Evidence map›Paper›PMID 32993619›Full record

ArticleBMC biotechnology2020

Novel kinase platform for the validation of the anti-tubercular activities of Pelargonium sidoides (Geraniaceae).

V Lukman, S W Odeyemi, R L Roth, L Mbabala, N Tshililo, N M Vlok, M J B Dewar, C P Kenyon

Open access · goldAbstract read
In one paragraph

Article in BMC biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.1field-weighted citation impact, top 46% 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

5 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Chemical Composition and Biological Activities ofMolecules (Basel, Switzerland) · 2025
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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

8 authors at 4 institutions in 1 country.

V LukmanDepartment of Life and Consumer Sciences, College of Agriculture and Environmental Sciences, University of South Africa, Johannesburg, 1709, South Africa.
S W OdeyemiDepartment of Life and Consumer Sciences, College of Agriculture and Environmental Sciences, University of South Africa, Johannesburg, 1709, South Africa.
R L RothCouncil for Scientific and Industrial Research, Pretoria, South Africa.
L MbabalaDST-NRF Centre of Excellence for Biomedical Tuberculosis Research, South African Medical Research Council Centre for Tuberculosis Research, Division of Molecular Biology and Human Genetics, Faculty of Medicine and Health Sciences, Stellenbosch University, Cape Town, 7505, South Africa.
N TshililoDST-NRF Centre of Excellence for Biomedical Tuberculosis Research, South African Medical Research Council Centre for Tuberculosis Research, Division of Molecular Biology and Human Genetics, Faculty of Medicine and Health Sciences, Stellenbosch University, Cape Town, 7505, South Africa.
N M VlokProteomics Spectrometry Unit, Central Analytical Facility, University of Stellenbosch, Private Bag X1, Matieland, Stellenbsoch, 7600, South Africa.
M J B DewarDepartment of Life and Consumer Sciences, College of Agriculture and Environmental Sciences, University of South Africa, Johannesburg, 1709, South Africa.
C P KenyonCouncil for Scientific and Industrial Research, Pretoria, South Africa. kenyon@sun.ac.za.ORCID 0000-0003-1590-7230
South African Medical Research Council · ZAUniversity of South Africa · ZACouncil for Scientific and Industrial Research · ZAStellenbosch University · ZA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundPelargonium sidoides is an important traditional medicine in South Africa with a well-defined history of both traditional and documented use of an aqueous-ethanolic formulation of the roots of P. sidoides (EPs 7630), which is successfully employed for the treatment of respiratory tract infections. There is also historical evidence of use in the treatment of tuberculosis. The aim of this study was to develop a platform of Mycobacterium tuberculosis (Mtb) kinase enzymes that may be used for the identification of therapeutically relevant ethnobotanical extracts that will allow drug target identification, as well as the subsequent isolation of the active compounds.

resultsMtb kinases, Nucleoside diphosphokinase, Homoserine kinase, Acetate kinase, Glycerol kinase, Thiamine monophosphate kinase, Ribokinase, Aspartokinase and Shikimate kinase were cloned, produced in Escherichia coli and characterized. HPLC-based assays were used to determine the enzyme activities and subsequently the inhibitory potentials of varying concentrations of a P. sidoides extract against the produced enzymes. The enzyme activity assays indicated that these enzymes were active at low ATP concentrations. The 50% inhibitory concentration (IC

conclusionThis study suggests P. sidoides is potentially a source of anti-tubercular compounds and the Mtb kinase platform has significant potential as a tool for the subsequent screening of P. sidoides extracts and plant extracts in general, for compound identification and elaboration by selected extract target inhibitor profiling.

Indexed as

Antitubercular AgentsCloning, MolecularEscherichia coliGeraniaceaeMicrobial Sensitivity TestsMycobacterium tuberculosisPelargoniumPhosphotransferasesPlant ExtractsTuberculosisAntitubercular AgentsEPs 7630PhosphotransferasesPlant ExtractsAnti-tubercularKinasesMycobacterium tuberculosisTarget identification

Identifiers

PMID32993619
PMCPMC7523293
OpenAlexW3089923888

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.