Associated Papers
3D Visualization and Proteomic Analysis of Human Cardiac Transthyretin Amyloidosis Tissue Reveals Microangiopathy and Capillary Occlusion.
Donnelly JP et al.
Biorxiv : the Preprint Server for Biology, 2026
Clinical and Biochemical Characterization of Hereditary ATTR Amyloidosis Caused by a Novel Transthyretin Variant V121A (p.V141A).
Yoshinaga T et al.
International Journal of Molecular Sciences, 2025
The conformational landscape of human transthyretin revealed by cryo-EM.
Basanta B et al.
Nature Structural & Molecular Biology, 2025
Differential Association of Transthyretin Stability with Variant and Wild-Type Transthyretin Amyloid Cardiomyopathy: The SCAN-MP Study.
Urina-Jassir M et al.
Jacc. Heart Failure, 2024
The conformational landscape of human transthyretin revealed by cryo-EM.
Basanta B et al.
Biorxiv : the Preprint Server for Biology, 2024
Tafamidis concentration required for transthyretin stabilisation in cerebrospinal fluid.
Tsai FJ et al.
Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis, 2023
Characterising diflunisal as a transthyretin kinetic stabilizer at relevant concentrations in human plasma using subunit exchange.
Tsai FJ et al.
Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis, 2023
ATF6 Activation Reduces Amyloidogenic Transthyretin Secretion through Increased Interactions with Endoplasmic Reticulum Proteostasis Factors.
Mesgarzadeh JS et al.
Cells, 2022
Mispacking of the Phe87 Side Chain Reduces the Kinetic Stability of Human Transthyretin.
Sun X et al.
Biochemistry, 2018
Amyloidogenic and non-amyloidogenic transthyretin variants interact differently with human cardiomyocytes: insights into early events of non-fibrillar tissue damage.
Manral P et al.
Bioscience Reports, 2015
Age-related oxidative modifications of transthyretin modulate its amyloidogenicity.
Zhao L et al.
Biochemistry, 2013
Transthyretin is a metallopeptidase with an inducible active site.
Liz MA et al.
The Biochemical Journal, 2012
The pathway by which the tetrameric protein transthyretin dissociates.
Foss TR et al.
Biochemistry, 2005
Cys114-linked dimers of transthyretin are compatible with amyloid formation.
Karlsson A et al.
Biochemistry, 2005
Kinetic stabilization of an oligomeric protein by a single ligand binding event.
Wiseman RL et al.
Journal of the American Chemical Society, 2005
The crystal structure of transthyretin in complex with diethylstilbestrol: a promising template for the design of amyloid inhibitors.
Morais-de-Sá E et al.
The Journal of Biological Chemistry, 2004
A comparative analysis of 23 structures of the amyloidogenic protein transthyretin.
Hörnberg A et al.
Journal of Molecular Biology, 2000