Biochemical characterization of a glycosyltransferase Gtf3 from

Mahfoud Bakli, Loukmane Karim, Nassima Mokhtari-Soulimane, Hafida Merzouk, Florence Vincent

Open access · greenAbstract read

In one paragraph

Article in 3 Biotech, 2020. 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

0.3field-weighted citation impact, top 42% 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

1 citing paper in PubMed, 6 citations in OpenAlex.

Insertion Mutation ofInfection and drug resistance · 2022
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

5 authors at 2 institutions in 2 countries.

Mahfoud BakliDepartment of Science of Nature and Life, Institute of Science, University Center Belhadj Bouchaib of Ain Temouchent, Po Box 284, 46000 Ain Temouchent, Algeria.ORCID 0000-0002-1427-2985

Loukmane KarimUniversity of Strasbourg, CNRS, Architecture and Reactivity of RNA, UPR9002 Strasbourg, France.

Nassima Mokhtari-SoulimaneLaboratory of Physiology, Pathophysiology and Biochemistry of Nutrition, University Abou-Bekr Belkaid of Tlemcen, Tlemcen, Algeria.

Hafida MerzoukLaboratory of Physiology, Pathophysiology and Biochemistry of Nutrition, University Abou-Bekr Belkaid of Tlemcen, Tlemcen, Algeria.

Florence VincentArchitecture et Fonction des Macromolécules Biologiques, CNRS, Aix-Marseille University, Marseille, France.

Centre National de la Recherche Scientifique · FRUniversity of Abou Bekr Belkaïd · DZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosyltransferases (GTs) are widely present in several organisms. These enzymes specifically transfer sugar moieties to a range of substrates. The processes of bacterial glycosylation of the cell wall and their relations with host-pathogen interactions have been studied extensively, yet the majority of mycobacterial GTs involved in the cell wall synthesis remain poorly characterized. Glycopeptidolipids (GPLs) are major class of glycolipids present on the cell wall of various mycobacterial species. They play an important role in drug resistance and host-pathogen interaction virulence. Gtf3 enzyme performs a key step in the biosynthesis of triglycosylated GPLs. Here, we describe a general procedure to achieve expression, purification, and crystallization of recombinant protein Gtf3 from

Indexed as

Expression and purification of recombinant proteinGlycosyltransferaseMycobacterium smegmatisProtein solubilization

Identifiers

PMID32999813

DOI10.1007/s13205-020-02431-x

PMCPMC7494702

OpenAlexW3085565998

What OpenQuestion holds

Textmetadata

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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.