Evidence map›Paper›PMID 30605723›Full record

ReviewProgress in neurobiology2019

It's all about tau.

Cheril Tapia-Rojas, Fabian Cabezas-Opazo, Carol A Deaton, Erick H Vergara, Gail V W Johnson, Rodrigo A Quintanilla

Abstract readReview
In one paragraph

Review in Progress in neurobiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
9.6field-weighted citation impact, top 1% 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

97 citing papers in PubMed, 186 citations in OpenAlex.

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  9. PI31 expression is neuroprotective in a mouse model of early-onset parkinsonism.Proceedings of the National Academy of Sciences of the United States of America · 2025
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37 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

6 authors at 3 institutions in 2 countries.

Cheril Tapia-RojasLaboratory of Neurobiology of Aging, Centro de Biología Celular y Biomedicina (CEBICEM), Universidad San Sebastián, Santiago, Chile.
Fabian Cabezas-OpazoLaboratory of Neurodegenerative Diseases, Centro de Investigación Biomédica, Universidad Autónoma de Chile, Santiago, Chile.
Carol A DeatonDepartment of Anesthesiology and Perioperative Medicine, University of Rochester Medical Center, NY, USA.
Erick H VergaraLaboratory of Neurodegenerative Diseases, Centro de Investigación Biomédica, Universidad Autónoma de Chile, Santiago, Chile.
Gail V W JohnsonDepartment of Anesthesiology and Perioperative Medicine, University of Rochester Medical Center, NY, USA.
Rodrigo A QuintanillaLaboratory of Neurodegenerative Diseases, Centro de Investigación Biomédica, Universidad Autónoma de Chile, Santiago, Chile; Centro de Investigación y Estudio del Consumo de Alcohol en Adolescentes (CIIA), Santiago, Chile. Electronic address: rodrigo.quintanilla@uautonoma.cl.
Universidad Autónoma de Chile · CLUniversity of Rochester Medical Center · USSan Sebastián University · CL

Funding

The degradation of tau by selective autophagyR01NS098769 · NINDS · UNIVERSITY OF ROCHESTER · PI JOHNSON, GAIL V. W. · 2017 to 2020
$1.8M
Autophagy, p62 and the Nrf2 Intersect to Protect Against Tau ToxicityR21NS076789 · NINDS · UNIVERSITY OF ROCHESTER · PI JOHNSON, GAIL V. W. · 2012 to 2013
$418k
NINDS NIH HHS R01 NS098769NINDS NIH HHS R21 NS076789
6 · The paper itself

Abstract

Tau is a protein that is highly enriched in neurons and was originally defined by its ability to bind and stabilize microtubules. However, it is now becoming evident that the functions of tau extend beyond its ability to modulate microtubule dynamics. Tau plays a role in mediating axonal transport, synaptic structure and function, and neuronal signaling pathways. Although tau plays important physiological roles in neurons, its involvement in neurodegenerative diseases, and most prominently in the pathogenesis of Alzheimer disease (AD), has directed the majority of tau studies. However, a thorough knowledge of the physiological functions of tau and its post-translational modifications under normal conditions are necessary to provide the foundation for understanding its role in pathological settings. In this review, we will focus on human tau, summarizing tau structure and organization, as well as its posttranslational modifications associated with physiological processes. We will highlight possible mechanisms involved in mediating the turnover of tau and finally discuss newly elucidated tau functions in a physiological context.

Indexed as

BrainHumanstau Proteinstau ProteinsAxonal transportDendritesMicrotubulesPosttranslational modificationsTau

Identifiers

PMID30605723
PMCPMC6397676
OpenAlexW2908092937

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.