Structural analysis of APOB variants, p.(Arg3527Gln), p.(Arg1164Thr) and p.(Gln4494del), causing Familial Hypercholesterolaemia provides novel insights into variant pathogenicity

Human LDL Structural Diversity Studied by IR Spectroscopy

(2014) José A. Fernández-Higuero et al.   PLoS One

Advantages and Versatility of Fluorescence-Based Methodology to Characterize the Functionality of LDLR and Class Mutation Assignment

(2014) Aitor Etxebarria et al.   PLoS One

Novel functional APOB mutations outside LDL-binding region causing familial hypercholesterolaemia

(2013) Ana Catarina Alves et al.   HUMAN MOLECULAR GENETICS

Identification and biochemical analysis of a novelAPOBmutation that causes autosomal dominant hypercholesterolemia

(2013) Ellen R. A. Thomas et al.   Molecular Genetics & Genomic Medicine

Deletion of a single helix from the transmembrane domain causes large changes in membrane insertion properties and secondary structure of the bacterial conjugation protein TrwB

(2012) Ana Julia Vecino et al.   BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES

Functional characterization of splicing and ligand-binding domain variants in the LDL receptor

(2011) Aitor Etxebarria et al.   HUMAN MUTATION