Evidence map›Paper›PMID 38827344›Full record

ArticleIranian journal of biotechnology2024

Recombinant Expression and Functional Assessment of Uricase from a Pertinent Origin of the Enzyme,

Mohaddeseh Nasir Shirazi, Sajjad Sarikhan, Hossein Ghafouri, Hamideh Amirmojahedi, Seyed Abolhassan Shahzadeh Fazeli, Mohammad Ali Amoozegar

Abstract read
In one paragraph

Article in Iranian journal of biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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

6 authors.

Mohaddeseh Nasir ShiraziMSc of Cellular and Molecular Biology, University of Science and Culture, Tehran, Iran.
Sajjad SarikhanMolecular Bank, Iranian Biological Resource Center (IBRC), ACECR, Tehran, Iran.
Hossein GhafouriDeprtment of Biology, Faculty of Science, University of Guilan, Rasht, Iran.
Hamideh AmirmojahediMSc of Genetics, Faculty of Biology, University of Kharazmi, Tehran, Iran.
Seyed Abolhassan Shahzadeh FazeliDepartment of Genetics, Reproductive Biomedicine Research Center, Royan Institute for Reproductive Biomedicine, ACECR, Tehran, Iran.
Mohammad Ali AmoozegarDepartment of Microbiology, Faculty of Biology, University of Tehran, Tehran, Iran.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Background: Uricase or urate oxidase, as a therapeutic enzyme, is extensively applied to oxidize accumulated uric acid in the body to soluble form to treat related illnesses. Objectives: This study was conducted with the aim of searching for potential sources of uricase-producing Materials and Methods: Main screening was conducted by cultivation of the strains on a medium enriched with 0.3 percent (w/v) uric acid. The uricase gene from the most potent strain was then recombinantly expressed in Results: Out of the tested strains, only seven showed uricase activity. The highest level of native uricase activity (11.5735 U.mL Conclusions: This enzyme is a promising candidate for further applicable investigations and large-scale production in terms of its large volume of soluble expression and selective competitive activity.

Indexed as

ActinobacteriapET28a+StreptomycesUricase

Identifiers

PMID38827344
PMCPMC11139450

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