Evidence map›Paper›PMID 28823106›Full record

ReviewBiophysical reviews2017

Mitochondrial outer membrane permeabilization: a focus on the role of mitochondrial membrane structural organization.

Siti Haji Suhaili, Hamed Karimian, Matthew Stellato, Tzong-Hsien Lee, Marie-Isabel Aguilar

Abstract readReview
In one paragraph

Review in Biophysical reviews, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
–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

60 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Article
  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

5 authors.

Siti Haji SuhailiBiomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Wellington Rd, Clayton, VIC, 3800, Australia.
Hamed KarimianBiomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Wellington Rd, Clayton, VIC, 3800, Australia.
Matthew StellatoBiomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Wellington Rd, Clayton, VIC, 3800, Australia.
Tzong-Hsien LeeBiomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Wellington Rd, Clayton, VIC, 3800, Australia.
Marie-Isabel AguilarBiomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Wellington Rd, Clayton, VIC, 3800, Australia. mibel.aguilar@monash.edu.

Funding

National Health and Medical Research Council ID#1084648
6 · The paper itself

Abstract

Apoptosis is important in regulating cell death turnover and is mediated by the intrinsic and death receptor-based extrinsic pathways which converge at the mitochondrial outer membrane (MOM) leading to mitochondrial outer membrane permeabilization (MOMP). MOMP results in the release of apoptotic proteins that further activate the downstream pathway of apoptosis. Thus, tight regulation of MOMP is crucial in controlling apoptosis, and a lack of control may lead to tissue and organ malformation and the development of cancers. Despite a growing number of studies focusing on the structure and activity of the proteins involved in mediating MOMP, such as the Bcl-2 family proteins, the mechanism of MOMP is not well understood. In particular, the crucial role of the various structural properties and changes in lipid components of the MOM in mediating the recruitment and activation of different Bcl-2 proteins remains poorly understood. Furthermore, the factors that control the changes in mitochondrial membrane integrity from the initiation to the final disruption of MOM have yet to be clearly defined. In this review, we provide an overview of studies that focus on the mitochondrial membrane with a biophysical analysis of the interactions of the Bcl-2 proteins with the mitochondrial membrane.

Indexed as

ApoptosisBcl-2 proteinsMembrane interactionsMitochondriaMitochondrial outer membrane permeabilization (MOMP)

Identifiers

PMID28823106
PMCPMC5578938

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.