Cryptic Extensibility in von Willebrand Factor Revealed by Molecular Nanodissection.
atomic force microscopy
mechanosensitive domains
nanomanipulation
receding meniscus
single-molecule mechanics
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
02 Jul 2024
02 Jul 2024
Historique:
received:
20
05
2024
revised:
19
06
2024
accepted:
29
06
2024
medline:
13
7
2024
pubmed:
13
7
2024
entrez:
13
7
2024
Statut:
epublish
Résumé
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
Identifiants
pubmed: 39000402
pii: ijms25137296
doi: 10.3390/ijms25137296
pii:
doi:
Substances chimiques
von Willebrand Factor
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Hungarian National Research, Development and Innovation Office
ID : 2020-1.1.6-JÖVŐ-2021-00013
Organisme : Hungarian National Research, Development and Innovation Office
ID : NVKP_16-1-2016-0017
Organisme : Ministry for Innovation and Technology of Hungary
ID : 2020-4.1.1.-TKP2020
Organisme : Ministry for Innovation and Technology of Hungary
ID : TKP2021-NVA-15
Organisme : Ministry for Innovation and Technology of Hungary
ID : TKP2021-EGA-23
Organisme : European Union
ID : RRF-2.3.1-21-2022-00003