Evidence map›Paper›PMID 34168795›Full record

ArticleChemical science2021

CHIP-mediated hyperubiquitylation of tau promotes its self-assembly into the insoluble tau filaments.

Ji Hyeon Kim, Jeeyoung Lee, Won Hoon Choi, Seoyoung Park, Seo Hyeong Park, Jung Hoon Lee, Sang Min Lim, Ji Young Mun, Hyun-Soo Cho, Dohyun Han and 2 more

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

21 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. The Ubiquitin-Proteasome System in Brain Disorders: Pathogenic Pathways, Post-Translational Tweaks, and Therapeutic Frontiers.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2025
    Review
  4. Review
  5. Review
  6. Cellular and pathological functions of tau.Nature reviews. Molecular cell biology · 2024
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Neurodegenerative Disease Tauopathies.Annual review of pathology · 2024
    Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. Phosphorylated Tau in Alzheimer's Disease and Other Tauopathies.International journal of molecular sciences · 2022
    Review
  18. Review
  19. Article
  20. Smuggle tau through a secret(ory) pathway.The Biochemical journal · 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

12 authors at 5 institutions in 5 countries.

Ji Hyeon KimDepartment of Biomedical Sciences, Seoul National University Graduate School Seoul 03080 Korea minjlee@snu.ac.k +82 2-744-4534 +82 2-740-8254.ORCID https://orcid.org/0000-0003-1737-8619
Jeeyoung LeeDepartment of Biomedical Sciences, Seoul National University Graduate School Seoul 03080 Korea minjlee@snu.ac.k +82 2-744-4534 +82 2-740-8254.ORCID https://orcid.org/0000-0002-0766-8500
Won Hoon ChoiDepartment of Biomedical Sciences, Seoul National University Graduate School Seoul 03080 Korea minjlee@snu.ac.k +82 2-744-4534 +82 2-740-8254.ORCID https://orcid.org/0000-0002-6206-4937
Seoyoung ParkDepartment of Biochemistry & Molecular Biology, Neuroscience Research Institute, Seoul National University College of Medicine Seoul 03080 Korea.ORCID https://orcid.org/0000-0001-7340-2594
Seo Hyeong ParkDepartment of Biomedical Sciences, Seoul National University Graduate School Seoul 03080 Korea minjlee@snu.ac.k +82 2-744-4534 +82 2-740-8254.
Jung Hoon LeeDepartment of Biochemistry & Molecular Biology, Neuroscience Research Institute, Seoul National University College of Medicine Seoul 03080 Korea.ORCID https://orcid.org/0000-0003-3432-4487
Sang Min LimConvergence Research Center for Diagnosis, Treatment and Care System of Dementia, Korea Institute of Science and Technology Seoul 02792 Korea.ORCID https://orcid.org/0000-0003-0419-8950
Ji Young MunNeural Circuit Research Group, Korea Brain Research Institute Daegu 41062 Korea.ORCID https://orcid.org/0000-0003-0820-6233
Hyun-Soo ChoDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University Seoul 03722 Korea.ORCID https://orcid.org/0000-0003-4067-4715
Dohyun HanProteomics Core Facility, Biomedical Research Institute, Seoul National University Hospital Seoul 03080 Korea.ORCID https://orcid.org/0000-0002-0841-1598
Young Ho SuhDepartment of Biomedical Sciences, Seoul National University Graduate School Seoul 03080 Korea minjlee@snu.ac.k +82 2-744-4534 +82 2-740-8254.ORCID https://orcid.org/0000-0003-3979-1615
Min Jae LeeDepartment of Biomedical Sciences, Seoul National University Graduate School Seoul 03080 Korea minjlee@snu.ac.k +82 2-744-4534 +82 2-740-8254.ORCID https://orcid.org/0000-0002-3252-6467
Seoul National University · KRCircuit Therapeutics (United States) · USSeoul National University Hospital · KRThe Seoul Institute · KRYonsei University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The tau protein is a highly soluble and natively unfolded protein. Under pathological conditions, tau undergoes multiple post-translational modifications (PTMs) and conformational changes to form insoluble filaments, which are the proteinaceous signatures of tauopathies. To dissect the crosstalk among tau PTMs during the aggregation process, we phosphorylated and ubiquitylated recombinant tau

Identifiers

PMID34168795
PMCPMC8179656
OpenAlexW3139430110

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.