Evidence map›Paper›PMID 27363332›Full record

ArticleBiochemical and biophysical research communications2016

Structural differences between amyloid beta oligomers.

Leonid Breydo, Dmitry Kurouski, Suhail Rasool, Saskia Milton, Jessica W Wu, Vladimir N Uversky, Igor K Lednev, Charles G Glabe

Abstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed, 1 pooled it
–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

35 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
  3. Article
  4. Exploring the AβFrontiers in molecular biosciences · 2024
    Article
  5. Article
  6. Communications chemistry · 2023
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Review
  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

8 authors.

Leonid BreydoDepartment of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, United States; Department of Molecular Medicine and Byrd Alzheimer's Institute, University of South Florida, Tampa, FL 33612, United States. Electronic address: lbreydo@health.usf.edu.
Dmitry KurouskiDepartment of Chemistry, University at Albany, SUNY, 1400 Washington Avenue, Albany, NY 12222, United States.
Suhail RasoolDepartment of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, United States.
Saskia MiltonDepartment of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, United States.
Jessica W WuDepartment of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, United States.
Vladimir N UverskyDepartment of Molecular Medicine and Byrd Alzheimer's Institute, University of South Florida, Tampa, FL 33612, United States; Department of Biological Sciences, Faculty of Sciences, King Abdulaziz University, Jeddah, Saudi Arabia.
Igor K LednevDepartment of Chemistry, University at Albany, SUNY, 1400 Washington Avenue, Albany, NY 12222, United States.
Charles G GlabeDepartment of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, United States; Biochemistry Department, Faculty of Science and Experimental Biochemistry Unit, King Fahd Medical Research Center, King Abdulaziz University, Jeddah, Saudi Arabia.

Funding

TISSUE REPOSITORY COREP01AG000538 · NIA · UNIVERSITY OF CALIFORNIA-IRVINE · PI LAFERLA, FRANK M · 1985 to 2018
$24.8M
Biophysical determination of the underlying cause of α-Syn oligomer toxicityR35GM142869 · NIGMS · TEXAS A&M AGRILIFE RESEARCH · PI KUROUSKI, DMITRY · 2021 to 2025
$1.6M
Structure and conformational diversity of amyloid oligomersR01AG033069 · NIA · UNIVERSITY OF CALIFORNIA-IRVINE · PI GLABE, CHARLES G. · 2010 to 2014
$1.4M
Structural Characterization of Amyloid Fibrils Using Deep UV Raman SpectroscopyR01AG033719 · NIA · STATE UNIVERSITY OF NEW YORK AT ALBANY · PI LEDNEV, IGOR K · 2010 to 2014
$1.0M
NIA NIH HHS P01 AG000538NIA NIH HHS R01 AG033069NIA NIH HHS R01 AG033719NIGMS NIH HHS R35 GM142869
6 · The paper itself

Abstract

In Alzheimer's disease, soluble Aβ oligomers are believed to play important roles in the disease pathogenesis, and their levels correlate with cognitive impairment. We have previously shown that Aβ oligomers can be categorized into multiple structural classes based on their reactivity with conformation-dependent antibodies. In this study, we analyzed the structures of Aβ40 oligomers belonging to two of these classes: fibrillar and prefibrillar oligomers. We found that fibrillar oligomers were similar in structure to fibrils but were less stable towards denaturation while prefibrillar oligomers were found to be partially disordered. These results are consistent with previously proposed structures for both oligomer classes while providing additional structural information.

Indexed as

AmyloidAmyloid beta-PeptidesDimerizationPeptide FragmentsProtein ConformationAmyloidAmyloid beta-Peptidesamyloid beta-protein (1-40)Peptide FragmentsAlzheimer’s diseaseAmyloid betaOligomersProtein aggregation

Identifiers

PMID27363332
PMCPMC11247950

What OpenQuestion holds

Textmetadata
LicenceTDM
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.