Disease-relevant β2-microglobulin variants share a common amyloid fold

M Wilkinson, RU Gallardo, RM Martinez… - Nature …, 2023 - nature.com
Abstract β2-microglobulin (β2m) and its truncated variant ΔΝ6 are co-deposited in amyloid
fibrils in the joints, causing the disorder dialysis-related amyloidosis (DRA). Point mutations …

The role of the IT-state in D76N β2-microglobulin amyloid assembly: A crucial intermediate or an innocuous bystander?

HI Smith, N Guthertz, EE Cawood… - Journal of Biological …, 2020 - ASBMB
The D76N variant of human β 2-microglobulin (β 2 m) is the causative agent of a hereditary
amyloid disease. Interestingly, D76N-associated amyloidosis has a distinctive pathology …

[BOOK][B] Protein folding: An introduction

CM Gomes, PFN Faísca, CM Gomes, PFN Faísca - 2019 - Springer
We have come a long way since coining of the term protein and the early findings that
proteins are charged macromolecules composed of strings of amino acids linked by peptide …

A Self-Consistent Molecular Mechanism of β2-Microglobulin Aggregation

V Tammara, A Das - The Journal of Physical Chemistry B, 2024 - ACS Publications
Despite the consensus on the origin of dialysis-related amyloidosis (DRA) being β2-
microglobulin (β2m) aggregation, the debate on the underlying mechanism persists …

Fibril fragments from the amyloid core of lysozyme: An accelerated molecular dynamics study

EA Ermakova, ON Makshakova, YF Zuev… - Journal of Molecular …, 2021 - Elsevier
Protein aggregation and formation of amyloid fibrils are associated with many diseases and
present a ubiquitous problem in protein science. Hen egg white lysozyme (HEWL) can form …

The early phase of β2-microglobulin aggregation: perspectives from molecular simulations

RJS Loureiro, PFN Faísca - Frontiers in molecular biosciences, 2020 - frontiersin.org
Protein β2-microglobulin is the causing agent of two amyloidosis, dialysis related
amyloidosis (DRA), affecting the bones and cartilages of individuals with chronic renal …

Investigation of D76N β2-Microglobulin Using Protein Footprinting and Structural Mass Spectrometry

O Cornwell, JR Ault, NJ Bond, SE Radford… - Journal of the …, 2021 - ACS Publications
NMR studies and X-ray crystallography have shown that the structures of the 99-residue
amyloidogenic protein β2-microglobulin (β2m) and its more aggregation-prone variant …

Transient intermediates are populated in the folding pathways of single-domain two-state folding protein L

H Maity, G Reddy - The Journal of Chemical Physics, 2018 - pubs.aip.org
Small single-domain globular proteins, which are believed to be dominantly two-state
folders, played an important role in elucidating various aspects of the protein folding …

Loosening of Side-Chain Packing Associated with Perturbations in Peripheral Dynamics Induced by the D76N Mutation of β2-Microglobulin Revealed by Pressure …

K Sakurai, R Tomiyama, T Shiraki, Y Yonezawa - Biomolecules, 2019 - mdpi.com
β2-Microglobulin (β2m) is the causative protein of dialysis-related amyloidosis, and its D76N
variant is less stable and more prone to aggregation. Since their crystal structures are …

The early phase of β2m aggregation: an integrative computational study framed on the D76N mutant and the ΔN6 variant

R JS Loureiro, D Vila-Viçosa, M Machuqueiro… - Biomolecules, 2019 - mdpi.com
Human β2-microglobulin (b2m) protein is classically associated with dialysis-related
amyloidosis (DRA). Recently, the single point mutant D76N was identified as the causative …