Evidence map›Paper›PMID 33304310›Full record

ReviewFrontiers in neurology2020

Cellular Biology of Tau Diversity and Pathogenic Conformers.

Sang-Gyun Kang, Ghazaleh Eskandari-Sedighi, Lenka Hromadkova, Jiri G Safar, David Westaway

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in neurology, 2020. 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
1.6field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Genome-wide association studies identify novel loci in rapidly progressive Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2024
    Article
  10. Review
  11. Article
  12. Prion-like strain effects in tauopathies.Cell and tissue research · 2023
    Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Tau: A Signaling Hub Protein.Frontiers in molecular neuroscience · 2021
    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 2 institutions in 2 countries.

Sang-Gyun KangCenter for Prions and Protein Folding Diseases, University of Alberta, Edmonton, AB, Canada.
Ghazaleh Eskandari-SedighiDepartment of Biochemistry, University of Alberta, Edmonton, AB, Canada.
Lenka HromadkovaDepartment of Neurology and Pathology, Case Western Reserve University, Cleveland, OH, United States.
Jiri G SafarDepartment of Neurology and Pathology, Case Western Reserve University, Cleveland, OH, United States.
David WestawayCenter for Prions and Protein Folding Diseases, University of Alberta, Edmonton, AB, Canada.
University of Alberta · CACase Western Reserve University · US

Funding

Structural determinants of amyloid strain heterogeneity in distinct phenotypes of Alzheimer's diseaseRF1AG061797 · NIA · CASE WESTERN RESERVE UNIVERSITY · PI JARONIEC, CHRISTOPHER P, SAFAR, JIRI G. · 2018 to 2021
$4.4M
Characterization of Rapidly Progressive Alzheimer's DiseaseRF1AG058267 · NIA · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI HAINES, JONATHAN L, SAFAR, JIRI G. · 2017 to 2017
$4.0M
NIA NIH HHS RF1 AG058267NIA NIH HHS RF1 AG061797
6 · The paper itself

Abstract

Tau accumulation is a prominent feature in a variety of neurodegenerative disorders and remarkable effort has been expended working out the biochemistry and cell biology of this cytoplasmic protein. Tau's wayward properties may derive from germline mutations in the case of frontotemporal lobar degeneration (FTLD-MAPT) but may also be prompted by less understood cues-perhaps environmental or from molecular damage as a consequence of chronological aging-in the case of idiopathic tauopathies. Tau properties are undoubtedly affected by its covalent structure and in this respect tau protein is not only subject to changes in length produced by alternative splicing and endoproteolysis, but different types of posttranslational modifications that affect different amino acid residues. Another layer of complexity concerns alternate conformations-"conformers"-of the same covalent structures;

Indexed as

cell-to-cell transmissionliquid-liquid phase separationmolecular heterogeneitytauopathytransgenic miceubiquitin-proteasome system

Identifiers

PMID33304310
PMCPMC7693435
OpenAlexW3103000250

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.