Implications for Alzheimer's disease of an atomic resolution structure of amyloid-β(1-42) fibrils

Proceedings of the National Academy of Sciences of the United States of America

Volumn 113, Issue 34, 2016, Pages 9398-9400

  Eisenberg, David S ^a,b,c   Sawaya, Michael R ^a,b,c  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; AMYLOID; AMYLOID BETA PROTEIN; PEPTIDE FRAGMENT;

ALZHEIMER DISEASE; ATOM; CRYOELECTRON MICROSCOPY; HUMAN; NEUROPATHOLOGY; NONHUMAN; NOTE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN POLYMORPHISM; PROTEIN STRUCTURE; CHEMISTRY; PROTEIN SECONDARY STRUCTURE;

ALZHEIMER DISEASE; AMYLOID; AMYLOID BETA-PEPTIDES; HUMANS; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY;

EID: 84983365256     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1610806113     Document Type: Note

References (16)

1. Wälti MA, et al. (2016) Atomic resolution structure of a disease-relevant Aβ(1-42) amyloid fibril. Proc Natl Acad Sci USA 113:E4976-E4984.
2. Paravastu AK, Leapman RD, Yau W-M, Tycko R (2008) Molecular structural basis for polymorphism in Alzheimer's beta-amyloid fibrils. Proc Natl Acad Sci USA 105(47):18349-18354.
3. Colvin MT, et al. (July 14, 2016) Atomic resolution structure of monomorphic Aβ42 amyloid fibrils. J Am Chem Soc, 10.1021/jacs.6b05129.
4. Nelson R, et al. (2005) Structure of the cross-beta spine of amyloid-like fibrils. Nature 435(7043):773-778.
5. Sawaya MR, et al. (2007) Atomic structures of amyloid cross-beta spines reveal varied steric zippers. Nature 447(7143):453-457.
6. Tsemekhman K, Goldschmidt L, Eisenberg D, Baker D (2007) Cooperative hydrogen bonding in amyloid formation. Protein Soc 16(4):761-764.
7. Schmidt M, et al. (2015) Peptide dimer structure in an Aβ(1-42) fibril visualized with cryo-EM. Proc Natl Acad Sci USA 112(38):11858-11863.
8. Petkova AT, et al. (2005) Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 307(5707):262-265.
9. Petkova AT, Yau W-M, Tycko R (2006) Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils. Biochemistry (Mosc) 45(2):498-512.
10. Jucker M, Walker LC (2011) Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders. Ann Neurol 70(4):532-540.
11. Cohen SIA, et al. (2013) Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism. Proc Natl Acad Sci USA 110(24):9758-9763.
12. Roher AE, et al. (1993) Beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: Implications for the pathology of Alzheimer disease. Proc Natl Acad Sci USA 90(22):10836-10840.
13. Jarrett JT, Berger EP, Lansbury PT (1993) The C-terminus of the beta protein is critical for seeding of amyloid formation. Biochemistry 32(18):4693-4697.
14. Katzman R, et al. (1988) Clinical, pathological, and neurochemical changes in dementia: A subgroup with preserved mental status and numerous neocortical plaques. Ann Neurol 23(2):138-144.
15. Arriagada PV, Growdon JH, Hedley-Whyte ET, Hyman BT (1992) Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease. Neurology 42(3 Pt 1):631-639.
16. Li T, et al. (July 4, 2016) The neuritic plaque facilitates pathological conversion of tau in an Alzheimer's disease mouse model. Nat Commun, 10.1038/ncomms12082.