Evidence map›Paper›PMID 35211074›Full record

ReviewFrontiers in neurology2021

Tau Ubiquitination in Alzheimer's Disease.

Longfei Li, Yanli Jiang, Jian-Zhi Wang, Rong Liu, Xiaochuan Wang

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in neurology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
5.0field-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

33 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. STAT4-dependent regulation of neuroinflammation in atherosclerosis.bioRxiv : the preprint server for biology · 2026
    Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Tau degradation in Alzheimer's disease: Mechanisms and therapeutic opportunities.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025
    Review
  15. Review
  16. Cellular and pathological functions of tau.Nature reviews. Molecular cell biology · 2024
    Review
  17. Review
  18. Review
  19. Review
  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 2 institutions in 1 country.

Longfei LiKey Laboratory of Education Ministry/Hubei Province of China for Neurological Disorders, Department of Pathophysiology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.
Yanli JiangKey Laboratory of Education Ministry/Hubei Province of China for Neurological Disorders, Department of Pathophysiology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.
Jian-Zhi WangKey Laboratory of Education Ministry/Hubei Province of China for Neurological Disorders, Department of Pathophysiology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.
Rong LiuKey Laboratory of Education Ministry/Hubei Province of China for Neurological Disorders, Department of Pathophysiology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.
Xiaochuan WangKey Laboratory of Education Ministry/Hubei Province of China for Neurological Disorders, Department of Pathophysiology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.
Huazhong University of Science and Technology · CNJianghan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Paired helical filaments (PHFs) from the Alzheimer's disease (AD) brain are highly ubiquitinated and ubiquitination likely plays a vital role in tau filament formation. Whether tau ubiquitination is the causality or consequence of the disease in AD remains elusive. The following questions are worth considering: What does the extent of tau ubiquitination contribute to tau pathology in AD? Does tau ubiquitination influence aggregation or spreading during disease progression? In addition, tau is polyubiquitinated in nerve growth factor-induced PC12 cells and participates in mitogen-activated protein kinase signaling, in addition to its microtubule stabilization function. Therefore, ubiquitination possibly mediates tau signaling under physiological conditions, but tau aggregation in the pathobiology of AD. Here, we review the advancements in tau ubiquitination and the potential therapeutic effects of targeting tau ubiquitination to alleviate tau pathology in AD.

Indexed as

Alzheimer's diseaseNGFPHFtauubiquitination

Identifiers

PMID35211074
PMCPMC8860969
OpenAlexW4210866627

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.