Evidence map›Paper›PMID 32096030›Full record

ReviewAdvances in experimental medicine and biology2019

Tau and Axonal Transport Misregulation in Tauopathies.

Benjamin Combs, Rebecca L Mueller, Gerardo Morfini, Scott T Brady, Nicholas M Kanaan

Open access · greenAbstract readReview
In one paragraph

Review in Advances in experimental medicine and biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
21.6field-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

62 citing papers in PubMed, 82 citations in OpenAlex.

  1. Review
  2. Tau protein as a regulator of mitochondrial function and dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Patient-derived forebrain cortical organoids reveal biphasic tau-MAP6-microtubule axis dysfunction in tauopathy.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026
    Article
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2 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

5 authors at 3 institutions in 1 country.

Benjamin CombsDepartment of Translational Neuroscience, College of Human Medicine, Michigan State University, Grand Rapids, MI, USA.
Rebecca L MuellerDepartment of Translational Neuroscience, College of Human Medicine, Michigan State University, Grand Rapids, MI, USA.
Gerardo MorfiniDepartment of Anatomy and Cell Biology, University of Illinois at Chicago, Chicago, IL, USA.
Scott T BradyDepartment of Anatomy and Cell Biology, University of Illinois at Chicago, Chicago, IL, USA.
Nicholas M KanaanDepartment of Translational Neuroscience, College of Human Medicine, Michigan State University, Grand Rapids, MI, USA. nkanaan@msu.edu.
Michigan State University · USUniversity of Illinois Chicago · USMercy Health Saint Mary's · US

Funding

Tau Conformation in Tauopathies and Neuronal FunctionR01NS082730 · NINDS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI BRADY, SCOTT THOMAS, KANAAN, NICHOLAS M · 2014 to 2023
$7.0M
Tau-induced axonal degeneration in Alzheimer's disease and tauopathiesR01AG044372 · NIA · MICHIGAN STATE UNIVERSITY · PI KANAAN, NICHOLAS M · 2014 to 2018
$1.9M
Integrative Training in the Pharmacological SciencesT32GM092715 · NIGMS · MICHIGAN STATE UNIVERSITY · PI NEUBIG, RICHARD R · 2011 to 2020
$1.5M
NIA NIH HHS R01 AG044372NIGMS NIH HHS T32 GM092715NINDS NIH HHS R01 NS082730
6 · The paper itself

Abstract

Tau is a microtubule-associated protein that is involved in both normal and pathological processes in neurons. Since the discovery and characterization of tau over 40 years ago, our understanding of tau's normal functions and toxic roles in neurodegenerative tauopathies has continued to expand. Fast axonal transport is a critical process for maintaining axons and functioning synapses, critical subcellular compartments underlying neuronal connectivity. Signs of fast axonal transport disruption are pervasive in Alzheimer's disease and other tauopathies and various mechanisms have been proposed for regulation of fast axonal transport by tau. Post-translational modifications of tau including phosphorylation at specific sites, FTDP-17 point mutations, and oligomerization, confer upon tau a toxic effect on fast axonal transport. Consistent with the well-established dependence of axons on fast axonal transport, these disease-related modifications are closely associated temporally and spatially with axonal degeneration in the early disease stages. These factors position tau as a potentially critical factor mediating the disruption of fast axonal transport that precedes synaptic dysfunction and axonal degeneration at later disease stages. In this chapter, we review the evidence that tau affects fast axonal transport and examine several potential mechanisms proposed to underlie this toxicity.

Indexed as

Axonal TransportAlzheimer DiseaseHumansPhosphorylationTauopathiestau Proteinstau ProteinsAlzheimer’s diseaseAxonal transportAxonsKinasesNeurodegenerationPhosphatasesTauopathiesTau protein

Identifiers

PMID32096030
PMCPMC7099581
OpenAlexW3008261604

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.