Evidence map›Paper›PMID 31939065›Full record

ArticleMolecular diversity2021

Targeting the menaquinol binding loop of mycobacterial cytochrome bd oxidase.

Amaravadhi Harikishore, Sherilyn Shi Min Chong, Priya Ragunathan, Roderick W Bates, Gerhard Grüber

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular diversity, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

14 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Carbon Monoxide and Prokaryotic Energy Metabolism.International journal of molecular sciences · 2025
    Review
  3. Article
  4. Target Identification in Anti-Tuberculosis Drug Discovery.International journal of molecular sciences · 2023
    Review
  5. Article
  6. Response ofInternational journal of molecular sciences · 2022
    Article
  7. Bioenergetics and Reactive Nitrogen Species in Bacteria.International journal of molecular sciences · 2022
    Review
  8. Recent Advances in Structural Studies of CytochromeInternational journal of molecular sciences · 2022
    Review
  9. Review
  10. Structure ofeLife · 2021
    Article
  11. Article
  12. Review
  13. Article
  14. Review
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 1 institution in 1 country.

Amaravadhi HarikishoreDivision of Chemistry and Biological Chemistry, School of Physical and Mathematical Sciences, Nanyang Technological University, 21 Nanyang Link, Singapore, 637371, Republic of Singapore.
Sherilyn Shi Min ChongDivision of Chemistry and Biological Chemistry, School of Physical and Mathematical Sciences, Nanyang Technological University, 21 Nanyang Link, Singapore, 637371, Republic of Singapore.
Priya RagunathanSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore, 637551, Republic of Singapore.
Roderick W BatesDivision of Chemistry and Biological Chemistry, School of Physical and Mathematical Sciences, Nanyang Technological University, 21 Nanyang Link, Singapore, 637371, Republic of Singapore.
Gerhard GrüberSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore, 637551, Republic of Singapore. ggrueber@ntu.edu.sg.ORCID http://orcid.org/0000-0002-5730-8319
Nanyang Technological University · SG

Funding

NRF Competitive Research Programme NRF-CRP18-2017-01
6 · The paper itself

Abstract

Mycobacteria have shown enormous resilience to survive and persist by remodeling and altering metabolic requirements. Under stringent conditions or exposure to drugs, mycobacteria have adapted to rescue themselves by shutting down their major metabolic activity and elevate certain survival factor levels and efflux pathways to survive and evade the effects of drug treatments. A fundamental feature in this adaptation is the ability of mycobacteria to vary the enzyme composition of the electron transport chain (ETC), which generates the proton motive force for the synthesis of adenosine triphosphate via oxidative phosphorylation. Mycobacteria harbor dehydrogenases to fuel the ETC, and two terminal respiratory oxidases, an aa3-type cytochrome c oxidase (cyt-bcc-aa3) and a bacterial specific cytochrome bd-type menaquinol oxidase (cyt-bd). In this study, we employed homology modeling and structure-based virtual screening studies to target mycobacteria-specific residues anchoring the b558 menaquinol binding region of Mycobacterium tuberculosis cyt-bd oxidase to obtain a focused library. Furthermore, ATP synthesis inhibition assays were carried out. One of the ligands MQL-H

Indexed as

Adenosine TriphosphateAmino Acid SequenceBinding SitesDrug Evaluation, PreclinicalElectron Transport Complex IVEpitopesLigandsModels, MolecularMycobacterium tuberculosisNaphtholsOxidation-ReductionStructural Homology, ProteinAdenosine TriphosphateElectron Transport Complex IVEpitopesLigandsNaphtholsCytochrome bd oxidaseDrug resistanceMycobacteriaOXPHOS pathwayRespirationTuberculosis

Identifiers

PMID31939065
OpenAlexW3000136817

What OpenQuestion holds

Textmetadata
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.