Matches in SemOpenAlex for { <https://semopenalex.org/work/W2515666541> ?p ?o ?g. }
Showing items 1 to 79 of
79
with 100 items per page.
- W2515666541 abstract "The central feature of prion disease is the conversion of normal host-encoded cellular prion protein, PrPc, to an abnormal isoform, PrP. PrP80 appears to be the principal, if not the sole, component of infectious prions. Prion strain diversity seems to be encoded within PrP itself through a combination of PrP conformation, glycosylation and possibly other, as yet, unidentified post-translational modifications. Efficient purification of PrP will facilitate detailed chemical characterisation and investigation of conformations or assembly states required for prion infectivity. Purification of denatured PrP has been achieved through enrichment from brain homogenate using selective precipitation followed by chemical and thermal denaturation and isolation by immunoafTinity chromatography. These methods have isolated PrP from rodent prion strains with a yield of 50 % and purity of > 90 % of total protein and for the first time permit isolation of full length denatured PrPSc facilitating comprehensive structural analysis. Purified denatured PrP is expected to have all the covalent post-translational modifications that may be required for prion infectivity. In attempts to reconstitute prion infectivity, denatured PrP was refolded under different solvent conditions and assessed for changes in solubility, resistance to proteolytic digestion and infectivity in bioassay. Although distinct changes in the physicochemical properties of PrP were observed, to-date no evidence for reconstitution of prion infectivity has been found. In the course of these studies, it was discovered that Cu2f ions inhibit proteinase K activity and a detailed kinetic description of this inhibition was obtained. The lack of prion infectivity seen in refolded preparations of denatured PrP suggests a requirement for other as yet unidentified co-factors. The identity of PrP interacting proteins was investigated during the purification of PrP under differential extraction conditions in which prion infectivity was observed using an in vitro assay. Proteinase K digestion gave a change in prion infectivity implying that a correlation with the removal of a protease sensitive component occurred. Continuation of these studies may facilitate the identification of co-factors required for specific prion infectivity." @default.
- W2515666541 created "2016-09-16" @default.
- W2515666541 creator A5039067837 @default.
- W2515666541 date "2006-12-31" @default.
- W2515666541 modified "2023-09-27" @default.
- W2515666541 title "Physicochemical characterisation of disease associated abnormal prion proteins" @default.
- W2515666541 hasPublicationYear "2006" @default.
- W2515666541 type Work @default.
- W2515666541 sameAs 2515666541 @default.
- W2515666541 citedByCount "0" @default.
- W2515666541 crossrefType "dissertation" @default.
- W2515666541 hasAuthorship W2515666541A5039067837 @default.
- W2515666541 hasConcept C104317684 @default.
- W2515666541 hasConcept C106358424 @default.
- W2515666541 hasConcept C133571119 @default.
- W2515666541 hasConcept C13965031 @default.
- W2515666541 hasConcept C142724271 @default.
- W2515666541 hasConcept C159047783 @default.
- W2515666541 hasConcept C181199279 @default.
- W2515666541 hasConcept C185592680 @default.
- W2515666541 hasConcept C2522874641 @default.
- W2515666541 hasConcept C2776735649 @default.
- W2515666541 hasConcept C2776923230 @default.
- W2515666541 hasConcept C2777313579 @default.
- W2515666541 hasConcept C2778471508 @default.
- W2515666541 hasConcept C2779134260 @default.
- W2515666541 hasConcept C3019804061 @default.
- W2515666541 hasConcept C40767141 @default.
- W2515666541 hasConcept C53345823 @default.
- W2515666541 hasConcept C55493867 @default.
- W2515666541 hasConcept C71924100 @default.
- W2515666541 hasConcept C86803240 @default.
- W2515666541 hasConceptScore W2515666541C104317684 @default.
- W2515666541 hasConceptScore W2515666541C106358424 @default.
- W2515666541 hasConceptScore W2515666541C133571119 @default.
- W2515666541 hasConceptScore W2515666541C13965031 @default.
- W2515666541 hasConceptScore W2515666541C142724271 @default.
- W2515666541 hasConceptScore W2515666541C159047783 @default.
- W2515666541 hasConceptScore W2515666541C181199279 @default.
- W2515666541 hasConceptScore W2515666541C185592680 @default.
- W2515666541 hasConceptScore W2515666541C2522874641 @default.
- W2515666541 hasConceptScore W2515666541C2776735649 @default.
- W2515666541 hasConceptScore W2515666541C2776923230 @default.
- W2515666541 hasConceptScore W2515666541C2777313579 @default.
- W2515666541 hasConceptScore W2515666541C2778471508 @default.
- W2515666541 hasConceptScore W2515666541C2779134260 @default.
- W2515666541 hasConceptScore W2515666541C3019804061 @default.
- W2515666541 hasConceptScore W2515666541C40767141 @default.
- W2515666541 hasConceptScore W2515666541C53345823 @default.
- W2515666541 hasConceptScore W2515666541C55493867 @default.
- W2515666541 hasConceptScore W2515666541C71924100 @default.
- W2515666541 hasConceptScore W2515666541C86803240 @default.
- W2515666541 hasLocation W25156665411 @default.
- W2515666541 hasOpenAccess W2515666541 @default.
- W2515666541 hasPrimaryLocation W25156665411 @default.
- W2515666541 hasRelatedWork W165936009 @default.
- W2515666541 hasRelatedWork W1799199106 @default.
- W2515666541 hasRelatedWork W1964241324 @default.
- W2515666541 hasRelatedWork W1965234000 @default.
- W2515666541 hasRelatedWork W1970810860 @default.
- W2515666541 hasRelatedWork W1983007765 @default.
- W2515666541 hasRelatedWork W1998887586 @default.
- W2515666541 hasRelatedWork W2023247652 @default.
- W2515666541 hasRelatedWork W2034806764 @default.
- W2515666541 hasRelatedWork W2037927479 @default.
- W2515666541 hasRelatedWork W2041407304 @default.
- W2515666541 hasRelatedWork W2135768422 @default.
- W2515666541 hasRelatedWork W2163035210 @default.
- W2515666541 hasRelatedWork W2167092933 @default.
- W2515666541 hasRelatedWork W2180283457 @default.
- W2515666541 hasRelatedWork W2184562158 @default.
- W2515666541 hasRelatedWork W2193958840 @default.
- W2515666541 hasRelatedWork W2737821906 @default.
- W2515666541 hasRelatedWork W2985903850 @default.
- W2515666541 hasRelatedWork W3020484597 @default.
- W2515666541 isParatext "false" @default.
- W2515666541 isRetracted "false" @default.
- W2515666541 magId "2515666541" @default.
- W2515666541 workType "dissertation" @default.