Evidence map›Paper›PMID 27775452›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2017

Isatin: a privileged scaffold for the design of carbonic anhydrase inhibitors.

Claudia Melis, Rita Meleddu, Andrea Angeli, Simona Distinto, Giulia Bianco, Clemente Capasso, Filippo Cottiglia, Rossella Angius, Claudiu T Supuran, Elias Maccioni

Open access · hybridAbstract read
In one paragraph

Article in Journal of enzyme inhibition and medicinal chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

28 citing papers in PubMed, 59 citations in OpenAlex.

  1. Synthesis, structure and energy calculations of 4-{4-[(2,3-dioxoindol-1-yl)meth-yl]-1Acta crystallographica. Section E, Crystallographic communications · 2026
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  10. Thiazole Ring-A Biologically Active Scaffold.Molecules (Basel, Switzerland) · 2021
    Review
  11. A structure-based approach towards the identification of novel antichagasic compounds:Journal of enzyme inhibition and medicinal chemistry · 2020
    Article
  12. Article
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  16. Journal of enzyme inhibition and medicinal chemistry · 2019
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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

10 authors at 4 institutions in 1 country.

Claudia Melisa Department of Life and Environmental Sciences , University of Cagliari , Cagliari , Italy.
Rita Meleddua Department of Life and Environmental Sciences , University of Cagliari , Cagliari , Italy.
Andrea Angelib Dipartimento NEUROFARBA, Sezione di Scienze Farmaceutiche , Università degli Studi di Firenze , Sesto Fiorentino , Florence , Italy.
Simona Distintoa Department of Life and Environmental Sciences , University of Cagliari , Cagliari , Italy.
Giulia Biancoa Department of Life and Environmental Sciences , University of Cagliari , Cagliari , Italy.
Clemente Capassoc Istituto di Bioscienze e Biorisorse, CNR , Napoli , Italy.
Filippo Cottigliaa Department of Life and Environmental Sciences , University of Cagliari , Cagliari , Italy.
Rossella Angiusd Laboratorio NMR e Tecnologie Bioanalitiche, Sardegna Ricerche , Pula , CA , Italy.
Claudiu T Supuranb Dipartimento NEUROFARBA, Sezione di Scienze Farmaceutiche , Università degli Studi di Firenze , Sesto Fiorentino , Florence , Italy.
Elias Maccionia Department of Life and Environmental Sciences , University of Cagliari , Cagliari , Italy.
University of Cagliari · ITUniversity of Florence · ITInstitute of Biosciences and Bioresources · ITSardegna Ricerche (Italy) · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The isatin scaffold is the constitutive fragment of several natural and synthetic bioactive molecules. Albeit several benzene sulphonamide-based carbonic anhydrase inhibitors (CAIs) have been reported, only recently isatin benzene sulphonamides have been studied and proposed as CAIs. In this study we have designed, synthesised, and evaluated the biological activity of a series of differently substituted isatin-based benzene sulphonamides which have been designed for the inhibition of carbonic anhydrase isoforms. The activity of all the synthesised compounds was evaluated towards human carbonic anhydrase I, II, IX, and XII isozymes. Our results indicate that the nature and position of substituents on the isatin ring can modulate both activity and isozyme selectivity.

Indexed as

Drug DesignCarbonic Anhydrase InhibitorsIsatinCarbonic Anhydrase InhibitorsIsatinAntitumour agentscarbonic anhydrase inhibitorsisatin hybrid molecules

Identifiers

PMID27775452
PMCPMC6010117
OpenAlexW2538009965

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.