Evidence map›Paper›PMID 19526294›Full record

ArticleNeurotoxicity research2009

Amyloid-beta-induced ion flux in artificial lipid bilayers and neuronal cells: resolving a controversy.

Ricardo Capone, Felipe Garcia Quiroz, Panchika Prangkio, Inderjeet Saluja, Anna M Sauer, Mahealani R Bautista, Raymond S Turner, Jerry Yang, Michael Mayer

Open access · hybridAbstract read
In one paragraph

Article in Neurotoxicity research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
7.9field-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

59 citing papers in PubMed, 113 citations in OpenAlex.

  1. Toxic mechanisms of amyloid oligomers and therapeutic strategies.Protein science : a publication of the Protein Society · 2026
    Review
  2. Article
  3. Article
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  16. Metal Ion Effects on Aβ and Tau Aggregation.International journal of molecular sciences · 2018
    Review
  17. Article
  18. Small molecule NPT-440-1 inhibits ionic flux through AβNanomedicine : nanotechnology, biology, and medicine · 2016
    Article
  19. Article
  20. Review
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

9 authors at 2 institutions in 1 country.

Ricardo CaponeDepartment of Biomedical Engineering, University of Michigan, 1101 Beal Ave, Ann Arbor, MI 48109-2110, USA.
Felipe Garcia Quiroz
Panchika Prangkio
Inderjeet Saluja
Anna M Sauer
Mahealani R Bautista
Raymond S Turner
Jerry Yang
Michael Mayer
University of Michigan–Ann Arbor · USUniversity of California, San Diego · US

Funding

VIRUS-INDUCED BRAIN PATHOLOGYP50AG005131 · NIA · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BREWER, JAMES B · 1985 to 2018
$55.4M
TELEPHONE COUNSELING INTERVENTION TO PROMOTE CAREGIVER SELF CARE BEHAVIORP50AG008671 · NIA · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI GILMAN, SID · 1989 to 2010
$18.9M
NIA NIH HHS 3P50 AG005131NIA NIH HHS P50 AG005131NIA NIH HHS P50 AG008671
6 · The paper itself

Abstract

Understanding the pathogenicity of amyloid-beta (Abeta) peptides constitutes a major goal in research on Alzheimer's disease (AD). One hypothesis entails that Abeta peptides induce uncontrolled, neurotoxic ion flux through cellular membranes. The exact biophysical mechanism of this ion flux is, however, a subject of an ongoing controversy which has attenuated progress toward understanding the importance of Abeta-induced ion flux in AD. The work presented here addresses two prevalent controversies regarding the nature of transmembrane ion flux induced by Alphabeta peptides. First, the results clarify that Alphabeta can induce stepwise ion flux across planar lipid bilayers as opposed to a gradual increase in transmembrane current; they show that the previously reported gradual thinning of membranes with concomitant increase in transmembrane current arises from residues of the solvent hexafluoroisopropanol, which is commonly used for the preparation of amyloid samples. Second, the results provide additional evidence suggesting that Abeta peptides can induce ion channel-like ion flux in cellular membranes that is independent from the postulated ability of Alphabeta to modulate intrinsic cellular ion channels or transporter proteins.

Indexed as

Amyloid beta-PeptidesAmyloid beta-Protein PrecursorAnimalsBiophysicsCell MembraneCells, CulturedCerebral CortexEmbryo, MammalianFemaleHumansHydrocarbons, FluorinatedIon Channel GatingIonsIon TransportLipid BilayersMaleAmyloid beta-Peptidesamyloid beta-protein (1-40)amyloid beta-protein (1-42)Amyloid beta-Protein PrecursorhexafluoroisopropanolHydrocarbons, FluorinatedIonsLipid BilayersMembranes, ArtificialPeptide FragmentsPresenilin-1Propanols

Identifiers

PMID19526294
PMCPMC2864106
OpenAlexW2105949921

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.