Evidence map›Paper›PMID 27312603›Full record

ReviewBMB reports2016

Precise assembly and regulation of 26S proteasome and correlation between proteasome dysfunction and neurodegenerative diseases.

Eunju Im, Kwang Chul Chung

Abstract readReview
In one paragraph

Review in BMB reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. Article
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  6. Review
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  13. Regulation of proteasome assembly and activity in health and disease.Nature reviews. Molecular cell biology · 2018
    Review
  14. Article
  15. Article
  16. Article
  17. [Mechanism of heat shock protein 90 for regulating 26S proteasome in hyperthermia].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2016
    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.

Eunju ImDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Korea.
Kwang Chul ChungDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neurodegenerative diseases (NDs) often involve the formation of abnormal and toxic protein aggregates, which are thought to be the primary factor in ND occurrence and progression. Aged neurons exhibit marked increases in aggregated protein levels, which can lead to increased cell death in specific brain regions. As no specific drugs/therapies for treating the symptoms or/and progression of NDs are available, obtaining a complete understanding of the mechanism underlying the formation of protein aggregates is needed for designing a novel and efficient removal strategy. Intracellular proteolysis generally involves either the lysosomal or ubiquitin-proteasome system. In this review, we focus on the structure and assembly of the proteasome, proteasome-mediated protein degradation, and the multiple dynamic regulatory mechanisms governing proteasome activity. We also discuss the plausibility of the correlation between changes in proteasome activity and the occurrence of NDs. [BMB Reports 2016; 49(9): 459-473].

Indexed as

ArchaeaHumansNeurodegenerative DiseasesPhosphorylationProteasome Endopeptidase ComplexProtein SubunitsSumoylationUbiquitination26S proteasome non-ATPase regulatory subunit 13Proteasome Endopeptidase ComplexProtein Subunits

Identifiers

PMID27312603
PMCPMC5227139

What OpenQuestion holds

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LicenceCC BY-NC
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.