Evidence map›Paper›PMID 22949111›Full record

ReviewAdvances in experimental medicine and biology2012

Death by caspase dimerization.

Sarah H MacKenzie, A Clay Clark

Open access · greenAbstract readReview
In one paragraph

Review in Advances in experimental medicine and biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
19.4field-weighted citation impact, top 1% of its field
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

54 citing papers in PubMed, 98 citations in OpenAlex.

  1. Article
  2. Role of oxeiptosis in disease mechanisms and therapeutic opportunities.Apoptosis : an international journal on programmed cell death · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Microorganisms · 2023
    Review
  7. Article
  8. Sequential unfolding mechanisms of monomeric caspases.bioRxiv : the preprint server for biology · 2023
    Article
  9. Review
  10. Article
  11. Evolution of the folding landscape of effector caspases.The Journal of biological chemistry · 2021
    Article
  12. Small Molecules Targeting Programmed Cell Death in Breast Cancer Cells.International journal of molecular sciences · 2021
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Cardioprotective Effect of (Cardiovascular therapeutics · 2020
    Article
  19. Article
  20. 7-3 Biotech · 2019
    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

2 authors at 1 institution in 1 country.

Sarah H MacKenzieDepartment of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina, USA.
A Clay Clark
North Carolina State University · US

Funding

Dimerization mechanisms of two procaspase subfamiliesR01GM065970 · NIGMS · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI CLARK, ALLAN CLAY · 2003 to 2012
$2.4M
NIGMS NIH HHS GM 065970NIGMS NIH HHS R01 GM065970
6 · The paper itself

Abstract

Controlled cell death, or apoptosis, occurs in response to many different environmental stimuli. The apoptotic cascade that occurs within the cell in response to these cues leads to morphological and biochemical changes that trigger the dismantling and packaging of the cell. Caspases are a family of cysteine-dependent aspartate-directed proteases that play an integral role in the cascade that leads to apoptosis. Caspases are grouped as either initiators or effectors of apoptosis, depending on where they enter the cell death process. Prior to activation, initiator caspases are present as monomers that must dimerize for full activation whereas effector caspases are present as dimeric zymogens that must be processed for full activation. The stability of the dimer may be due predominately to the interactions in the dimer interface as each caspase has unique properties in this region that lend to its specific mode of activation. Moreover, dimerization is responsible for active site formation because both monomers contribute residues that enable the formation of a fully functional active site. Overall, dimerization plays a key role in the ability of caspases to form fully functional proteases.

Indexed as

Amino Acid SequenceApoptosisCaspasesCatalytic DomainDimerizationEnzyme ActivationEnzyme PrecursorsHumansIsoenzymesModels, MolecularMolecular Sequence DataProtein ConformationProtein StabilitySequence AlignmentSequence Homology, Amino AcidCaspasesEnzyme PrecursorsIsoenzymes

Identifiers

PMID22949111
PMCPMC3877935
OpenAlexW2166356964

What OpenQuestion holds

Textmetadata
LicenceTDM
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.