Evidence map›Paper›PMID 21954360›Full record

ReviewInternational journal of molecular sciences2011

Reviewing ligand-based rational drug design: the search for an ATP synthase inhibitor.

Chia-Hsien Lee, Hsuan-Cheng Huang, Hsueh-Fen Juan

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2011. 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
–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

11 citing papers in PubMed.

  1. Review
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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

3 authors.

Chia-Hsien LeeGraduate Institute of Biomedical Electronics and Bioinformatics, National Taiwan University, Taipei 106, Taiwan; E-Mail: r99945042@ntu.edu.tw.
Hsuan-Cheng Huang
Hsueh-Fen Juan

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Following major advances in the field of medicinal chemistry, novel drugs can now be designed systematically, instead of relying on old trial and error approaches. Current drug design strategies can be classified as being either ligand- or structure-based depending on the design process. In this paper, by describing the search for an ATP synthase inhibitor, we review two frequently used approaches in ligand-based drug design: The pharmacophore model and the quantitative structure-activity relationship (QSAR) method. Moreover, since ATP synthase ligands are potentially useful drugs in cancer therapy, pharmacophore models were constructed to pave the way for novel inhibitor designs.

Indexed as

Drug DesignLigandsBinding SitesEnzyme InhibitorsHumansHydrophobic and Hydrophilic InteractionsMitochondrial Proton-Translocating ATPasesModels, MolecularProtein BindingProtein SubunitsQuantitative Structure-Activity RelationshipEnzyme InhibitorsLigandsMitochondrial Proton-Translocating ATPasesProtein SubunitsATP synthase ligandspharmacophorequantitative structure-activity relationships

Identifiers

PMID21954360
PMCPMC3179167

What OpenQuestion holds

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LicenceCC BY
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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.