Evidence map›Paper›PMID 28083916›Full record

ReviewBioEssays : news and reviews in molecular, cellular and developmental biology2017

Acetylated tau in Alzheimer's disease: An instigator of synaptic dysfunction underlying memory loss: Increased levels of acetylated tau blocks the postsynaptic signaling required for plasticity and promotes memory deficits associated with tauopathy.

Tara E Tracy, Li Gan

Open access · greenAbstract readReview
In one paragraph

Review in BioEssays : news and reviews in molecular, cellular and developmental biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

35 citing papers in PubMed, 73 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Atlas of lysine acetylation in the mouse.bioRxiv : the preprint server for biology · 2026
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Role of Aβ in Alzheimer's-related synaptic dysfunction.Frontiers in cell and developmental biology · 2022
    Review
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Tara E TracyGladstone Institute of Neurological Disease, San Francisco, CA, USA.
Li GanGladstone Institute of Neurological Disease, San Francisco, CA, USA.
Gladstone Institutes · US

Funding

SIRT1 Limits Microglial Toxicity in Alzheimer's DiseaseR01AG036884 · NIA · J. DAVID GLADSTONE INSTITUTES · PI GAN, LI · 2012 to 2016
$2.0M
The Role of Cathepsin B and Cystatin C in Alzheimer's DiseaseR01AG030207 · NIA · J. DAVID GLADSTONE INSTITUTES · PI GAN, LI · 2010 to 2014
$1.9M
Pathogenic events triggered by tau acetylation in neurodegenerative tauopathyF32AG043301 · NIA · J. DAVID GLADSTONE INSTITUTES · PI TRACY, TARA · 2012 to 2014
$156k
NIA NIH HHS F32 AG043301NIA NIH HHS R01 AG030207NIA NIH HHS R01 AG036884
6 · The paper itself

Abstract

Pathogenesis in tauopathies involves the accumulation of tau in the brain and progressive synapse loss accompanied by cognitive decline. Pathological tau is found at synapses, and it promotes synaptic dysfunction and memory deficits. The specific role of toxic tau in disrupting the molecular networks that regulate synaptic strength has been elusive. A novel mechanistic link between tau toxicity and synaptic plasticity involves the acetylation of two lysines on tau, K274, and K281, which are associated with dementia in Alzheimer's disease (AD). We propose that an increase in tau acetylated on these lysines blocks the expression of long-term potentiation at hippocampal synapses leading to impaired memory in AD. Acetylated tau could inhibit the activity-dependent recruitment of postsynaptic AMPA-type glutamate receptors required for plasticity by interfering with the postsynaptic localization of KIBRA, a memory-associated protein. Strategies that reduce the acetylation of tau may lead to effective treatments for cognitive decline in AD.

Indexed as

Protein Processing, Post-TranslationalAcetylationAlzheimer DiseaseAnimalsBrainDisease Models, AnimalHumansMemory DisordersSynapsesTauopathiestau Proteinstau ProteinsacetylationAlzheimer's diseaseKIBRAlong-term potentiationsynaptic plasticitytau

Identifiers

PMID28083916
PMCPMC5903676
OpenAlexW2576013293

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.