Evidence map›Paper›PMID 36884105›Full record

ArticleJournal, genetic engineering & biotechnology2023

Purification, characterization, and enzyme kinetics of a glutathione S transferase from larvae of the camel tick Hyalomma dromedarii.

Hassan M M Masoud, Mohamed S Helmy, Doaa A Darwish, Mahmoud A Ibrahim

Open access · diamondAbstract read
In one paragraph

Article in Journal, genetic engineering & biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 38% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. 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 1 institution in 1 country.

Hassan M M MasoudMolecular Biology Department, National Research Centre, El-Tahrir St, Dokki, Giza, Egypt. hssnmasoud@yahoo.com.ORCID http://orcid.org/0000-0003-4080-767X
Mohamed S HelmyMolecular Biology Department, National Research Centre, El-Tahrir St, Dokki, Giza, Egypt.
Doaa A DarwishMolecular Biology Department, National Research Centre, El-Tahrir St, Dokki, Giza, Egypt.
Mahmoud A IbrahimMolecular Biology Department, National Research Centre, El-Tahrir St, Dokki, Giza, Egypt.
National Research Centre · EG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundGlutathione s-transferases (GSTs) perform an essential role in detoxification of xenobiotics and endogenous compounds via their conjugation to reduce glutathione.

resultsA GST enzyme, designated tick larvae glutathione S transferase (TLGST), was purified from larvae of the camel tick Hyalomma dromedarii via ammonium sulfate precipitation, glutathione-Sepharose affinity column and Sephacryl S-300 chromatography. TLGST-specific activity was found to be 1.56 Umg

conclusionsThese findings will help to understand the various physiologic conditions of ticks and targeting TLGST could be significant tool for development of prospective vaccines against ticks as a bio-control strategy to overcome the rapid grows in pesticide-resistant tick populations.

Indexed as

Camel tickCharacterizationGlutathione-S-transferaseHyalomma dromedariiPurification

Identifiers

PMID36884105
PMCPMC9995618
OpenAlexW4323533722

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.