Evidence map›Paper›PMID 37108724›Full record

ArticleInternational journal of molecular sciences2023

Nanoscale Structural Comparison of Fibrillin-1 Microfibrils Isolated from Marfan and Non-Marfan Syndrome Human Aorta.

Cristina M Șulea, Zsolt Mártonfalvi, Csilla Csányi, Dóra Haluszka, Miklós Pólos, Bence Ágg, Roland Stengl, Kálmán Benke, Zoltán Szabolcs, Miklós S Z Kellermayer

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

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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

10 authors at 1 institution in 2 countries.

Cristina M ȘuleaDepartment of Biophysics and Radiation Biology, Semmelweis University, 1094 Budapest, Hungary.ORCID 0000-0001-5622-9136
Zsolt MártonfalviDepartment of Biophysics and Radiation Biology, Semmelweis University, 1094 Budapest, Hungary.ORCID 0000-0001-7820-8109
Csilla CsányiDepartment of Biophysics and Radiation Biology, Semmelweis University, 1094 Budapest, Hungary.
Dóra HaluszkaDepartment of Biophysics and Radiation Biology, Semmelweis University, 1094 Budapest, Hungary.ORCID 0000-0003-3760-2016
Miklós PólosHeart and Vascular Center, Semmelweis University, 1122 Budapest, Hungary.
Bence ÁggHeart and Vascular Center, Semmelweis University, 1122 Budapest, Hungary.ORCID 0000-0002-6492-0426
Roland StenglHeart and Vascular Center, Semmelweis University, 1122 Budapest, Hungary.
Kálmán BenkeHeart and Vascular Center, Semmelweis University, 1122 Budapest, Hungary.
Zoltán SzabolcsHeart and Vascular Center, Semmelweis University, 1122 Budapest, Hungary.
Miklós S Z KellermayerDepartment of Biophysics and Radiation Biology, Semmelweis University, 1094 Budapest, Hungary.
Semmelweis University · HU

Funding

European Union RRF-2.3.1-21-2022-00003Hungarian National Research, Development and Innovation Office K135360Hungarian National Research, Development and Innovation Office TKP2021-EGA-23New National Excellence Program of the Ministry for Culture and Innovation from the source of the National Research, Development, and Innovation Fund ÚNKP-22-3-I-SE-49
6 · The paper itself

Abstract

Fibrillin-1 microfibrils are essential elements of the extracellular matrix serving as a scaffold for the deposition of elastin and endowing connective tissues with tensile strength and elasticity. Mutations in the fibrillin-1 gene (FBN1) are linked to Marfan syndrome (MFS), a systemic connective tissue disorder that, besides other heterogeneous symptoms, usually manifests in life-threatening aortic complications. The aortic involvement may be explained by a dysregulation of microfibrillar function and, conceivably, alterations in the microfibrils' supramolecular structure. Here, we present a nanoscale structural characterization of fibrillin-1 microfibrils isolated from two human aortic samples with different FBN1 gene mutations by using atomic force microscopy, and their comparison with microfibrillar assemblies purified from four non-MFS human aortic samples. Fibrillin-1 microfibrils displayed a characteristic "beads-on-a-string" appearance. The microfibrillar assemblies were investigated for bead geometry (height, length, and width), interbead region height, and periodicity. MFS fibrillin-1 microfibrils had a slightly higher mean bead height, but the bead length and width, as well as the interbead height, were significantly smaller in the MFS group. The mean periodicity varied around 50-52 nm among samples. The data suggest an overall thinner and presumably more frail structure for the MFS fibrillin-1 microfibrils, which may play a role in the development of MFS-related aortic symptomatology.

Indexed as

Marfan SyndromeMicrofibrilsAortaFibrillin-1Fibrillin-2FibrillinsHumansMicrofilament ProteinsFibrillin-1Fibrillin-2FibrillinsMicrofilament Proteinsaortaatomic force microscopyfibrillin microfibrilshumanMarfan syndrome

Identifiers

PMID37108724
PMCPMC10145871
OpenAlexW4366597299

What Socratic holds

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LicenceCC BY
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 Socratic graph.