Evidence map›Paper›PMID 28760828›Full record

ArticleThe Journal of biological chemistry2017

An acetylation-phosphorylation switch that regulates tau aggregation propensity and function.

Yari Carlomagno, Dah-Eun Chloe Chung, Mei Yue, Monica Castanedes-Casey, Benjamin J Madden, Judy Dunmore, Jimei Tong, Michael DeTure, Dennis W Dickson, Leonard Petrucelli and 1 more

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
8.6field-weighted citation impact, top 2% 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

80 citing papers in PubMed, 134 citations in OpenAlex.

  1. A complex of MAST1 and 14-3-3η regulates Tau phosphorylation in the developing cortex.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  11. CTE-Type Tau Filaments in Alzheimer's Disease with Co-morbid LATE-NC.bioRxiv : the preprint server for biology · 2025
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20 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

11 authors at 3 institutions in 1 country.

Yari CarlomagnoFrom the Department of Neuroscience, Mayo Clinic, Jacksonville, Florida 32224.
Dah-Eun Chloe ChungFrom the Department of Neuroscience, Mayo Clinic, Jacksonville, Florida 32224.
Mei YueFrom the Department of Neuroscience, Mayo Clinic, Jacksonville, Florida 32224.
Monica Castanedes-CaseyFrom the Department of Neuroscience, Mayo Clinic, Jacksonville, Florida 32224.
Benjamin J Maddenthe Medical Genome Facility Proteomics Core, Mayo Clinic, Rochester, Minnesota 55905.
Judy DunmoreFrom the Department of Neuroscience, Mayo Clinic, Jacksonville, Florida 32224.
Jimei TongFrom the Department of Neuroscience, Mayo Clinic, Jacksonville, Florida 32224.
Michael DeTureFrom the Department of Neuroscience, Mayo Clinic, Jacksonville, Florida 32224.
Dennis W DicksonFrom the Department of Neuroscience, Mayo Clinic, Jacksonville, Florida 32224.
Leonard PetrucelliFrom the Department of Neuroscience, Mayo Clinic, Jacksonville, Florida 32224, petrucelli.leonard@mayo.edu.
Casey CookFrom the Department of Neuroscience, Mayo Clinic, Jacksonville, Florida 32224, cook.casey@mayo.edu.
Mayo Clinic in Florida · USJacksonville College · USMayo Clinic · US

Funding

THE PGRN/TDP-43 AXIS IN ALZHEIMER?S DISEASE AND NEURODEGENERATIONP50AG016574 · NIA · MAYO CLINIC ROCHESTER · PI VEMURI, PRASHANTHI · 1999 to 2018
$36.9M
Expanding insights into FTD disease mechanismsR35NS097273 · NINDS · MAYO CLINIC JACKSONVILLE · PI PETRUCELLI, LEONARD · 2017 to 2024
$10.6M
Project 2: Identifying genes and Pathways that impact Tau Toxicity in FTDU54NS100693 · NINDS · MAYO CLINIC JACKSONVILLE · PI DICKSON, DENNIS WILLIAM · 2016 to 2020
$6.2M
The role of acetylation in regulating pathophysiology of tauR01NS089544 · NINDS · MAYO CLINIC JACKSONVILLE · PI PETRUCELLI, LEONARD, WOLOZIN, BENJAMIN L · 2014 to 2018
$1.9M
Manipulating tau's posttranslational modifications to block disease progression in vivoR21NS094489 · NINDS · MAYO CLINIC JACKSONVILLE · PI COOK, CASEY N · 2015 to 2016
$430k
NIA NIH HHS P50 AG016574NINDS NIH HHS R01 NS089544NINDS NIH HHS R21 NS094489NINDS NIH HHS R35 NS097273NINDS NIH HHS U54 NS100693
6 · The paper itself

Abstract

The aberrant accumulation of tau protein is a pathological hallmark of a class of neurodegenerative diseases known as tauopathies, including Alzheimer's disease and related dementias. On the basis of previous observations that tau is a direct substrate of histone deacetylase 6 (HDAC6), we sought to map all HDAC6-responsive sites in tau and determine how acetylation in a site-specific manner affects tau's biophysical properties

Indexed as

Protein Processing, Post-TranslationalAcetylationAgedAlzheimer DiseaseAmino Acid SubstitutionAnimalsAnimals, NewbornCells, CulturedCerebral CortexFemaleHistone Deacetylase 6Histone Deacetylase InhibitorsHistone DeacetylasesHumansLysineMaleHDAC6 protein, humanHdac6 protein, mouseHistone Deacetylase 6Histone Deacetylase InhibitorsHistone DeacetylasesLysineSerinetau ProteinsacetylationaggregationAlzheimer diseasehistone deacetylase 6 (HDAC6)neurodegenerative diseasephosphorylationtauopathyTau protein (Tau)

Identifiers

PMID28760828
PMCPMC5602388
OpenAlexW2741056309

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.