Evidence map›Paper›PMID 30257460›Full record

ArticleInternational journal of molecular sciences2018

Filamentous Aggregates of Tau Proteins Fulfil Standard Amyloid Criteria Provided by the Fuzzy Oil Drop (FOD) Model.

Dawid Dułak, Małgorzata Gadzała, Mateusz Banach, Magdalena Ptak, Zdzisław Wiśniowski, Leszek Konieczny, Irena Roterman

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Hierarchical Structure of Protein Sequence.International journal of molecular sciences · 2021
    Article
  2. The Structure of Amyloid Versus the Structure of Globular Proteins.International journal of molecular sciences · 2020
    Article
  3. Article
  4. Alternative Structures of α-Synuclein.Molecules (Basel, Switzerland) · 2020
    Article
  5. Article
  6. Review
  7. Different Synergy in Amyloids and Biologically Active Forms of Proteins.International journal of molecular sciences · 2019
    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

7 authors.

Dawid DułakABB Business Services Sp. z o.o. ul. Żegańska 1, 04-713 Warszawa, Poland. dawid.dulak@gmail.com.
Małgorzata GadzałaACK-Cyfronet AGH, Nawojki 11, 30-950 Kraków, Poland. m.k.gadzala@gmail.com.
Mateusz BanachDepartment of Bioinformatics and Telemedicine, Medical College, Jagiellonian University, Łazarza 16, 31-530 Kraków, Poland. mateusz.banach@uj.edu.pl.
Magdalena PtakDepartment of Bioinformatics and Telemedicine, Medical College, Jagiellonian University, Łazarza 16, 31-530 Kraków, Poland. magdalena.ptak@uj.edu.pl.
Zdzisław WiśniowskiDepartment of Bioinformatics and Telemedicine, Medical College, Jagiellonian University, Łazarza 16, 31-530 Kraków, Poland. mywisnio@cyf-kr.edu.pl.
Leszek KoniecznyChair of Medical Biochemistry, Medical College, Jagiellonian University, Kopernika 7, 31-034 Kraków, Poland. mbkoniec@cyf-kr.edu.pl.
Irena RotermanDepartment of Bioinformatics and Telemedicine, Medical College, Jagiellonian University, Łazarza 16, 31-530 Kraków, Poland. myroterm@cyf-kr.edu.pl.

Funding

Jagiellonian University - Medical college - Krakow Poland and K/ZDS/006363 and K/ZDS/006366] and PLGrid Infrastructure - Cyfronet AGH, University of Science and Technology K/ZDS/006363 and K/ZDS/006366
6 · The paper itself

Abstract

Abnormal filamentous aggregates that are formed by tangled tau protein turn out to be classic amyloid fibrils, meeting all the criteria defined under the fuzzy oil drop model in the context of amyloid characterization. The model recognizes amyloids as linear structures where local hydrophobicity minima and maxima propagate in an alternating manner along the fibril's long axis. This distribution of hydrophobicity differs greatly from the classic monocentric hydrophobic core observed in globular proteins. Rather than becoming a globule, the amyloid instead forms a ribbonlike (or cylindrical) structure.

Indexed as

Alzheimer DiseaseAmyloidHumansHydrophobic and Hydrophilic InteractionsModels, BiologicalModels, MolecularProtein AggregatesProtein Aggregation, PathologicalProtein ConformationTauopathiestau ProteinsAmyloidProtein Aggregatestau ProteinsAlzheimer’s diseasetau amyloidtauopathy

Identifiers

PMID30257460
PMCPMC6213535

What OpenQuestion holds

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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.