Evidence map›Paper›PMID 29233753›Full record

ReviewTrends in molecular medicine2018

Targeting the 26S Proteasome To Protect Against Proteotoxic Diseases.

Natura Myeku, Karen E Duff

Abstract readReview
In one paragraph

Review in Trends in molecular medicine, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed, 1 pooled it
2.5field-weighted citation impact, top 10% 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

25 citing papers in PubMed, 1 synthesis or guideline pooled it, 57 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Impairment of Proteasome Function in Podocytes Leads to CKD.Journal of the American Society of Nephrology : JASN · 2021
    Article
  13. Article
  14. Tauopathies: Deciphering Disease Mechanisms to Develop Effective Therapies.International journal of molecular sciences · 2020
    Review
  15. Review
  16. Article
  17. Article
  18. 15-Deoxy-ΔThe Journal of biological chemistry · 2019
    Article
  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 1 institution in 1 country.

Natura MyekuDepartment of Pathology and Cell Biology, The Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University Medical Center, New York, NY, USA. Electronic address: nm2631@cumc.columbia.edu.
Karen E DuffDepartment of Pathology and Cell Biology, The Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University Medical Center, New York, NY, USA; Division of Integrative Neuroscience, New York State Psychiatric Institute, New York, NY, USA. Electronic address: ked2115@cumc.columbia.edu.
Columbia University Irving Medical Center · US

Funding

Tauopathy in AD and FTD - Molecular Determinants of Phenotypic DiversityRF1AG056151 · NIA · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI CARLSON, GEORGE A., DUFF, KAREN · 2017 to 2017
$4.1M
The Role of Synaptic Proteolysis in Alzheimer's Disease and Therapeutic ImplicationsR01AG064244 · NIA · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI MYEKU, NATURA · 2019 to 2023
$2.8M
Receptor-mediated clearance of synaptic tau as a novel therapy for Alzheimer's disease.K01AG055694 · NIA · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI MYEKU, NATURA · 2017 to 2022
$745k
NIA NIH HHS K01 AG055694NIA NIH HHS R01 AG064244NIA NIH HHS RF1 AG056151
6 · The paper itself

Abstract

Aggregates of misfolded proteins can compromise the function of the 26S proteasome complex, leaving neurons susceptible to accelerated and impaired protein homeostasis, thereby contributing to the pathogenesis of neurodegeneration. Strategies aimed at enhancing the function of the 26S proteasome via phosphorylation of key subunit epitopes have been effective in reducing protein aggregates in mouse models of disease. We discuss how phosphodiesterase (PDE) inhibitors and G protein-coupled receptor (GPCR)-targeted drugs might be considered as candidate therapeutics, acting on second messenger signal transduction. The range of candidates might address the need for region-, cell-, or even cellular compartment-specific modulation. Given the array of clinical and experimental drugs targeting cAMP/cGMP signaling, we propose that proteasome activators targeting secondary messengers might be exploited as novel agents for the treatment or prevention of some neurodegenerative diseases.

Indexed as

AnimalsDrug DiscoveryEnzyme ActivatorsHumansMolecular Targeted TherapyNeurodegenerative DiseasesPhosphodiesterase InhibitorsPhosphorylationProteasome Endopeptidase ComplexProteolysisReceptors, G-Protein-CoupledSignal TransductionUbiquitinATP dependent 26S proteaseEnzyme ActivatorsPhosphodiesterase InhibitorsProteasome Endopeptidase ComplexReceptors, G-Protein-CoupledUbiquitin

Identifiers

PMID29233753
PMCPMC5905406
OpenAlexW2773477944

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.