Results 11 to 20 of about 3,647,798 (263)
Role of Protein Misfolding and Proteostasis Deficiency in Protein Misfolding Diseases and Aging [PDF]
International Journal of Cell Biology, 2013 The misfolding, aggregation, and tissue accumulation of proteins are common events in diverse chronic diseases, known as protein misfolding disorders.
Karina Cuanalo-Contreras +2 more
doaj +4 more sources
Protein misfolding thermodynamics [PDF]
The Journal of Physical Chemistry Letters, 2019 It is known that protein misfolding is governed by the hydrophobic effect of solutes at hydrophobic amino acid side chains. The hydrophobic force of nonaqueous solutes acts as a driving force for the spatial rearrangement of protein side chains, whose ...
Haque, M., Bayford, R.
core +5 more sources
Protein Misfolding and Neurodegeneration [PDF]
Archives of Neurology, 2008 Akey molecular pathway implicated in diverse neurodegenerative diseases is the misfolding, aggregation, and accumulation of proteins in the brain. Compelling evidence strongly supports the hypothesis that accumulation of misfolded proteins leads to ...
Estrada, Lisbell D., Soto, Claudio
core +4 more sources
Prion Protein Misfolding [PDF]
Current Molecular Medicine, 2009 The crucial event in the development of transmissible spongiform encephalopathies (TSEs) is the conformational change of a host-encoded membrane protein - the cellular PrPC - into a disease associated, fibril-forming isoform PrPSc.
Kupfer, Leila +2 more
core +3 more sources
Protein misfolding in neurodegenerative diseases
Neuropathology and Applied Neurobiology, 2004 A common pathogenic mechanism shared by diverse neurodegenerative disorders, like Alzheimer's disease, Parkinson's disease, Huntington's disease and transmissible spongiform encephalopathies, may be altered protein homeostasis leading to protein ...
Hadjigeorgiou, G. M. +7 more
core +3 more sources
Protein Misfolding Cyclic Amplification
, 2023 Prion diseases are caused by a conformational conversion of the cellular prion protein (PrPC) to a pathological conformer (PrPSc). The “prion-only” hypothesis suggests that PrPSc is the infectious agent that propagates the disease acting as a template ...
Soto, Claudio +2 more
core +4 more sources
Protein Misfolding and Human Disease [PDF]
The Scientific World Journal, 2002 Protein folding is perhaps the most fundamental process associated with the generation of functional structures in biology. There has been considerable progress in the last few years in understanding the underlying principles that govern this highly complex process.
Christopher Dobson
doaj +3 more sources
Protein Misfolding and Neurodegenerative Diseases [PDF]
International Journal of Cell Biology, 2014 This special issue includes fifteen reviews and two original research articles by leading scientists in the fields of neuropathology, biochemistry, and cell biology, dealing with the role of protein aggregation and prion-like propagation of protein misfolding in neurodegenerative diseases.
Alessio Cardinale +2 more
doaj +3 more sources
Protein Misfolding and the Serpinopathies [PDF]
Prion, 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]
PLoS 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