Evidence map›Paper›PMID 14634622›Full record

ReviewOncogene2003

Regulation of apoptosis by endoplasmic reticulum pathways.

David G Breckenridge, Marc Germain, Jaigi P Mathai, Mai Nguyen, Gordon C Shore

Abstract readReview
PubMed Publisher
In one paragraph

Review in Oncogene, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 247 papers.

0numbers the graph read from it
0cells of the map it votes in
247citing 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

247 citing papers in PubMed.

  1. Article
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  9. Review
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  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

187 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

5 authors.

David G BreckenridgeDepartment of Biochemistry, McIntyre Medical Sciences Building, McGill University, Montreal, Quebec, Canada H3G 1Y6.
Marc Germain
Jaigi P Mathai
Mai Nguyen
Gordon C Shore

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Apoptotic programmed cell death pathways are activated by a diverse array of cell extrinsic and intrinsic signals, most of which are ultimately coupled to the activation of effector caspases. In many instances, this involves an obligate propagation through mitochondria, causing egress of critical proapoptotic regulators to the cytosol. Central to the regulation of the mitochondrial checkpoint is a complex three-way interplay between members of the BCL-2 family, which are comprised of an antiapoptotic subgroup including BCL-2 itself, and the proapoptotic BAX,BAK and BH3-domain-only subgroups. Constituents of all three of these BCL-2 classes, however, also converge on the endoplasmic reticulum (ER), an organelle whose critical contributions to apoptosis is only now becoming apparent. In addition to propagating death-inducing stress signals itself, the ER also contributes in a fundamental way to Fas-mediated apoptosis and to p53-dependent pathways resulting from DNA damage and oncogene expression. Mobilization of ER calcium stores can initiate the activation of cytoplasmic death pathways as well as sensitize mitochondria to direct proapoptotic stimuli. Additionally, the existence of BCL-2-regulated initiator procaspase activation complexes at the ER membrane has also been described. Here, we review the potential underlying mechanisms involved in these events and discuss pathways for ER-mitochondrial crosstalk pertinent to a number of cell death stimuli.

Indexed as

ApoptosisAmyloid beta-Protein PrecursorAnimalsbcl-2-Associated X Proteinbcl-2 Homologous Antagonist-Killer ProteinCalciumCaspasesDNA-Binding ProteinsEndoplasmic ReticulumHumansMembrane ProteinsMitochondriaPeptide FragmentsProto-Oncogene ProteinsProto-Oncogene Proteins c-bcl-2Sterol Regulatory Element Binding Protein 2Amyloid beta-Protein PrecursorBAK1 protein, humanBax protein (53-86)BAX protein, humanBCAP31 protein, humanbcl-2-Associated X Proteinbcl-2 Homologous Antagonist-Killer ProteinCalciumCaspasesDNA-Binding ProteinsMembrane ProteinsPeptide FragmentsProto-Oncogene ProteinsProto-Oncogene Proteins c-bcl-2SREBF2 protein, humanSterol Regulatory Element Binding Protein 2Transcription Factors

Identifiers

PMID14634622

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.