Evidence map›Paper›PMID 29414778›Full record

ArticleThe Journal of biological chemistry2018

Modifications to a common phosphorylation network provide individualized control in caspases.

Melvin E Thomas, Robert Grinshpon, Paul Swartz, A Clay Clark

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

16 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Evolution of the folding landscape of effector caspases.The Journal of biological chemistry · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Evolution of an allosteric "off switch" in apoptotic caspases.The Journal of biological chemistry · 2018
    Review
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

4 authors at 2 institutions in 1 country.

Melvin E ThomasFrom the Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina 27608 and.
Robert GrinshponFrom the Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina 27608 and.
Paul SwartzFrom the Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina 27608 and.
A Clay Clarkthe Department of Biology, University of Texas, Arlington, Texas 76019 clay.clark@uta.edu.
North Carolina State University · USThe University of Texas at Arlington · 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 R01 GM065970
6 · The paper itself

Abstract

Caspase-3 activation and function have been well-defined during programmed cell death, but caspase activity, at low levels, is also required for developmental processes such as lymphoid proliferation and erythroid differentiation. Post-translational modification of caspase-3 is one method used by cells to fine-tune activity below the threshold required for apoptosis, but the allosteric mechanism that reduces activity is unknown. Phosphorylation of caspase-3 at a conserved allosteric site by p38-MAPK (mitogen-activated protein kinase) promotes survival in human neutrophils, and the modification of the loop is thought to be a key regulator in many developmental processes. We utilized phylogenetic, structural, and biophysical studies to define the interaction networks that facilitate the allosteric mechanism in caspase-3. We show that, within the modified loop, Ser

Indexed as

Caspase 3Evolution, MolecularAllosteric RegulationAmino Acid SubstitutionAnimalsHumansMutation, Missensep38 Mitogen-Activated Protein KinasesPhosphorylationProtein DomainsProtein Structure, SecondaryCASP3 protein, humanCaspase 3p38 Mitogen-Activated Protein Kinasesallosteric regulationapoptosisbiophysicscaspasecomputational biologyfluorescencemolecular dynamicsprotein evolutionX-ray crystallography

Identifiers

PMID29414778
PMCPMC5900778
OpenAlexW2785482385

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.