Cryptic Extensibility in von Willebrand Factor Revealed by Molecular Nanodissection.

Mária Csilla Csányi, Dominik Sziklai, Tímea Feller, Jolán Hársfalvi, Miklós Kellermayer

Abstract read

In one paragraph

Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing 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

1 citing paper in PubMed.

Identification of missense variants in the C-domains of von Willebrand factor that cause gain-of-function-like activity.Blood advances · 2026
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

5 authors.

Mária Csilla CsányiInstitute of Biophysics and Radiation Biology, Semmelweis University, Tűzoltó u. 37-47, H1094 Budapest, Hungary.

Dominik SziklaiInstitute of Biophysics and Radiation Biology, Semmelweis University, Tűzoltó u. 37-47, H1094 Budapest, Hungary.ORCID 0000-0003-3590-7449

Tímea FellerDiscovery and Translational Science Department, Leeds Institute of Cardiovascular and Metabolic Medicine, University of Leeds, Leeds LS29JT, UK.

Jolán HársfalviInstitute of Biophysics and Radiation Biology, Semmelweis University, Tűzoltó u. 37-47, H1094 Budapest, Hungary.

Miklós KellermayerInstitute of Biophysics and Radiation Biology, Semmelweis University, Tűzoltó u. 37-47, H1094 Budapest, Hungary.

Funding

European Union RRF-2.3.1-21-2022-00003Hungarian National Research, Development and Innovation Office 2020-1.1.6-JÖVŐ-2021-00013Hungarian National Research, Development and Innovation Office NVKP_16-1-2016-0017Ministry for Innovation and Technology of Hungary 2020-4.1.1.-TKP2020Ministry for Innovation and Technology of Hungary TKP2021-EGA-23Ministry for Innovation and Technology of Hungary TKP2021-NVA-15

6 · The paper itself

Abstract

Von Willebrand factor (VWF) is a multimer with a variable number of protomers, each of which is a head-to-head dimer of two multi-domain monomers. VWF responds to shear through the unfolding and extension of distinct domains, thereby mediating platelet adhesion and aggregation to the injured blood vessel wall. VWF's C

Indexed as

Microscopy, Atomic Forcevon Willebrand FactorHumansProtein DomainsProtein Multimerizationvon Willebrand Factoratomic force microscopymechanosensitive domainsnanomanipulationreceding meniscussingle-molecule mechanics

Identifiers

PMID39000402

DOI10.3390/ijms25137296

PMCPMC11242059

What OpenQuestion holds

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LicenceCC BY

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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.