Evidence map›Paper›PMID 36070019›Full record

ArticleWorld journal of microbiology & biotechnology2022

Molecular study on recombinant cold-adapted, detergent- and alkali stable esterase (EstRag) from Lysinibacillus sp.: a member of family VI.

Amira A Matrawy, Ahmed I Khalil, Amira M Embaby

Open access · hybridAbstract read
In one paragraph

Article in World journal of microbiology & biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

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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.

Amira A MatrawyEnvironmental Studies Department, Institute of Graduate Studies and Research, Alexandria University, 163 Horreya Avenue, P.O. Box 832, Chatby, 21526, Alexandria, Egypt.
Ahmed I KhalilEnvironmental Studies Department, Institute of Graduate Studies and Research, Alexandria University, 163 Horreya Avenue, P.O. Box 832, Chatby, 21526, Alexandria, Egypt.
Amira M EmbabyBiotechnology Department, Institute of Graduate Studies and Research, Alexandria University, 163 Horreya Avenue, P.O. Box 832, Chatby, 21526, Alexandria, Egypt. amira.embaby@alexu.edu.eg.ORCID http://orcid.org/0000-0001-8068-4200
Alexandria University · EG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cold-adapted esterases have potential industrial applications. To fulfil the global continuous demand for these enzymes, a cold-adapted esterase member of family VI from Lysinibacillus sp. YS11 was cloned on pET-28b (+) vector and expressed in E. coli BL21(DE3) Rosetta cells for the first time. The open reading frame (654 bp: GenBank MT120818.1) encodes a polypeptide (designated EstRag: 217 amino acid residues). EstRag amino acid sequence has conserved esterase signature motifs: pentapeptide (GFSQG) and catalytic triad Ser

Indexed as

BacillaceaeEsterasesAlkaliesCold TemperatureDetergentsEnzyme StabilityEscherichia coliProspective StudiesAlkaliesDetergentsEsterasesCold-adaptedCu2+ resistantDetergent stableFamily VILysinibacillus sp.Recombinant esterase

Identifiers

PMID36070019
PMCPMC9452428
OpenAlexW4294922109

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.