Evidence map›Paper›PMID 30076665›Full record

ArticleProtein science : a publication of the Protein Society2018

The CaspBase: a curated database for evolutionary biochemical studies of caspase functional divergence and ancestral sequence inference.

Robert D Grinshpon, Anna Williford, James Titus-McQuillan, A Clay Clark

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2018. 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
1.1field-weighted citation impact, top 22% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Enzyme Databases in the Era of Omics and Artificial Intelligence.International journal of molecular sciences · 2023
    Review
  5. Article
  6. Sequential unfolding mechanisms of monomeric caspases.bioRxiv : the preprint server for biology · 2023
    Article
  7. Article
  8. Article
  9. Review
  10. Evolution of the folding landscape of effector caspases.The Journal of biological chemistry · 2021
    Article
  11. Article
  12. Article
  13. Review
  14. 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

4 authors at 2 institutions in 1 country.

Robert D GrinshponDepartment of Molecular and Structural Biochemistry, NC State University, Raleigh, North Carolina, 27608.
Anna WillifordDepartment of Biology, University of Texas at Arlington, Arlington, Texas, 76019.
James Titus-McQuillanDepartment of Biology, University of Texas at Arlington, Arlington, Texas, 76019.
A Clay ClarkDepartment of Biology, University of Texas at Arlington, Arlington, Texas, 76019.
The University of Texas at Arlington · USNorth Central State College · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sequence databases are powerful tools for the contemporary scientists' toolkit. However, most functional annotations in public databases are determined computationally and are not verified by a human expert. While hypotheses generated from computational studies are now amenable to experimentation, the quality of the results relies on the quality of input data. We developed the CaspBase to expedite high-quality dataset compilation of annotated caspase sequences, to maximize phylogenetic signal, and to reduce the noise contributed from public databanks. We describe our methods of curation for the CaspBase and how researchers can acquire sequences from CaspBase.org. Our immediate goal for developing the CaspBase was to optimize the ancestral protein reconstruction (APR) of caspases, and we demonstrate the utility of the CaspBase in APR studies. We also developed the Common Position (CP) system for comparing human caspase family paralogs and suggest the CP system as an update to current reporting methods of caspase amino acid positions. We present a standardized multiple sequence alignment (MSA) for the CP system and show the advantage of using large databases such as the CaspBase in defining structural positions in proteins. Although the results described here pertain to caspase evolution and structure-function studies, the methods can be adapted to any gene family.

Indexed as

CaspasesComputational BiologyDatabases, ProteinHumansModels, MolecularSequence AlignmentSequence Analysis, ProteinCaspasesancestral protein reconstructioncaspasecomputational biologydatabase curationprotein evolutionsequence analysis

Identifiers

PMID30076665
PMCPMC6199153
OpenAlexW2886133886

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.