Evidence map›Paper›PMID 28506438›Full record

ReviewBiological psychiatry2018

Prion-like Spreading in Tauopathies.

Jacob I Ayers, Benoit I Giasson, David R Borchelt

Abstract readReview
In one paragraph

Review in Biological psychiatry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

65 citing papers in PubMed, 104 citations in OpenAlex.

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5 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Jacob I AyersDepartment of Neuroscience, University of Florida, Gainesville, Florida; Center for Translational Research in Neurodegenerative Disease, University of Florida, Gainesville, Florida; McKnight Brain Institute, University of Florida, Gainesville, Florida.
Benoit I GiassonDepartment of Neuroscience, University of Florida, Gainesville, Florida; Center for Translational Research in Neurodegenerative Disease, University of Florida, Gainesville, Florida; McKnight Brain Institute, University of Florida, Gainesville, Florida.
David R BorcheltDepartment of Neuroscience, University of Florida, Gainesville, Florida; Center for Translational Research in Neurodegenerative Disease, University of Florida, Gainesville, Florida; McKnight Brain Institute, University of Florida, Gainesville, Florida. Electronic address: drb1@ufl.edu.
University of Florida · US

Funding

University of Florida - Mt. Sinai Medical Center AD Research CenterP50AG047266 · NIA · UNIVERSITY OF FLORIDA · PI FEBO, MARCELO · 2015 to 2019
$7.3M
NIA NIH HHS P50 AG047266
6 · The paper itself

Abstract

Tau is a microtubule-associated protein that functions in regulating cytoskeleton dynamics, especially in neurons. Misfolded and aggregated forms of tau produce pathological structures in a number of neurodegenerative diseases, including Alzheimer's disease (AD) and tauopathy dementias. These disorders can present with a sporadic etiology, such as in AD, or a familial etiology, such as in some cases of frontotemporal dementia with parkinsonism. Notably, the pathological features of tau pathology in these diseases can be very distinct. For example, the tau pathology in corticobasal degeneration is distinct from that of an AD patient. A wealth of evidence has emerged within the last decade to suggest that the misfolded tau in tauopathies possesses prion-like features and that such features may explain the diverse characteristics of tauopathies. The prion-like concept for tauopathies arose initially from the observation that the progressive accumulation of tau pathology as the symptoms of AD progress seemed to follow anatomically linked pathways. Subsequent studies in cell and animal models revealed that misfolded tau can propagate from cell to cell and from region to region in the brain through direct neuroanatomical connections. Studies in these cell and mouse models have demonstrated that experimentally propagated forms of misfolded tau can exist as conformationally distinct "strains" with unique biochemical, morphological, and neuropathological characteristics. This review discusses the clinical, pathological, and genetic diversity of tauopathies and the discoveries underlying the emerging view that the unique features of clinically distinct tauopathies may be a reflection of the strain of misfolded tau that propagates in each disease.

Indexed as

AnimalsHumansPrionsTauopathiestau ProteinsPrionstau ProteinsAlzheimer’s diseaseAnimal modelsPrionStrainsTauTransmission

Identifiers

PMID28506438
PMCPMC5640465
OpenAlexW2606978132

What OpenQuestion holds

Textmetadata
LicenceTDM
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.