Evidence map›Paper›PMID 29774342›Full record

ArticleChemical communications (Cambridge, England)2018

The distinct structural preferences of tau protein repeat domains.

Xuhua Li, Xuewei Dong, Guanghong Wei, Martin Margittai, Ruth Nussinov, Buyong Ma

Abstract read
In one paragraph

Article in Chemical communications (Cambridge, England), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Disrupting Amyloid Filaments of Tau by Means of Electric Fields.The journal of physical chemistry. B · 2025
    Article
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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.

Xuhua LiDepartment of Physics, State Key Laboratory of Surface Physics, Key Laboratory for Computational Physical Science (Ministry of Education), Collaborative Innovation Center of Advanced Microstructures (Nanjing), Fudan University, Shanghai 200433, People's Republic of China. ghwei@fudan.edu.cn.
Xuewei Dong
Guanghong Wei
Martin Margittai
Ruth Nussinov
Buyong Ma

Funding

Protein Structure, Stability, and Amyloid FormationZIABC010440 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NUSSINOV, RUTH · 2009 to 2025
$11.8M
Method Development: Efficient Computer Vision Based AlgorithmsZIABC010442 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NUSSINOV, RUTH · 2009 to 2025
$2.4M
Protein Structure, Stability, and Amyloid FormationZ01BC010440 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NUSSINOV, RUTH · 2002 to 2008
$1.4M
CCR NIH HHS HHSN261200800001CIntramural NIH HHS Z01 BC010440NCI NIH HHS HHSN261200800001E
6 · The paper itself

Abstract

The tau fibrillar structures from the brain of an Alzheimer's patient have a core with a C-shaped motif of the third and fourth repeat domains (R3-R4). Our simulations indicated that the C-shaped motif is only stable for R3-R4, while R1-R2 tends to be linear in shape. These two structural motifs appear in the most stable K18 protofilament. Heparin can further stabilize the C-shaped R3-R4 motif, but not other repeats.

Indexed as

HeparinHumansHydrogen BondingMolecular Dynamics SimulationProtein AggregatesProtein BindingProtein DomainsProtein MultimerizationProtein StabilityProtein Structure, SecondaryRepetitive Sequences, Amino Acidtau ProteinsHeparinProtein Aggregatestau Proteins

Identifiers

PMID29774342
PMCPMC5986281

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Registered trials

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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.