Evidence map›Paper›PMID 35159365›Full record

ReviewCells2022

Deubiquitinases in Neurodegeneration.

Abudu I Bello, Rituparna Goswami, Shelby L Brown, Kara Costanzo, Taylor Shores, Shefaa Allan, Revan Odah, Ryan D Mohan

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
3.7field-weighted citation impact, top 5% 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

21 citing papers in PubMed, 1 synthesis or guideline pooled it, 42 citations in OpenAlex.

  1. International journal of molecular sciences · 2025
    Pooled it
  2. Glycine Alleviates HMolecular neurobiology · 2026
    Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. The role of deubiquitinases in cardiac disease.Expert reviews in molecular medicine · 2024
    Review
  11. Review
  12. Review
  13. Article
  14. Review
  15. Review
  16. Review
  17. Review
  18. Review
  19. Neurodegenerative Disorder Risk in Krabbe Disease Carriers.International journal of molecular sciences · 2022
    Article
  20. 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

8 authors at 1 institution in 1 country.

Abudu I BelloDivision of Biological and Biomedical Systems, School of Science and Engineering, University of Missouri-Kansas City, Kansas City, MO 64110, USA.
Rituparna GoswamiDivision of Biological and Biomedical Systems, School of Science and Engineering, University of Missouri-Kansas City, Kansas City, MO 64110, USA.
Shelby L BrownDivision of Biological and Biomedical Systems, School of Science and Engineering, University of Missouri-Kansas City, Kansas City, MO 64110, USA.
Kara CostanzoDivision of Biological and Biomedical Systems, School of Science and Engineering, University of Missouri-Kansas City, Kansas City, MO 64110, USA.
Taylor ShoresDivision of Biological and Biomedical Systems, School of Science and Engineering, University of Missouri-Kansas City, Kansas City, MO 64110, USA.
Shefaa AllanDivision of Biological and Biomedical Systems, School of Science and Engineering, University of Missouri-Kansas City, Kansas City, MO 64110, USA.
Revan OdahDivision of Biological and Biomedical Systems, School of Science and Engineering, University of Missouri-Kansas City, Kansas City, MO 64110, USA.
Ryan D MohanDivision of Biological and Biomedical Systems, School of Science and Engineering, University of Missouri-Kansas City, Kansas City, MO 64110, USA.ORCID 0000-0002-7624-4605
University of Missouri–Kansas City · US

Funding

Mechanism and effects of communication between actin and gene regulatory complexesR01NS117539 · NINDS · WAYNE STATE UNIVERSITY · PI MOHAN, RYAN DAVID · 2021 to 2025
$1.9M
NIH HHS 1R01NS117539-01A1NINDS NIH HHS R01 NS117539
6 · The paper itself

Abstract

Ubiquitination refers to the conjugation of the ubiquitin protein (a small protein highly conserved among eukaryotes) to itself or to other proteins through differential use of ubiquitin's seven internal linkage sites or the amino-terminal amino group. By creating different chain lengths, an enormous proteomic diversity may be formed. This creates a signaling system that is central to controlling almost every conceivable protein function, from proteostasis to regulating enzyme function and everything in between. Protein ubiquitination is reversed through the activity of deubiquitinases (DUBs), enzymes that function to deconjugate ubiquitin from itself and protein substrates. DUBs are regulated through several mechanisms, from controlled subcellular localization within cells to developmental and tissue specific expression. Misregulation of DUBs has been implicated in several diseases including cancer and neurodegeneration. Here we present a brief overview of the role of DUBs in neurodegeneration, and as potential therapeutic targets.

Indexed as

Deubiquitinating EnzymesHumansNeurodegenerative DiseasesDeubiquitinating EnzymesdeubiquitinaseDrosophilaneurodegenerationubiquitinubiquitin-specific protease

Identifiers

PMID35159365
PMCPMC8834042
OpenAlexW4210481979

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.