Associated Papers
Phenomenological model of transthyretin stabilization.
Lisowski B et al.
Scientific Reports, 2026
Selective recognition of human small transthyretin aggregates by a novel monoclonal antibody.
Teixeira AC et al.
Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis, 2023
Oligomerization Profile of Human Transthyretin Variants with Distinct Amyloidogenicity.
Frangolho A et al.
Molecules (basel, Switzerland), 2020
Transthyretin Stabilization: An Emerging Strategy for the Treatment of Alzheimer's Disease?
Saponaro F et al.
International Journal of Molecular Sciences, 2020
Copper mediated amyloid-β binding to Transthyretin.
Ciccone L et al.
Scientific Reports, 2018
A New Folding Kinetic Mechanism for Human Transthyretin and the Influence of the Amyloidogenic V30M Mutation.
Jesus CS et al.
International Journal of Molecular Sciences, 2016
Transthyretin variants with improved inhibition of β-amyloid aggregation.
Mangrolia P et al.
Protein Engineering, Design & Selection : Peds, 2016
Transthyretin microheterogeneity and molecular interactions: implications for amyloid formation.
Landreh M et al.
Biomolecular Concepts, 2014
Statistical discovery of site inter-dependencies in sub-molecular hierarchical protein structuring.
Durston KK et al.
Eurasip Journal on Bioinformatics & Systems Biology, 2012
Identification of beta-amyloid-binding sites on transthyretin.
Du J et al.
Protein Engineering, Design & Selection : Peds, 2012
Stability of the transthyretin molecule as a key factor in the interaction with a-beta peptide--relevance in Alzheimer's disease.
Ribeiro CA et al.
Plos One, 2012
Structural insights into a zinc-dependent pathway leading to Leu55Pro transthyretin amyloid fibrils.
Castro-Rodrigues AF et al.
Acta Crystallographica. Section D, Biological Crystallography, 2011
The molecular biology and clinical features of amyloid neuropathy.
Benson MD et al.
Muscle & Nerve, 2007
Destabilization of transthyretin by pathogenic mutations in the DE loop.
Takeuchi M et al.
Proteins, 2007
The sequence-dependent unfolding pathway plays a critical role in the amyloidogenicity of transthyretin.
Yang M et al.
Biochemistry, 2006
Intrinsic versus mutation dependent instability/flexibility: a comparative analysis of the structure and dynamics of wild-type transthyretin and its pathogenic variants.
Lei M et al.
Journal of Structural Biology, 2004
Native state hydrogen exchange study of suppressor and pathogenic variants of transthyretin.
Liu K et al.
Journal of Molecular Biology, 2002
Transthyretin mutations in hyperthyroxinemia and amyloid diseases.
Saraiva MJ
Human Mutation, 2001
The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions.
Lashuel HA et al.
Biochemistry, 1999
Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry.
Nettleton EJ et al.
Journal of Molecular Biology, 1998