Evidence map›Paper›PMID 22985956›Full record

ArticleBioorganic & medicinal chemistry2013

Insights towards sulfonamide drug specificity in α-carbonic anhydrases.

Mayank Aggarwal, Bhargav Kondeti, Robert McKenna

Open access · greenAbstract read
In one paragraph

Article in Bioorganic & medicinal chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

44 citing papers in PubMed, 121 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Di-Journal of medicinal chemistry · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Carbonic anhydrase, its inhibitors and vascular function.Frontiers in molecular biosciences · 2024
    Review
  9. 3Journal of enzyme inhibition and medicinal chemistry · 2023
    Article
  10. Aryl derivatives of 3Journal of enzyme inhibition and medicinal chemistry · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. 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 at 1 institution in 1 country.

Mayank AggarwalDepartment of Biochemistry and Molecular Biology, College of Medicine, University of Florida, 1600 SW Archer Rd., PO Box 100245, Gainesville, FL 32610, USA.
Bhargav Kondeti
Robert McKenna
University of Florida · US

Funding

CATALYTIC MECHANISM OF CARBONIC ANHYDRASER01GM025154 · NIGMS · UNIVERSITY OF FLORIDA · PI SILVERMAN, DAVID N · 1985 to 2012
$4.5M
Howard Hughes Medical InstituteNIGMS NIH HHS GM25154NIGMS NIH HHS R01 GM025154
6 · The paper itself

Abstract

Carbonic anhydrases (CAs, EC 4.2.1.1) are a group of metalloenzymes that play important roles in carbon metabolism, pH regulation, CO2 fixation in plants, ion transport etc., and are found in all eukaryotic and many microbial organisms. This family of enzymes catalyzes the interconversion of CO2 and HCO3(-). There are at least 16 different CA isoforms in the alpha structural class (α-CAs) that have been isolated in higher vertebrates, with CA isoform II (CA II) being ubiquitously abundant in all human cell types. CA inhibition has been exploited clinically for decades for various classes of diuretics and anti-glaucoma treatment. The characterization of the overexpression of CA isoform IX (CA IX) in certain tumors has raised interest in CA IX as a diagnostic marker and drug target for aggressive cancers and therefore the development of CA IX specific inhibitors. An important goal in the field of CA is to identify, rationalize, and design potential compounds that will preferentially inhibit CA IX over all other isoforms of CA. The variations in the active sites between isoforms of CA are subtle and this causes non-specific CA inhibition which leads to various side effects. In the case of CA IX inhibition, CA II along with other isoforms of CA provide off-target binding sites which is undesirable for cancer treatment. The focus of this article is on CA IX inhibition and two different structural approaches to CA isoform specific drug designing: tail approach and fragment addition approach.

Indexed as

Binding SitesCarbonic Anhydrase InhibitorsCarbonic AnhydrasesCatalytic DomainDatabases, ProteinDrug DesignHumansIsoenzymesNeoplasmsProtein BindingSulfonamidesCarbonic Anhydrase InhibitorsCarbonic AnhydrasesIsoenzymesSulfonamides

Identifiers

PMID22985956
PMCPMC3593968
OpenAlexW2061983779

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.