Evidence map›Paper›PMID 36250581›Full record

ArticleChembiochem : a European journal of chemical biology2023

Serendipitous Identification of a Covalent Activator of Liver Pyruvate Kinase.

Umberto Maria Battisti, Chunxia Gao, Oscar Nilsson, Fady Akladios, Aleksei Lulla, Agnieszka Bogucka, Amalyn Nain-Perez, Liliana Håversen, Woonghee Kim, Jan Boren and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Genome-scale models in human metabologenomics.Nature reviews. Genetics · 2025
    Review
  2. Article
  3. Serendipitous Identification of a Covalent Activator of Liver Pyruvate Kinase.Chembiochem : a European journal of chemical biology · 2023
    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

14 authors at 4 institutions in 2 countries.

Umberto Maria BattistiDepartment of Chemistry and Molecular Biology, University of Gothenburg, 412 96, Gothenburg, Sweden.ORCID 0000-0002-1012-8644
Chunxia GaoDepartment of Chemistry and Molecular Biology, University of Gothenburg, 412 96, Gothenburg, Sweden.
Oscar NilssonDepartment of Chemistry and Molecular Biology, University of Gothenburg, 412 96, Gothenburg, Sweden.ORCID 0000-0003-2716-2563
Fady AkladiosDepartment of Chemistry and Molecular Biology, University of Gothenburg, 412 96, Gothenburg, Sweden.
Aleksei LullaDepartment of Biochemistry, University of Cambridge, Cambridge, CB2 1GA, UK.
Agnieszka BoguckaDepartment of Biochemistry, University of Cambridge, Cambridge, CB2 1GA, UK.
Amalyn Nain-PerezDepartment of Chemistry and Molecular Biology, University of Gothenburg, 412 96, Gothenburg, Sweden.ORCID 0000-0002-0784-0446
Liliana HåversenDepartment of Molecular and Clinical Medicine, University of Gothenburg and Sahlgrenska University Hospital, 413 45, Gothenburg, Sweden.ORCID 0000-0001-5180-7830
Woonghee KimScience for Life Laboratory, KTH-Royal Institute of Technology, 171 21, Stockholm, Sweden.
Jan BorenDepartment of Molecular and Clinical Medicine, University of Gothenburg and Sahlgrenska University Hospital, 413 45, Gothenburg, Sweden.ORCID 0000-0003-0786-8091
Marko HyvönenDepartment of Biochemistry, University of Cambridge, Cambridge, CB2 1GA, UK.ORCID 0000-0001-8683-4070
Mathias UhlenScience for Life Laboratory, KTH-Royal Institute of Technology, 171 21, Stockholm, Sweden.ORCID 0000-0002-4858-8056
Adil MardinogluScience for Life Laboratory, KTH-Royal Institute of Technology, 171 21, Stockholm, Sweden.ORCID 0000-0002-4254-6090
Morten GrøtliDepartment of Chemistry and Molecular Biology, University of Gothenburg, 412 96, Gothenburg, Sweden.ORCID 0000-0003-3621-4222
University of Gothenburg · SEScience for Life Laboratory · SEUniversity of Cambridge · GBSahlgrenska University Hospital · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymes are effective biological catalysts that accelerate almost all metabolic reactions in living organisms. Synthetic modulators of enzymes are useful tools for the study of enzymatic reactions and can provide starting points for the design of new drugs. Here, we report on the discovery of a class of biologically active compounds that covalently modifies lysine residues in human liver pyruvate kinase (PKL), leading to allosteric activation of the enzyme (EC

Indexed as

LysinePyruvate KinaseAllosteric RegulationCatalytic DomainHumansLiverTandem Mass SpectrometryLysinePyruvate Kinasecovalent activatorsenzymesligand designPKLstructure-activity relationships

Identifiers

PMID36250581
PMCPMC10099687
OpenAlexW4306405723

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.