Evidence map›Paper›PMID 34401998›Full record

ReviewThe protein journal2021

The Structure Biology of Tau and Clue for Aggregation Inhibitor Design.

Dan Wang, Xianlong Huang, Lu Yan, Luoqi Zhou, Chang Yan, Jinhu Wu, Zhengding Su, Yongqi Huang

Abstract readReview
PubMed Publisher
In one paragraph

Review in The protein journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

11 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Alzheimer's Disease: Significant Benefit from the Yeast-Based Models.International journal of molecular sciences · 2023
    Review
  8. Review
  9. Degradation of Bone Quality in a Transgenic Mouse Model of Alzheimer's Disease.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2022
    Article
  10. Article
  11. 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

8 authors at 1 institution in 1 country.

Dan Wang *Key Laboratory of Industrial Fermentation (Ministry of Education), Hubei University of Technology, Wuhan, 430068, China.
Xianlong Huang *Key Laboratory of Industrial Fermentation (Ministry of Education), Hubei University of Technology, Wuhan, 430068, China.
Lu YanKey Laboratory of Industrial Fermentation (Ministry of Education), Hubei University of Technology, Wuhan, 430068, China.
Luoqi ZhouKey Laboratory of Industrial Fermentation (Ministry of Education), Hubei University of Technology, Wuhan, 430068, China.
Chang YanKey Laboratory of Industrial Fermentation (Ministry of Education), Hubei University of Technology, Wuhan, 430068, China.
Jinhu WuKey Laboratory of Industrial Fermentation (Ministry of Education), Hubei University of Technology, Wuhan, 430068, China.
Zhengding SuKey Laboratory of Industrial Fermentation (Ministry of Education), Hubei University of Technology, Wuhan, 430068, China.
Yongqi HuangKey Laboratory of Industrial Fermentation (Ministry of Education), Hubei University of Technology, Wuhan, 430068, China. yqhuang@hbut.edu.cn.ORCID 0000-0002-9463-8325
Hubei University of Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tau is a microtubule-associated protein that is mainly expressed in central and peripheral nerve systems. Tau binds to tubulin and regulates assembly and stabilization of microtubule, thus playing a critical role in neuron morphology, axon development and navigation. Tau is highly stable under normal conditions; however, there are several factors that can induce or promote aggregation of tau, forming neurofibrillary tangles. Neurofibrillary tangles are toxic to neurons, which may be related to a series of neurodegenerative diseases including Alzheimer's disease. Thus, tau is widely accepted as an important therapeutic target for neurodegenerative diseases. While the monomeric structure of tau is highly disordered, the aggregate structure of tau is formed by closed packing of β-stands. Studies on the structure of tau and the structural transition mechanism provide valuable information on the occurrence, development, and therapy of tauopathies. In this review, we summarize recent progress on the structural investigation of tau and based on which we discuss aggregation inhibitor design.

Indexed as

Protein AggregatesAlzheimer DiseaseHumansNeurofibrillary TanglesNeuronstau ProteinsMAPT protein, humanProtein Aggregatestau ProteinsDrug designFibril structureNeurodegenerative diseasesProtein aggregationTauopathies

Identifiers

PMID34401998
OpenAlexW3195118901

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.