Evidence map›Paper›PMID 25296312›Full record

ArticleBiophysical journal2014

Beta-amyloid oligomers activate apoptotic BAK pore for cytochrome c release.

Jaewook Kim, Yoosoo Yang, Seung Soo Song, Jung-Hyun Na, Kyoung Joon Oh, Cherlhyun Jeong, Yeon Gyu Yu, Yeon-Kyun Shin

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. Toxic mechanisms of amyloid oligomers and therapeutic strategies.Protein science : a publication of the Protein Society · 2026
    Review
  2. Review
  3. Review
  4. Article
  5. Review
  6. Dual Role of NMDAR Containing NR2A and NR2B Subunits in Alzheimer's Disease.International journal of molecular sciences · 2024
    Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. A New Hypothesis for Alzheimer's Disease: The Lipid Invasion Model.Journal of Alzheimer's disease reports · 2022
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Impact of membrane curvature on amyloid aggregation.Biochimica et biophysica acta. Biomembranes · 2018
    Review
  17. The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade.Journal of Alzheimer's disease : JAD · 2018
    Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 2 countries.

Jaewook KimBiomedical Research Institute, Korea Institute of Science and Technology (KIST), Seoul, Republic of Korea.
Yoosoo YangBiomedical Research Institute, Korea Institute of Science and Technology (KIST), Seoul, Republic of Korea.
Seung Soo SongDepartment of Chemistry, Kookmin University, Seoul, Republic of Korea.
Jung-Hyun NaBiomedical Research Institute, Korea Institute of Science and Technology (KIST), Seoul, Republic of Korea; Department of Chemistry, Kookmin University, Seoul, Republic of Korea.
Kyoung Joon OhDepartment of Biochemistry and Molecular Biology, Chicago Medical School, Rosalind Franklin University of Medicine and Science, North Chicago, Illinois.
Cherlhyun JeongBiomedical Research Institute, Korea Institute of Science and Technology (KIST), Seoul, Republic of Korea.
Yeon Gyu YuDepartment of Chemistry, Kookmin University, Seoul, Republic of Korea.
Yeon-Kyun ShinBiomedical Research Institute, Korea Institute of Science and Technology (KIST), Seoul, Republic of Korea; Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa. Electronic address: colishin@iastate.edu.
Kookmin University · KRKorea Institute of Science and Technology · KRIowa State University · USRosalind Franklin University of Medicine and Science · US

Funding

Regulations of SNARE-dependent membrane fusionR01GM051290 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI SHIN, YEON-KYUN · 1999 to 2019
$5.0M
BAX/BAK-Mediated Mitochondrial Outer Membrane Permeabilization in ApoptosisR01GM097508 · NIGMS · ROSALIND FRANKLIN UNIV OF MEDICINE & SCI · PI OH, KYOUNG JOON · 2012 to 2016
$1.5M
NIGMS NIH HHS 5 R01 GM097508NIGMS NIH HHS R01 GM051290NIGMS NIH HHS R01 GM097508
6 · The paper itself

Abstract

In Alzheimer's disease, cytochrome c-dependent apoptosis is a crucial pathway in neuronal cell death. Although beta-amyloid (Aβ) oligomers are known to be the neurotoxins responsible for neuronal cell death, the underlying mechanisms remain largely elusive. Here, we report that the oligomeric form of synthetic Aβ of 42 amino acids elicits death of HT-22 cells. But, when expression of a bcl-2 family protein BAK is suppressed by siRNA, Aβ oligomer-induced cell death was reduced. Furthermore, significant reduction of cytochrome c release was observed with mitochondria isolated from BAK siRNA-treated HT-22 cells. Our in vitro experiments demonstrate that Aβ oligomers bind to BAK on the membrane and induce apoptotic BAK pores and cytochrome c release. Thus, the results suggest that Aβ oligomers function as apoptotic ligands and hijack the intrinsic apoptotic pathway to cause unintended neuronal cell death.

Indexed as

Protein Multimerizationalpha-SynucleinAmyloid beta-PeptidesAnimalsApoptosisbcl-2 Homologous Antagonist-Killer ProteinBH3 Interacting Domain Death Agonist ProteinCell LineCytochromes cMicePeptide FragmentsPorosityProtein Structure, Secondarytau Proteinsalpha-SynucleinAmyloid beta-Peptidesamyloid beta-protein (1-42)bcl-2 Homologous Antagonist-Killer ProteinBH3 Interacting Domain Death Agonist ProteinCytochromes cPeptide Fragmentstau Proteins

Identifiers

PMID25296312
PMCPMC4190645
OpenAlexW2038906428

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.