Evidence map›Paper›PMID 35923158›Full record

ArticleBeilstein journal of organic chemistry2022

Synthesis and HDAC inhibitory activity of pyrimidine-based hydroxamic acids.

Virginija Jakubkiene, Gabrielius Ernis Valiulis, Markus Schweipert, Asta Zubriene, Daumantas Matulis, Franz-Josef Meyer-Almes, Sigitas Tumkevicius

Open access · diamondAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Beilstein journal of organic chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

2 citing papers in PubMed, 8 citations in OpenAlex.

  1. Synthesis and crystal structure of HDAC6 selective inhibitor ofActa crystallographica. Section E, Crystallographic communications · 2026
    Article
  2. 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

7 authors at 2 institutions in 2 countries.

Virginija JakubkieneDepartment of Organic Chemistry, Faculty of Chemistry and Geosciences, Vilnius University, Naugarduko 24, 03225 Vilnius, Lithuania.
Gabrielius Ernis ValiulisDepartment of Organic Chemistry, Faculty of Chemistry and Geosciences, Vilnius University, Naugarduko 24, 03225 Vilnius, Lithuania.
Markus SchweipertDepartment of Chemical Engineering and Biotechnology, University of Applied Sciences, Stephanstr. 7, 64295 Darmstadt, Germany.
Asta ZubrieneDepartment of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Sauletekio 7, 10257 Vilnius, Lithuania.ORCID https://orcid.org/0000-0001-5996-1883
Daumantas MatulisDepartment of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Sauletekio 7, 10257 Vilnius, Lithuania.
Franz-Josef Meyer-AlmesDepartment of Chemical Engineering and Biotechnology, University of Applied Sciences, Stephanstr. 7, 64295 Darmstadt, Germany.ORCID https://orcid.org/0000-0002-1001-3249
Sigitas TumkeviciusDepartment of Organic Chemistry, Faculty of Chemistry and Geosciences, Vilnius University, Naugarduko 24, 03225 Vilnius, Lithuania.ORCID https://orcid.org/0000-0002-3279-1770
Vilnius University · LTTechnische Universität Darmstadt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone deacetylases (HDACs) play an essential role in the transcriptional regulation of cells through the deacetylation of nuclear histone and non-histone proteins and are promising therapeutic targets for the treatment of various diseases. Here, the synthesis of new compounds in which a hydroxamic acid residue is attached to differently substituted pyrimidine rings via a methylene group bridge of varying length as potential HDAC inhibitors is described. The target compounds were obtained by alkylation of 2-(alkylthio)pyrimidin-4(3

Indexed as

alkylationaminolysisHDAC inhibitorshydroxamic acidpyrimidine

Identifiers

PMID35923158
PMCPMC9296983
OpenAlexW4285085462

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.