Evidence map›Paper›PMID 24974292›Full record

ArticleMethods in enzymology2014

A multipronged approach for compiling a global map of allosteric regulation in the apoptotic caspases.

Kevin Dagbay, Scott J Eron, Banyuhay P Serrano, Elih M Velázquez-Delgado, Yunlong Zhao, Di Lin, Sravanti Vaidya, Jeanne A Hardy

Abstract read
In one paragraph

Article in Methods in enzymology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Evolution of the folding landscape of effector caspases.The Journal of biological chemistry · 2021
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Tunable allosteric library of caspase-3 identifies coupling between conserved water molecules and conformational selection.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. 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

8 authors.

Kevin DagbayDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts, USA.
Scott J EronDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts, USA.
Banyuhay P SerranoDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts, USA.
Elih M Velázquez-DelgadoDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts, USA.
Yunlong ZhaoDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts, USA.
Di LinDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts, USA.
Sravanti VaidyaDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts, USA.
Jeanne A HardyDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts, USA. Electronic address: hardy@chem.umass.edu.

Funding

CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAINING GRANTST32GM008515 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1995 to 2020
$4.3M
Control of Executioner Caspases with an allosteric switch - SupplementR01GM080532 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI HARDY, JEANNE ANN · 2008 to 2022
$3.8M
NIGMS NIH HHS GM80532NIGMS NIH HHS R01 GM080532NIGMS NIH HHS T32 GM008515NIGMS NIH HHS T32 GM08515
6 · The paper itself

Abstract

One of the most promising and as yet underutilized means of regulating protein function is exploitation of allosteric sites. All caspases catalyze the same overall reaction, but they perform different biological roles and are differentially regulated. It is our hypothesis that many allosteric sites exist on various caspases and that understanding both the distinct and overlapping mechanisms by which each caspase can be allosterically controlled should ultimately enable caspase-specific inhibition. Here we describe the ongoing work and methods for compiling a comprehensive map of apoptotic caspase allostery. Central to this approach are the use of (i) the embedded record of naturally evolved allosteric sites that are sensitive to zinc-mediated inhibition, phosphorylation, and other posttranslational modifications, (ii) structural and mutagenic approaches, and (iii) novel binding sites identified by both rationally-designed and screening-derived small-molecule inhibitors.

Indexed as

Allosteric SiteAllosteric RegulationAnimalsCaspase InhibitorsCaspasesCrystallography, X-RayDrug DiscoveryHumansModels, MolecularMutagenesisProtein ConformationProtein Processing, Post-TranslationalCaspase InhibitorsCaspasesAllosteryAnomalous X-ray diffractionApoptosisCaspaseChemical ligandsConformational changeCysteine proteaseExositeInductively coupled plasmaPhosphorylationZinc

Identifiers

PMID24974292
PMCPMC4237280

What OpenQuestion holds

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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.