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 PrP(C) - into a disease associated, fibril-forming isoform PrP(Sc). This conformational transition from the alpha-helix-rich cellular form into the mainly beta-sheet containing ...
Kupfer, L, Hinrichs, W, Groschup, M.H
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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
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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 ...
Daggett, Valerie, van der Kamp, Marc W
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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
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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
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Systematic interaction network filtering identifies CRMP1 as a novel suppressor of huntingtin misfolding and neurotoxicity [PDF]
, 2015 Assemblies of huntingtin (HTT) fragments with expanded polyglutamine (polyQ) tracts are a pathological hallmark of Huntington's disease (HD). The molecular mechanisms by which these structures are formed and cause neuronal dysfunction and toxicity are ...
Andrade-Navarro, Miguel A. +24 more
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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
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Neuroprotection targeting protein misfolding on chronic cerebral hypoperfusion in the context of metabolic syndrome [PDF]
, 2018 Metabolic syndrome (MetS) is a cluster of risk factors that lead to microvascular dysfunction and chronic cerebral hypoperfusion (CCH). Long-standing reduction in oxygen and energy supply leads to brain hypoxia and protein misfolding, thereby linking CCH
Capani, Francisco +6 more
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Theoretical model of prion propagation: A misfolded protein induces misfolding [PDF]
Proceedings of the National Academy of Sciences, 2005 There is a hypothesis that dangerous diseases such as bovine spongiform encephalopathy, Creutzfeldt-Jakob, Alzheimer's, fatal familial insomnia, and several others are induced by propagation of wrong or misfolded conformations of some vital proteins. If for some reason the misfolded conformations were acquired by many such protein molecules it might ...
Edyta, Małolepsza +3 more
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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
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