Article

Characterising the early aggregation events of human lysozyme using single-molecule microscopy

2019-01-01

Abstract excerpt

Human lysozyme (HuL) is a widely characterised protein whose mutational variants misfold, forming amyloid fibrils that are associated with a rare systemic amyloidosis. Given that a number of proteins, including lysozyme, can misfold and give rise to disorders such as Alzheimer's disease, Parkinson's disease, and type II diabetes, it is vital to understand the mechanistic features by which this process occurs, in o...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: e6d21dec-55af-5abb-a66a-883fed1680d1
DOI: 10.17863/cam.38140

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Characterising the early aggregation events of human lysozyme using single-molecule microscopyDOI 10.17863/cam.38140Read

Local cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution.Semantic proximity Read

Characterisation of the structural, dynamic and aggregation properties of the W64R amyloidogenic variant of human lysozyme.Semantic proximity Read

An interdisciplinary approach to studying mechanistic, structural and toxic features of protein aggregates associated with neurodegenerative disordersSemantic proximity Read

Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants.Semantic proximity Read

Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme.Semantic proximity Read

Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme.Semantic proximity Read

A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation.Semantic proximity Read

In silico prediction of novel residues involved in amyloid primary nucleation of human I56T and D67H lysozyme.Semantic proximity Read

Structural and folding dynamic properties of the T70N variant of human lysozyme.Semantic proximity Read

Wild-type hen egg white lysozyme aggregation in vitro can form self-seeding amyloid conformational variantsSemantic proximity Read

Early stages for Parkinson's development: alpha-synuclein misfolding and aggregation.Semantic proximity Read

Amyloidogenic lysozymes accumulate in the endoplasmic reticulum accompanied by the augmentation of ER stress signals.Semantic proximity Read