Evidence map›Paper›PMID 30792387›Full record

ReviewCell death & disease2019

BCL-2 family isoforms in apoptosis and cancer.

Chloe F A Warren, Michelle W Wong-Brown, Nikola A Bowden

Abstract readReview
In one paragraph

Review in Cell death & disease, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 365 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
365citing papers in PubMed, 1 pooled it
–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

365 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Targeting protein-protein interactions in the BCL-2 family: opportunities for precision oncology.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2026
    Review
  8. Pyroptosis: Molecular mechanisms and function.Journal of physiology and biochemistry · 2026
    Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. HCellular & molecular biology letters · 2026
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

305 more citing papers are in PubMed but not listed here.

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

3 authors.

Chloe F A WarrenFaculty of Health and Medicine, School of Biomedical Sciences and Pharmacy, University of Newcastle, Newcastle, NSW, Australia.
Michelle W Wong-BrownFaculty of Health and Medicine, School of Biomedical Sciences and Pharmacy, University of Newcastle, Newcastle, NSW, Australia.
Nikola A BowdenHunter Medical Research Institute, Newcastle, NSW, Australia. Nikola.bowden@newcastle.edu.au.ORCID http://orcid.org/0000-0002-6047-1694

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The BCl-2 family has long been identified for its role in apoptosis. Following the initial discovery of BCL-2 in the context of B-cell lymphoma in the 1980s, a number of homologous proteins have since been identified. The members of the Bcl-2 family are designated as such due to their BCL-2 homology (BH) domains and involvement in apoptosis regulation. The BH domains facilitate the family members' interactions with each other and can indicate pro- or anti-apoptotic function. Traditionally, these proteins are categorised into one of the three subfamilies; anti-apoptotic, BH3-only (pro-apoptotic), and pore-forming or 'executioner' (pro-apoptotic) proteins. Each of the BH3-only or anti-apoptotic proteins has a distinct pattern of activation, localisation and response to cell death or survival stimuli. All of these can vary across cell or stress types, or developmental stage, and this can cause the delineation of the roles of BCL-2 family members. Added to this complexity is the presence of relatively uncharacterised isoforms of many of the BCL-2 family members. There is a gap in our knowledge regarding the function of BCL-2 family isoforms. BH domain status is not always predictive or indicative of protein function, and several other important sequences, which can contribute to apoptotic activity have been identified. While therapeutic strategies targeting the BCL-2 family are constantly under development, it is imperative that we understand the molecules, which we are attempting to target. This review, discusses our current knowledge of anti-apoptotic BCL-2 family isoforms. With significant improvements in the potential for splicing therapies, it is important that we begin to understand the distinctions of the BCL-2 family, not limited to just the mechanisms of apoptosis control, but in their roles outside of apoptosis.

Indexed as

Amino Acid SequenceAnimalsApoptosisApoptosis Regulatory Proteinsbcl-X ProteinBiomimeticsHumansMembrane ProteinsMitochondrial Membrane Transport ProteinsMyeloid Cell Leukemia Sequence 1 ProteinNeoplasmsProtein IsoformsProto-Oncogene Proteins c-bcl-2Apoptosis Regulatory ProteinsBCL2 protein, humanbcl-X ProteinMCL1 protein, humanMembrane ProteinsMitochondrial Membrane Transport ProteinsMyeloid Cell Leukemia Sequence 1 ProteinProtein IsoformsProto-Oncogene Proteins c-bcl-2RTL10 protein, human

Identifiers

PMID30792387
PMCPMC6384907

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.