Evidence map›Paper›PMID 37365352›Full record

ArticleInternational microbiology : the official journal of the Spanish Society for Microbiology2024

Characterization of a putative metal-dependent PTP-like phosphatase from Lactobacillus helveticus 2126.

Paul Priyodip, Seetharaman Balaji

Open access · hybridAbstract read
In one paragraph

Article in International microbiology : the official journal of the Spanish Society for Microbiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 97% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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.

Paul PriyodipDepartment of Biotechnology, Manipal Institute of Technology, Manipal Academy of Higher Education, -576104, Manipal, Karnataka, India.
Seetharaman BalajiDepartment of Biotechnology, Manipal Institute of Technology, Manipal Academy of Higher Education, -576104, Manipal, Karnataka, India. s.balaji@manipal.edu.ORCID http://orcid.org/0000-0002-0557-4623
Manipal Academy of Higher Education · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To date, there are very limited reports on sequence analysis and structure-based molecular modeling of phosphatases produced by probiotic bacteria. Therefore, a novel protein tyrosine-like phosphatase was characterized from L. helveticus 2126 in this study. The purified bacterial phosphatase was subjected to mass spectrometric analysis, and the identity of constructed sequence was analyzed using peptide mass fingerprint. The 3-D structure of protein was elucidated using homology modeling, while its stability was assessed using Ramachandran plot, VERIFY 3D, and PROCHECK. The bacterium produced an extracellular phosphatase of zone diameter 15 ± 0.8 mm on screening medium within 24 h of incubation. This bacterial phosphatase was highly specific towards sodium phytate as it yielded the lowest K

Indexed as

Lactobacillus helveticusProtein Tyrosine PhosphatasesAmino Acid SequenceCatalytic DomainMetalsPhosphorylationMetalsProtein Tyrosine PhosphatasesHomology modelingLactobacillus helveticusPhytasePhytateProbioticProtein tyrosine phosphatase

Identifiers

PMID37365352
PMCPMC10830716
OpenAlexW4382139322

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.