{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Machha VR"],"funding":["Mayo Clinic Comprehensive Hemophilia Treatment Center","National Heart, Lung, and Blood Institute","NHLBI NIH HHS","Health Resources and Services Administration","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["ugae021"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11664255"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["1(4)"],"pubmed_abstract":["The A1 domain in Von Willebrand Factor (VWF) initiates coagulation through binding to platelet glycoprotein GPIbα receptors. Von Willebrand Disease (VWD)-Mutations in A1 that either impair (type 2M) or enhance (type 2B) platelet adhesion to VWF can locally destabilize and even misfold the domain. We leveraged misfolding in the gain-of-function type 2B VWD phenotype as a target, distinct from the normal conformation. Two nuclease-resistant 2'-fluoropyrimidine RNA aptamers were selected to discriminate normal A1 domains from a type 2B V1314D A1 variant in a glycosylated A1A2A3 tri-domain VWF-fragment. Two aptamers, W9 and V1, were isolated that selectively recognize, bind, and inhibit the A1-GPIbα interaction with WT A1A2A3 and V1314D A1A2A3, respectively. These aptamers were tested against "],"journal":["NAR molecular medicine"],"pubmed_title":["Conformation-specific RNA aptamers for phenotypic distinction between normal von Willebrand factor and type 2B von Willebrand disease."],"pmcid":["PMC11664255"],"funding_grant_id":["GM143949","HL146508 to M.A.","R01 HL146508","R35 GM143949","H30MC24052"],"pubmed_authors":["Moon-Tasson L","Santiago-Davis A","Machha VR","Tischer A","Tange J","Pruthi RK","Auton M","Chen D","Maher LJ"],"additional_accession":[]},"is_claimable":false,"name":"Conformation-specific RNA aptamers for phenotypic distinction between normal von Willebrand factor and type 2B von Willebrand disease.","description":"The A1 domain in Von Willebrand Factor (VWF) initiates coagulation through binding to platelet glycoprotein GPIbα receptors. Von Willebrand Disease (VWD)-Mutations in A1 that either impair (type 2M) or enhance (type 2B) platelet adhesion to VWF can locally destabilize and even misfold the domain. We leveraged misfolding in the gain-of-function type 2B VWD phenotype as a target, distinct from the normal conformation. Two nuclease-resistant 2'-fluoropyrimidine RNA aptamers were selected to discriminate normal A1 domains from a type 2B V1314D A1 variant in a glycosylated A1A2A3 tri-domain VWF-fragment. Two aptamers, W9 and V1, were isolated that selectively recognize, bind, and inhibit the A1-GPIbα interaction with WT A1A2A3 and V1314D A1A2A3, respectively. These aptamers were tested against ","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Oct","modification":"2026-04-07T21:22:12.168Z","creation":"2025-04-04T13:41:45.596Z"},"accession":"S-EPMC11664255","cross_references":{"pubmed":["39719968"],"doi":["10.1093/narmme/ugae021"]}}