Associated Papers
Misfolding of transthyretin in vivo is controlled by the redox environment and macromolecular crowding.
Jayaweera SW et al.
The Journal of Biological Chemistry, 2025
Mispacking of the F87 sidechain drives aggregation-promoting conformational fluctuations in the subunit interfaces of the transthyretin tetramer.
Sun X et al.
Protein Science : a Publication of the Protein Society, 2024
Conformational Dynamics of an Amyloidogenic Intermediate of Transthyretin: Implications for Structural Remodeling and Amyloid Formation.
Leach BI et al.
Journal of Molecular Biology, 2024
Mispacking of the F87 sidechain drives aggregation-promoting conformational fluctuations in the subunit interfaces of the transthyretin tetramer.
Sun X et al.
Biorxiv : the Preprint Server for Biology, 2024
Probing the Dissociation Pathway of a Kinetically Labile Transthyretin Mutant.
Sun X et al.
Journal of the American Chemical Society, 2024
Hydrogen bonds connecting the N-terminal region and the DE loop stabilize the monomeric structure of transthyretin.
Inada Y et al.
Journal of Biochemistry, 2023
A transthyretin monomer intermediate undergoes local unfolding and transient interaction with oligomers in a kinetically concerted aggregation pathway.
Sun X et al.
The Journal of Biological Chemistry, 2022
Thermodynamic Stability and Aggregation Kinetics of EF Helix and EF Loop Variants of Transthyretin.
Ferguson JA et al.
Biochemistry, 2021
Mispacking of the Phe87 Side Chain Reduces the Kinetic Stability of Human Transthyretin.
Sun X et al.
Biochemistry, 2018
Formation of cytotoxic transthyretin is not dependent on inter-molecular disulphide bridges commonly found within the amyloid form.
Lindhagen-Persson M et al.
Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis, 2008
Transthyretin interacts with metallothionein 2.
Gonçalves I et al.
Biochemistry, 2008
Cys114-linked dimers of transthyretin are compatible with amyloid formation.
Karlsson A et al.
Biochemistry, 2005
Cys-10 mixed disulfide modifications exacerbate transthyretin familial variant amyloidogenicity: a likely explanation for variable clinical expression of amyloidosis and the lack of pathology in C10S/V30M transgenic mice?
Zhang Q et al.
Biochemistry, 2005
X-ray absorption spectroscopy reveals a substantial increase of sulfur oxidation in transthyretin (TTR) upon fibrillization.
Gales L et al.
The Journal of Biological Chemistry, 2003
Exposure of cryptic epitopes on transthyretin only in amyloid and in amyloidogenic mutants.
Goldsteins G et al.
Proceedings of the National Academy of Sciences of the United States of America, 1999