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Differences in the free energies between the excited states of A40 and A42 monomers encode their aggregation propensities.
Proc Natl Acad Sci U S A. 2020 Aug 18;117(33):19926-19937. doi: 10.1073/pnas.2002570117. Epub 2020 Jul 30.
2
Energy landscapes of Aβ monomers are sculpted in accordance with Ostwald's rule of stages.
Sci Adv. 2023 Mar 22;9(12):eadd6921. doi: 10.1126/sciadv.add6921.
3
A new structural model of Alzheimer's Aβ42 fibrils based on electron paramagnetic resonance data and Rosetta modeling.
J Struct Biol. 2016 Apr;194(1):61-7. doi: 10.1016/j.jsb.2016.01.013. Epub 2016 Jan 28.
8
Ionic Strength Modulation of the Free Energy Landscape of Aβ40 Peptide Fibril Formation.
J Am Chem Soc. 2016 Jun 1;138(21):6893-902. doi: 10.1021/jacs.6b04511. Epub 2016 May 23.
10
Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes.
Nature. 2017 Jan 12;541(7636):217-221. doi: 10.1038/nature20814. Epub 2017 Jan 4.

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3
The mechanism of amyloid fibril growth from Φ-value analysis.
Nat Chem. 2025 Mar;17(3):403-411. doi: 10.1038/s41557-024-01712-9. Epub 2025 Jan 16.
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Heterotypic Seeding Generates Mixed Amyloid Polymorphs.
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Molecular Insight into the Effect of HIV-TAT Protein on Amyloid-β Peptides.
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8
Can local heating and molecular crowders disintegrate amyloid aggregates?
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Hairpin trimer transition state of amyloid fibril.
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Helix-to-sheet transition of the Aβ42 peptide revealed using an enhanced sampling strategy and Markov state model.
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1
Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer's brain tissue.
Nat Commun. 2019 Oct 29;10(1):4760. doi: 10.1038/s41467-019-12683-8.
2
Simulation Studies of Amyloidogenic Polypeptides and Their Aggregates.
Chem Rev. 2019 Jun 26;119(12):6956-6993. doi: 10.1021/acs.chemrev.8b00731. Epub 2019 Apr 11.
3
Sequence Effects on Size, Shape, and Structural Heterogeneity in Intrinsically Disordered Proteins.
J Phys Chem B. 2019 Apr 25;123(16):3462-3474. doi: 10.1021/acs.jpcb.9b02575. Epub 2019 Apr 15.
4
The combined force field-sampling problem in simulations of disordered amyloid-β peptides.
J Chem Phys. 2019 Mar 14;150(10):104108. doi: 10.1063/1.5078615.
5
Highly Disordered Amyloid-β Monomer Probed by Single-Molecule FRET and MD Simulation.
Biophys J. 2018 Feb 27;114(4):870-884. doi: 10.1016/j.bpj.2017.12.025.
6
Comparing the Aggregation Free Energy Landscapes of Amyloid Beta(1-42) and Amyloid Beta(1-40).
J Am Chem Soc. 2017 Nov 22;139(46):16666-16676. doi: 10.1021/jacs.7b08089. Epub 2017 Nov 7.
7
Fibril structure of amyloid-β(1-42) by cryo-electron microscopy.
Science. 2017 Oct 6;358(6359):116-119. doi: 10.1126/science.aao2825. Epub 2017 Sep 7.
8
Endocytic vesicle rupture is a conserved mechanism of cellular invasion by amyloid proteins.
Acta Neuropathol. 2017 Oct;134(4):629-653. doi: 10.1007/s00401-017-1722-x. Epub 2017 May 19.
9
The role of histidines in amyloid β fibril assembly.
FEBS Lett. 2017 Apr;591(8):1167-1175. doi: 10.1002/1873-3468.12616. Epub 2017 Apr 3.
10
Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes.
Nature. 2017 Jan 12;541(7636):217-221. doi: 10.1038/nature20814. Epub 2017 Jan 4.

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