Evolution of Amyloid: What Normal Protein Folding May Tell Us About Fibrillogenesis and Disease

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1999 Mar 31

PMID 10097040

Citations 133

Authors

P T Lansbury Jr

Affiliations

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References

Harper J, Lansbury Jr P . Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu Rev Biochem. 1997; 66:385-407. DOI: 10.1146/annurev.biochem.66.1.385. View

Chiti F, Webster P, Taddei N, Clark A, Stefani M, Ramponi G . Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc Natl Acad Sci U S A. 1999; 96(7):3590-4. PMC: 22338. DOI: 10.1073/pnas.96.7.3590. View

Chiesa R, Piccardo P, Ghetti B, Harris D . Neurological illness in transgenic mice expressing a prion protein with an insertional mutation. Neuron. 1999; 21(6):1339-51. DOI: 10.1016/s0896-6273(00)80653-4. View

Herzfeld J . Entropically Driven Order in Crowded Solutions: From Liquid Crystals to Cell Biology. Acc Chem Res. 2017; 29(1):31-37. DOI: 10.1021/ar9500224. View

Harper J, Wong S, Lieber C, Lansbury P . Observation of metastable Abeta amyloid protofibrils by atomic force microscopy. Chem Biol. 1997; 4(2):119-25. DOI: 10.1016/s1074-5521(97)90255-6. View

Spillantini M, Murrell J, Goedert M, Farlow M, Klug A, Ghetti B . Mutation in the tau gene in familial multiple system tauopathy with presenile dementia. Proc Natl Acad Sci U S A. 1998; 95(13):7737-41. PMC: 22742. DOI: 10.1073/pnas.95.13.7737. View

Friedhoff P, Schneider A, Mandelkow E, Mandelkow E . Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution. Biochemistry. 1998; 37(28):10223-30. DOI: 10.1021/bi980537d. View

Blake C, Serpell L . Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous beta-sheet helix. Structure. 1996; 4(8):989-98. DOI: 10.1016/s0969-2126(96)00104-9. View

Lashuel H, Lai Z, Kelly J . Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: implications for wild-type, V30M, and L55P amyloid fibril formation. Biochemistry. 1999; 37(51):17851-64. DOI: 10.1021/bi981876+. View

10.

Klement I, Skinner P, Kaytor M, Yi H, Hersch S, Clark H . Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice. Cell. 1998; 95(1):41-53. DOI: 10.1016/s0092-8674(00)81781-x. View

11.

Selkoe D . Alzheimer's disease: genotypes, phenotypes, and treatments. Science. 1997; 275(5300):630-1. DOI: 10.1126/science.275.5300.630. View

12.

Guijarro J, Sunde M, Jones J, Campbell I, Dobson C . Amyloid fibril formation by an SH3 domain. Proc Natl Acad Sci U S A. 1998; 95(8):4224-8. PMC: 22470. DOI: 10.1073/pnas.95.8.4224. View

13.

Polymeropoulos M, Lavedan C, Leroy E, Ide S, Dehejia A, Dutra A . Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science. 1997; 276(5321):2045-7. DOI: 10.1126/science.276.5321.2045. View

14.

Booth D, Sunde M, Bellotti V, Robinson C, Hutchinson W, Fraser P . Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature. 1997; 385(6619):787-93. DOI: 10.1038/385787a0. View

15.

Crawford F, Soto C, Suo Z, Fang C, Parker T, Sawar A . Alzheimer's beta-amyloid vasoactivity: identification of a novel beta-amyloid conformational intermediate. FEBS Lett. 1998; 436(3):445-8. DOI: 10.1016/s0014-5793(98)01170-3. View

16.

Lambert M, Barlow A, Chromy B, Edwards C, Freed R, Liosatos M . Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci U S A. 1998; 95(11):6448-53. PMC: 27787. DOI: 10.1073/pnas.95.11.6448. View

17.

Saudou F, Finkbeiner S, Devys D, Greenberg M . Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell. 1998; 95(1):55-66. DOI: 10.1016/s0092-8674(00)81782-1. View

18.

ASAKURA S . A kinetic study of in vitro polymerization of flagellin. J Mol Biol. 1968; 35(1):237-9. DOI: 10.1016/s0022-2836(68)80051-8. View

19.

Wetzel R . For protein misassembly, it's the "I" decade. Cell. 1996; 86(5):699-702. DOI: 10.1016/s0092-8674(00)80143-9. View

20.

Kruger R, Kuhn W, Muller T, Woitalla D, Graeber M, Kosel S . Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease. Nat Genet. 1998; 18(2):106-8. DOI: 10.1038/ng0298-106. View