Intrinsically disordered proteins: regulation and disease

MM Babu, R van der Lee, NS de Groot… - Current opinion in …, 2011 - Elsevier
Intrinsically disordered proteins (IDPs) are enriched in signaling and regulatory functions
because disordered segments permit interaction with several proteins and hence the re-use …

[HTML][HTML] Biology of amyloid: structure, function, and regulation

J Greenwald, R Riek - Structure, 2010 - cell.com
Amyloids are highly ordered cross-β sheet protein aggregates associated with many
diseases including Alzheimer's disease, but also with biological functions such as hormone …

Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils

M Ahmed, J Davis, D Aucoin, T Sato, S Ahuja… - Nature structural & …, 2010 - nature.com
Abstract The amyloid-β1–42 (Aβ42) peptide rapidly aggregates to form oligomers, protofibils
and fibrils en route to the deposition of amyloid plaques associated with Alzheimer's …

Ion mobility–mass spectrometry reveals a conformational conversion from random assembly to β-sheet in amyloid fibril formation

C Bleiholder, NF Dupuis, T Wyttenbach, MT Bowers - Nature chemistry, 2011 - nature.com
Amyloid cascades that lead to peptide β-sheet fibrils and plaques are central to many
important diseases. Recently, intermediate assemblies of these cascades were identified as …

Structural characterization of a soluble amyloid β-peptide oligomer

L Yu, R Edalji, JE Harlan, TF Holzman, AP Lopez… - Biochemistry, 2009 - ACS Publications
Alzheimer's disease (AD) is a neurodegenerative disorder that is linked to the presence of
amyloid β-peptides that can form insoluble fibrils or soluble oligomeric assemblies. Soluble …

Impact of nanoparticles on amyloid peptide and protein aggregation: a review with a focus on gold nanoparticles

T John, A Gladytz, C Kubeil, LL Martin, HJ Risselada… - Nanoscale, 2018 - pubs.rsc.org
Society is increasingly exposed to nanoparticles as they are ubiquitous in nature and
introduced as man-made air pollutants and as functional ingredients in cosmetic products as …

Structure–activity Relationships of amyloid beta‐aggregation inhibitors based on curcumin: influence of linker length and flexibility

AA Reinke, JE Gestwicki - Chemical biology & drug design, 2007 - Wiley Online Library
Self‐assembly of amyloid beta into fibrillar plaques is characteristic of Alzheimer's disease
and oligomers of this peptide are believed to be involved in neurodegeneration. Natural …

Fundamentals of cross-seeding of amyloid proteins: an introduction

B Ren, Y Zhang, M Zhang, Y Liu, D Zhang… - Journal of materials …, 2019 - pubs.rsc.org
Misfolded protein aggregates formed by the same (homologous) or different
(heterologous/cross) sequences are the pathological hallmarks of many protein misfolding …

Non‐native protein aggregation kinetics

CJ Roberts - Biotechnology and bioengineering, 2007 - Wiley Online Library
Experimental kinetics of non‐native protein aggregation are of practical importance in that
they help dictate viable processing, formulation, and storage conditions for biotechnology …

Principles, approaches, and challenges for predicting protein aggregation rates and shelf life

WF Weiss IV, TM Young, CJ Roberts - Journal of pharmaceutical sciences, 2009 - Elsevier
Control and prevention of unwanted aggregation for therapeutic proteins is a ubiquitous
hurdle during biopharmaceutical product manufacture, storage, shipping, and …