Evidence map›Paper›PMID 19843697›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Comparison of Alzheimer Abeta(1-40) and Abeta(1-42) amyloid fibrils reveals similar protofilament structures.

Matthias Schmidt, Carsten Sachse, Walter Richter, Chen Xu, Marcus Fändrich, Nikolaus Grigorieff

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.

0numbers the graph read from it
0cells of the map it votes in
121citing papers in PubMed
9.1field-weighted citation impact, top 2% of its field
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

121 citing papers in PubMed, 266 citations in OpenAlex.

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  9. Lateral Piezoelectricity of Alzheimer's Aβ Aggregates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
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  19. Targeting NLRP3-Mediated Neuroinflammation in Alzheimer's Disease Treatment.International journal of molecular sciences · 2022
    Review
  20. Article

61 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 4 institutions in 2 countries.

Matthias SchmidtRosenstiel Basic Medical Sciences Research Center and Howard Hughes Medical Institute, Brandeis University, MS 029, Waltham, MA 02454-9110, USA.
Carsten Sachse
Walter Richter
Chen Xu
Marcus Fändrich
Nikolaus Grigorieff
Martin Luther University Halle-Wittenberg · DEBrandeis University · USFriedrich Schiller University Jena · DEMax Planck Research Unit for Enzymology of Protein Folding · DE

Funding

Single particle reconstructionP01GM062580 · NIGMS · HARVARD MEDICAL SCHOOL · PI HARRISON, STEPHEN COPLAN · 2001 to 2016
$23.7M
NIGMS NIH HHS 1 P01 GM-62580NIGMS NIH HHS P01 GM062580
6 · The paper itself

Abstract

We performed mass-per-length (MPL) measurements and electron cryomicroscopy (cryo-EM) with 3D reconstruction on an Abeta(1-42) amyloid fibril morphology formed under physiological pH conditions. The data show that the examined Abeta(1-42) fibril morphology has only one protofilament, although two protofilaments were observed with a previously studied Abeta(1-40) fibril. The latter fibril was resolved at 8 A resolution showing pairs of beta-sheets at the cores of the two protofilaments making up a fibril. Detailed comparison of the Abeta(1-42) and Abeta(1-40) fibril structures reveals that they share an axial twofold symmetry and a similar protofilament structure. Furthermore, the MPL data indicate that the protofilaments of the examined Abeta(1-40) and Abeta(1-42) fibrils have the same number of Abeta molecules per cross-beta repeat. Based on this data and the previously studied Abeta(1-40) fibril structure, we describe a model for the arrangement of peptides within the Abeta(1-42) fibril.

Indexed as

Protein Structure, TertiaryAlzheimer DiseaseAmyloidAmyloid beta-PeptidesCryoelectron MicroscopyHydrogen-Ion ConcentrationImage Processing, Computer-AssistedMicroscopy, Electron, TransmissionModels, MolecularMolecular Sequence DataPeptide FragmentsSpectroscopy, Fourier Transform InfraredAmyloidAmyloid beta-Peptidesamyloid beta-protein (1-40)amyloid beta-protein (1-42)Peptide Fragments

Identifiers

PMID19843697
PMCPMC2764733
OpenAlexW1980709154

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.