2005
DOI: 10.1590/s0100-879x2005000800006
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Abstract: The main hypothesis for prion diseases proposes that the cellular protein (PrP C ) can be altered into a misfolded, ß-sheet-rich isoform, the PrP Sc (from scrapie). The formation of this abnormal isoform then triggers the transmissible spongiform encephalopathies. Here, we discuss the use of high pressure as a tool to investigate this structural transition and to populate possible intermediates in the folding/unfolding pathway of the prion protein. The latest findings on the application of high pressure to the… Show more

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Cited by 10 publications
(9 citation statements)
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“…The freeenergy diagram depicted in Figure 2 highlights a model in which the cellular isoform is in a metastable conformation. High-pressure FTIR and pressure perturbation calorimetry studies have demonstrated that the cellular PrP isoform is more hydrated and has a larger solvent-accessible surface area than aggregated a-rPrP obtained by thermal treatment (55)(56)(57). The role of hydration in the folding stability and amyloidogenicity of PrP has been corroborated by computer modeling and molecular dynamics (58,59).…”
Section: The Prion Scrapie (Prp Sc ) and The Conversion Reactionmentioning
confidence: 95%
“…The freeenergy diagram depicted in Figure 2 highlights a model in which the cellular isoform is in a metastable conformation. High-pressure FTIR and pressure perturbation calorimetry studies have demonstrated that the cellular PrP isoform is more hydrated and has a larger solvent-accessible surface area than aggregated a-rPrP obtained by thermal treatment (55)(56)(57). The role of hydration in the folding stability and amyloidogenicity of PrP has been corroborated by computer modeling and molecular dynamics (58,59).…”
Section: The Prion Scrapie (Prp Sc ) and The Conversion Reactionmentioning
confidence: 95%
“…Fax: þ36-1-2666656. 1 Abbreviations: PGK, yeast (Saccharomyces cerevisiae) phosphoglycerate kinase (UniProtKB/Swiss-Prot accession number P00560); EDTA, ethylenediaminetetraacetic acid disodium salt; Tris, tris-(hydroxymethyl)aminomethane; DTT, dithiothreitol.…”
Section: Methodsmentioning
confidence: 99%
“…The flip side of protein folding and unfolding by high hydrostatic pressure and temperature was also explored from a physicochemical point of view using membrane proteins and soluble proteins as models, and a threedimensional free energy surface diagram for protein stability was presented (13). Prof. Jerson L. Silva presented New Insights into the Mechanism of Protein Folding and Misfolding Derived from Pressure Studies, with an emphasis on the prion diseases (14). Protein misfolding can lead to conformational diseases such as amyloidosis, Alzheimer's, Parkinson's, prion and tumor diseases in humans, related diseases in animals (such as ovine scrapie or bovine spongiform encephalitis), or formation of inclusion bodies of proteins overexpressed in bacteria.…”
Section: The Conference On High Pressure Bioscience and Biotechnologymentioning
confidence: 99%
“…Thus, high hydrostatic pressure obviously is a powerful technique regarding the attempts to develop therapies for the disease-related misfolding of proteins and strategies to disperse inclusion bodies of proteins of biotechnological relevance. Furthermore, the use of high hydrostatic pressure promises to contribute to the identification of the mechanisms underlying these defects and to the development of therapies against these diseases (14). Dr. Igor Polikarpov (Institute of Physics, São Carlos, USP, Brazil) presented a Study on the Multimeric Forms of Retinoic Acid x Receptor in Solution.…”
Section: The Conference On High Pressure Bioscience and Biotechnologymentioning
confidence: 99%