Evidence map›Paper›PMID 26834532›Full record

ReviewFrontiers in neuroscience2016

The Metamorphic Nature of the Tau Protein: Dynamic Flexibility Comes at a Cost.

Jonathan J Sabbagh, Chad A Dickey

Abstract readReview
In one paragraph

Review in Frontiers in neuroscience, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Review
  2. Review
  3. Thionine modulates tau phosphorylation in an Alzheimer's disease cell culture model.Turkish journal of biology = Turk biyoloji dergisi · 2025
    Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Tau: A Signaling Hub Protein.Frontiers in molecular neuroscience · 2021
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. The Dark Matter of Biology.Biophysical journal · 2016
    Review
  17. Article
  18. 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

2 authors.

Jonathan J SabbaghDepartment of Molecular Medicine, Byrd Alzheimer's Research Institute, University of South Florida Tampa, FL, USA.
Chad A DickeyDepartment of Molecular Medicine, Byrd Alzheimer's Research Institute, University of South Florida Tampa, FL, USA.

Funding

The Hsp90 cochaperone FKBP51 regulates tau structure and functionR01NS073899 · NINDS · UNIVERSITY OF SOUTH FLORIDA · PI Laura J Blair · 2011 to 2026
$6.9M
NINDS NIH HHS R01 NS073899
6 · The paper itself

Abstract

Accumulation of the microtubule associated protein tau occurs in several neurodegenerative diseases including Alzheimer's disease (AD). The tau protein is intrinsically disordered, giving it unique structural properties that can be dynamically altered by post-translational modifications such as phosphorylation and cleavage. Over the last decade, technological advances in nuclear magnetic resonance (NMR) spectroscopy and structural modeling have permitted more in-depth insights into the nature of tau. These studies have helped elucidate how metamorphism of tau makes it ideally suited for dynamic microtubule regulation, but how it also facilitates tau self-assembly, oligomerization, and neurotoxicity. This review will focus on how the distinct structure of tau governs its function, accumulation, and toxicity as well as how other cellular factors such as molecular chaperones control these processes.

Indexed as

microtubulesneurodegenerative diseasesNMRstructuretau

Identifiers

PMID26834532
PMCPMC4720746

What OpenQuestion holds

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Registered trials

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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.