Evidence map›Paper›PMID 38414868›Full record

ReviewFrontiers in molecular biosciences2023

Deciphering non-canonical ubiquitin signaling: biology and methodology.

Nila K van Overbeek, Tim Aguirre, Gerbrand J van der Heden van Noort, Blagoy Blagoev, Alfred C O Vertegaal

Abstract readReview
In one paragraph

Review in Frontiers in molecular biosciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. The Molecular Toolbox for Linkage Type-Specific Analysis of Ubiquitin Signaling.Chembiochem : a European journal of chemical biology · 2025
    Review
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

5 authors.

Nila K van OverbeekDepartment of Cell and Chemical Biology, Leiden University Medical Center, Leiden, Netherlands.
Tim AguirreDepartment of Cell and Chemical Biology, Leiden University Medical Center, Leiden, Netherlands.
Gerbrand J van der Heden van NoortDepartment of Cell and Chemical Biology, Leiden University Medical Center, Leiden, Netherlands.
Blagoy BlagoevDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark.
Alfred C O VertegaalDepartment of Cell and Chemical Biology, Leiden University Medical Center, Leiden, Netherlands.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitination is a dynamic post-translational modification that regulates virtually all cellular processes by modulating function, localization, interactions and turnover of thousands of substrates. Canonical ubiquitination involves the enzymatic cascade of E1, E2 and E3 enzymes that conjugate ubiquitin to lysine residues giving rise to monomeric ubiquitination and polymeric ubiquitination. Emerging research has established expansion of the ubiquitin code by non-canonical ubiquitination of N-termini and cysteine, serine and threonine residues. Generic methods for identifying ubiquitin substrates using mass spectrometry based proteomics often overlook non-canonical ubiquitinated substrates, suggesting that numerous undiscovered substrates of this modification exist. Moreover, there is a knowledge gap between

Indexed as

affinity purificationE3 ligasemass spectrometrynon-canonical ubiquitinationoxyesterproteomicsthioesterubiquitin

Identifiers

PMID38414868
PMCPMC10897730

What OpenQuestion holds

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LicenceCC BY
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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.