Evidence map›Paper›PMID 26090622›Full record

ArticleToxins2015

Proteasome as a Molecular Target of Microcystin-LR.

Zhu Zhu, Li Zhang, Guoqing Shi

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Toxins, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

1 citing paper in PubMed, 8 citations in OpenAlex.

  1. 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

3 authors at 1 institution in 1 country.

Zhu ZhuSchool of Chemistry and Biological Engineering, University of Science and Technology Beijing, Beijing 100083, China. zhuzhu@ustb.edu.cn.
Li ZhangSchool of Chemistry and Biological Engineering, University of Science and Technology Beijing, Beijing 100083, China. lizhang890125@163.com.
Guoqing ShiSchool of Chemistry and Biological Engineering, University of Science and Technology Beijing, Beijing 100083, China. shiguoqing@ustb.edu.cn.
University of Science and Technology Beijing · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteasome degrades proteins in eukaryotic cells. As such, the proteasome is crucial in cell cycle and function. This study proved that microcystin-LR (MC-LR), which is a toxic by-product of algal bloom, can target cellular proteasome and selectively inhibit proteasome trypsin-like (TL) activity. MC-LR at 1 nM can inhibit up to 54% of the purified 20S proteasome TL activity and 43% of the proteasome TL activity in the liver of the cyprinid rare minnow (Gobiocypris rarus). Protein degradation was retarded in GFP-CL1-transfected PC-3 cells because MC-LR inhibited the proteasome TL activity. Docking studies indicated that MC-LR blocked the active site of the proteasome β2 subunit; thus, the proteasome TL activity was inhibited. In conclusion, MC-LR can target proteasome, selectively inhibit proteasome TL activity, and retard protein degradation. This study may be used as a reference of future research on the toxic mechanism of MC-LR.

Indexed as

AnimalsCell Line, TumorCyprinidaeGreen Fluorescent ProteinsHumansLiverMarine ToxinsMicrocystinsMolecular Docking SimulationProteasome Endopeptidase ComplexProteasome InhibitorsProtein SubunitsProteolysiscyanoginosin LRGreen Fluorescent ProteinsMarine ToxinsMicrocystinsProteasome Endopeptidase ComplexProteasome InhibitorsProtein Subunitsmechanismmicrocystin-LRmolecular dockingproteasome trypsin-like activity

Identifiers

PMID26090622
PMCPMC4488699
OpenAlexW1568258452

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.