[HTML][HTML] Small heat shock proteins: role in cellular functions and pathology

R Bakthisaran, R Tangirala, CM Rao - Biochimica et Biophysica Acta (BBA) …, 2015 - Elsevier
Small heat shock proteins (sHsps) are conserved across species and are important in stress
tolerance. Many sHsps exhibit chaperone-like activity in preventing aggregation of target …

Self‐assembling amphiphilic peptides

A Dehsorkhi, V Castelletto… - Journal of Peptide …, 2014 - Wiley Online Library
The self‐assembly of several classes of amphiphilic peptides is reviewed, and selected
applications are discussed. We discuss recent work on the self‐assembly of lipopeptides …

Amyloid fibers provide structural integrity to Bacillus subtilis biofilms

D Romero, C Aguilar, R Losick… - Proceedings of the …, 2010 - National Acad Sciences
Bacillus subtilis forms biofilms whose constituent cells are held together by an extracellular
matrix. Previous studies have shown that the protein TasA and an exopolysaccharide are …

Structure of the cross-β spine of amyloid-like fibrils

R Nelson, MR Sawaya, M Balbirnie, AØ Madsen… - Nature, 2005 - nature.com
Numerous soluble proteins convert to insoluble amyloid-like fibrils that have common
properties. Amyloid fibrils are associated with fatal diseases such as Alzheimer's, and …

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 …

[PDF][PDF] 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 …

Conformational constraints for amyloid fibrillation: the importance of being unfolded

VN Uversky, AL Fink - Biochimica et Biophysica Acta (BBA)-Proteins and …, 2004 - Elsevier
Recent reports give strong support to the idea that amyloid fibril formation and the
subsequent development of protein deposition diseases originate from conformational …

Molecular basis for insulin fibril assembly

MI Ivanova, SA Sievers, MR Sawaya… - Proceedings of the …, 2009 - National Acad Sciences
In the rare medical condition termed injection amyloidosis, extracellular fibrils of insulin are
observed. We found that the segment of the insulin B-chain with sequence LVEALYL is the …

Molecular basis for amyloid fibril formation and stability

OS Makin, E Atkins, P Sikorski… - Proceedings of the …, 2005 - National Acad Sciences
The molecular structure of the amyloid fibril has remained elusive because of the difficulty of
growing well diffracting crystals. By using a sequence-designed polypeptide, we have …

Prediction of “aggregation-prone” and “aggregation-susceptible” regions in proteins associated with neurodegenerative diseases

AP Pawar, KF Dubay, J Zurdo, F Chiti… - Journal of molecular …, 2005 - Elsevier
Increasing evidence indicates that many peptides and proteins can be converted in vitro into
highly organised amyloid structures, provided that the appropriate experimental conditions …