Evidence map›Paper›PMID 34375097›Full record

ArticleJournal of the American Chemical Society2021

Constraints on the Structure of Fibrils Formed by a Racemic Mixture of Amyloid-β Peptides from Solid-State NMR, Electron Microscopy, and Theory.

Jevgenij A Raskatov, Alejandro R Foley, John M Louis, Wai-Ming Yau, Robert Tycko

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed.

  1. Article
  2. Article
  3. The Rippled Beta-Sheet: An Old Prediction Inspires a New Field.Chembiochem : a European journal of chemical biology · 2026
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Chemical science · 2023
    Article
  9. Article
  10. Article
  11. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Jevgenij A RaskatovDepartment of Chemistry and Biochemistry, University of California, Santa Cruz, California 95064, United States.ORCID 0000-0002-0082-9113
Alejandro R FoleyDepartment of Chemistry and Biochemistry, University of California, Santa Cruz, California 95064, United States.
John M LouisLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, United States.
Wai-Ming YauLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, United States.
Robert TyckoLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, United States.ORCID 0000-0001-7039-7275

Funding

UNIVERSITY OF CALIFORNIA, SANTA CRUZ IMSD PROGRAMR25GM058903 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI JURICA, MELISSA S · 1999 to 2019
$12.2M
Structural Studies of Alzheimer's beta-Amyloid FibrilsZIADK029061 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI TYCKO, ROBERT · 2009 to 2025
$8.4M
Using Chirality to Understand and Control Amyloid Beta Neuronal Uptake and ToxicityR01AG074954 · NIA · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI Jevgenij Raskatov · 2022 to 2026
$1.9M
Structural Studies of Alzheimer's beta-Amyloid FibrilsZ01DK029061 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI TYCKO, ROBERT · 2007 to 2008
$671k
Chiral Inactivation of Amyloid beta Actions in Cytotoxicity, Synaptic transmission and PlasticityR21AG058074 · NIA · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI RASKATOV, JEVGENIJ · 2017 to 2018
$430k
Intramural NIH HHS Z01 DK029061NIA NIH HHS R01 AG074954NIA NIH HHS R21 AG058074NIGMS NIH HHS R25 GM058903
6 · The paper itself

Abstract

Previous studies have shown that racemic mixtures of 40- and 42-residue amyloid-β peptides (d,l-Aβ40 and d,l-Aβ42) form amyloid fibrils with accelerated kinetics and enhanced stability relative to their homochiral counterparts (l-Aβ40 and l-Aβ42), suggesting a "chiral inactivation" approach to abrogating the neurotoxicity of Aβ oligomers (Aβ-CI). Here we report a structural study of d,l-Aβ40 fibrils, using electron microscopy, solid-state nuclear magnetic resonance (NMR), and density functional theory (DFT) calculations. Two- and three-dimensional solid-state NMR spectra indicate molecular conformations in d,l-Aβ40 fibrils that resemble those in known l-Aβ40 fibril structures. However, quantitative measurements of

Indexed as

Density Functional TheoryNuclear Magnetic Resonance, BiomolecularAmyloidAmyloid beta-PeptidesHumansMicroscopy, ElectronAmyloidAmyloid beta-Peptides

Identifiers

PMID34375097
PMCPMC8456612

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.