Evidence map›Paper›PMID 23432591›Full record

ReviewCurrent medicinal chemistry2013

ATP synthase: a molecular therapeutic drug target for antimicrobial and antitumor peptides.

Zulfiqar Ahmad, Florence Okafor, Sofiya Azim, Thomas F Laughlin

Abstract readReview
In one paragraph

Review in Current medicinal chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
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

26 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Cell-Wall-Degrading Enzymes-Related Genes Originating fromInternational journal of molecular sciences · 2022
    Article
  7. Article
  8. Comparative Proteomic Analysis ofTurkish journal of pharmaceutical sciences · 2021
    Article
  9. Article
  10. Potential Inhibitory Effect ofAntibiotics (Basel, Switzerland) · 2020
    Article
  11. Article
  12. Article
  13. Proteolytic Control of Lipid Metabolism.ACS chemical biology · 2019
    Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Safranal and its analogs inhibit Escherichia coli ATP synthase and cell growth.International journal of biological macromolecules · 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

4 authors.

Zulfiqar AhmadDepartment of Biological & Environmental Sciences, Alabama A&M University, Normal, AL 35762, USA. Zulfiqar.ahmad@aamu.edu
Florence Okafor
Sofiya Azim
Thomas F Laughlin

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 role of ATP synthase as a molecular drug target for natural and synthetic antimicrobial/ antitumor peptides. We start with an introduction of the universal nature of the ATP synthase enzyme and its role as a biological nanomotor. Significant structural features required for catalytic activity and motor functions of ATP synthase are described. Relevant details regarding the presence of ATP synthase on the surface of several animal cell types, where it is associated with multiple cellular processes making it a potential drug target with respect to antimicrobial peptides and other inhibitors such as dietary polyphenols, is also reviewed. ATP synthase is known to have about twelve discrete inhibitor binding sites including peptides and other inhibitors located at the interface of α/β subunits on the F(1) sector of the enzyme. Molecular interaction of peptides at the β DEELSEED site on ATP synthase is discussed with specific examples. An inhibitory effect of other natural/synthetic inhibitors on ATP is highlighted to explore the therapeutic roles played by peptides and other inhibitors. Lastly, the effect of peptides on the inhibition of the Escherichia coli model system through their action on ATP synthase is presented.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceAnimalsAnti-Infective AgentsAntineoplastic AgentsBacteriaBacterial InfectionsEnzyme InhibitorsFungiHumansModels, MolecularMolecular Sequence DataMolecular Targeted TherapyMycosesNeoplasmsPeptidesAdenosine TriphosphatasesAnti-Infective AgentsAntineoplastic AgentsEnzyme InhibitorsPeptides

Identifiers

PMID23432591
PMCPMC4734648

What OpenQuestion holds

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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.