Evidence map›Paper›PMID 32709994›Full record

ReviewMolecular psychiatry2021

Remodeling without destruction: non-proteolytic ubiquitin chains in neural function and brain disorders.

Alexis Zajicek, Wei-Dong Yao

Open access · greenAbstract readReview
In one paragraph

Review in Molecular psychiatry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed, 1 pooled it
1.3field-weighted citation impact, top 20% 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, 1 synthesis or guideline pooled it, 24 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. The K63 deubiquitinase CYLD modulates autism-like behaviors and hippocampal plasticity by regulating autophagy and mTOR signaling.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Review
  14. 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 1 institution in 1 country.

Alexis ZajicekDepartments of Psychiatry & Behavioral Sciences, and of Neuroscience & Physiology, State University of New York Upstate Medical University, Syracuse, NY, 13210, USA.
Wei-Dong YaoDepartments of Psychiatry & Behavioral Sciences, and of Neuroscience & Physiology, State University of New York Upstate Medical University, Syracuse, NY, 13210, USA. yaow@upstate.edu.ORCID http://orcid.org/0000-0001-5124-1486
SUNY Upstate Medical University · US

Funding

Investigating Common Molecular Pathogenic Pathways in Frontotemporal Dementia Patients iPSC-Derived NeuronsR01NS057553 · NINDS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI Fen-Biao Gao · 2008 to 2026
$4.5M
Prefrontal AMPA receptors in FTD PathogenesisR01NS093097 · NINDS · UPSTATE MEDICAL UNIVERSITY · PI GAO, FEN-BIAO, YAO, WEI-DONG · 2016 to 2020
$2.4M
Nonproteolytic Polyubiquitin Chains at the SynapseR01MH106489 · NIMH · UPSTATE MEDICAL UNIVERSITY · PI YAO, WEI-DONG · 2015 to 2019
$2.1M
NIMH NIH HHS R01 MH106489NINDS NIH HHS R01 NS057553NINDS NIH HHS R01 NS093097
6 · The paper itself

Abstract

Ubiquitination is a fundamental posttranslational protein modification that regulates diverse biological processes, including those in the CNS. Several topologically and functionally distinct polyubiquitin chains can be assembled on protein substrates, modifying their fates. The classical and most prevalent polyubiquitin chains are those that tag a substrate to the proteasome for degradation, which has been established as a major mechanism driving neural circuit deconstruction and remodeling. In contrast, proteasome-independent non-proteolytic polyubiquitin chains regulate protein scaffolding, signaling complex formation, and kinase activation, and play essential roles in an array of signal transduction processes. Despite being a cornerstone in immune signaling and abundant in the mammalian brain, these non-proteolytic chains are underappreciated in neurons and synapses in the brain. Emerging studies have begun to generate exciting insights about some fundamental roles played by these non-degradative chains in neuronal function and plasticity. In addition, their roles in a number of brain diseases are being recognized. In this article, we discuss recent advances on these nonconventional ubiquitin chains in neural development, function, plasticity, and related pathologies.

Indexed as

UbiquitinationAnimalsBrain DiseasesHumansNeuronsPolyubiquitinProteasome Endopeptidase ComplexPolyubiquitinProteasome Endopeptidase Complex

Identifiers

PMID32709994
PMCPMC9229342
OpenAlexW3045312971

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.