Evidence map›Paper›PMID 31816172›Full record

ArticleChemMedChem2020

Structure-Based Design, Synthesis, and Biological Evaluation of Triazole-Based smHDAC8 Inhibitors.

Dmitrii V Kalinin, Sunit K Jana, Maxim Pfafenrot, Alokta Chakrabarti, Jelena Melesina, Tajith B Shaik, Julien Lancelot, Raymond J Pierce, Wolfgang Sippl, Christophe Romier and 2 more

Open access · hybridAbstract read
In one paragraph

Article in ChemMedChem, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

13 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  3. Novel 1ACS infectious diseases · 2026
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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

12 authors at 5 institutions in 2 countries.

Dmitrii V KalininDepartment of Chemistry Institute of Organic Chemistry, University of Hamburg, Martin-Luther-King-Platz 6, 20146, Hamburg, Germany.
Sunit K JanaInstitute of Pharmaceutical and Medicinal Chemistry, University of Münster, Corrensstr. 48, 48149, Münster, Germany.
Maxim PfafenrotInstitute of Pharmaceutical and Medicinal Chemistry, University of Münster, Corrensstr. 48, 48149, Münster, Germany.
Alokta ChakrabartiInstitute of Pharmaceutical Sciences, Albert-Ludwigs-Universität Freiburg, Albertstr. 25, 79104, Freiburg, Germany.
Jelena MelesinaInstitute of Pharmacy, Martin Luther University of Halle-Wittenberg, Wolfgang-Langenbeck Str. 4, 06120, Halle/Saale, Germany.
Tajith B ShaikDépartement de Biologie Structurale Intégrative Institut de Génétique et Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg, CNRS, INSERM, 1 rue Laurent Fries, 67404, Illkirch Cedex, France.
Julien LancelotUniversité de Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille U1019-UMR 8204-CIIL-Centre d'Infection et d'Immunité de Lille, 59000, Lille, France.
Raymond J PierceUniversité de Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille U1019-UMR 8204-CIIL-Centre d'Infection et d'Immunité de Lille, 59000, Lille, France.
Wolfgang SipplInstitute of Pharmacy, Martin Luther University of Halle-Wittenberg, Wolfgang-Langenbeck Str. 4, 06120, Halle/Saale, Germany.
Christophe RomierDépartement de Biologie Structurale Intégrative Institut de Génétique et Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg, CNRS, INSERM, 1 rue Laurent Fries, 67404, Illkirch Cedex, France.
Manfred JungInstitute of Pharmaceutical Sciences, Albert-Ludwigs-Universität Freiburg, Albertstr. 25, 79104, Freiburg, Germany.
Ralph HollDepartment of Chemistry Institute of Organic Chemistry, University of Hamburg, Martin-Luther-King-Platz 6, 20146, Hamburg, Germany.ORCID 0000-0001-8511-3546
Centre National de la Recherche Scientifique · FRMartin Luther University Halle-Wittenberg · DEUniversität Hamburg · DEUniversity of Freiburg · DEUniversity of Münster · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Schistosomiasis is a neglected tropical disease caused by parasitic flatworms of the genus Schistosoma, which affects over 200 million people worldwide and leads to at least 300,000 deaths every year. In this study, initial screening revealed the triazole-based hydroxamate 2 b (N-hydroxy-1-phenyl-1H-1,2,3-triazole-4-carboxamide) exhibiting potent inhibitory activity toward the novel antiparasitic target Schistosoma mansoni histone deacetylase 8 (smHDAC8) and promising selectivity over the major human HDACs. Subsequent crystallographic studies of the 2 b/smHDAC8 complex revealed key interactions between the inhibitor and the enzyme's active site, thus explaining the unique selectivity profile of the inhibitor. Further chemical modifications of 2 b led to the discovery of 4-fluorophenoxy derivative 21 (1-[5-chloro-2-(4-fluorophenoxy)phenyl]-N-hydroxy-1H-1,2,3-triazole-4-carboxamide), a nanomolar smHDAC8 inhibitor (IC

Indexed as

Drug DesignAnimalsHistone Deacetylase InhibitorsHistone DeacetylasesHumansModels, MolecularMolecular StructureRepressor ProteinsSchistosoma mansoniSchistosomiasisTriazolesHDAC8 protein, humanHistone Deacetylase InhibitorsHistone DeacetylasesRepressor ProteinsTriazolescrystal structureshistone deacetylasesmolecular docking studiesSchistosoma mansonitriazole derivatives

Identifiers

PMID31816172
PMCPMC7187165
OpenAlexW2994959816

What OpenQuestion holds

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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.