[HTML][HTML] Understanding mesangial pathobiology in AL-Amyloidosis and monoclonal Ig light chain deposition disease

GA Herrera, J Teng, EA Turbat-Herrera, C Zeng… - Kidney international …, 2020 - Elsevier
Patients with plasma cell dyscrasias produce free abnormal monoclonal immunoglobulin
light chains that circulate in the blood stream. Some of them, termed glomerulopathic light …

[HTML][HTML] Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins

V Oliveri - Molecules, 2023 - mdpi.com
Amyloid diseases have become a global concern due to their increasing prevalence.
Transition metals, including copper, can affect the aggregation of the pathological proteins …

[HTML][HTML] Concurrent structural and biophysical traits link with immunoglobulin light chains amyloid propensity

L Oberti, P Rognoni, A Barbiroli, F Lavatelli, R Russo… - Scientific reports, 2017 - nature.com
Light chain amyloidosis (AL), the most common systemic amyloidosis, is caused by the
overproduction and the aggregation of monoclonal immunoglobulin light chains (LC) in …

Opposite structural effects of epigallocatechin-3-gallate and dopamine binding to α-synuclein

A Konijnenberg, S Ranica, J Narkiewicz… - Analytical …, 2016 - ACS Publications
The intrinsically disordered and amyloidogenic protein α-synuclein (AS) has been linked to
several neurodegenerative states, including Parkinson's disease. Here, nanoelectrospray …

[HTML][HTML] (−)-Epigallocatechin-3-gallate (EGCG) inhibits fibrillation, disaggregates amyloid fibrils of α-synuclein, and protects PC12 cells against α-synuclein-induced …

J Zhao, Q Liang, Q Sun, C Chen, L Xu, Y Ding, P Zhou - Rsc Advances, 2017 - pubs.rsc.org
α-Synuclein (α-Syn) aggregates are the major component of Lewy bodies (LB), which is a
pathological hallmark in the brain tissue of Parkinson's disease (PD) patients. It has been …

[HTML][HTML] Inhibition by small-molecule ligands of formation of amyloid fibrils of an immunoglobulin light chain variable domain

B Brumshtein, SR Esswein, L Salwinski, ML Phillips… - Elife, 2015 - elifesciences.org
Overproduction of immunoglobulin light chains leads to systemic amyloidosis, a lethal
disease characterized by the formation of amyloid fibrils in patients' tissues. Excess light …

[HTML][HTML] Aggregation of full-length immunoglobulin light chains from systemic light chain amyloidosis (AL) patients is remodeled by epigallocatechin-3-gallate

K Andrich, U Hegenbart, C Kimmich, N Kedia… - Journal of Biological …, 2017 - ASBMB
Intervention into amyloid deposition with anti-amyloid agents like the polyphenol
epigallocatechin-3-gallate (EGCG) is emerging as an experimental secondary treatment …

EGCG inhibits the oligomerization of amyloid beta (16-22) hexamer: Theoretical studies

ST Ngo, DT Truong, NM Tam, MT Nguyen - Journal of Molecular Graphics …, 2017 - Elsevier
An extensive replica exchange molecular dynamics (REMD) simulation was performed to
investigate the progress patterns of the inhibition of (−)-epigallocatechin-3-gallate (EGCG) …

Unfolding and aggregation pathways of variable domains from immunoglobulin light chains

Y Meunier-Carmenate, G Valdés-García… - Biochemistry, 2023 - ACS Publications
Light chain amyloidosis is the most common form of systemic amyloidosis. This disease is
caused by the formation and deposition of amyloid fibers made from immunoglobulin light …

A Substantial Structural Conversion of the Native Monomer Leads to in‐Register Parallel Amyloid Fibril Formation in Light‐Chain Amyloidosis

L Lecoq, T Wiegand, FJ Rodriguez‐Alvarez… - …, 2019 - Wiley Online Library
Amyloid light‐chain (AL) amyloidosis is a rare disease in which plasma‐cell‐produced
monoclonal immunoglobulin light chains misfold and become deposited as fibrils in the …