Evidence map›Paper›PMID 31432317›Full record

ArticleNeuroscience bulletin2019

Gedunin Degrades Aggregates of Mutant Huntingtin Protein and Intranuclear Inclusions via the Proteasomal Pathway in Neurons and Fibroblasts from Patients with Huntington's Disease.

Weiqi Yang, Jingmo Xie, Qiang Qiang, Li Li, Xiang Lin, Yiqing Ren, Wenlei Ren, Qiong Liu, Guomin Zhou, Wenshi Wei and 2 more

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

Article in Neuroscience bulletin, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.8field-weighted citation impact, top 34% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Review
  3. A Novel SPAST Mutation Results in Spastin Accumulation and Defects in Microtubule Dynamics.Movement disorders : official journal of the Movement Disorder Society · 2022
    Article
  4. Review
  5. Article
  6. Review
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

12 authors at 5 institutions in 1 country.

Weiqi YangDepartment of Anatomy, Histology and Embryology, School of Basic Medical Sciences, Fudan University, Shanghai, 200032, China.
Jingmo XieDepartment of Anatomy, Histology and Embryology, Zhaoqing Medical College, Zhaoqing, 526000, China.
Qiang QiangDepartment of Neurology, Huadong Hospital, Fudan University, Shanghai, 200040, China.
Li LiDepartment of Anesthesiology, Huashan Hospital, Fudan University, Shanghai, 200040, China.
Xiang LinDepartment of Neurology and Institute of Neurology, First Affiliated Hospital, Fujian Medical University, Fuzhou, 350005, China.
Yiqing RenDepartment of Neurology, Huadong Hospital, Fudan University, Shanghai, 200040, China.
Wenlei RenDepartment of Neurology, Huadong Hospital, Fudan University, Shanghai, 200040, China.
Qiong LiuDepartment of Anatomy, Histology and Embryology, School of Basic Medical Sciences, Fudan University, Shanghai, 200032, China.
Guomin ZhouDepartment of Anatomy, Histology and Embryology, School of Basic Medical Sciences, Fudan University, Shanghai, 200032, China.
Wenshi WeiDepartment of Neurology, Huadong Hospital, Fudan University, Shanghai, 200040, China.
Hexige SaiyinSchool of Life Sciences, Fudan University, Shanghai, 200438, China. saiyin@fudan.edu.cn.
Lixiang MaDepartment of Anatomy, Histology and Embryology, School of Basic Medical Sciences, Fudan University, Shanghai, 200032, China. lxma@fudan.edu.cn.
Fudan University · CNHuadong Hospital · CNFirst Affiliated Hospital of Fujian Medical University · CNHuashan Hospital · CNZhaoqing University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Huntington's disease (HD) is a deadly neurodegenerative disease with abnormal expansion of CAG repeats in the huntingtin gene. Mutant Huntingtin protein (mHTT) forms abnormal aggregates and intranuclear inclusions in specific neurons, resulting in cell death. Here, we tested the ability of a natural heat-shock protein 90 inhibitor, Gedunin, to degrade transfected mHTT in Neuro-2a cells and endogenous mHTT aggregates and intranuclear inclusions in both fibroblasts from HD patients and neurons derived from induced pluripotent stem cells from patients. Our data showed that Gedunin treatment degraded transfected mHTT in Neuro-2a cells, endogenous mHTT aggregates and intranuclear inclusions in fibroblasts from HD patients, and in neurons derived from induced pluripotent stem cells from patients in a dose- and time-dependent manner, and its activity depended on the proteasomal pathway rather than the autophagy route. These findings also showed that although Gedunin degraded abnormal mHTT aggregates and intranuclear inclusions in cells from HD patient, it did not affect normal cells, thus providing a new perspective for using Gedunin to treat HD.

Indexed as

AnimalsCell Culture TechniquesFibroblastsHeat-Shock ProteinsHumansHuntingtin ProteinHuntington DiseaseInduced Pluripotent Stem CellsIntranuclear Inclusion BodiesLeupeptinsLimoninsMiceMutant ProteinsMutationNeuronsProteasome Endopeptidase Complexbenzyloxycarbonylleucyl-leucyl-leucine aldehydegeduninHeat-Shock ProteinsHuntingtin ProteinLeupeptinsLimoninsMutant ProteinsProteasome Endopeptidase ComplexProtein AggregatesDegradationGeduninHuntington’s diseaseMutant Huntingtin protein

Identifiers

PMID31432317
PMCPMC6864009
OpenAlexW2969459503

What OpenQuestion holds

Textmetadata
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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.