Results 21 to 30 of about 3,403,581 (279)

Insights from nature: A review of natural compounds that target protein misfolding in vivo

open access: yesCurrent Research in Biotechnology, 2020
Protein misfolding is fundamental to a number of human disorders including Alzheimer’s disease, prion diseases, Parkinson’s disease and type 2 diabetes mellitus. To date, there are still no cures for protein misfolding disorders.
Cassandra Terry
doaj   +1 more source

Protein Misfolding and the Serpinopathies [PDF]

open access: yesPrion, 2007
The serpins are the largest superfamily of protease inhibitors. They are found in almost all branches of life including viruses, prokaryotes and eukaryotes. They inhibit their target protease by a unique mechanism that involves a large conformational transition and the translocation of the enzyme from the upper to the lower pole of the protein.
Didier, Belorgey   +3 more
openaire   +2 more sources

Highly efficient protein misfolding cyclic amplification. [PDF]

open access: yesPLoS Pathogens, 2011
Protein misfolding cyclic amplification (PMCA) provides faithful replication of mammalian prions in vitro and has numerous applications in prion research.
Nuria Gonzalez-Montalban   +6 more
doaj   +1 more source

Molecular dynamics as an approach to study prion protein misfolding and the effect of pathogenic mutations [PDF]

open access: yes, 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]

open access: yes, 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

Protein Misfolding and Aggregation in Proteinopathies: Causes, Mechanism and Cellular Response

open access: yesDiseases, 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

Comparing the folding and misfolding energy landscapes of phosphoglycerate kinase. [PDF]

open access: yes, 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   +8 more
core   +1 more source

Therapeutic Targeting of Proteostasis in Amyotrophic Lateral Sclerosis—a Systematic Review and Meta-Analysis of Preclinical Research

open access: yesFrontiers 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

Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease. [PDF]

open access: yesPLoS 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

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