Evidence map›Paper›PMID 30737281›Full record

ArticleThe Journal of biological chemistry2019

Solid-state NMR reveals a comprehensive view of the dynamics of the flexible, disordered N-terminal domain of amyloid-β fibrils.

Dan Fai Au, Dmitry Ostrovsky, Riqiang Fu, Liliya Vugmeyster

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Trial
  2. Review
  3. Article
  4. Investigation of biomolecular dynamics by sensitivity-enhancedJournal of magnetic resonance open · 2024
    Article
  5. Article
  6. Article
  7. Effect of Cross-Seeding of Wild-Type Amyloid-βThe journal of physical chemistry. B · 2023
    Article
  8. Article
  9. Article
  10. Deuteron rotating frame relaxation for the detection of slow motions in rotating solids.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2022
    Article
  11. The N-Terminal Domain of AβThe journal of physical chemistry. B · 2022
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Simple Selection Procedure to Distinguish between Static and Flexible Loops.International journal of molecular sciences · 2020
    Article
  19. Article
  20. 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

4 authors.

Dan Fai AuFrom the Department of Chemistry, University of Colorado, Denver, Colorado 80204.
Dmitry OstrovskyDepartment of Mathematics, University of Colorado, Denver, Colorado 80204.
Riqiang FuNational High Field Magnetic Laboratory, Tallahassee, Florida 32310.
Liliya VugmeysterFrom the Department of Chemistry, University of Colorado, Denver, Colorado 80204. Electronic address: liliya.vugmeyster@ucdenver.edu.

Funding

Variant-specific dynamics of amyloid-b fibrilsR15GM111681 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI VUGMEYSTER, LILIYA · 2014 to 2021
$1.3M
NIGMS NIH HHS R15 GM111681
6 · The paper itself

Abstract

Amyloid fibril deposits observed in Alzheimer's disease comprise amyloid-β (Aβ) protein possessing a structured hydrophobic core and a disordered N-terminal domain (residues 1-16). The internal flexibility of the disordered domain is likely essential for Aβ aggregation. Here, we used

Indexed as

Molecular Dynamics SimulationAmyloid beta-PeptidesHumansNuclear Magnetic Resonance, BiomolecularPeptide FragmentsProtein DomainsZincAmyloid beta-Peptidesamyloid beta-protein (1-42)Peptide FragmentsZincamyloidfibrilintrinsically disordered proteinneurodegenerationnuclear magnetic resonance (NMR)protein dynamicsprotein misfoldingR1ρ relaxationsolid state NMRzinc

Identifiers

PMID30737281
PMCPMC6463690

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Registered trials

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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.