Evidence map›Paper›PMID 26636947›Full record

ArticleBiophysical journal2015

Oxidative Stress Alters the Morphology and Toxicity of Aortic Medial Amyloid.

Hannah A Davies, Marie M Phelan, Mark C Wilkinson, Raymond Q Migrino, Seth Truran, Daniel A Franco, Lu-Ning Liu, Christopher J Longmore, Jillian Madine

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 24 citations in OpenAlex.

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  12. Idiopathic degenerative thoracic aneurysms are associated with increased aortic medial amyloid.Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis · 2019
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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

9 authors at 2 institutions in 2 countries.

Hannah A DaviesInstitute of Integrative Biology, University of Liverpool, Liverpool, UK.
Marie M PhelanInstitute of Integrative Biology, University of Liverpool, Liverpool, UK; Technology Directorate, University of Liverpool, Liverpool, UK.
Mark C WilkinsonInstitute of Integrative Biology, University of Liverpool, Liverpool, UK.
Raymond Q MigrinoOffice of Research, Phoenix Veterans Affairs Health Care System, Phoenix, Arizona.
Seth TruranOffice of Research, Phoenix Veterans Affairs Health Care System, Phoenix, Arizona.
Daniel A FrancoOffice of Research, Phoenix Veterans Affairs Health Care System, Phoenix, Arizona.
Lu-Ning LiuInstitute of Integrative Biology, University of Liverpool, Liverpool, UK.
Christopher J LongmoreInstitute of Integrative Biology, University of Liverpool, Liverpool, UK.
Jillian MadineInstitute of Integrative Biology, University of Liverpool, Liverpool, UK. Electronic address: j.madine@liv.ac.uk.
University of Liverpool · GBPhoenix VA Health Care System · US

Funding

Human vascular model to study Alzheimer's DiseaseR21AG044723 · NIA · ARIZONA VETERANS RESEARCH AND EDUCATION FOUNDATION · PI MIGRINO, RAYMOND QUEZON · 2014 to 2015
$343k
Nanoliposome-based Treatment of Amyloid Protein (AL) ToxicityI01BX001990 · VA · PHOENIX VA HEALTH CARE SYSTEM · PI MIGRINO, RAYMOND QUEZON · 2013 to 2015
–
Biotechnology and Biological Sciences Research Council BB/M024202/1BLRD VA I01 BX001990British Heart Foundation FS/12/61/29877NIA NIH HHS 1R21AG044723NIA NIH HHS R21 AG044723
6 · The paper itself

Abstract

The aggregation and fibril deposition of amyloid proteins have been implicated in a range of neurodegenerative and vascular diseases, and yet the underlying molecular mechanisms are poorly understood. Here, we use a combination of cell-based assays, biophysical analysis, and atomic force microscopy to investigate the potential involvement of oxidative stress in aortic medial amyloid (AMA) pathogenesis and deposition. We show that medin, the main constituent of AMA, can induce an environment rich in oxidative species, increasing superoxide and reducing bioavailable nitric oxide in human cells. We investigate the role that this oxidative environment may play in altering the aggregation process of medin and identify potential posttranslational modification sites where site-specific modification and interaction can be unambiguously demonstrated. In an oxidizing environment, medin is nitrated at tyrosine and tryptophan residues, with resultant effects on morphology that lead to longer fibrils with increased toxicity. This provides further motivation to investigate the role of oxidative stress in AMA pathogenicity.

Indexed as

Antigens, SurfaceAortaHumansHuman Umbilical Vein Endothelial CellsMilk ProteinsNitratesOxidative StressAntigens, SurfaceMFGE8 protein, humanMilk ProteinsNitrates

Identifiers

PMID26636947
PMCPMC4675884
OpenAlexW2187470614

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.