Evidence map›Paper›PMID 30919022›Full record

ReviewCellular and molecular life sciences : CMLS2019

Using proteomics to identify ubiquitin ligase-substrate pairs: how novel methods may unveil therapeutic targets for neurodegenerative diseases.

Stephanie L Rayner, Marco Morsch, Mark P Molloy, Bingyang Shi, Roger Chung, Albert Lee

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Ubiquitin system mutations in neurological diseases.Trends in biochemical sciences · 2024
    Review
  3. iScience · 2024
    Article
  4. Article
  5. Article
  6. Insights in Post-Translational Modifications: Ubiquitin and SUMO.International journal of molecular sciences · 2022
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Review
  14. 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

6 authors at 2 institutions in 1 country.

Stephanie L RaynerDepartment of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, 2 Technology Place, Macquarie Park, Sydney, NSW, 2109, Australia.ORCID https://orcid.org/0000-0003-1590-0071
Marco MorschDepartment of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, 2 Technology Place, Macquarie Park, Sydney, NSW, 2109, Australia.ORCID https://orcid.org/0000-0001-9484-8050
Mark P MolloyFaculty of Medicine and Health, Sydney School of Medicine, Royal North Shore Hospital, Pacific Hwy, St Leonards, Sydney, NSW, 2065, Australia.ORCID https://orcid.org/0000-0003-4679-5868
Bingyang ShiDepartment of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, 2 Technology Place, Macquarie Park, Sydney, NSW, 2109, Australia.ORCID https://orcid.org/0000-0002-1043-3163
Roger ChungDepartment of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, 2 Technology Place, Macquarie Park, Sydney, NSW, 2109, Australia.ORCID https://orcid.org/0000-0002-9286-947X
Albert LeeDepartment of Biomedical Sciences, Faculty of Medicine and Health Sciences, Macquarie University, 2 Technology Place, Macquarie Park, Sydney, NSW, 2109, Australia. albert.lee@mq.edu.au.ORCID https://orcid.org/0000-0001-5156-0567
Macquarie University · AURoyal North Shore Hospital · AU

Funding

Cure for MND Foundation GIA 1638Motor Neurone Disease Research Institute of Australia 1628Motor Neurone Disease Research Institute of Australia 1715National Health and Medical Research Council APP1095215National Health and Medical Research Council APP1107644
6 · The paper itself

Abstract

Ubiquitin ligases play an integral role in fine-tuning signaling cascades necessary for normal cell function. Aberrant regulation of ubiquitin ligases has been implicated in several neurodegenerative diseases, generally, due to mutations within the E3 ligase itself. Several proteomic-based methods have recently emerged to facilitate the rapid identification of ligase-substrate pairs-a previously challenging feat due to the transient nature of ligase-substrate interactions. These novel methods complement standard immunoprecipitations (IPs) and include proximity-dependent biotin identification (BioID), ubiquitin ligase-substrate trapping, tandem ubiquitin-binding entities (TUBEs), and a molecular trapping unit known as the NEDDylator. The implementation of these techniques is expected to facilitate the rapid identification of novel substrates of E3 ubiquitin ligases, a process that is likely to enhance our understanding of neurodegenerative diseases and highlight novel therapeutic targets for the treatment of neurodegenerative diseases.

Indexed as

Molecular Targeted TherapyAnimalsHumansNeurodegenerative DiseasesProteomicsSubstrate SpecificityUbiquitinUbiquitinationUbiquitin-Protein LigasesUbiquitinUbiquitin-Protein LigasesBioIDE3 ubiquitin ligasesImmunoprecipitationLigase trappingNEDDylatorProteomicsTUBEUbiquitylation

Identifiers

PMID30919022
PMCPMC11105231
OpenAlexW2924903005

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.