclein strains , 2013, Nature Communications.
[17] M. Farrer,et al. Alpha‐synuclein p.H50Q, a novel pathogenic mutation for Parkinson's disease , 2013, Movement disorders : official journal of the Movement Disorder Society.
[18] Ronald Melki,et al. G51D α‐synuclein mutation causes a novel Parkinsonian–pyramidal syndrome , 2013, Annals of neurology.
[19] Sjors H.W. Scheres,et al. RELION: Implementation of a Bayesian approach to cryo-EM structure determination , 2012, Journal of structural biology.
[20] A. Björklund,et al. Alpha-Synuclein Cell-to-Cell Transfer and Seeding in Grafted Dopaminergic Neurons In Vivo , 2012, PloS one.
[21] Z. Zhou,et al. Hydrogen-bonding networks and RNA bases revealed by cryo electron microscopy suggest a triggering mechanism for calcium switches , 2011, Proceedings of the National Academy of Sciences.
[22] Jacqueline Cloos,et al. Cell sensitivity assays: the MTT assay. , 2011, Methods in molecular biology.
[23] Jens Meiler,et al. ROSETTA3: an object-oriented software suite for the simulation and design of macromolecules. , 2011, Methods in enzymology.
[24] Xing Zhang,et al. 3.3 Å Cryo-EM Structure of a Nonenveloped Virus Reveals a Priming Mechanism for Cell Entry , 2010, Cell.
[25] Randy J. Read,et al. Acta Crystallographica Section D Biological , 2003 .
[26] Henning Stahlberg,et al. The fold of α-synuclein fibrils , 2008, Proceedings of the National Academy of Sciences.
[27] A. Brunger. Version 1.2 of the Crystallography and NMR system , 2007, Nature Protocols.
[28] Anchi Cheng,et al. Automated molecular microscopy: the new Leginon system. , 2005, Journal of structural biology.
[29] J. Hoenicka,et al. The new mutation, E46K, of α‐synuclein causes parkinson and Lewy body dementia , 2004, Annals of neurology.
[30] R. Henderson,et al. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. , 2003, Journal of molecular biology.
[31] Y. Fujiyoshi,et al. Structure and gating mechanism of the acetylcholine receptor pore , 2003, Nature.
[32] Nancy A. Jenkins,et al. Human α-synuclein-harboring familial Parkinson's disease-linked Ala-53 → Thr mutation causes neurodegenerative disease with α-synuclein aggregation in transgenic mice , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[33] D. Price,et al. Human alpha-synuclein-harboring familial Parkinson's disease-linked Ala-53 --> Thr mutation causes neurodegenerative disease with alpha-synuclein aggregation in transgenic mice. , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[34] Susan E Daniel,et al. Characterisation of isolated α-synuclein filaments from substantia nigra of Parkinson's disease brain , 2000, Neuroscience Letters.
[35] W Chiu,et al. EMAN: semiautomated software for high-resolution single-particle reconstructions. , 1999, Journal of structural biology.
[36] Nigel J. Cairns,et al. Filamentous α-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies , 1998, Neuroscience Letters.
[37] R. Crowther,et al. α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with Lewy bodies , 1998 .
[38] R A Crowther,et al. alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[39] H. Wolfson,et al. Shape complementarity at protein–protein interfaces , 1994, Biopolymers.