Evidence map›Paper›PMID 23561537›Full record

ArticleBiophysical journal2013

A tunable, modular approach to fluorescent protease-activated reporters.

Peng Wu, Samantha B Nicholls, Jeanne A Hardy

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Protein Engineering for Spatiotemporally Resolved Cellular Monitoring.Annual review of analytical chemistry (Palo Alto, Calif.) · 2025
    Review
  5. Review
  6. Molecular Engineering ofMolecules (Basel, Switzerland) · 2023
    Article
  7. Article
  8. Article
  9. Tracking exogenous intracellular casp-3 using split GFP.Protein science : a publication of the Protein Society · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. 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

3 authors at 1 institution in 1 country.

Peng WuDepartment of Chemistry, University of Massachusetts Amherst, Amherst, Massachusetts, USA.
Samantha B Nicholls
Jeanne A Hardy
University of Massachusetts Amherst · US

Funding

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 GM080532
6 · The paper itself

Abstract

Proteases are one of the most important and historically utilized classes of drug targets. To effectively interrogate this class of proteins, which encodes nearly 2% of the human proteome, it is necessary to develop effective and cost-efficient methods that report on their activity both in vitro and in vivo. We have developed a robust reporter of caspase proteolytic activity, called caspase-activatable green fluorescent protein (CA-GFP). The caspases play central roles in homeostatic regulation, as they execute programmed cell death, and in drug design, as caspases are involved in diseases ranging from cancer to neurodegeneration. CA-GFP is a genetically encoded dark-to-bright fluorescent reporter of caspase activity in in vitro, cell-based, and animal systems. Based on the CA-GFP platform, we developed reporters that can discriminate the activities of caspase-6 and -7, two highly related proteases. A second series of reporters, activated by human rhinovirus 3C protease, demonstrated that we could alter the specificity of the reporter by reengineering the protease recognition sequence. Finally, we took advantage of the spectrum of known fluorescent proteins to generate green, yellow, cyan, and red reporters, paving the way for multiplex protease monitoring.

Indexed as

Protein EngineeringCaspasesEnzyme AssaysGreen Fluorescent ProteinsHumansModels, MolecularMolecular ProbesProtein Structure, SecondaryProteolysisCaspasesGreen Fluorescent ProteinsMolecular Probes

Identifiers

PMID23561537
PMCPMC3617415
OpenAlexW2091475809

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.