Evidence map›Paper›PMID 20586714›Full record

ReviewCurrent medicinal chemistry2010

Medicinal chemistry of ATP synthase: a potential drug target of dietary polyphenols and amphibian antimicrobial peptides.

Zulfiqar Ahmad, Thomas F Laughlin

Open access · bronzeAbstract readReview
In one paragraph

Review in Current medicinal chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
1.1field-weighted citation impact, top 24% 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

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 57 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Advances of medical nanorobots for future cancer treatments.Journal of hematology & oncology · 2023
    Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Safranal and its analogs inhibit Escherichia coli ATP synthase and cell growth.International journal of biological macromolecules · 2017
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Proteomic screening of molecular targets of crocin.Daru : journal of Faculty of Pharmacy, Tehran University of Medical Sciences · 2014
    Article
  19. Review
  20. Affinity-based target deconvolution of safranal.Daru : journal of Faculty of Pharmacy, Tehran University of Medical Sciences · 2013
    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

2 authors at 1 institution in 1 country.

Zulfiqar AhmadDepartment of Biological Sciences, East Tennessee State University, Johnson City, 37614, USA. ahmadz@etsu.edu
Thomas F Laughlin
East Tennessee State University · US

Funding

Molecular Modulation of Catalytic Sites of Escherichia coli F1Fo ATP SynthaseR15GM085771 · NIGMS · EAST TENNESSEE STATE UNIVERSITY · PI AHMAD, ZULFIQAR · 2009 to 2009
$209k
NIGMS NIH HHS GM085771NIGMS NIH HHS R15 GM085771
6 · The paper itself

Abstract

In this review we discuss the inhibitory effects of dietary polyphenols and amphibian antimicrobial/antitumor peptides on ATP synthase. In the beginning general structural features highlighting catalytic and motor functions of ATP synthase will be described. Some details on the presence of ATP synthase on the surface of several animal cell types, where it is associated with multiple cellular processes making it an interesting drug target with respect to dietary polyphenols and amphibian antimicrobial peptides will also be reviewed. ATP synthase is known to have distinct polyphenol and peptide binding sites at the interface of α/β subunits. Molecular interaction of polyphenols and peptides with ATP synthase at their respective binding sites will be discussed. Binding and inhibition of other proteins or enzymes will also be covered so as to understand the therapeutic roles of both types of molecules. Lastly, the effects of polyphenols and peptides on the inhibition of Escherichia coli cell growth through their action on ATP synthase will also be presented.

Indexed as

Molecular Targeted TherapyAmphibiansAnimalsAnti-Infective AgentsBinding SitesEscherichia coliFlavonoidsHumansMitochondrial Proton-Translocating ATPasesMolecular Sequence DataPeptidesPhenolsPolyphenolsProtein BindingRatsAnti-Infective AgentsF1F0-ATP synthaseFlavonoidsMitochondrial Proton-Translocating ATPasesPeptidesPhenolsPolyphenols

Identifiers

PMID20586714
PMCPMC4734657
OpenAlexW2038593692

What OpenQuestion holds

Textmetadata
LicenceTDM
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.