Fibril structure of amyloid-β(1–42) by cryo–electron microscopy

Science

Volumn 358, Issue 6359, 2017, Pages 116-119

  Gremer, Lothar ^a,b   Schölzel, Daniel ^a,b   Schenk, Carla ^a   Reinartz, Elke ^b   Labahn, Jörg ^a,b,c   Ravelli, Raimond B G ^d   Tusche, Markus ^a   Lopez Iglesias, Carmen ^d   Hoyer, Wolfgang ^a,b   Heise, Henrike ^a,b   Willbold, Dieter ^a,b   Schröder, Gunnar F ^a,b  

^a FORSCHUNGSZENTRUM JÜLICH   (Germany)

^b HEINRICH HEINE UNIVERSITY   (Germany)

^c DESY   (Germany)

^d MAASTRICHT UNIVERSITY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

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

AGGREGATE; BRAIN; ELECTRON MICROSCOPY; HYDROPHOBICITY; NERVOUS SYSTEM DISORDER; NUCLEAR MAGNETIC RESONANCE; PROTEIN; SOLVENT; TOPOLOGY;

AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CARBOXY TERMINAL SEQUENCE; CRYOELECTRON MICROSCOPY; IMAGE RECONSTRUCTION; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN STRUCTURE; X RAY DIFFRACTION; CHEMISTRY; HUMAN; PROTEIN MULTIMERIZATION; PROTEIN SECONDARY STRUCTURE; ULTRASTRUCTURE;

AMYLOID BETA-PEPTIDES; CRYOELECTRON MICROSCOPY; HUMANS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; X-RAY DIFFRACTION;

EID: 85029058064     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aao2825     Document Type: Article

References (21)

1. R. Riek, D. S. Eisenberg, Nature 539, 227–235 (2016).
2. T. P. Knowles, M. Vendruscolo, C. M. Dobson, Nat. Rev. Mol. Cell Biol. 15, 384–396 (2014).
3. M. Jucker, L. C. Walker, Nature 501, 45–51 (2013).
4. D. J. Selkoe, J. Hardy, EMBO Mol. Med. 8, 595–608 (2016).
5. M. Fändrich, J. Meinhardt, N. Grigorieff, Prion 3, 89–93 (2009).
6. J. X. Lu et al., Cell 154, 1257–1268 (2013).
7. A. K. Paravastu, R. D. Leapman, W. M. Yau, R. Tycko, Proc. Natl. Acad. Sci. U.S.A. 105, 18349–18354 (2008).
8. J. M. Lopez del Amo et al., Angew. Chem. Int. Ed. 51, 6136–6139 (2012).
9. M. Schmidt et al., Proc. Natl. Acad. Sci. U.S.A. 112, 11858–11863 (2015).
10. D. S. Eisenberg, M. R. Sawaya, Annu. Rev. Biochem. 86, 69–95 (2017).
11. M. T. Colvin et al., J. Am. Chem. Soc. 138, 9663–9674 (2016).
12. A. K. Schütz et al., Angew. Chem. Int. Ed. Engl. 54, 331–335 (2015).
13. M. A. Wälti et al., Proc. Natl. Acad. Sci. U.S.A. 113, E4976–E4984 (2016).
14. Y. Xiao et al., Nat. Struct. Mol. Biol. 22, 499–505 (2015).
15. T. Lührs et al., Proc. Natl. Acad. Sci. U.S.A. 102, 17342–17347 (2005).
16. Materials and methods and additional analyses are available as supplementary materials.
17. A. W. P. Fitzpatrick et al., Nature 547, 185–190 (2017).
18. W. Qiang, W. M. Yau, J. X. Lu, J. Collinge, R. Tycko, Nature 541, 217–221 (2017).
19. A. H. DePace, J. S. Weissman, Nat. Struct. Biol. 9, 389–396 (2002).
20. Y. Inoue, A. Kishimoto, J. Hirao, M. Yoshida, H. Taguchi, J. Biol. Chem. 276, 35227–35230 (2001).
21. R. Zhang et al., Proc. Natl. Acad. Sci. U.S.A. 106, 4653–4658 (2009).