Evidence map›Paper›PMID 23713800›Full record

ReviewBritish journal of clinical pharmacology2014

Structure-based drug design of catechol-O-methyltransferase inhibitors for CNS disorders.

Zhiguo Ma, Hongming Liu, Baojian Wu

Open access · bronzeAbstract readReview
In one paragraph

Review in British journal of clinical pharmacology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

30 citing papers in PubMed, 69 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. A large conserved family of small-molecule carboxyl methyltransferases identified from microorganisms.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Methyltransferases: Functions and Applications.Chembiochem : a European journal of chemical biology · 2022
    Review
  16. Discovery of Small Molecules as Membrane-Bound Catechol-Pharmaceuticals (Basel, Switzerland) · 2021
    Article
  17. Inhibition of catechol-Journal of enzyme inhibition and medicinal chemistry · 2021
    Article
  18. Interaction of silver nanoparticles with catecholBiochemistry and biophysics reports · 2021
    Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Zhiguo MaDivision of Pharmaceutics, College of Pharmacy, Jinan University, Guangzhou, Guangdong, China.
Hongming Liu
Baojian Wu
Jinan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Catechol-O-methyltransferase (COMT) is of great importance in pharmacology because it catalyzes the metabolism (methylation) of endogenous and xenobiotic catechols. Moreover, inhibition of COMT is the drug target in the management of central nervous system (CNS) disorders such as Parkinson's disease due to its role in regulation of the dopamine level in the brain. The X-ray crystal structures for COMT have been available since 1994. The active sites for cofactor and substrate/inhibitor binding are well resolved to an atomic level, providing valuable insights into the catalytic mechanisms as well as the role of magnesium ions in catalysis. Determination of how the substrates/inhibitors bind to the protein leads to a structure-based approach that has resulted in potent and selective inhibitors. This review focuses on the design of two types of inhibitors (nitrocatechol-type and bisubstrate inhibitors) for COMT using the protein structures.

Indexed as

Catechol O-Methyltransferase InhibitorsDrug DesignAnimalsBinding SitesCatalytic DomainCatechol O-MethyltransferaseCentral Nervous SystemCentral Nervous System AgentsCentral Nervous System DiseasesEnzyme InhibitorsHumansModels, MolecularProtein ConformationStructure-Activity RelationshipCatechol O-MethyltransferaseCatechol O-Methyltransferase InhibitorsCentral Nervous System AgentsCOMT protein, humanEnzyme Inhibitorscatechol-O-methyltransferaseCOMTcrystal structuredrug discoverydrug metabolism

Identifiers

PMID23713800
PMCPMC3952716
OpenAlexW1796841535

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.