Evidence map›Paper›PMID 27671637›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Adenosine A1 receptor antagonist rolofylline alleviates axonopathy caused by human Tau ΔK280.

Frank J A Dennissen, Marta Anglada-Huguet, Astrid Sydow, Eckhard Mandelkow, Eva-Maria Mandelkow

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
6.1field-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

24 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Article
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  6. Review
  7. Spreading of Tau Protein Does Not Depend on Aggregation Propensity.Journal of molecular neuroscience : MN · 2023
    Article
  8. Article
  9. Article
  10. Alzheimer's disease: an axonal injury disease?Frontiers in aging neuroscience · 2023
    Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Higher CSF Tau Levels Are Related to Hippocampal Hyperactivity and Object Mnemonic Discrimination in Older Adults.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019
    Observational
  17. Propagation of Tau via Extracellular Vesicles.Frontiers in neuroscience · 2019
    Review
  18. Article
  19. Article
  20. 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

5 authors at 3 institutions in 1 country.

Frank J A DennissenGerman Center for Neurodegenerative Diseases, 53127 Bonn, Germany; Center of Advanced European Studies and Research, 53175 Bonn, Germany; frank.dennissen@DZNE.de eva.mandelkow@dzne.de.
Marta Anglada-HuguetGerman Center for Neurodegenerative Diseases, 53127 Bonn, Germany; Max Planck Institute for Metabolism Research, 22607 Hamburg, Germany.
Astrid SydowGerman Center for Neurodegenerative Diseases, 53127 Bonn, Germany; Max Planck Institute for Metabolism Research, 22607 Hamburg, Germany.
Eckhard MandelkowGerman Center for Neurodegenerative Diseases, 53127 Bonn, Germany; Center of Advanced European Studies and Research, 53175 Bonn, Germany; Max Planck Institute for Metabolism Research, 22607 Hamburg, Germany.
Eva-Maria MandelkowGerman Center for Neurodegenerative Diseases, 53127 Bonn, Germany; Center of Advanced European Studies and Research, 53175 Bonn, Germany; Max Planck Institute for Metabolism Research, 22607 Hamburg, Germany frank.dennissen@DZNE.de eva.mandelkow@dzne.de.
German Center for Neurodegenerative Diseases · DEMax Planck Institute for Metabolism Research · DECenter of Advanced European Studies and Research · DE

Funding

Wellcome Trust
6 · The paper itself

Abstract

Accumulation of Tau is a characteristic hallmark of several neurodegenerative diseases but the mode of toxic action of Tau is poorly understood. Here, we show that the Tau protein is toxic due to its aggregation propensity, whereas phosphorylation and/or missorting is not sufficient to cause neuronal dysfunction. Aggregate-prone Tau accumulates, when expressed in vitro at near-endogenous levels, in axons as spindle-shaped grains. These axonal grains contain Tau that is folded in a pathological (MC-1) conformation. Proaggregant Tau induces a reduction of neuronal ATP, concomitant with loss of dendritic spines. Counterintuitively, axonal grains of Tau are not targeted for degradation and do not induce a molecular stress response. Proaggregant Tau causes neuronal and astrocytic hypoactivity and presynaptic dysfunction instead. Here, we show that the adenosine A

Indexed as

Sequence DeletionAdenosine A1 Receptor AntagonistsAdenosine TriphosphateAnimalsAxonsDendritic SpinesDisease Models, AnimalFluorescent Antibody TechniqueGene ExpressionHippocampusHumansMemory, Long-TermMiceMice, TransgenicMitochondriaNeuronsAdenosine A1 Receptor AntagonistsAdenosine TriphosphateProtein Aggregatesrolofyllinetau ProteinsXanthinesaxonshypoactivityrolofyllinetauopathiestreatment

Identifiers

PMID27671637
PMCPMC5068267
OpenAlexW2526669622

What OpenQuestion holds

Textmetadata
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.