Evidence map›Paper›PMID 23709689›Full record

ArticleJournal of lipid research2013

Alkyne lipids as substrates for click chemistry-based in vitro enzymatic assays.

Anne Gaebler, Robin Milan, Leon Straub, Dominik Hoelper, Lars Kuerschner, Christoph Thiele

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

34 citing papers in PubMed, 74 citations in OpenAlex.

  1. Bioconjugation Strategies for Revealing the Roles of Glycerophospholipids in Cells.Chembiochem : a European journal of chemical biology · 2026
    Review
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  3. Lipid Metabolism and Immune Function: Chemical Tools for Insights into T-Cell Biology.Chembiochem : a European journal of chemical biology · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Analytical Techniques for Single-Cell Biochemical Assays of Lipids.Annual review of biomedical engineering · 2023
    Review
  9. Chemical Tools for Lipid Cell Biology.Accounts of chemical research · 2023
    Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. The Journal of biological chemistry · 2020
    Article
  20. 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

6 authors at 1 institution in 1 country.

Anne GaeblerLIMES Life and Medical Sciences Institute, University of Bonn, 53115 Bonn, Germany.
Robin MilanLIMES Life and Medical Sciences Institute, University of Bonn, 53115 Bonn, Germany.
Leon StraubLIMES Life and Medical Sciences Institute, University of Bonn, 53115 Bonn, Germany.
Dominik HoelperLIMES Life and Medical Sciences Institute, University of Bonn, 53115 Bonn, Germany.
Lars KuerschnerLIMES Life and Medical Sciences Institute, University of Bonn, 53115 Bonn, Germany.
Christoph ThieleLIMES Life and Medical Sciences Institute, University of Bonn, 53115 Bonn, Germany. Electronic address: cthiele@uni-bonn.de.
University of Bonn · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Click chemistry is evolving as a powerful tool in biological applications because it allows the sensitive and specific detection of compounds with alkyne or azido groups. Here we describe the use of alkyne lipids as substrates for in vitro enzymatic assays of lipid modifying enzymes. The small alkyne moiety is introduced synthetically at the terminus of the hydrocarbon chain of various substrate lipids. After the assay, the label is click-reacted with the azide-bearing fluorogenic dye 3-azido-7-hydroxycoumarin, followed by the separation of the lipid mix by thin-layer chromatography and fluorescence detection, resulting in high sensitivity and wide-range linearity. Kinetic analyses using alkyne-labeled substrates for lysophosphatidic acid acyltransferases, lysophosphatidylcholine acyltransferases, and ceramide synthases resulted in Michaelis-Menten constants similar to those for radiolabeled or natural substrates. We tested additional alkyne substrates for several hydrolases and acyltransferases in lipid metabolism. In this pilot study we establish alkyne lipids as a new class of convenient substrates for in vitro enzymatic assays.

Indexed as

Click Chemistry1-Acylglycerophosphocholine O-AcyltransferaseAcyltransferasesAlkynesAnimalsCells, CulturedEnzyme AssaysHumansKineticsLipidsMiceMice, Inbred C57BLMolecular StructureOxidoreductasesSubstrate Specificity1-Acylglycerophosphocholine O-Acyltransferase2-acylglycerophosphate acyltransferaseAcyltransferasesAlkynesdihydroceramide desaturaseLipidsOxidoreductasesacyltransferaseceramide synthaseclick-labelingclick lipidenzyme kineticsfatty acid amide hydrolasein vitro assaylipid substrate

Identifiers

PMID23709689
PMCPMC3708378
OpenAlexW2145325288

What OpenQuestion holds

Textmetadata
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.