Evidence map›Paper›PMID 27438828›Full record

ReviewInternational journal of molecular sciences2016

Non-Classical Inhibition of Carbonic Anhydrase.

Carrie L Lomelino, Claudiu T Supuran, Robert McKenna

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
7.7field-weighted citation impact, top 2% 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

51 citing papers in PubMed, 126 citations in OpenAlex.

  1. Article
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  11. Unraveling Potential Glyoxalase-I Inhibitors Utilizing Structure-Based Drug Design Techniques.Advances and applications in bioinformatics and chemistry : AABC · 2024
    Article
  12. Article
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  16. Review
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  19. Ibuprofen: a weak inhibitor of carbonic anhydrase II.Acta crystallographica. Section F, Structural biology communications · 2022
    Article
  20. 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

3 authors at 2 institutions in 2 countries.

Carrie L LomelinoDepartment of Biochemistry and Molecular Biology, University of Florida, Gainesville, FL 32611, USA. clomelino@ufl.edu.
Claudiu T SupuranNeurofarba Department, University of Florence, Piazza di San Marco, Firenze 50019, Italy. claudiu.supuran@unifi.it.
Robert McKennaDepartment of Biochemistry and Molecular Biology, University of Florida, Gainesville, FL 32611, USA. rmckenna@ufl.edu.
University of Florida · USUniversity of Florence · IT

Funding

Using social networks to map and evaluate team science across CTSA hubsUL1TR001427 · NCATS · UNIVERSITY OF FLORIDA · PI MITCHELL, DUANE A. · 2015 to 2024
$37.2M
Together: Transforming and Translating Discovery to Improve HealthTL1TR001428 · NCATS · UNIVERSITY OF FLORIDA · PI MCCORMACK, WAYNE T. · 2015 to 2023
$3.9M
NCATS NIH HHS TL1 TR001428NCATS NIH HHS UL1 TR001427
6 · The paper itself

Abstract

Specific isoforms from the carbonic anhydrase (CA) family of zinc metalloenzymes have been associated with a variety of diseases. Isoform-specific carbonic anhydrase inhibitors (CAIs) are therefore a major focus of attention for specific disease treatments. Classical CAIs, primarily sulfonamide-based compounds and their bioisosteres, are examined as antiglaucoma, antiepileptic, antiobesity, antineuropathic pain and anticancer compounds. However, many sulfonamide compounds inhibit all CA isoforms nonspecifically, diluting drug effectiveness and causing undesired side effects due to off-target inhibition. In addition, a small but significant percentage of the general population cannot be treated with sulfonamide-based compounds due to a sulfa allergy. Therefore, CAIs must be developed that are not only isoform specific, but also non-classical, i.e. not based on sulfonamides, sulfamates, or sulfamides. This review covers the classes of non-classical CAIs and the recent advances in the development of isoform-specific inhibitors based on phenols, polyamines, coumarins and their derivatives.

Indexed as

AnimalsCarbonic Anhydrase InhibitorsCarbonic AnhydrasesHumansCarbonic Anhydrase InhibitorsCarbonic Anhydrasescarbonic anhydrasecarboxylatecoumarinnon-classical

Identifiers

PMID27438828
PMCPMC4964523
OpenAlexW2491212689

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.