Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases

DJ Rinauro, F Chiti, M Vendruscolo… - Molecular …, 2024 - Springer
The conversion of native peptides and proteins into amyloid aggregates is a hallmark of over
50 human disorders, including Alzheimer's and Parkinson's diseases. Increasing evidence …

Hereditary transthyretin amyloid neuropathies: advances in pathophysiology, biomarkers, and treatment

D Adams, Y Sekijima, I Conceição… - The Lancet …, 2023 - thelancet.com
Hereditary transthyretin (TTR) amyloid polyneuropathy is an autosomal dominant life-
threatening disorder. TTR is produced mainly by the liver but also by the choroid plexus and …

Transthyretin mutagenesis: impact on amyloidogenesis and disease

ZL Almeida, DC Vaz, RMM Brito - Critical Reviews in Clinical …, 2024 - Taylor & Francis
Transthyretin (TTR), a homotetrameric protein found in plasma, cerebrospinal fluid, and the
eye, plays a pivotal role in the onset of several amyloid diseases with high morbidity and …

EGCG-Mediated Protection of Transthyretin Amyloidosis by Stabilizing Transthyretin Tetramers and Disrupting Transthyretin Aggregates

H Zou, S Zhou - International Journal of Molecular Sciences, 2023 - mdpi.com
Transthyretin amyloidosis (ATTR) is a progressive and systemic disease caused by the
misfolding and amyloid aggregation of transthyretin (TTR). Stabilizing the TTR tetramers and …

Histidine tautomerism-mediated transthyretin amyloidogenesis: A molecular insight

S Chatterjee, A Salimi, JY Lee - Archives of Biochemistry and Biophysics, 2023 - Elsevier
Abstract Characterization of the conformational alterations involved in monomer misfolding
is essential for elucidating the molecular basis of the initial stage of protein accumulation …