Evidence map›Paper›PMID 35205650›Full record

ReviewCancers2022

Novel Insights on the Use of L-Asparaginase as an Efficient and Safe Anti-Cancer Therapy.

Maaike Van Trimpont, Evelien Peeters, Yanti De Visser, Amanda M Schalk, Veerle Mondelaers, Barbara De Moerloose, Arnon Lavie, Tim Lammens, Steven Goossens, Pieter Van Vlierberghe

Open access · goldAbstract readReview
In one paragraph

Review in Cancers, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
24.1field-weighted citation impact, top 1% 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

69 citing papers in PubMed, 125 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Prevention of Subsequent L-Asparaginase Hypersensitivity in Children Through Premedication: A Single-Center Experience.The journal of pediatric pharmacology and therapeutics : JPPT : the official journal of PPAG · 2026
    Article
  10. Article
  11. The Asparaginase Database: a comprehensive resource and classification of l-asparaginases.Database : the journal of biological databases and curation · 2026
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

9 more citing papers are in PubMed but not listed here.

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

10 authors at 3 institutions in 2 countries.

Maaike Van TrimpontCancer Research Institute Ghent (CRIG), 9000 Ghent, Belgium.ORCID 0000-0001-7033-9569
Evelien PeetersCancer Research Institute Ghent (CRIG), 9000 Ghent, Belgium.ORCID 0000-0001-9438-1876
Yanti De VisserCancer Research Institute Ghent (CRIG), 9000 Ghent, Belgium.
Amanda M SchalkDepartment of Biochemistry and Molecular Genetics, University of Illinois, Chicago, IL 60607, USA.
Veerle MondelaersDepartment of Pediatric Hemato-Oncology and Stem Cell Transplantation, Ghent University Hospital, 9000 Ghent, Belgium.
Barbara De MoerlooseCancer Research Institute Ghent (CRIG), 9000 Ghent, Belgium.ORCID 0000-0002-2449-539X
Arnon LavieDepartment of Biochemistry and Molecular Genetics, University of Illinois, Chicago, IL 60607, USA.
Tim LammensCancer Research Institute Ghent (CRIG), 9000 Ghent, Belgium.ORCID 0000-0001-8733-4027
Steven GoossensCancer Research Institute Ghent (CRIG), 9000 Ghent, Belgium.ORCID 0000-0002-5693-8570
Pieter Van VlierbergheCancer Research Institute Ghent (CRIG), 9000 Ghent, Belgium.ORCID 0000-0001-9063-7205
Ghent University · BEGhent University Hospital · BEUniversity of Illinois Chicago · US

Funding

A novel glutaminase-free mammalian asparaginase with minimized immunogenicity to enable expanded use in cancer therapyR44CA228622 · NCI · ENZYME BY DESIGN, INC. · PI SCHALK, AMANDA M · 2020 to 2022
$2.0M
BLRD VA I01 BX001919BLRD VA I01 BX004589NCI NIH HHS R44 CA228622
6 · The paper itself

Abstract

L-Asparaginase (L-ASNase) is an enzyme that hydrolyses the amino acid asparagine into aspartic acid and ammonia. Systemic administration of bacterial L-ASNase is successfully used to lower the bioavailability of this non-essential amino acid and to eradicate rapidly proliferating cancer cells with a high demand for exogenous asparagine. Currently, it is a cornerstone drug in the treatment of the most common pediatric cancer, acute lymphoblastic leukemia (ALL). Since these lymphoblasts lack the expression of asparagine synthetase (ASNS), these cells depend on the uptake of extracellular asparagine for survival. Interestingly, recent reports have illustrated that L-ASNase may also have clinical potential for the treatment of other aggressive subtypes of hematological or solid cancers. However, immunogenic and other severe adverse side effects limit optimal clinical use and often lead to treatment discontinuation. The design of optimized and novel L-ASNase formulations provides opportunities to overcome these limitations. In addition, identification of multiple L-ASNase resistance mechanisms, including ASNS promoter reactivation and desensitization, has fueled research into promising novel drug combinations to overcome chemoresistance. In this review, we discuss recent insights into L-ASNase adverse effects, resistance both in hematological and solid tumors, and how novel L-ASNase variants and drug combinations can expand its clinical applicability.

Indexed as

acute lymphoblastic leukemiaasparaginaseasparagineglutaminesolid cancers

Identifiers

PMID35205650
PMCPMC8870365
OpenAlexW4213226315

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.