Evidence map›Paper›PMID 18588978›Full record

ArticleNeurobiology of disease2008

Pre-assembled tau filaments phosphorylated by GSK-3b form large tangle-like structures.

Carolyn A Rankin, Qian Sun, T Chris Gamblin

Open access · greenAbstract read
In one paragraph

Article in Neurobiology of disease, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Non-Proteasomal UbL-UbA Family of Proteins in Neurodegeneration.International journal of molecular sciences · 2019
    Review
  6. Article
  7. Article
  8. In vitro aggregation assays using hyperphosphorylated tau protein.Journal of visualized experiments : JoVE · 2015
    Article
  9. Protein phosphorylation in neurodegeneration: friend or foe?Frontiers in molecular neuroscience · 2014
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
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.

Carolyn A RankinDepartment of Molecular Biosciences, University of Kansas, 1200 Sunnyside Avenue, Lawrence, KS 66045, USA.
Qian Sun
T Chris Gamblin
University of Kansas · US

Funding

Modulation of Tau function by AD-type PhosphorylationR01AG022428 · NIA · UNIVERSITY OF KANSAS LAWRENCE · PI GAMBLIN, TRUMAN C · 2003 to 2007
$1.4M
Tau polymerization as a target for Alzheimer's diseaseK02AG025898 · NIA · UNIVERSITY OF KANSAS LAWRENCE · PI GAMBLIN, TRUMAN C · 2006 to 2010
$510k
NIA NIH HHS AG022428NIA NIH HHS AG025898NIA NIH HHS K02 AG025898NIA NIH HHS R01 AG022428
6 · The paper itself

Abstract

Hyperphosphorylated tau protein is a major component of neurofibrillary tangles, a prominent intracellular hallmark of Alzheimer's disease. Both hyperphosphorylated tau and neurofibrillary tangles have been shown to correlate with dementia in Alzheimer's disease, but the relationship between hyperphosphorylation and tangle formation is not clear. Using a cell-free in vitro model system, in which tau polymerization is induced by arachidonic acid, we show that GSK-3beta phosphorylation of pre-assembled tau filaments makes those filaments prone to coalesce into large neurofibrillary tangle-like structures. Five phosphorylation sites, S199, T205, T231, S396 and S404, were identified in the phosphorylated filaments; many of the five are within epitopes recognized by Alzheimer's disease-associated antibodies. These tangle-like structures are optically visible and are similar to those formed by polymerization of GSK-3beta phosphorylated tau monomer and to those isolated from Alzheimer's disease tissue. We conclude that the phosphorylation of tau by GSK-3beta either prior to or following polymerization promotes polymer/polymer interactions that result in stable clusters of tau filaments.

Indexed as

Alzheimer DiseaseBrainCatalytic DomainCell-Free SystemEpitopesGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaHumansModels, BiologicalNeurofibrillary TanglesNeuronsPhosphorylationPolymersProtein Bindingtau ProteinsEpitopesGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaGSK3B protein, humanPolymerstau Proteins

Identifiers

PMID18588978
PMCPMC2607042
OpenAlexW2079100944

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.