Evidence map›Paper›PMID 28843272›Full record

ArticleMolecules and cells2017

Inhibition of the DevSR Two-Component System by Overexpression of Mycobacterium tuberculosis PknB in Mycobacterium smegmatis.

Hyun-Jung Bae, Ha-Na Lee, Mi-Na Baek, Eun-Jin Park, Chi-Yong Eom, In-Jeong Ko, Ho-Young Kang, Jeong-Il Oh

Open access · diamondAbstract read
In one paragraph

Article in Molecules and cells, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

11 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Potential therapeutic approaches for a sleeping pathogen: tuberculosis a case for bioinorganic chemistry.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Review
  6. Article
  7. Protein post-translational modifications in bacteria.Nature reviews. Microbiology · 2019
    Review
  8. Article
  9. A Genome-Scale Co-Functional Network ofMolecules and cells · 2019
    Article
  10. Article
  11. Frontiers in microbiology · 2017
    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

8 authors at 3 institutions in 1 country.

Hyun-Jung BaeDepartment of Microbiology, Pusan National University, Busan 46241, Korea.
Ha-Na LeeDepartment of Microbiology, Pusan National University, Busan 46241, Korea.
Mi-Na BaekDepartment of Microbiology, Pusan National University, Busan 46241, Korea.
Eun-Jin ParkDepartment of Microbiology, Pusan National University, Busan 46241, Korea.
Chi-Yong EomKorea Basic Science Institute, Seoul 02855, Korea.
In-Jeong KoKorea Science Academy of KAIST, Busan 47162, Korea.
Ho-Young KangDepartment of Microbiology, Pusan National University, Busan 46241, Korea.
Jeong-Il OhDepartment of Microbiology, Pusan National University, Busan 46241, Korea.
Pusan National University · KRKorea Basic Science Institute · KRKorean Academy of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The DevSR (DosSR) two-component system, which is a major regulatory system involved in oxygen sensing in mycobacteria, plays an important role in hypoxic induction of many genes in mycobacteria. We demonstrated that overexpression of the kinase domain of Mycobacterium tuberculosis (Mtb) PknB inhibited transcriptional activity of the DevR response regulator in Mycobacterium smegmatis and that this inhibitory effect was exerted through phosphorylation of DevR on Thr180 within its DNA-binding domain. Moreover, the purified kinase domain of Mtb PknB significantly phosphorylated RegX3, NarL, KdpE, TrcR, DosR, and MtrA response regulators of Mtb that contain the Thr residues corresponding to Thr180 of DevR in their DNA-binding domains, implying that transcriptional activities of these response regulators might also be inhibited when the kinase domain of PknB is overexpressed.

Indexed as

Bacterial ProteinsCell HypoxiaDNA-Binding ProteinsGene Expression Regulation, BacterialHumansMycobacterium smegmatisMycobacterium tuberculosisOxygenPhosphorylationProtamine KinaseProtein KinasesProtein Serine-Threonine KinasesTuberculosisBacterial ProteinsDevS protein, Mycobacterium tuberculosisDNA-Binding ProteinsDosR protein, Mycobacterium tuberculosisOxygenPknB protein, Mycobacterium tuberculosisProtamine KinaseProtein KinasesProtein Serine-Threonine KinasesDevSRmycobacteriumSer/Thr protein kinasetwo-component system

Identifiers

PMID28843272
PMCPMC5638771
OpenAlexW2912943138

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.