Evidence map›Paper›PMID 27506787›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Implications for Alzheimer's disease of an atomic resolution structure of amyloid-β(1-42) fibrils.

David S Eisenberg, Michael R Sawaya

Abstract readComment
PubMed Full text at PMC Publisher
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
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  12. Review
  13. How the hydrophobic factor drives protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

David S EisenbergUCLA-DOE Institute, University of California, Los Angeles, CA 90095; Department of Biological Chemistry, University of California, Los Angeles, CA 90095; Howard Hughes Medical Institute, University of California, Los Angeles, CA 90095 david@mbi.ucla.edu.
Michael R SawayaUCLA-DOE Institute, University of California, Los Angeles, CA 90095; Department of Biological Chemistry, University of California, Los Angeles, CA 90095; Howard Hughes Medical Institute, University of California, Los Angeles, CA 90095.

Funding

Structural Biology of Amyloid DiseaseR01AG029430 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI EISENBERG, DAVID · 2007 to 2016
$3.9M
NIA NIH HHS R01 AG029430
6 · The paper itself

Abstract

PubMed holds no abstract for this paper.

Indexed as

Alzheimer DiseaseAmyloidAmyloid beta-PeptidesHumansPeptide FragmentsProtein Structure, SecondaryAmyloidAmyloid beta-PeptidesPeptide Fragments

Identifiers

PMID27506787
PMCPMC5003263

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.