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Amyloidogenic Unfolding Intermediates Differentiate Sheep Prion Protein Variants
Journal of Molecular Biology, 2002Sheep is a unique example among mammalian species to present a strong correlation between genotype and prion disease susceptibility phenotype. Indeed a well-defined set of PrP polymorphisms at positions 136, 154 and 171 (sheep numbering) govern scrapie susceptibility, ranging from very high susceptibility for V136-R154-Q171 variant (VRQ) to resistance ...
Rezaei, Human +7 more
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Amyloidogenic Proteins in Mice
1986Amyloidosis can be induced in mice by casein, endotoxin, or other substances. Results of biochemical studies on the amyloid protein in experimentally induced amyloidosis (1–2) are similar to the findings of secondary amyloidosis in humans. There have also been numerous reports on spontaneous amyloidosis in mice (3–6).
Keiichi Higuchi, Toshio Takeda
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Probing the interactions between amyloidogenic proteins and bio-membranes
Biophysical Chemistry, 2023Protein misfolding diseases (PMDs) in humans are characterized by the deposition of protein aggregates in tissues, including Alzheimer's disease, Parkinson's disease, type 2 diabetes, and amyotrophic lateral sclerosis. Misfolding and aggregation of amyloidogenic proteins play a central role in the onset and progression of PMDs, and these processes are ...
Liang, Ma +4 more
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Molecular dynamics studies on amyloidogenic proteins
2014Molecular dynamics simulations, coupled with experimental investigations, could improve our understanding of the protein aggregation and fibrillization process of amyloidogenic proteins. Computational tools are being applied to solve the protein aggregation and fibrillization problem, providing insight into amyloid structures and aggregation mechanisms.
Sylwia Rodziewicz-Motowidło +2 more
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Dipyridamole for tracking amyloidogenic proteins aggregation and enhancing polyubiquitination
Archives of Biochemistry and Biophysics, 2022Dipyridamole is currently used as a medication that inhibits blood clot formation and it is also investigated in the context of neurodegenerative and other amyloid related diseases. Here, we propose this molecule as a new diagnostic tool to follow the aggregation properties of three different amyloidogenic proteins tested (insulin, amylin and amyloid β
Laneri, Francesca +6 more
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Amyloid oligomers: spectroscopic characterization of amyloidogenic protein states
The FEBS Journal, 2010It is assumed that protein fibrils manifested in amyloidosis result from an aggregation reaction involving small misfolded protein sequences being in an ‘oligomeric’ or ‘prefibrillar’ state. This review covers recent optical spectroscopic studies of amyloid protein misfolding, oligomerization and amyloid fibril growth.
Mikael, Lindgren, Per, Hammarström
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The role of amyloidogenic protein oligomerization in neurodegenerative disease
Journal of Molecular Medicine, 2013A common pathological hallmark in many neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease, and Huntington's disease, is the formation of fibrillar protein aggregates referred to as amyloids. The amyloidogenic aggregates were long thought to be toxic, but mounting evidence supports the notion that a variety of amyloid ...
Gregor P, Lotz, Justin, Legleiter
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Single-Molecule Studies of Amyloidogenic Proteins
2012Single-molecule biophysical tools have developed in the past two decades from jaw-dropping attractions to essential laboratory tools. In recent years, these methods have been applied to the exploration of the structure, mechanics, and mechanically driven conformational changes of amyloidogenic protein systems as well.
Miklós S. Z. Kellermayer +5 more
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Alternative conformations of amyloidogenic proteins govern their behavior
Current Opinion in Structural Biology, 1996Recent publications strongly support the hypothesis that conformational changes in amyloidogenic proteins lead to amyloid fibril formation and cause disease. Biophysical studies on several amyloidogenic proteins provide insights into the conformational changes required for fibrilogenesis.
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Interaction of selected biomolecules and metabolites with amyloidogenic proteins
Journal of Biomolecular Structure and Dynamics, 2020The current manuscript reports docking and molecular interaction analyses of three FDA approved acetylcholinesterase inhibitors, nitrogenous bases and nucleotides with amyloidogenic proteins like hen egg white lysozyme (HEWL) and amyloid β peptide. After prediction of aggregation-prone regions in hen egg-white lysozyme and amyloid β peptide, grid boxes
Debanjan, Kundu +2 more
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