Evidence map›Paper›PMID 39337272›Full record

ReviewInternational journal of molecular sciences2024

Pathophysiology of Arginases in Cancer and Efforts in Their Pharmacological Inhibition.

Patrycja Marzęta-Assas, Damian Jacenik, Zbigniew Zasłona

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Article
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  4. Review
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  9. Avicenna journal of phytomedicine
    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

3 authors.

Patrycja Marzęta-AssasMolecure S.A., 101 Żwirki i Wigury St., 02-089 Warsaw, Poland.
Damian JacenikMolecure S.A., 101 Żwirki i Wigury St., 02-089 Warsaw, Poland.ORCID 0000-0003-4563-2303
Zbigniew ZasłonaMolecure S.A., 101 Żwirki i Wigury St., 02-089 Warsaw, Poland.

Funding

European Funds Smart Growth and European Regional Development Fund POIR.01.01.01-00-0415/17National Centre for Research and Development STRATEGMED2/265503/3/NCBR/15
6 · The paper itself

Abstract

Arginases are key enzymes that hydrolyze L-arginine to urea and L-ornithine in the urea cycle. The two arginase isoforms, arginase 1 (ARG1) and arginase 2 (ARG2), regulate the proliferation of cancer cells, migration, and apoptosis; affect immunosuppression; and promote the synthesis of polyamines, leading to the development of cancer. Arginases also compete with nitric oxide synthase (NOS) for L-arginine, and their participation has also been confirmed in cardiovascular diseases, stroke, and inflammation. Due to the fact that arginases play a crucial role in the development of various types of diseases, finding an appropriate candidate to inhibit the activity of these enzymes would be beneficial for the therapy of many human diseases. In this review, based on numerous experimental, preclinical, and clinical studies, we provide a comprehensive overview of the biological and physiological functions of ARG1 and ARG2, their molecular mechanisms of action, and affected metabolic pathways. We summarize the recent clinical trials' advances in targeting arginases and describe potential future drugs.

Indexed as

ArginaseNeoplasmsAnimalsAntineoplastic AgentsArginineEnzyme InhibitorsHumansAntineoplastic AgentsArginaseArginineEnzyme Inhibitorsarginasecancerdrug therapyinhibitorsL-argininemetabolism

Identifiers

PMID39337272
PMCPMC11431790

What OpenQuestion holds

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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.