Evidence map›Paper›PMID 26041011›Full record

ArticleScientific reports2015

Facilitated Tau Degradation by USP14 Aptamers via Enhanced Proteasome Activity.

Jung Hoon Lee, Seung Kyun Shin, Yanxialei Jiang, Won Hoon Choi, Chaesun Hong, Dong-Eun Kim, Min Jae Lee

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

38 citing papers in PubMed, 66 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. AKT and DUBs: a bidirectional relationship.Cellular & molecular biology letters · 2025
    Review
  5. Tau degradation in Alzheimer's disease: Mechanisms and therapeutic opportunities.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025
    Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Concept and application of circulating proteasomes.Experimental & molecular medicine · 2021
    Review
  18. Article
  19. Article
  20. The Antipsychotic Drug Clozapine Suppresses the RGS4 Polyubiquitylation and Proteasomal Degradation Mediated by the Arg/N-Degron Pathway.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2021
    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

7 authors at 3 institutions in 1 country.

Jung Hoon LeeDepartment of Biochemistry and Molecular Biology, Neuroscience Research Institute, Seoul National University College of Medicine, Seoul 110-799, Republic of Korea.
Seung Kyun ShinDepartment of Applied Chemistry, College of Applied Sciences, Kyung Hee University, Yongin 446-701, Republic of Korea.
Yanxialei JiangDepartment of Applied Chemistry, College of Applied Sciences, Kyung Hee University, Yongin 446-701, Republic of Korea.
Won Hoon ChoiDepartment of Biochemistry and Molecular Biology, Neuroscience Research Institute, Seoul National University College of Medicine, Seoul 110-799, Republic of Korea.
Chaesun HongDepartment of Bioscience and Biotechnology, Konkuk University, Seoul 143-701, Republic of Korea.
Dong-Eun KimDepartment of Bioscience and Biotechnology, Konkuk University, Seoul 143-701, Republic of Korea.
Min Jae LeeDepartment of Biochemistry and Molecular Biology, Neuroscience Research Institute, Seoul National University College of Medicine, Seoul 110-799, Republic of Korea.
Konkuk University · KRKyung Hee University · KRSeoul National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ubiquitin-proteasome system (UPS) is the primary mechanism by which intracellular proteins, transcription factors, and many proteotoxic proteins with aggregation-prone structures are degraded. The UPS is reportedly downregulated in various neurodegenerative disorders, with increased proteasome activity shown to be beneficial in many related disease models. Proteasomes function under tonic inhibitory conditions, possibly via the ubiquitin chain-trimming function of USP14, a proteasome-associated deubiquitinating enzyme (DUB). We identified three specific RNA aptamers of USP14 (USP14-1, USP14-2, and USP14-3) that inhibited its deubiquitinating activity. The nucleotide sequences of these non-cytotoxic USP14 aptamers contained conserved GGAGG motifs, with G-rich regions upstream, and similar secondary structures. They efficiently elevated proteasomal activity, as determined by the increased degradation of small fluorogenic peptide substrates and physiological polyubiquitinated Sic1 proteins. Additionally, proteasomal degradation of tau proteins was facilitated in the presence of the UPS14 aptamers in vitro. Our results indicate that these novel inhibitory UPS14 aptamers can be used to enhance proteasome activity, and to facilitate the degradation of proteotoxic proteins, thereby protecting cells from various neurodegenerative stressors.

Indexed as

Aptamers, NucleotideBase SequenceCell LineCells, CulturedHumansNucleic Acid ConformationOxidative StressProteasome Endopeptidase ComplexProtein BindingProteolysisRecombinant ProteinsSELEX Aptamer TechniqueSubstrate Specificitytau ProteinsUbiquitinationUbiquitin ThiolesteraseAptamers, NucleotideProteasome Endopeptidase ComplexRecombinant Proteinstau ProteinsUbiquitin ThiolesteraseUSP14 protein, human

Identifiers

PMID26041011
PMCPMC4455164
OpenAlexW590305535

What OpenQuestion 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 OpenQuestion graph.