Evidence map›Paper›PMID 24568254›Full record

ReviewBiotechnology & genetic engineering reviews2013

Proteomic identification of protein ubiquitination events.

Guoqiang Xu, Samie R Jaffrey

Open access · greenAbstract readReview
In one paragraph

Review in Biotechnology & genetic engineering reviews, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

30 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. CXXC5 is a ubiquitinated protein and is degraded by the ubiquitin-proteasome pathway.Protein science : a publication of the Protein Society · 2025
    Article
  3. Article
  4. Article
  5. The Ubiquitin Tale: Current Strategies and Future Challenges.ACS pharmacology & translational science · 2024
    Review
  6. Decoding Ubiquitin Modifications by Mass Spectrometry.Advances in experimental medicine and biology · 2024
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Post-translational modifications in MeHg-induced neurotoxicity.Biochimica et biophysica acta. Molecular basis of disease · 2019
    Review
  17. Review
  18. Review
  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

2 authors at 2 institutions in 2 countries.

Guoqiang Xua Laboratory of Chemical Biology, Department of Pharmacology , College of Pharmaceutical Sciences, Soochow University , Suzhou , China.
Samie R Jaffrey
Cornell University · USSoochow University · CN

Funding

CANCER PHARMACOLOGYT32CA062948 · NCI · WEILL MEDICAL COLL OF CORNELL UNIV · PI LORRAINE J GUDAS · 1994 to 2026
$12.1M
Comprehensive profiling of ubiquitination in neuronsR21MH086128 · NIMH · WEILL MEDICAL COLL OF CORNELL UNIV · PI JAFFREY, SAMIE R · 2010 to 2011
$420k
NCI NIH HHS T32 CA062948NCI NIH HHS T32CA062948NIMH NIH HHS MH086128NIMH NIH HHS R21 MH086128
6 · The paper itself

Abstract

Protein ubiquitination is an important post-translational modification that regulates almost every aspect of cellular function and many cell signaling pathways in eukaryotes. Alterations of protein ubiquitination have been linked to many diseases, such as cancer, neurodegenerative diseases, cardiovascular diseases, immunological disorders and inflammatory diseases. To understand the roles of protein ubiquitination in these diseases and in cell signaling pathways, it is necessary to identify ubiquitinated proteins and their modification sites. However, owing to the nature of protein ubiquitination, it is challenging to identify the exact modification sites under physiological conditions. Recently, ubiquitin-remnant profiling, an immunoprecipitation approach, which uses monoclonal antibodies specifically to enrich for peptides derived from the ubiquitinated portion of proteins and mass spectrometry for their identification, was developed to determine ubiquitination events from cell lysates. This approach has now been widely applied to profile protein ubiquitination in several cellular contexts. In this review, we discuss mass-spectrometry-based methods for the identification of protein ubiquitination sites, analyze their advantages and disadvantages, and discuss their application for proteomic analysis of ubiquitination.

Indexed as

ProteomicsAmino Acid SequenceHumansLysineMass SpectrometryProtein ConformationProtein Processing, Post-TranslationalSignal TransductionUbiquitinated ProteinsUbiquitinationLysineUbiquitinated Proteins

Identifiers

PMID24568254
PMCPMC3937853
OpenAlexW1967618958

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.