Results 11 to 20 of about 95,914 (208)
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 structural transitions need to be regulated in both time and space.
Md Mozzammel Haque, Richard Bayford
openaire +3 more sources
Misfolding of a bacterial autotransporter [PDF]
Protein Science, 2005 AbstractThe adhesin involved in diffuse adherence (AIDA) is an autotransporter protein that confers the diffuse adherence phenotype to certain diarrheagenic Escherichia coli strains. It consists of a 49 amino acid signal peptide, a 797 amino acid passenger domain, and a 440 amino acid β‐domain integrated into the outer membrane.
Mogensen, Jesper E. +3 more
openaire +4 more sources
Protein Misfolding and Neurodegeneration [PDF]
Archives of Neurology, 2008 A key 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 synaptic dysfunction, neuronal apoptosis, brain damage, and disease.
Soto, Claudio, Estrada, Lisbell D.
openaire +2 more sources
Identifying rescuers of misfolding [PDF]
Nature Biomedical Engineering, 2017 High-throughput screening of large libraries of cyclic peptides expressed in bacteria yields rescuers of the pathogenic misfolding of proteins associated with neurodegenerative diseases.
Langenberg, Tobias +2 more
openaire +2 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
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
openaire +2 more sources
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
openaire +2 more sources
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
core +2 more sources
Misfolding and Amyloid Aggregation of Apomyoglobin [PDF]
International Journal of Molecular Sciences, 2013 Apomyoglobin is an excellent example of a monomeric all α-helical globular protein whose folding pathway has been extensively studied and well characterized. Structural perturbation induced by denaturants or high temperature as well as amino acid substitution have been described to induce misfolding and, in some cases, aggregation.
IANNUZZI, Clara +3 more
openaire +3 more sources
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
core +1 more source