Evidence map›Paper›PMID 30297752›Full record

ArticleNature chemistry2018

Mining the cellular inventory of pyridoxal phosphate-dependent enzymes with functionalized cofactor mimics.

Annabelle Hoegl, Matthew B Nodwell, Volker C Kirsch, Nina C Bach, Martin Pfanzelt, Matthias Stahl, Sabine Schneider, Stephan A Sieber

Abstract read
In one paragraph

Article in Nature chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed, 1 pooled it
2.7field-weighted citation impact, top 9% 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

37 citing papers in PubMed, 1 synthesis or guideline pooled it, 58 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. CPP-PNA Conjugate-Mediated Inhibition ofInternational journal of molecular sciences · 2026
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  9. Proteomic strategies to interrogate the Fe-S proteome.Biochimica et biophysica acta. Molecular cell research · 2024
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. A de novo protein catalyzes the synthesis of semiconductor quantum dots.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. Bidirectional sequestration between a bacterial hibernation factor and a glutamate metabolizing protein.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  19. Article
  20. The pathway for coenzyme M biosynthesis in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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

8 authors at 1 institution in 1 country.

Annabelle HoeglDepartment of Chemistry, Center for Integrated Protein Science Munich (CIPSM), Technische Universität München, Garching, Germany.
Matthew B NodwellDepartment of Chemistry, Center for Integrated Protein Science Munich (CIPSM), Technische Universität München, Garching, Germany.
Volker C KirschDepartment of Chemistry, Center for Integrated Protein Science Munich (CIPSM), Technische Universität München, Garching, Germany.
Nina C BachDepartment of Chemistry, Center for Integrated Protein Science Munich (CIPSM), Technische Universität München, Garching, Germany.
Martin PfanzeltDepartment of Chemistry, Center for Integrated Protein Science Munich (CIPSM), Technische Universität München, Garching, Germany.
Matthias StahlDepartment of Chemistry, Center for Integrated Protein Science Munich (CIPSM), Technische Universität München, Garching, Germany.
Sabine SchneiderDepartment of Chemistry, Center for Integrated Protein Science Munich (CIPSM), Technische Universität München, Garching, Germany.ORCID http://orcid.org/0000-0003-1054-8689
Stephan A SieberDepartment of Chemistry, Center for Integrated Protein Science Munich (CIPSM), Technische Universität München, Garching, Germany. stephan.sieber@tum.de.ORCID http://orcid.org/0000-0002-9400-906X
Center for Integrated Protein Science Munich · DE

Funding

European Research Council 725085
6 · The paper itself

Abstract

Pyridoxal phosphate (PLP) is an enzyme cofactor required for the chemical transformation of biological amines in many central cellular processes. PLP-dependent enzymes (PLP-DEs) are ubiquitous and evolutionarily diverse, making their classification based on sequence homology challenging. Here we present a chemical proteomic method for reporting on PLP-DEs using functionalized cofactor probes. We synthesized pyridoxal analogues modified at the 2'-position, which are taken up by cells and metabolized in situ. These pyridoxal analogues are phosphorylated to functional cofactor surrogates by cellular pyridoxal kinases and bind to PLP-DEs via an aldimine bond which can be rendered irreversible by NaBH

Indexed as

Alanine RacemaseCoenzymesDopa DecarboxylaseGlycine HydroxymethyltransferaseKineticsModels, MolecularMolecular StructureOrnithine DecarboxylasePhosphorylationPyridoxal PhosphateTransaminasesAlanine RacemaseCoenzymesDopa DecarboxylaseGlycine HydroxymethyltransferaseOrnithine DecarboxylasePyridoxal PhosphateTransaminases

Identifiers

PMID30297752
PMCPMC6252082
OpenAlexW2806667678

What OpenQuestion holds

Textmetadata
LicenceTDM
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.