[HTML][HTML] Small heat shock proteins: role in cellular functions and pathology
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 …
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 …
applications are discussed. We discuss recent work on the self‐assembly of lipopeptides …
Amyloid fibers provide structural integrity to Bacillus subtilis biofilms
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 …
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 …
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 …
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 …
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 …
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 …
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 …
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
Increasing evidence indicates that many peptides and proteins can be converted in vitro into
highly organised amyloid structures, provided that the appropriate experimental conditions …
highly organised amyloid structures, provided that the appropriate experimental conditions …