Evidence map›Paper›PMID 36310196›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

Solid-State NMR Structure of Amyloid-β Fibrils.

Beat H Meier, Anja Böckmann

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. High-qualitySolid state nuclear magnetic resonance · 2025
    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

2 authors.

Beat H MeierPhysical Chemistry, ETH Zurich, Zurich, Switzerland. beme@ethz.ch.
Anja BöckmannMolecular Microbiology and Structural Biochemistry, Labex Ecofect, Lyon, France. a.bockmann@ibcp.fr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloid fibrils are involved in a number of diseases and notably play a role in neurodegeneration, where they are present in plaques in the brain. Their structure determination might help in finding ways to interfere with their formation, and ultimately prevent disease, by revealing the structure-function relationship and helping to design molecules targeting initial assembly steps and further propagation. Here, we describe the different steps in NMR protocols which allowed the 3D structure determination of amyloid-β fibrils.

Indexed as

AmyloidAmyloid beta-PeptidesBrainMagnetic Resonance ImagingNuclear Magnetic Resonance, BiomolecularAmyloidAmyloid beta-PeptidesAmyloid fibrilSolid-state NMRStructure determination

Identifiers

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.