Evidence map›Paper›PMID 31456657›Full record

ArticleFrontiers in neuroscience2019

EFhd2 Affects Tau Liquid-Liquid Phase Separation.

Irving E Vega, Andrew Umstead, Nicholas M Kanaan

Open access · goldAbstract read
In one paragraph

Article in Frontiers in neuroscience, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
  3. Maturation and Conformational Switching of aJournal of the American Chemical Society · 2024
    Article
  4. Liquid-liquid phase separation in Alzheimer's disease.Journal of molecular medicine (Berlin, Germany) · 2024
    Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Protein interactions: anything new?Essays in biochemistry · 2022
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Liquid-liquid phase separation of tau: From molecular biophysics to physiology and disease.Protein science : a publication of the Protein Society · 2021
    Review
  19. The structure and phase of tau: from monomer to amyloid filament.Cellular and molecular life sciences : CMLS · 2021
    Review
  20. Liquid-Liquid Phase Separation in Crowded Environments.International journal of molecular sciences · 2020
    Review
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 2 institutions in 1 country.

Irving E VegaDepartment of Translational Science and Molecular Medicine, College of Human Medicine, Grand Rapids, MI, United States.
Andrew UmsteadDepartment of Translational Science and Molecular Medicine, College of Human Medicine, Grand Rapids, MI, United States.
Nicholas M KanaanDepartment of Translational Science and Molecular Medicine, College of Human Medicine, Grand Rapids, MI, United States.
Mercy Health Saint Mary's · USUniversity of Michigan–Ann Arbor · US

Funding

Michigan Alzheimer's Disease Core CenterP30AG053760 · NIA · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ALBIN, ROGER L · 2016 to 2020
$10.1M
Tau Conformation in Tauopathies and Neuronal FunctionR01NS082730 · NINDS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI BRADY, SCOTT THOMAS, KANAAN, NICHOLAS M · 2014 to 2023
$7.0M
Tau-induced axonal degeneration in Alzheimer's disease and tauopathiesR01AG044372 · NIA · MICHIGAN STATE UNIVERSITY · PI KANAAN, NICHOLAS M · 2014 to 2018
$1.9M
Tau Conformation in Tauopathies and Neuronal FunctionRF1NS082730 · NINDS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI BRADY, SCOTT THOMAS, KANAAN, NICHOLAS M · 2025 to 2025
$1.6M
NIA NIH HHS P30 AG053760NIA NIH HHS R01 AG044372NINDS NIH HHS R01 NS082730NINDS NIH HHS RF1 NS082730
6 · The paper itself

Abstract

The transition of tau proteins from its soluble physiological conformation to the pathological aggregate forms found in Alzheimer's disease and related dementias, is poorly understood. Therefore, understanding the process that modulates the formation of toxic tau oligomers and their conversion to putative neuroprotective neurofibrillary tangles will lead to better therapeutic strategies. We previously identified that EFhd2 is associated with aggregated tau species in AD brains and the coiled-coil domain in EFhd2 mediates the interaction with tau. To further characterize the association between EFhd2 and tau, we examined whether EFhd2 could affect the liquid-liquid phase separation properties of tau under molecular crowding conditions. We demonstrate that EFhd2 alters tau liquid phase behavior in a calcium and coiled-coil domain dependent manner. Co-incubation of EFhd2 and tau in the absence of calcium leads to the formation of solid-like structures containing both proteins, while in the presence of calcium these two proteins phase separate together into liquid droplets. EFhd2's coiled-coil domain is necessary to alter tau's liquid phase separation, indicating that protein-protein interaction is required. The results demonstrate that EFhd2 affects the liquid-liquid phase separation of tau proteins

Indexed as

Alzheimer’s diseaseEFhd2liquid–liquid phase separationneurodegenerationtautauopathy

Identifiers

PMID31456657
PMCPMC6700279
OpenAlexW2964376886

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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.