Evidence map›Paper›PMID 33078207›Full record

ReviewCellular and molecular life sciences : CMLS2021

The structure and phase of tau: from monomer to amyloid filament.

Yifan Zeng, Jing Yang, Bailing Zhang, Meng Gao, Zhengding Su, Yongqi Huang

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2021. 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
2.5field-weighted citation impact, top 10% 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, 40 citations in OpenAlex.

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  8. Neurological Diseases can be Regulated by Phase Separation.Reviews of physiology, biochemistry and pharmacology · 2025
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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

6 authors at 2 institutions in 1 country.

Yifan ZengKey Laboratory of Industrial Fermentation (Ministry of Education), Hubei University of Technology, Wuhan, China.
Jing YangKey Laboratory of Industrial Fermentation (Ministry of Education), Hubei University of Technology, Wuhan, China.
Bailing ZhangKey Laboratory of Industrial Fermentation (Ministry of Education), Hubei University of Technology, Wuhan, China.
Meng GaoKey Laboratory of Industrial Fermentation (Ministry of Education), Hubei University of Technology, Wuhan, China.
Zhengding SuKey Laboratory of Industrial Fermentation (Ministry of Education), Hubei University of Technology, Wuhan, China.ORCID http://orcid.org/0000-0003-3558-001X
Yongqi HuangKey Laboratory of Industrial Fermentation (Ministry of Education), Hubei University of Technology, Wuhan, China. yqhuang@pku.edu.cn.ORCID http://orcid.org/0000-0002-9463-8325
Hubei University of Technology · CNWuhan University of Technology · CN

Funding

Hubei University of Technology BSQD2017022Natural Science Foundation of Hubei Province 2019CFB713
6 · The paper itself

Abstract

Tau is a microtubule-associated protein involved in regulation of assembly and spatial organization of microtubule in neurons. However, in pathological conditions, tau monomers assemble into amyloid filaments characterized by the cross-β structures in a number of neurodegenerative diseases known as tauopathies. In this review, we summarize recent progression on the characterization of structures of tau monomer and filament, as well as the dynamic liquid droplet assembly. Our aim is to reveal how post-translational modifications, amino acid mutations, and interacting molecules modulate the conformational ensemble of tau monomer, and how they accelerate or inhibit tau assembly into aggregates. Structure-based aggregation inhibitor design is also discussed in the context of dynamics and heterogeneity of tau structures.

Indexed as

Protein Processing, Post-TranslationalAlzheimer DiseaseAmyloidAmyloidogenic ProteinsAnimalsHumansIntrinsically Disordered ProteinsProtein Aggregation, PathologicalTauopathiestau ProteinsAmyloidAmyloidogenic ProteinsIntrinsically Disordered Proteinstau ProteinsConformation transitionDrug designIntrinsically disordered proteinLiquid–liquid phase separationProtein aggregation

Identifiers

PMID33078207
PMCPMC11073437
OpenAlexW3093167895

What OpenQuestion holds

Textmetadata
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.