Evidence map›Paper›PMID 23028061›Full record

ArticleMolecular & cellular proteomics : MCP2013

A simple and effective cleavable linker for chemical proteomics applications.

Yinliang Yang, Hannes Hahne, Bernhard Kuster, Steven H L Verhelst

Abstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Review
  2. Review
  3. Recent Advances in the Linkers of Drug Conjugates.Current medicinal chemistry · 2025
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Traceless Cleavage of Protein-Biotin Conjugates under Biologically Compatible Conditions.Chembiochem : a European journal of chemical biology · 2017
    Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Cyclic acetals as cleavable linkers for affinity capture.Organic & biomolecular chemistry · 2015
    Article
  19. 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

4 authors.

Yinliang YangLehrstuhl für Chemie der Biopolymere, Technische Universität München, Weihenstephaner Berg 3, 85354 Freising, Germany.
Hannes Hahne
Bernhard Kuster
Steven H L Verhelst

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The study of metabolically labeled or probe-modified proteins is an important area in chemical proteomics. Isolation and purification of the protein targets is a necessary step before MS identification. The biotin-streptavidin system is widely used in this process, but the harsh denaturing conditions also release natively biotinylated proteins and non-selectively bound proteins. A cleavable linker strategy is a promising approach for solving this problem. Though several cleavable linkers have been developed and tested, an efficient, easily synthesized, and inexpensive cleavable linker is a desirable addition to the proteomics toolbox. Here, we describe the chemical proteomics application of a vicinal diol cleavable linker. Through easy-to-handle chemistry we incorporate this linker into an activity-based probe and a biotin alkyne tag amenable for bioorthogonal ligation. With these reagents, background protein identifications are significantly reduced relative to standard on-bead digestion.

Indexed as

BiotinCathepsinsCross-Linking ReagentsGlucosidesMass SpectrometryProteinsProteomeProteomicsPyrimidinonesBiotinCathepsinsCross-Linking ReagentsGlucosidesProteinsProteomePyrimidinonesvicine

Identifiers

PMID23028061
PMCPMC3536904

What OpenQuestion holds

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Registered trials

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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.