Evidence map›Paper›PMID 27824125›Full record

ArticleScientific reports2016

A scFv antibody targeting common oligomeric epitope has potential for treating several amyloidoses.

Jun Zha, Xiang-Meng Liu, Jie Zhu, Shu-Ying Liu, Shuai Lu, Peng-Xin Xu, Xiao-Lin Yu, Rui-Tian Liu

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

20 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Huntington's Disease: Complex Pathogenesis and Therapeutic Strategies.International journal of molecular sciences · 2024
    Review
  9. A Specific Mini-Intrabody Mediates Lysosome Degradation of Mutant Huntingtin.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  10. Review
  11. Current and Possible Future Therapeutic Options for Huntington's Disease.Journal of central nervous system disease · 2022
    Review
  12. Review
  13. Review
  14. Review
  15. The Role of α-Synuclein Oligomers in Parkinson's Disease.International journal of molecular sciences · 2020
    Review
  16. Article
  17. Article
  18. Review
  19. Targeting Alpha-Synuclein as a Therapy for Parkinson's Disease.Frontiers in molecular neuroscience · 2019
    Review
  20. 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

8 authors at 3 institutions in 1 country.

Jun ZhaState Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, China.
Xiang-Meng LiuState Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, China.
Jie ZhuState Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, China.
Shu-Ying LiuState Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, China.
Shuai LuState Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, China.
Peng-Xin XuSchool of Life Science, Ningxia University, Yinchuan, China.
Xiao-Lin YuState Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, China.
Rui-Tian LiuState Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, China.
Institute of Process Engineering · CNNingxia University · CNQilu University of Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Overproduction or poor clearance of amyloids lead to amyloid aggregation and even amyloidosis development. Different amyloids may interact synergistically to promote their aggregation and accelerate pathology in amyloidoses. Amyloid oligomers assembled from different amyloids share common structures and epitopes, and are considered the most toxic species in the pathologic processes of amyloidoses, which suggests that an agent targeting the common epitope of toxic oligomers could provide benefit to several amyloidoses. In this study, we firstly showed that an oligomer-specific single-chain variable fragment antibody, W20 simultaneously improved motor and cognitive function in Parkinson's disease and Huntington's disease mouse models, and attenuated a number of neuropathological features by reducing α-synuclein and mutant huntingtin protein aggregate load and preventing synaptic degeneration. Neuroinflammation and oxidative stress in vivo were also markedly inhibited. The proposed strategy targeting the common epitopes of amyloid oligomers presents promising potential for treating Parkinson's disease, Huntington's disease, Alzheimer's disease, and other amyloidoses.

Indexed as

AmyloidAmyloidosisAnimalsCognitionEpitopesHuntington DiseaseMaleMiceMice, Mutant StrainsMotor ActivityParkinson Disease, SecondarySingle-Chain AntibodiesAmyloidEpitopesSingle-Chain Antibodies

Identifiers

PMID27824125
PMCPMC5100551
OpenAlexW2552414547

What OpenQuestion holds

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Registered trials

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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.