RESCUE OF A PANEL OF SPLICING MUTATIONS CAUSING HEMOPHILIA A BY ENGINEERED U1-SNRNAS

A 5’ SPLICE-SITE MUTATION CAUSING MUCOLIPIDOSIS TYPE III CAN BE EFFICIENTLY RESCUED BY U1 SNRNA-BASED THERAPY

Reverting highly frequent f8 nonsense mutations: base and prime editing approach for hemophilia A

Base and Prime Editors as new correction approaches for recurrent Hemophilia A Nonsense Mutations

Tailored collagen binding confers distinct functional properties to engineered factor IX fusion proteins in hemophilia B mouse model

Prediction of inhibitor risk in haemophilia A using machine learning

Rescue of a panel of splicing mutations causing hemophilia A by engineered U1snRNAs

Engineered tRNAs as a novel tailored correction approach to restore protein biosynthesis and function from hemophilia-causing nonsense mutations

Design of an engineered coagulation factor X as a novel by-passing agent for hemophilia

A novel tailored correction approach for recurrent hemophilia-causing nonsense mutations through AntiCodon-Engineered suppressor tRNAs

Rescue of a hemophilia A-causing FVIII splicing variant via engineered U1SNRNAS

Rescue of a FVIII splicing variant with engineered U1snRNAs

Engineered suppressor tRNAs as a novel correction approach for recurrent hemophilia A-causing nonsense mutations

Base and Prime editing of DNA as a new therapeutic option for Hemophilia A

New Genome Editing Approaches: Base And Prime Editing To Revert Hemophilia A-Causing Point Mutations

Rescue of an F8 splicing variant (c.1752+5 G>C) with engineered U1snRNAs

A factor X variant with engineered activation peptide as innovative by-passing agent for haemophilia

A new type 1 von Willebrand Disease (VWD) characterized by increased clearance of von Willebrand Factor (VWF) due to the heterozygous p.P1127S mutation: clinical phenotype and pathogenic mechanisms

An engineered factor X variant as a novel by-passing agent for hemophilia

Comparative Analysis Of Residual Factor VIII Expression from Recurrent F8 Nonsense Mutations Indicates that Localization in the B- domain Favours Readthrough- mediated Protein Output