Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade

F Chiti, CM Dobson - Annual review of biochemistry, 2017 - annualreviews.org
Peptides and proteins have been found to possess an inherent tendency to convert from
their native functional states into intractable amyloid aggregates. This phenomenon is …

Protein aggregation–mechanisms, detection, and control

W Wang, CJ Roberts - International journal of pharmaceutics, 2018 - Elsevier
Protein aggregation has been recognized as one of the major challenges in the
development and commercialization of successful protein-based drug products because of …

[HTML][HTML] Leveraging knowledge of HDLs major protein ApoA1: Structure, function, mutations, and potential therapeutics

AS Bhale, K Venkataraman - Biomedicine & Pharmacotherapy, 2022 - Elsevier
Abstract Apolipoprotein A1 (ApoA1) is a member of the Apolipoprotein family of proteins. It's
a vital protein that helps in the production of high-density lipoprotein (HDL) particles, which …

Familial amyloid polyneuropathy

V Planté-Bordeneuve, G Said - The Lancet Neurology, 2011 - thelancet.com
Familial amyloid polyneuropathies (FAPs) are a group of life-threatening multisystem
disorders transmitted as an autosomal dominant trait. Nerve lesions are induced by deposits …

Apolipoprotein A‐I: the dual face of a protein

A Arciello, R Piccoli, DM Monti - FEBS letters, 2016 - Wiley Online Library
Conformational plasticity and flexibility are key structural features of Apo AI in lipid
metabolism. Amyloidogenic single point mutations, associated with incurable familial …

The crystal structure of the C-terminal truncated apolipoprotein AI sheds new light on amyloid formation by the N-terminal fragment

O Gursky, X Mei, D Atkinson - Biochemistry, 2012 - ACS Publications
Apolipoprotein AI (apoA-I) is the main protein of plasma high-density lipoproteins (HDL, or
good cholesterol) that remove excess cell cholesterol and protect against atherosclerosis. In …

Amyloidogenic 60–71 deletion/ValThr insertion mutation of apolipoprotein AI generates a new aggregation-prone segment that promotes nucleation through entropic …

N Namba, T Ohgita, H Tamagaki-Asahina… - Scientific reports, 2023 - nature.com
The N-terminal fragment of apolipoprotein AI (apoA-I), comprising residues 1–83, contains
three segments prone to aggregation: residues 14–22, 53–58, and 67–72. We previously …

Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions

K Yanagi, M Ashizaki, H Yagi, K Sakurai, YH Lee… - Journal of Biological …, 2011 - ASBMB
Although amyloid fibrils deposit with various proteins, the comprehensive mechanism by
which they form remains unclear. We studied the formation of fibrils of human islet amyloid …

Amyloidogenic mutations in human apolipoprotein A‐I are not necessarily destabilizing–a common mechanism of apolipoprotein A‐I misfolding in familial amyloidosis …

M Das, X Mei, S Jayaraman, D Atkinson… - The FEBS …, 2014 - Wiley Online Library
High‐density lipoproteins and their major protein, apolipoprotein A‐I (apoA‐I), remove
excess cellular cholesterol and protect against atherosclerosis. However, in acquired …

A new prion disease: relationship with central and peripheral amyloidoses

S Mead, MM Reilly - Nature Reviews Neurology, 2015 - nature.com
Prion diseases are typically recognized as rapidly progressive dementing illnesses that also
feature myoclonus and cerebellar ataxia. Several families have now been described with a …