Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

Alzheimer's disease (AD) challenges our society with an annual estimated cost of $1.08
trillion in the United States alone by 2050. 1 AD is a progressive irreversible neurological …

The present advances in biology are related to progress in genomics, proteomics, and other
“-omics”, including glycomics, working with a large amount of data regarding human and …

Protein aggregation has now become recognised as an important and generic aspect of
protein energy landscapes. Since the discovery that numerous human diseases are caused …

Intrinsically disordered proteins (IDPs) play many biological roles in the human proteome
ranging from vesicular transport, signal transduction to neurodegenerative diseases. The Aβ …

The progress toward understanding the molecular basis of Alzheimers's disease is strongly
connected to elucidating the early aggregation events of the amyloid-β (Aβ) peptide …

Amyloids can have normal biological functions. 1r3 However, amyloidogenic proteins can
also form unwanted oligomeric or polymeric aggregates when disturbed from their native …

We investigated the effects of 17 widely used atomistic molecular mechanics force fields
(MMFFs) on the structures and kinetics of amyloid peptide assembly. To this end, we …

Nanostructured scaffolds recently showed great promise in tissue engineering:
nanomaterials can be tailored at the molecular level and scaffold morphology may more …

We have revisited the protein coarse‐grained optimized potential for efficient structure
prediction (OPEP). The training and validation sets consist of 13 and 16 protein targets …