(Q74451974)

English

Dipolar recoupling NMR of biomolecular self-assemblies: determining inter- and intrastrand distances in fibrilized Alzheimer's beta-amyloid peptide

scientific article published on 01 December 1998

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scholarly article

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10 November 2019

Dipolar recoupling NMR of biomolecular self-assemblies: determining inter- and intrastrand distances in fibrilized Alzheimer's beta-amyloid peptide (English)

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10023844%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

Tammie L. Benzinger

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ORCID Public Data File 2021

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D M Gregory

1

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10 November 2019

T L Benzinger

2

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10 November 2019

T S Burkoth

3

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10 November 2019

H Miller-Auer

4

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10 November 2019

D G Lynn

5

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10 November 2019

S C Meredith

6

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10 November 2019

R E Botto

7

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10 November 2019

publication date

1 December 1998

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10 November 2019

Solid State Nuclear Magnetic Resonance

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10 November 2019

13

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10 November 2019

3

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10 November 2019

149-166

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10 November 2019

High-resolution NMR of biological solids

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An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: application of solid-state NMR to the determination of protein secondary structure.

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Rotational resonance in solid state NMR

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Amyloid deposition as the central event in the aetiology of Alzheimer's disease

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Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein

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Fibril formation by primate, rodent, and Dutch-hemorrhagic analogues of Alzheimer amyloid beta-protein

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Proton-Enhanced Dilute Spins in Solid

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Propagating structure of Alzheimer's beta-amyloid(10-35) is parallel beta-sheet with residues in exact register

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In vitro formation of amyloid fibrils from two synthetic peptides of different lengths homologous to Alzheimer's disease beta-protein

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Ten to fourteen residue peptides of Alzheimer's disease protein are sufficient for amyloid fibril formation and its characteristic x-ray diffraction pattern

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Molecular determinants of amyloid deposition in Alzheimer's disease: conformational studies of synthetic beta-protein fragments.

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The alpha-helical to beta-strand transition in the amino-terminal fragment of the amyloid beta-peptide modulates amyloid formation

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Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer's disease beta A4 peptides

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7 January 2021

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Point substitution in the central hydrophobic cluster of a human beta-amyloid congener disrupts peptide folding and abolishes plaque competence

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Identifiers

10.1016/S0926-2040(98)00086-1

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10023844%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

PubMed publication ID

1 reference

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PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10023844%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

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