Mass spectrometry is a central technology in the life sciences, providing our most
comprehensive account of the molecular inventory of the cell. In parallel with developments …

Peptides or proteins convert under some conditions from their soluble forms into highly
ordered fibrillar aggregates. Such transitions can give rise to pathological conditions ranging …

Parkinson's disease (PD) and Multiple System Atrophy (MSA) are clinically distinctive
diseases that feature a common neuropathological hallmark of aggregated α-synuclein …

Alzheimer's disease is the most fatal neurodegenerative disorder wherein the process of
amyloid-β (Aβ) amyloidogenesis appears causative. Here, we present the 3D structure of the …

Copper is too redox active to exist in an unbound form in the cell without causing oxidative
damage: an upper limit of 10-18 M for the free concentration of Cu (II) in unstressed cells has …

We describe solid-state nuclear magnetic resonance (NMR) measurements on fibrils formed
by the 40-residue β-amyloid peptide associated with Alzheimer's disease (Aβ1-40) that …

Recent reports give strong support to the idea that amyloid fibril formation and the
subsequent development of protein deposition diseases originate from conformational …

The aggregation of proteins into amyloid fibrils is associated with several neurodegenerative
diseases. In Parkinson's disease it is believed that the aggregation of α-synuclein (α-syn) …

The protein–nanoparticle (NP) interface is a current frontier of multiple disciplines, full of
challenges and opportunities. The unique behaviors of nanomaterials (NMs) bring many …

Many, perhaps most, proteins, are capable of forming self-propagating, β-sheet (amyloid)
aggregates. Amyloid-like aggregates are found in a wide range of diseases and underlie …