Evidence map›Paper›PMID 39808739›Full record

ArticleBioconjugate chemistry2025

l-Asparaginase Immobilized on Nanographene Oxide as an Efficient Nanobiocatalytic Tool for Asparagine Depletion in Leukemia Cells.

Paulina Erwardt, Bartosz Szymczak, Marek Wiśniewski, Bartosz Maciejewski, Michał Świdziński, Janusz Strzelecki, Wiesław Nowak, Katarzyna Roszek

Abstract read
In one paragraph

Article in Bioconjugate chemistry, 2025. 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
–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

2 citing papers in PubMed.

  1. Article
  2. Review
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

8 authors.

Paulina ErwardtDepartment of Materials Chemistry, Adsorption and Catalysis, Faculty of Chemistry, Nicolaus Copernicus University in Torun, ul. Gagarina 7, 87-100 Torun, Poland.
Bartosz SzymczakDepartment of Biochemistry, Faculty of Biological and Veterinary Sciences, Nicolaus Copernicus University in Torun, ul. Lwowska 1, 87-100 Torun, Poland.
Marek WiśniewskiDepartment of Materials Chemistry, Adsorption and Catalysis, Faculty of Chemistry, Nicolaus Copernicus University in Torun, ul. Gagarina 7, 87-100 Torun, Poland.ORCID 0000-0003-3478-5371
Bartosz MaciejewskiDepartment of Immunology, Faculty of Biological and Veterinary Sciences, Nicolaus Copernicus University in Torun, ul. Lwowska 1, 87-100 Torun, Poland.
Michał ŚwidzińskiDepartment of Cellular and Molecular Biology, Faculty of Biological and Veterinary Sciences, Nicolaus Copernicus University in Torun, ul. Lwowska 1, 87-100 Torun, Poland.
Janusz StrzeleckiDepartment of Biophysics, Institute of Physics, Faculty of Physics, Astronomy and Informatics, Nicolaus Copernicus University in Torun, ul. Grudziądzka 5, 87-100 Torun, Poland.
Wiesław NowakDepartment of Biophysics, Institute of Physics, Faculty of Physics, Astronomy and Informatics, Nicolaus Copernicus University in Torun, ul. Grudziądzka 5, 87-100 Torun, Poland.
Katarzyna RoszekDepartment of Biochemistry, Faculty of Biological and Veterinary Sciences, Nicolaus Copernicus University in Torun, ul. Lwowska 1, 87-100 Torun, Poland.ORCID 0000-0002-2854-6238

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

l-Asparaginase (l-ASNase) catalyzes the hydrolysis of l-asparagine, leading to its depletion and subsequent effects on the cellular proliferation and survival. In contrast to normal cells, malignant cells that lack asparagine synthase are extremely susceptible to asparagine deficiency. l-ASNase has been successfully employed in treating pediatric leukemias and non-Hodgkin lymphomas; however, its usage in adult patients and other types of cancer is limited due to significant side effects and drug resistance. Recent research has explored alternative formulations and delivery methods to enhance its efficacy and minimize adverse effects. One promising approach involves the immobilization of l-ASNase onto nanostructured materials, offering improved enzymatic activity and biocompatibility of the support. We harnessed an

Indexed as

Antineoplastic AgentsAsparaginaseAsparagineEnzymes, ImmobilizedGraphiteLeukemiaBiocatalysisHumansK562 CellsAntineoplastic AgentsAsparaginaseAsparagineEnzymes, Immobilizedgraphene oxideGraphite

Identifiers

PMID39808739
PMCPMC11843607

What OpenQuestion holds

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Registered trials

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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.