Evidence map›Paper›PMID 22837695›Full record

ReviewInternational journal of molecular sciences2012

The toxicity of amyloid β oligomers.

Li Na Zhao, Hon Wai Long, Yuguang Mu, Lock Yue Chew

Registry-linked trialOpen access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT04229186 (Pilot Study About Extra Virgin Oil "Coratina"), which is not on this map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
5.6field-weighted citation impact, top 3% 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.

NCT04229186 naunknown statusnot on this mapstarted 2020, after this paper: background citation

Pilot Study About Extra Virgin Oil "Coratina" (Evoo-c) in Mild Cognitive Impairment (MCI) and Alzheimer's Disease (AD) Patients (EVOO-c in MCI/AD)

TypeinterventionalSponsorUniversity of Bari Aldo MoroRan2020 to 2022Enrolled24ConditionsNeurodegenerative DiseasesArmsEVOO-C, ROO
3 · Its place in the literature

Who cites it

53 citing papers in PubMed, 147 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. A reaction-diffusion model of spatial propagation of AJournal of mathematical biology · 2021
    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 at 1 institution in 1 country.

Li Na ZhaoSchool of Physical and Mathematical Sciences, Nanyang Technological University, 21 Nanyang Link, 637731, Singapore.
Hon Wai LongSchool of Physical and Mathematical Sciences, Nanyang Technological University, 21 Nanyang Link, 637731, Singapore.
Yuguang MuSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551, Singapore.ORCID 0000-0002-2499-026X
Lock Yue ChewSchool of Physical and Mathematical Sciences, Nanyang Technological University, 21 Nanyang Link, 637731, Singapore.ORCID 0000-0003-1366-8205
Nanyang Technological University · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this review, we elucidate the mechanisms of Aβ oligomer toxicity which may contribute to Alzheimer's disease (AD). In particular, we discuss on the interaction of Aβ oligomers with the membrane through the process of adsorption and insertion. Such interaction gives rises to phase transitions in the sub-structures of the Aβ peptide from α-helical to β-sheet structure. By means of a coarse-grained model, we exhibit the tendency of β-sheet structures to aggregate, thus providing further insights to the process of membrane induced aggregation. We show that the aggregated oligomer causes membrane invagination, which is a precursor to the formation of pore structures and ion channels. Other pathological progressions to AD due to Aβ oligomers are also covered, such as their interaction with the membrane receptors, and their direct versus indirect effects on oxidative stress and intraneuronal accumulation. We further illustrate that the molecule curcumin is a potential Aβ toxicity inhibitor as a β-sheet breaker by having a high propensity to interact with certain Aβ residues without binding to them. The comprehensive understanding gained from these current researches on the various toxicity mechanisms show promises in the provision of better therapeutics and treatment strategies in the near future.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAnti-Inflammatory Agents, Non-SteroidalCell MembraneCurcuminProtein Aggregation, PathologicalAnimalsHumansProtein Structure, SecondaryAmyloid beta-PeptidesAnti-Inflammatory Agents, Non-SteroidalCurcuminAlzheimer’s diseaseamyloid β oligomer toxicity mechanismamyloid β peptidecurcuminmolecular dynamics simulation

Identifiers

PMID22837695
PMCPMC3397527
OpenAlexW2110165876

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

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.