Evidence map›Paper›PMID 29765111›Full record

ReviewCell death and differentiation2018

New insights into apoptosome structure and function.

Loretta Dorstyn, Christopher W Akey, Sharad Kumar

Abstract readReview
In one paragraph

Review in Cell death and differentiation, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 115 papers.

0numbers the graph read from it
0cells of the map it votes in
115citing 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

115 citing papers in PubMed.

  1. Programmable DNA Assemblies Reconstitute Supramolecular Protein Function.bioRxiv : the preprint server for biology · 2026
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55 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.

Loretta DorstynCenter for Cancer Biology, University of South Australia and SA Pathology, Frome Road, Adelaide, SA, 5001, Australia. Loretta.Dorstyn@unisa.edu.au.
Christopher W AkeyDepartment of Physiology and Biophysics, Boston University School of Medicine, 700 Albany Street, Boston, MA, 02118, USA.
Sharad KumarCenter for Cancer Biology, University of South Australia and SA Pathology, Frome Road, Adelaide, SA, 5001, Australia. Sharad.Kumar@unisa.edu.au.

Funding

STRUCTURAL OF THE APOPTOSOME &ITS ROLE IN CELL DEATHR01GM063834 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI AKEY, CHRISTOPHER W · 2001 to 2015
$3.2M
NIGMS NIH HHS R01 GM063834
6 · The paper itself

Abstract

The apoptosome is a platform that activates apical procaspases in response to intrinsic cell death signals. Biochemical and structural studies in the past two decades have extended our understanding of apoptosome composition and structure, while illuminating the requirements for initiator procaspase activation. A number of studies have now provided high-resolution structures for apoptosomes from C. elegans (CED-4), D. melanogaster (Dark), and H. sapiens (Apaf-1), which define critical protein interfaces, including intra and interdomain interactions. This work also reveals interactions of apoptosomes with their respective initiator caspases, CED-3, Dronc and procaspase-9. Structures of the human apoptosome have defined the requirements for cytochrome c binding, which triggers the conversion of inactive Apaf-1 molecules to an extended, assembly competent state. While recent data have provided a detailed understanding of apoptosome formation and procaspase activation, they also highlight important evolutionary differences with functional implications for caspase activation. Comparison of the CARD/CARD disks and apoptosomes formed by CED-4, Dark and Apaf-1. Cartoons of the active states of the CARD-CARD disks, illustrating the two CED-4 CARD tetrameric ring layers (CED4a and CED4b; top row) and the binding of 8 Dronc CARDs and between 3-4 pc-9 CARDs, to the Dark and Apaf-1 CARD disk respectively (middle and lower rows). Ribbon diagrams of the active CED-4, Dark and Apaf-1 apoptosomes are shown (right column).

Indexed as

AnimalsApoptosomesApoptotic Protease-Activating Factor 1Caenorhabditis elegansCaenorhabditis elegans ProteinsCaspase 9Drosophila melanogasterDrosophila ProteinsHumansAPAF1 protein, humanApoptosomesApoptotic Protease-Activating Factor 1Caenorhabditis elegans ProteinsCASP9 protein, humanCaspase 9Drosophila Proteins

Identifiers

PMID29765111
PMCPMC6030056

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.