Evidence map›Paper›PMID 27697150›Full record

ArticleeLife2016

A near atomic structure of the active human apoptosome.

Tat Cheung Cheng, Chuan Hong, Ildikó V Akey, Shujun Yuan, Christopher W Akey

Abstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing 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

56 citing papers in PubMed.

  1. Article
  2. Programmable DNA Assemblies Reconstitute Supramolecular Protein Function.bioRxiv : the preprint server for biology · 2026
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  3. Review
  4. TIR-like NADases act in bacterial immunity and the RNA vault.bioRxiv : the preprint server for biology · 2026
    Article
  5. Article
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  8. Article
  9. Article
  10. Article
  11. A structural atlas of death domain fold proteins reveals their versatile roles in biology and function.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Cardiac Tyrosine 97 Phosphorylation of CytochromeInternational journal of molecular sciences · 2025
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Altered conformational dynamics contribute to species-specific effects of cytochrome c mutations on caspase activation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Article
  19. Biomarkers of Response to Venetoclax Therapy in Acute Myeloid Leukemia.International journal of molecular sciences · 2024
    Review
  20. Activation of caspase-9 on the apoptosome as studied by methyl-TROSY NMR.Proceedings of the National Academy of Sciences of the United States of America · 2023
    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.

Tat Cheung ChengDepartment of Physiology and Biophysics, Boston University School of Medicine, Boston, United States.
Chuan HongJanelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States.
Ildikó V AkeyDepartment of Physiology and Biophysics, Boston University School of Medicine, Boston, United States.
Shujun YuanDepartment of Biologics Research - Protein Sciences, U.S. Innovation Center, Bayer Healthcare, San Franciso, United States.
Christopher W AkeyDepartment of Physiology and Biophysics, Boston University School of Medicine, Boston, United States.ORCID 0000-0002-3059-3121

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

In response to cell death signals, an active apoptosome is assembled from Apaf-1 and procaspase-9 (pc-9). Here we report a near atomic structure of the active human apoptosome determined by cryo-electron microscopy. The resulting model gives insights into cytochrome c binding, nucleotide exchange and conformational changes that drive assembly. During activation an acentric disk is formed on the central hub of the apoptosome. This disk contains four Apaf-1/pc-9 CARD pairs arranged in a shallow spiral with the fourth pc-9 CARD at lower occupancy. On average, Apaf-1 CARDs recruit 3 to 5 pc-9 molecules to the apoptosome and one catalytic domain may be parked on the hub, when an odd number of zymogens are bound. This suggests a stoichiometry of one or at most, two pc-9 dimers per active apoptosome. Thus, our structure provides a molecular framework to understand the role of the apoptosome in programmed cell death and disease.

Indexed as

ApoptosomesApoptotic Protease-Activating Factor 1Caspase 9Cryoelectron MicroscopyHumansAPAF1 protein, humanApoptosomesApoptotic Protease-Activating Factor 1Caspase 9apoptosomebiophysicscell biologyhumanprocaspase-9programmed cell deathstructural biology

Identifiers

PMID27697150
PMCPMC5050015

What OpenQuestion holds

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Registered trials

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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.