Evidence map›Paper›PMID 33608634›Full record

ArticleCommunications biology2021

Development of an α-synuclein knockdown peptide and evaluation of its efficacy in Parkinson's disease models.

Jack Wuyang Jin, Xuelai Fan, Esther Del Cid-Pellitero, Xing-Xing Liu, Limin Zhou, Chunfang Dai, Ebrima Gibbs, Wenting He, Hongjie Li, Xiaobin Wu and 9 more

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

Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed, 1 pooled it
2.2field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 1 synthesis or guideline pooled it, 29 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
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  5. Review
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  7. Review
  8. Review
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  11. Article
  12. aSynPEP-DB: a database of biogenic peptides for inhibiting α-synuclein aggregation.Database : the journal of biological databases and curation · 2023
    Article
  13. Review
  14. Article
  15. Alpha Synuclein: Neurodegeneration and Inflammation.International journal of molecular sciences · 2023
    Review
  16. Review
  17. 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

19 authors at 3 institutions in 2 countries.

Jack Wuyang Jin *The Djavad Mowafaghian Centre for Brain Health and Department of Medicine, University of British Columbia, Vancouver, BC, Canada.
Xuelai Fan *The Djavad Mowafaghian Centre for Brain Health and Department of Medicine, University of British Columbia, Vancouver, BC, Canada.
Esther Del Cid-Pellitero *McGill Parkinson Program, Neurodegenerative Diseases Group, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC, Canada.
Xing-Xing LiuMcGill Parkinson Program, Neurodegenerative Diseases Group, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC, Canada.
Limin ZhouMinistry of Education Key Laboratory of Child Development and Disorders, Children's Hospital of Chongqing Medical University, Chongqing, China.
Chunfang DaiMinistry of Education Key Laboratory of Child Development and Disorders, Children's Hospital of Chongqing Medical University, Chongqing, China.
Ebrima GibbsThe Djavad Mowafaghian Centre for Brain Health and Department of Medicine, University of British Columbia, Vancouver, BC, Canada.
Wenting HeMinistry of Education Key Laboratory of Child Development and Disorders, Children's Hospital of Chongqing Medical University, Chongqing, China.
Hongjie LiMinistry of Education Key Laboratory of Child Development and Disorders, Children's Hospital of Chongqing Medical University, Chongqing, China.
Xiaobin WuMinistry of Education Key Laboratory of Child Development and Disorders, Children's Hospital of Chongqing Medical University, Chongqing, China.
Austin HillDepartment of Medical Genetics, Centre for Molecular Medicine and Therapeutics, University of British Columbia, Vancouver, BC, Canada.
Blair R LeavittDepartment of Medical Genetics, Centre for Molecular Medicine and Therapeutics, University of British Columbia, Vancouver, BC, Canada.ORCID 0000-0002-4532-766X
Neil CashmanThe Djavad Mowafaghian Centre for Brain Health and Department of Medicine, University of British Columbia, Vancouver, BC, Canada.ORCID 0000-0002-0080-1006
Lidong LiuThe Djavad Mowafaghian Centre for Brain Health and Department of Medicine, University of British Columbia, Vancouver, BC, Canada.
Jie LuThe Djavad Mowafaghian Centre for Brain Health and Department of Medicine, University of British Columbia, Vancouver, BC, Canada.
Thomas M DurcanMcGill Parkinson Program, Neurodegenerative Diseases Group, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC, Canada.
Zhifang DongMinistry of Education Key Laboratory of Child Development and Disorders, Children's Hospital of Chongqing Medical University, Chongqing, China. zfdong@aliyun.com.ORCID 0000-0002-3411-7923
Edward A FonMcGill Parkinson Program, Neurodegenerative Diseases Group, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC, Canada. ted.fon@mcgill.ca.ORCID 0000-0002-5520-6239
Yu Tian WangThe Djavad Mowafaghian Centre for Brain Health and Department of Medicine, University of British Columbia, Vancouver, BC, Canada. ytwang@brain.ubc.ca.ORCID 0000-0001-8592-0698
University of British Columbia · CAChina International Science and Technology Cooperation · CNMontreal Neurological Institute and Hospital · CA

Funding

CIHR
6 · The paper itself

Abstract

Convincing evidence supports the premise that reducing α-synuclein levels may be an effective therapy for Parkinson's disease (PD); however, there has been lack of a clinically applicable α-synuclein reducing therapeutic strategy. This study was undertaken to develop a blood-brain barrier and plasma membrane-permeable α-synuclein knockdown peptide, Tat-βsyn-degron, that may have therapeutic potential. The peptide effectively reduced the level of α-synuclein via proteasomal degradation both in cell cultures and in animals. Tat-βsyn-degron decreased α-synuclein aggregates and microglial activation in an α-synuclein pre-formed fibril model of spreading synucleinopathy in transgenic mice overexpressing human A53T α-synuclein. Moreover, Tat-βsyn-degron reduced α-synuclein levels and significantly decreased the parkinsonian toxin-induced neuronal damage and motor impairment in a mouse toxicity model of PD. These results show the promising efficacy of Tat-βsyn-degron in two different animal models of PD and suggest its potential use as an effective PD therapeutic that directly targets the disease-causing process.

Indexed as

alpha-SynucleinAnimalsAntiparkinson AgentsBehavior, AnimalBrainDisease Models, AnimalDown-RegulationHEK293 CellsHumansMaleMiceMice, Inbred C57BLMice, TransgenicMotor ActivityMPTP PoisoningMutationalpha-SynucleinAntiparkinson AgentsPeptidesProteasome Endopeptidase ComplexSNCA protein, humanSnca protein, mouse

Identifiers

PMID33608634
PMCPMC7895943
OpenAlexW3129200898

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.