Evidence map›Paper›PMID 28135799›Full record

ArticleACS chemical neuroscience2017

Amyloid β Ion Channels in a Membrane Comprising Brain Total Lipid Extracts.

Joon Lee, Young Hun Kim, Fernando T Arce, Alan L Gillman, Hyunbum Jang, Bruce L Kagan, Ruth Nussinov, Jerry Yang, Ratnesh Lal

Open access · greenAbstract read
In one paragraph

Article in ACS chemical neuroscience, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

37 citing papers in PubMed, 79 citations in OpenAlex.

  1. Decoding the mechanisms of amyloid-β in synaptic toxicity.Journal of Alzheimer's disease : JAD · 2026
    Review
  2. Toxic mechanisms of amyloid oligomers and therapeutic strategies.Protein science : a publication of the Protein Society · 2026
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  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

9 authors at 3 institutions in 1 country.

Young Hun Kim
Fernando T ArceDivision of Translational and Regenerative Medicine, Department of Medicine, Department of Biomedical Engineering, University of Arizona , Tucson, Arizona 85721, United States.
Hyunbum JangCancer and Inflammation Program, National Cancer Institute at Frederick, Leidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research, Frederick, Maryland 21702, United States.
Bruce L KaganDepartment of Psychiatry, David Geffen School of Medicine, Semel Institute for Neuroscience and Human Behavior, University of California , Los Angeles, California 90024, United States.
Ruth NussinovCancer and Inflammation Program, National Cancer Institute at Frederick, Leidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research, Frederick, Maryland 21702, United States.
Ratnesh Lal
Leidos (United States) · USUniversity of Arizona · USUniversity of California, Los Angeles · US

Funding

Biomolecular Recognition and Binding MechanismsZIABC010441 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NUSSINOV, RUTH · 2009 to 2025
$9.4M
Amyloid ion channels to design therapeutics for neurodegenerative diseasesR01AG028709 · NIA · UNIVERSITY OF CHICAGO · PI LAL, RATNESHWAR · 2006 to 2018
$3.6M
Method Development: Efficient Computer Vision Based AlgorithmsZIABC010442 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NUSSINOV, RUTH · 2009 to 2025
$2.4M
Equipment Supplement to 'Development of promoters of dendritic spine formation'R01AG053577 · NIA · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI YANG, JERRY · 2016 to 2020
$1.9M
NCI NIH HHS HHSN261200800001ENIA NIH HHS R01 AG028709NIA NIH HHS R01 AG053577
6 · The paper itself

Abstract

Amyloid β (Aβ) oligomers are the predominant toxic species in the pathology of Alzheimer's disease. The prevailing mechanism for toxicity by Aβ oligomers includes ionic homeostasis destabilization in neuronal cells by forming ion channels. These channel structures have been previously studied in model lipid bilayers. In order to gain further insight into the interaction of Aβ oligomers with natural membrane compositions, we have examined the structures and conductivities of Aβ oligomers in a membrane composed of brain total lipid extract (BTLE). We utilized two complementary techniques: atomic force microscopy (AFM) and black lipid membrane (BLM) electrical recording. Our results indicate that Aβ

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesBrainIon ChannelsLipid BilayersMembrane LipidsAmyloid beta-PeptidesIon ChannelsLipid BilayersMembrane LipidsAlzheimer’s diseaseamyloid channelsamyloid−membrane interactionsamyloid β peptidesatomic force microscopyblack lipid membrane electrophysiologybrain total lipid extract

Identifiers

PMID28135799
PMCPMC6197823
OpenAlexW2580174306

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.