Evidence map›Paper›PMID 41543318›Full record

ReviewIUCrJ2026

Stereochemical aspects of the nucleophilic attack in different classes of L-asparaginases.

Miroslaw Gilski, Kinga Pokrywka, Mariusz Jaskolski

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in IUCrJ, 2026. 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. 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.

Miroslaw GilskiDepartment of Crystallography, Faculty of Chemistry, Adam Mickiewicz University, Poznan, Poland.ORCID 0000-0002-3941-9947
Kinga PokrywkaInstitute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland.
Mariusz JaskolskiDepartment of Crystallography, Faculty of Chemistry, Adam Mickiewicz University, Poznan, Poland.ORCID 0000-0003-1587-6489

Funding

Narodowe Centrum Nauki 2020/37/B/NZ1/03250
6 · The paper itself

Abstract

L-Asparaginases hydrolyze L-asparagine to L-aspartate with the release of ammonia. Currently, three completely unrelated structural classes of L-asparaginases are known, further subdivided into five types. In each class, the hydrolysis reaction is thought to proceed via a nucleophilic attack of an activated Thr or Ser residue on the carbonyl Csp

Indexed as

AsparaginaseAsparagineAspartic AcidHydrolysisStereoisomerismAsparaginaseAsparagineAspartic AcidamidohydrolasesBürgi–Dunitz angleFlippin–Lodge angleHerschlag dihedralhydrolasesl-asparaginasesreaction mechanismsstereochemistrystructural correlations

Identifiers

PMID41543318
PMCPMC12951835

What OpenQuestion holds

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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.