Evidence map›Paper›PMID 33053898›Full record

ReviewMolecules (Basel, Switzerland)2020

Therapeutic Perspectives of Adenosine Deaminase Inhibition in Cardiovascular Diseases.

Barbara Kutryb-Zajac, Paulina Mierzejewska, Ewa M Slominska, Ryszard T Smolenski

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed, 1 pooled it
5.2field-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, 1 synthesis or guideline pooled it, 60 citations in OpenAlex.

  1. Pooled it
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  15. Effect and mechanism ofFrontiers in microbiology · 2025
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  18. Correlation between serum adenosine deaminase levels and risk of diabetic foot ulcers in patients with type 2 diabetes mellitus.Zhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences · 2024
    Article
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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

4 authors at 1 institution in 1 country.

Barbara Kutryb-ZajacDepartment of Biochemistry, Medical University of Gdansk, Debinki 1 St., 80-211 Gdansk, Poland.ORCID 0000-0002-3324-9246
Paulina MierzejewskaDepartment of Biochemistry, Medical University of Gdansk, Debinki 1 St., 80-211 Gdansk, Poland.
Ewa M SlominskaDepartment of Biochemistry, Medical University of Gdansk, Debinki 1 St., 80-211 Gdansk, Poland.
Ryszard T SmolenskiDepartment of Biochemistry, Medical University of Gdansk, Debinki 1 St., 80-211 Gdansk, Poland.
Gdańsk Medical University · PL

Funding

Narodowe Centrum Nauki 2016/22/M/NZ4/00678Narodowe Centrum Nauki 2016/23/B/NZ4/03877Narodowe Centrum Nauki 2019/35/D/NZ3/03512
6 · The paper itself

Abstract

Adenosine deaminase (ADA) is an enzyme of purine metabolism that irreversibly converts adenosine to inosine or 2'deoxyadenosine to 2'deoxyinosine. ADA is active both inside the cell and on the cell surface where it was found to interact with membrane proteins, such as CD26 and adenosine receptors, forming ecto-ADA (eADA). In addition to adenosine uptake, the activity of eADA is an essential mechanism that terminates adenosine signaling. This is particularly important in cardiovascular system, where adenosine protects against endothelial dysfunction, vascular inflammation, or thrombosis. Besides enzymatic function, ADA protein mediates cell-to-cell interactions involved in lymphocyte co-stimulation or endothelial activation. Furthermore, alteration in ADA activity was demonstrated in many cardiovascular pathologies such as atherosclerosis, myocardial ischemia-reperfusion injury, hypertension, thrombosis, or diabetes. Modulation of ADA activity could be an important therapeutic target. This work provides a systematic review of ADA activity and anchoring inhibitors as well as summarizes the perspectives of their therapeutic use in cardiovascular pathologies associated with increased activity of ADA.

Indexed as

Adenosine Deaminase InhibitorsAnimalsDrug DiscoveryHeat-Shock ProteinsHumansMolecular Dynamics SimulationProtein BindingWaterAdenosine Deaminase InhibitorsHeat-Shock ProteinsWaterADAadenosine deaminaseatherosclerosishypertensioninflammationinhibitionmyocardial infarctiontherapythrombosistype II diabetes mellitus

Identifiers

PMID33053898
PMCPMC7587364
OpenAlexW3092454836

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.