Evidence map›Paper›PMID 32309596›Full record

ReviewDiscoveries (Craiova, Romania)2017

Strains of Pathological Protein Aggregates in Neurodegenerative Diseases.

Xinzhu Wang, Zeinab Noroozian, Madelaine Lynch, Nicholas Armstrong, Raphael Schneider, Mingzhe Liu, Farinaz Ghodrati, Ashley B Zhang, Yoo Jeong Yang, Amanda C Hall and 3 more

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Discoveries (Craiova, Romania), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

13 authors.

Xinzhu WangDepartment of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, Canada.
Zeinab NoroozianDepartment of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, Canada.
Madelaine LynchDepartment of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, Canada.
Nicholas ArmstrongDepartment of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, Canada.
Raphael SchneiderDepartment of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, Canada.
Mingzhe LiuDepartment of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, Canada.
Farinaz GhodratiDepartment of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, Canada.
Ashley B ZhangDepartment of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, Canada.
Yoo Jeong YangDepartment of Pharmacology and Toxicology, University of Toronto, Toronto, ON, Canada.
Amanda C HallDepartment of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, Canada.
Michael SolarskiDepartment of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, Canada.
Samuel A KillackeyDepartment of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, Canada.
Joel C WattsTanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, ON, Canada.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The presence of protein aggregates in the brain is a hallmark of neurodegenerative disorders such as Alzheimer's disease (AD) and Parkinson's disease (PD). Considerable evidence has revealed that the pathological protein aggregates in many neurodegenerative diseases are able to self-propagate, which may enable pathology to spread from cell-to-cell within the brain. This property is reminiscent of what occurs in prion diseases such as Creutzfeldt-Jakob disease. A widely recognized feature of prion disorders is the existence of distinct strains of prions, which are thought to represent unique protein aggregate structures. A number of recent studies have pointed to the existence of strains of protein aggregates in other, more common neurodegenerative illnesses such as AD, PD, and related disorders. In this review, we outline the pathobiology of prion strains and discuss how the concept of protein aggregate strains may help to explain the heterogeneity inherent to many human neurodegenerative disorders.

Indexed as

Alzheimer’s diseaseamyotrophic lateral sclerosisAβCreutzfeldt-Jakob diseaseevolutionParkinson’s diseasePrionSOD1strainstructuretautransmissionyeast prionα-synuclein

Identifiers

PMID32309596
PMCPMC7159837

What OpenQuestion holds

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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.