Evidence map›Paper›PMID 26612725›Full record

ArticleJournal of cellular and molecular medicine2016

Nrdp1S, short variant of Nrdp1, inhibits human glioma progression by increasing Nrdp1-mediated ErbB3 ubiquitination and degradation.

Yuxuan Wu, Lei Wang, Hanmo Bao, Shenshan Zou, Chunling Fu, Hui Gong, Yong Gao, Yuan Tang, Rutong Yu, Hengliang Shi

Open access · goldAbstract read
In one paragraph

Article in Journal of cellular and molecular medicine, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

11 citing papers in PubMed, 13 citations in OpenAlex.

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  6. Ubiquitin ligaseOncology letters · 2019
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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

10 authors at 2 institutions in 1 country.

Yuxuan WuInsititute of Nervous System Diseases, Xuzhou Medical College, Xuzhou, China.
Lei WangInsititute of Nervous System Diseases, Xuzhou Medical College, Xuzhou, China.
Hanmo BaoInsititute of Nervous System Diseases, Xuzhou Medical College, Xuzhou, China.
Shenshan ZouInsititute of Nervous System Diseases, Xuzhou Medical College, Xuzhou, China.
Chunling FuInstitute of Blood Diseases, Xuzhou Medical College, Xuzhou, China.
Hui GongInsititute of Nervous System Diseases, Xuzhou Medical College, Xuzhou, China.
Yong GaoInsititute of Nervous System Diseases, Xuzhou Medical College, Xuzhou, China.
Yuan TangInsititute of Nervous System Diseases, Xuzhou Medical College, Xuzhou, China.
Rutong YuInsititute of Nervous System Diseases, Xuzhou Medical College, Xuzhou, China.
Hengliang ShiInsititute of Nervous System Diseases, Xuzhou Medical College, Xuzhou, China.
Xuzhou Medical College · CNAffiliated Hospital of Xuzhou Medical College · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ubiquitin ligase neuregulin receptor degradation protein 1 (Nrdp1) is involved in the induction of apoptosis and suppression of tumour formation. We previously showed that it was expressed at lower levels in human glioma tissues compared with normal brain tissues. However, the mechanism underlying this is unclear. Here, we reported that a novel short variant (Nrdp1S), lacking 71 amino acids at the N-terminal, was expressed in normal human brain tissue, but absent from glioma tissues. Similar to Nrdp1, Nrdp1S could be degraded by the proteasomal pathway, but exhibited an even longer half-life than Nrdp1. Nrdp1S was also shown to form a heterodimer with Nrdp1, which increased its stability, thereby augmenting the Nrdp1-mediated ubiquitination and degradation of ErbB3. EdU incorporation, MTT assay and in vitro colony formation demonstrated that Nrdp1S significantly inhibited the cell tumourigenicity. These results together suggest that Nrdp1S is a tumour suppressor that which potentiates the Nrdp1-mediated ubiquitination and degradation of ErbB3. An Nrdp1S deficiency may also be an important factor in the loss of Nrdp1.

Indexed as

UbiquitinationBase SequenceBrain NeoplasmsCell Line, TumorCell ProliferationDisease ProgressionGliomaHEK293 CellsHumansProtein IsoformsProtein StabilityProteolysisReceptor, ErbB-3Ubiquitin-Protein LigasesERBB3 protein, humanProtein IsoformsReceptor, ErbB-3RNF41 protein, humanUbiquitin-Protein LigasesErbB3gliomaNrdp1Nrdp1Subiquitination

Identifiers

PMID26612725
PMCPMC4759470
OpenAlexW2177383114

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.