Applications of hydrogen/deuterium exchange MS from 2012 to 2014
Hydrogen/deuterium exchange (HDX) detected by mass spectrometry (MS) is extraordinarily
useful in the study of many aspects of proteins, especially the analysis of protein …
useful in the study of many aspects of proteins, especially the analysis of protein …
Analysis of protein aggregation in neurodegenerative disease
JT Pedersen, NHH Heegaard - Analytical chemistry, 2013 - ACS Publications
Pathological protein and peptide aggregation are key events in a number of chronic and
devastating neurodegenerative conditions including dementias such as Alzheimer's and …
devastating neurodegenerative conditions including dementias such as Alzheimer's and …
Cryo-EM structures of prion protein filaments from Gerstmann–Sträussler–Scheinker disease
Prion protein (PrP) aggregation and formation of PrP amyloid (APrP) are central events in
the pathogenesis of prion diseases. In the dominantly inherited prion protein amyloidosis …
the pathogenesis of prion diseases. In the dominantly inherited prion protein amyloidosis …
Protein-solvent interfaces in human Y145Stop prion protein amyloid fibrils probed by paramagnetic solid-state NMR spectroscopy
The C-terminally truncated Y145Stop variant of prion protein (PrP23-144), which is
associated with heritable PrP cerebral amyloid angiopathy in humans and also capable of …
associated with heritable PrP cerebral amyloid angiopathy in humans and also capable of …
Structure of prion β‐oligomers as determined by short‐distance crosslinking constraint‐guided discrete molecular dynamics simulations
JJ Serpa, KI Popov, EV Petrotchenko… - …, 2021 - Wiley Online Library
The conversion of the native monomeric cellular prion protein (PrPC) into an aggregated
pathological β‐oligomeric form (PrPβ) and an infectious form (PrPSc) is the central element …
pathological β‐oligomeric form (PrPβ) and an infectious form (PrPSc) is the central element …
Types and strains: their essential role in understanding protein aggregation in neurodegenerative diseases
WM Wemheuer, A Wrede… - Frontiers in aging …, 2017 - frontiersin.org
Protein misfolding and aggregation is a key event in diseases like Alzheimer's disease (AD)
or Parkinson's disease (PD) and is associated with neurodegeneration. Factors that initiate …
or Parkinson's disease (PD) and is associated with neurodegeneration. Factors that initiate …
N-terminal prion protein peptides (PrP (120–144)) form parallel in-register β-sheets via multiple nucleation-dependent pathways
The prion diseases are a family of fatal neurodegenerative diseases associated with the
misfolding and accumulation of normal prion protein (PrP C) into its pathogenic scrapie form …
misfolding and accumulation of normal prion protein (PrP C) into its pathogenic scrapie form …
Elucidating the structure of an infectious protein
M Zweckstetter, JR Requena, H Wille - PLoS Pathogens, 2017 - journals.plos.org
The infectious isoform of the mammalian prion protein, PrPSc, was the first protein to be
identified as an infectious protein [1](Table 1). PrPSc can be transmitted both from cell-to-cell …
identified as an infectious protein [1](Table 1). PrPSc can be transmitted both from cell-to-cell …
Structural characterization of semen coagulum-derived SEM1 (86–107) amyloid fibrils that enhance HIV-1 infection
KC French, NR Roan, GI Makhatadze - Biochemistry, 2014 - ACS Publications
SEM1 (86–107) is a 22-residue peptide corresponding to residues 86–107 in the
semenogelin I protein. SEM1 (86–107) is an abundant component of freshly liquefied semen …
semenogelin I protein. SEM1 (86–107) is an abundant component of freshly liquefied semen …
Using isotopically-coded hydrogen peroxide as a surface modification reagent for the structural characterization of prion protein aggregates
The conversion of the cellular prion protein (PrP C) into aggregated ß-oligomeric (PrP ß) and
fibril (PrP Sc) forms is the central element in the development of prion diseases. Here we …
fibril (PrP Sc) forms is the central element in the development of prion diseases. Here we …