The consequences of pathogenic mutations to the human prion protein
MW Van der Kamp, V Daggett - Protein Engineering, Design & …, 2009 - academic.oup.com
Prion diseases, in which the conformational transition of the native prion protein (PrP) to a
misfolded form causes aggregation and subsequent neurodegeneration, have fascinated …
misfolded form causes aggregation and subsequent neurodegeneration, have fascinated …
Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding
MW van der Kamp, V Daggett - Journal of molecular biology, 2010 - Elsevier
Transmissible spongiform encephalopathies, or prion diseases, are caused by misfolding
and aggregation of the prion protein PrP. These diseases can be hereditary in humans and …
and aggregation of the prion protein PrP. These diseases can be hereditary in humans and …
Influence of pH on the human prion protein: insights into the early steps of misfolding
MW Van der Kamp, V Daggett - Biophysical journal, 2010 - cell.com
Transmissible spongiform encephalopathies, or prion diseases, are caused by misfolding
and aggregation of the prion protein PrP. Conversion from the normal cellular form (PrP C) …
and aggregation of the prion protein PrP. Conversion from the normal cellular form (PrP C) …
Molecular dynamics as an approach to study prion protein misfolding and the effect of pathogenic mutations
MW van der Kamp, V Daggett - Prion proteins, 2011 - Springer
Computer simulation of protein dynamics offers unique high-resolution information that
complements experiment. Using experimentally derived structures of the natively folded …
complements experiment. Using experimentally derived structures of the natively folded …
Structural and dynamic properties of the human prion protein
Prion diseases involve the conformational conversion of the cellular prion protein (PrP C) to
its misfolded pathogenic form (PrP Sc). To better understand the structural mechanism of this …
its misfolded pathogenic form (PrP Sc). To better understand the structural mechanism of this …
Diverse effects on the native β-sheet of the human prion protein due to disease-associated mutations
Prion diseases are fatal neurodegenerative disorders that involve the conversion of the
normal cellular form of the prion protein (PrPC) to a misfolded pathogenic form (PrPSc) …
normal cellular form of the prion protein (PrPC) to a misfolded pathogenic form (PrPSc) …
Characterization of cell‐surface prion protein relative to its recombinant analogue: insights from molecular dynamics simulations of diglycosylated, membrane‐bound …
ML DeMarco, V Daggett - Journal of neurochemistry, 2009 - Wiley Online Library
The prion protein (PrP) is responsible for several fatal neurodegenerative diseases via
conversion from its normal to disease‐related isoform. The recombinant form of the protein is …
conversion from its normal to disease‐related isoform. The recombinant form of the protein is …
Molecular dynamics simulations capture the misfolding of the bovine prion protein at acidic pH
CJ Cheng, V Daggett - Biomolecules, 2014 - mdpi.com
Bovine spongiform encephalopathy (BSE), or mad cow disease, is a fatal
neurodegenerative disease that is transmissible to humans and that is currently incurable …
neurodegenerative disease that is transmissible to humans and that is currently incurable …
Early steps in thermal unfolding of superoxide dismutase 1 are similar to the conformational changes associated with the ALS-associated A4V mutation
T Schmidlin, K Ploeger, AL Jonsson… - … Engineering, Design & …, 2013 - academic.oup.com
There are over 100 mutations in Cu/Zn superoxide dismutase (SOD1) that result in a subset
of familial amyotrophic lateral sclerosis (fALS) cases. The hypothesis that dissociation of the …
of familial amyotrophic lateral sclerosis (fALS) cases. The hypothesis that dissociation of the …
Simulations of membrane‐bound diglycosylated human prion protein reveal potential protective mechanisms against misfolding
CJ Cheng, H Koldsø, MW Van der Kamp… - Journal of …, 2017 - Wiley Online Library
Prion diseases are associated with the misfolding of the prion protein (PrP) from its normal
cellular form (Pr PC) to its infectious scrapie form (Pr PS c). Post‐translational modifications …
cellular form (Pr PC) to its infectious scrapie form (Pr PS c). Post‐translational modifications …