Interaction between soluble Aβ-(1-40) monomer and Aβ-(1-42) fibrils probed by paramagnetic relaxation enhancement (Q24318268)

identical protein binding

GOA release 2020-03-11

1 reference

The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics

GOA release 2020-03-11

author name string

Takahiro Yamaguchi

series ordinal

1

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Katsumi Matsuzaki

series ordinal

2

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Masaru Hoshino

series ordinal

3

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language of work or name

English

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publication date

18 March 2013

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published in

FEBS Letters

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volume

587

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issue

6

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page(s)

620-4

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cites work

1 reference

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The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease

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Amyloid beta-protein (Abeta)1-40 protects neurons from damage induced by Abeta1-42 in culture and in rat brain

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Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB

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Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism

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A disulfide-linked amyloid-beta peptide dimer forms a protofibril-like oligomer through a distinct pathway from amyloid fibril formation

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Transient formation of intermediate conformational states of amyloid-β peptide revealed by heteronuclear magnetic resonance spectroscopy

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Synthesis, aggregation, neurotoxicity, and secondary structure of various A beta 1-42 mutants of familial Alzheimer's disease at positions 21-23.

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NMRPipe: a multidimensional spectral processing system based on UNIX pipes

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Interaction between A beta(1-42) and A beta(1-40) in Alzheimer's beta-amyloid fibril formation in vitro.

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The ratio of monomeric to aggregated forms of Abeta40 and Abeta42 is an important determinant of amyloid-beta aggregation, fibrillogenesis, and toxicity

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Structural basis for increased toxicity of pathological aβ42:aβ40 ratios in Alzheimer disease

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Ultrasonication-dependent production and breakdown lead to minimum-sized amyloid fibrils.

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Thermodynamics of A beta(1-40) amyloid fibril elongation

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Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrils

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3D structure of Alzheimer's amyloid-beta(1-42) fibrils

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Verification of the C-terminal intramolecular beta-sheet in Abeta42 aggregates using solid-state NMR: implications for potent neurotoxicity through the formation of radicals.

21 January 2018

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Amide solvent protection analysis demonstrates that amyloid-beta(1-40) and amyloid-beta(1-42) form different fibrillar structures under identical conditions

21 January 2018

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A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR

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Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils

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Structural and dynamic features of Alzheimer's Abeta peptide in amyloid fibrils studied by site-directed spin labeling.

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Atomic-resolution dynamics on the surface of amyloid-β protofibrils probed by solution NMR

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Abeta40 protects non-toxic Abeta42 monomer from aggregation

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inferred from DOI database lookup

7 January 2021

based on heuristic

Kinetic analysis of amyloid fibril formation

1 reference

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