Evidence map›Paper›PMID 37121501›Full record

ReviewBiochimica et biophysica acta. Gene regulatory mechanisms2023

Proteomic approaches to study ubiquitinomics.

Indrajit Sahu, He Zhu, Sara J Buhrlage, Jarrod A Marto

Open access · hybridAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Gene regulatory mechanisms, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.9field-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

17 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. [Ubiquitination-mediated regulation of T cell homeostasis and autoimmune diseases].Zhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences · 2026
    Review
  4. Article
  5. Review
  6. Review
  7. Using Biological Networks to Guide Biomedical Prediction.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. The Ubiquitin Tale: Current Strategies and Future Challenges.ACS pharmacology & translational science · 2024
    Review
  16. Article
  17. 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 at 3 institutions in 1 country.

Indrajit SahuDepartment of Cancer Biology and the Linde Program in Cancer Chemical Biology, Dana-Farber Cancer Institute, Boston, MA, USA.
He ZhuDepartment of Cancer Biology and the Linde Program in Cancer Chemical Biology, Dana-Farber Cancer Institute, Boston, MA, USA.
Sara J BuhrlageDepartment of Cancer Biology and the Linde Program in Cancer Chemical Biology, Dana-Farber Cancer Institute, Boston, MA, USA; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA; Center for Emergent Drug Targets, USA. Electronic address: saraj_buhrlage@dfci.harvard.edu.
Jarrod A MartoDepartment of Cancer Biology and the Linde Program in Cancer Chemical Biology, Dana-Farber Cancer Institute, Boston, MA, USA; Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA, USA; Blais Proteomics Center, Dana-Farber Cancer Institute, Boston, MA, USA; Center for Emergent Drug Targets, USA. Electronic address: jarrod_marto@dfci.harvard.edu.
Dana-Farber Cancer Institute · USBrigham and Women's Hospital · USTarget (United States) · US

Funding

Illuminating Function of the Understudied Druggable KinomeU24DK116204 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI JOHNSON, GARY L. · 2017 to 2022
$13.6M
Novel Screening Platform for Discovery of DUB Targeting ProbesR01CA233800 · NCI · DANA-FARBER CANCER INST · PI BUHRLAGE, SARA J, MARTO, JARROD A. · 2019 to 2022
$2.5M
Tools for DUB Drug DiscoveryR21CA247671 · NCI · DANA-FARBER CANCER INST · PI BUHRLAGE, SARA J, MARTO, JARROD A. · 2020 to 2021
$648k
NCI NIH HHS R01 CA233800NCI NIH HHS R21 CA247671NIDDK NIH HHS U24 DK116204
6 · The paper itself

Abstract

As originally described some 40 years ago, protein ubiquitination was thought to serve primarily as a static mark for protein degradation. In the ensuing years, it has become clear that 'ubiquitination' is a structurally diverse and dynamic post-translational modification and is intricately involved in a myriad of signaling pathways in all eukaryote cells. And like other key pathways in the functional proteome, ubiquitin signaling is often disrupted, sometimes severely so, in human pathophysiology. As a result of its central role in normal physiology and human disease, the ubiquitination field is now represented across the full landscape of biomedical research from fundamental structural and biochemical studies to translational and clinical research. In recent years, mass spectrometry has emerged as a powerful technology for the detection and characterization of protein ubiquitination. Herein we detail qualitative and quantitative proteomic methods using a compare/contrast approach to highlight their strengths and weaknesses.

Indexed as

ProteomicsUbiquitinHumansProtein Processing, Post-TranslationalUbiquitinationUbiquitin-Protein LigasesUbiquitinUbiquitin-Protein LigasesdiGly peptidesKεGGMass-spectrometryMiddle-downProteomicsUbiquitin

Identifiers

PMID37121501
PMCPMC10612121
OpenAlexW4367301655

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.