Molecular dynamics as an approach to study prion protein misfolding and the effect of pathogenic mutations [PDF]
, 2011 Computer simulation of protein dynamics offers unique high-resolution information that complements experiment. Using experimentally derived structures of the natively folded prion protein (PrP), physically realistic dynamics and conformational changes ...
Valerie Daggett +3 more
core +1 more source
Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding [PDF]
, 2010 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 four of the many disease-associated missense mutants of PrP are in the ...
Valerie Daggett +3 more
core +1 more source
Mathematics of protein pathological misfolding.
, 2011 Mathematics of protein pathological ...
Ebenezer O. Armah (7937210)
core +4 more sources
Comparing the folding and misfolding energy landscapes of phosphoglycerate kinase. [PDF]
, 2011 Partitioning of polypeptides between protein folding and amyloid formation is of outstanding pathophysiological importance. Using yeast phosphoglycerate kinase as model, here we identify the features of the energy landscape that decide the fate of the ...
Gottfried Köhler +7 more
core +1 more source
Protein misfolding: understanding biology to classify and treat synucleinopathies. [PDF]
J Neural Transm (Vienna)Protein misfolding and aggregation is a major pathological hallmark in a variety of human conditions, including cancer, diabetes, and neurodegeneration. However, we still do not fully understand the role of protein accumulation in disease. Interestingly,
Outeiro TF +3 more
europepmc +3 more sources
Frontiers in Neuroscience, 2020 Background: Amyotrophic lateral sclerosis (ALS) is a rapidly progressive fatal neurodegenerative condition. There are no effective treatments. The only globally licensed medication, that prolongs life by 2–3 months, was approved by the FDA in 1995.
Elizabeth Elliott +27 more
doaj +1 more source
Protein Misfolding and Aggregation in Proteinopathies: Causes, Mechanism and Cellular Response
Diseases, 2023 Proteins are central to life functions. Alterations in the structure of proteins are reflected in their function. Misfolded proteins and their aggregates present a significant risk to the cell.
Mohammad Rehan Ajmal
doaj +1 more source
Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease. [PDF]
PLoS Biology, 2010 Neurodegenerative diseases such as Huntington disease are devastating disorders with no therapeutic approaches to ameliorate the underlying protein misfolding defect inherent to poly-glutamine (polyQ) proteins.
Daniel W Neef +2 more
doaj +1 more source
Effect of spermidine on misfolding and interactions of alpha-synuclein. [PDF]
PLoS ONE, 2012 Alpha-synuclein (α-Syn) is a 140 aa presynaptic protein which belongs to a group of natively unfolded proteins that are unstructured in aqueous solutions.
Alexey V Krasnoslobodtsev +5 more
doaj +1 more source
Impact of translational error‐induced and error‐free misfolding on the rate of protein evolution
Molecular Systems Biology, 2010 What determines the rate of protein evolution is a fundamental question in biology. Recent genomic studies revealed a surprisingly strong anticorrelation between the expression level of a protein and its rate of sequence evolution.
Jian‐Rong Yang +2 more
doaj +1 more source