[HTML][HTML] Implications of peptide assemblies in amyloid diseases

PC Ke, MA Sani, F Ding, A Kakinen, I Javed… - Chemical Society …, 2017 - pubs.rsc.org
Neurodegenerative disorders and type 2 diabetes are global epidemics compromising the
quality of life of millions worldwide, with profound social and economic implications. Despite …

Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution

M Stefani, CM Dobson - Journal of molecular medicine, 2003 - Springer
The deposition of proteins in the form of amyloid fibrils and plaques is the characteristic
feature of more than 20 degenerative conditions affecting either the central nervous system …

Stimuli-responsive, pentapeptide, nanofiber hydrogel for tissue engineering

JD Tang, C Mura, KJ Lampe - Journal of the American Chemical …, 2019 - ACS Publications
Short peptides are uniquely versatile building blocks for self-assembly. Supramolecular
peptide assemblies can be used to construct functional hydrogel biomaterials—an attractive …

Neurotoxicity of Alzheimer's disease Aβ peptides is induced by small changes in the Aβ42 to Aβ40 ratio

I Kuperstein, K Broersen, I Benilova, J Rozenski… - The EMBO …, 2010 - embopress.org
The amyloid peptides Aβ40 and Aβ42 of Alzheimer's disease are thought to contribute
differentially to the disease process. Although Aβ42 seems more pathogenic than Aβ40, the …

Understanding amyloid aggregation by statistical analysis of atomic force microscopy images

J Adamcik, JM Jung, J Flakowski, P De Los Rios… - Nature …, 2010 - nature.com
The aggregation of proteins is central to many aspects of daily life, including food
processing, blood coagulation, eye cataract formation disease and prion-related …

The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions

R Mezzenga, P Fischer - Reports on Progress in Physics, 2013 - iopscience.iop.org
The aggregation of proteins is of fundamental relevance in a number of daily phenomena,
as important and diverse as blood coagulation, medical diseases, or cooking an egg in the …

Principles of protein folding, misfolding and aggregation

CM Dobson - Seminars in cell & developmental biology, 2004 - Elsevier
This review summarises our current understanding of the underlying and universal
mechanism by which newly synthesised proteins achieve their biologically functional states …

The structural basis of protein folding and its links with human disease

CM Dobson - … Transactions of the Royal Society of …, 2001 - royalsocietypublishing.org
The ability of proteins to fold to their functional states following synthesis in the intracellular
environment is one of the most remarkable features of biology. Substantial progress has …

The protofilament structure of insulin amyloid fibrils

JL Jiménez, EJ Nettleton, M Bouchard… - Proceedings of the …, 2002 - National Acad Sciences
Under solution conditions where the native state is destabilized, the largely helical
polypeptide hormone insulin readily aggregates to form amyloid fibrils with a characteristic …

FoldAmyloid: a method of prediction of amyloidogenic regions from protein sequence

SO Garbuzynskiy, MY Lobanov, OV Galzitskaya - Bioinformatics, 2010 - academic.oup.com
Motivation: Amyloidogenic regions in polypeptide chains are very important because such
regions are responsible for amyloid formation and aggregation. It is useful to be able to …