Evidence map›Paper›PMID 22521743›Full record

ArticleGene2012

Molecular characterization of a catalase from Hydra vulgaris.

Bhagirathi Dash, Timothy D Phillips

Open access · greenAbstract read
In one paragraph

Article in Gene, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

11 citing papers in PubMed, 35 citations in OpenAlex.

  1. Adsorption and detoxification of ochratoxin A using hydrophobic bentonite clay.Toxicon : official journal of the International Society on Toxinology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
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  8. Article
  9. Catalase from larvae of the camel tickBiochemistry and biophysics reports · 2015
    Article
  10. Article
  11. 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.

Bhagirathi DashFaculty of Toxicology, Department of Veterinary Integrative Biosciences, College of Veterinary Medicine and Biomedical Sciences, Texas A&M University, College Station, TX 77843, USA.
Timothy D Phillips
Texas A&M University · US

Funding

WASTE SITE ASSESSMENTP42ES004917 · NIEHS · TEXAS A&M UNIVERSITY SYSTEM · PI SAFE, STEPHEN H. · 1989 to 2009
$10.4M
NIEHS NIH HHS P42 ES004917NIEHS NIH HHS P42-ES04917
6 · The paper itself

Abstract

Catalase, an antioxidant and hydroperoxidase enzyme protects the cellular environment from harmful effects of hydrogen peroxide by facilitating its degradation to oxygen and water. Molecular information on a cnidarian catalase and/or peroxidase is, however, limited. In this work an apparent full length cDNA sequence coding for a catalase (HvCatalase) was isolated from Hydra vulgaris using 3'- and 5'- (RLM) RACE approaches. The 1859 bp HvCatalase cDNA included an open reading frame of 1518 bp encoding a putative protein of 505 amino acids with a predicted molecular mass of 57.44 kDa. The deduced amino acid sequence of HvCatalase contained several highly conserved motifs including the heme-ligand signature sequence RLFSYGDTH and the active site signature FXRERIPERVVHAKGXGA. A comparative analysis showed the presence of conserved catalytic amino acids [His(71), Asn(145), and Tyr(354)] in HvCatalase as well. Homology modeling indicated the presence of the conserved features of mammalian catalase fold. Hydrae exposed to thermal, starvation, metal and oxidative stress responded by regulating its catalase mRNA transcription. These results indicated that the HvCatalase gene is involved in the cellular stress response and (anti)oxidative processes triggered by stressor and contaminant exposure.

Indexed as

Amino Acid SequenceAnimalsBase SequenceCatalaseGene Expression Regulation, EnzymologicHot TemperatureHydraMetalsMolecular Sequence DataOpen Reading FramesOxidative StressSequence AlignmentStarvationCatalaseMetals

Identifiers

PMID22521743
PMCPMC3387816
OpenAlexW2066715755

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.