Evidence map›Paper›PMID 31439664›Full record

ArticleThe Journal of biological chemistry2019

Membrane-mediated fibrillation and toxicity of the tau hexapeptide PHF6.

Adeline M Fanni, Crystal M Vander Zanden, Paulina V Majewska, Jaroslaw Majewski, Eva Y Chi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

24 citing papers in PubMed, 66 citations in OpenAlex.

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  14. Membrane-induced tau amyloid fibrils.Communications biology · 2023
    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

5 authors at 2 institutions in 1 country.

Adeline M FanniCenter for Biomedical Engineering, University of New Mexico, Albuquerque, New Mexico 87131.ORCID 0000-0002-7240-2792
Crystal M Vander ZandenCenter for Biomedical Engineering, University of New Mexico, Albuquerque, New Mexico 87131.ORCID 0000-0003-3248-6028
Paulina V MajewskaCenter for Biomedical Engineering, University of New Mexico, Albuquerque, New Mexico 87131.
Jaroslaw MajewskiDepartment of Chemical and Biological Engineering, University of New Mexico, Albuquerque, New Mexico 87131.
Eva Y ChiCenter for Biomedical Engineering, University of New Mexico, Albuquerque, New Mexico 87131 evachi@unm.edu.
University of New Mexico · USU.S. National Science Foundation · US

Funding

FAIR Data Competency and Machine Learning Readiness for Biomedical ScientistsK12GM088021 · NIGMS · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI REBECCA S. HARTLEY, Diane Lidke · 2009 to 2026
$16.4M
NIGMS NIH HHS K12 GM088021
6 · The paper itself

Abstract

The aggregation of the tau protein into neurofibrillary tangles is believed to correlate with cognitive decline in several neurodegenerative disorders, including Alzheimer's disease. Recent studies suggest that tau's interactions with the cell membrane could serve as a toxicity pathway and also enhance fibrillation into paired helical filaments (PHFs). Conformational changes associated with tau-membrane interactions are poorly understood, and their characterization could improve our understanding of tau pathogenicity. In this study, we investigated the molecular level structural changes associated with the interaction of the tau hexapeptide PHF6 with model lipid membranes and characterized the effects of these interactions on membrane stability and peptide fibrillation. We used two PHF6 forms, the aggregation-prone PHF6 with N-terminal acetylation (Ac-PHF6) and the non-aggregation prone PHF6 with a standard N terminus (NH

Indexed as

AcetylationAlzheimer DiseaseAmino Acid MotifsCell MembraneHumansNeurofibrillary TanglesPeptidesProtein Structure, Secondarytau ProteinsPeptidestau ProteinsAlzheimer diseaseamyloidmembrane-mediated fibrillationmembrane structureneurodegenerationpaired helical filamentPHF6tauopathyTau protein (Tau)toxicity

Identifiers

PMID31439664
PMCPMC6802503
OpenAlexW2969380363

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.