Matches in SemOpenAlex for { <https://semopenalex.org/work/W1547850596> ?p ?o ?g. }
Showing items 1 to 88 of
88
with 100 items per page.
- W1547850596 endingPage "423" @default.
- W1547850596 startingPage "410" @default.
- W1547850596 abstract "The formation of amyloid β (Aβ) peptide aggregates, oligomers, and fibrils is a dynamic process; however, the kinetics of their formation is not well understood. This study compares the time course of aggregate/fibril formation by transmission electron microscopy (TEM) analyses with that of oligomer/fibril formation by Western blot analysis under native and denaturing conditions. Efforts to deaggregate/defibrillate these peptides by using hexafluoroisopropanol, ammonium hydroxide, or dimethylsulfoxide did not change the nondenaturing polyacrylamide gel electrophoresis (PAGE) footprints or drive the peptides to a monomeric species. Regardless of the pretreatment protocol, TEM analyses reveal that all Aβ peptides (Aβ40, Aβ42, Aβ39E22Δ [Osaka], Aβ40E22G [Arctic], Aβ40E22Q [Dutch], and Aβ40A2T [Icelandic]) immediately formed nonfibrillar, amorphous aggregates when first placed into solution with the Osaka mutation, quickly forming early-stage fibrils. The extent of fibril formation for other Aβ peptides is time dependent, with the Arctic mutation forming fibrils at 1 hr, the Dutch and Icelandic at 4 hr, Aβ42 at 8 hr, and Aβ40 at 24 hr. In contrast, nondenaturing PAGE revealed unique footprints for the different Aβ species. The rapidity of aggregate formation and the rapid transition to fibrils, particularly for the Osaka deletion, suggest an important role for aggregates/fibrils of Aβ in the development of neuronal degeneration." @default.
- W1547850596 created "2016-06-24" @default.
- W1547850596 creator A5033609567 @default.
- W1547850596 creator A5080381270 @default.
- W1547850596 date "2014-11-06" @default.
- W1547850596 modified "2023-10-05" @default.
- W1547850596 title "Unique molecular signatures of Alzheimer's disease amyloid β peptide mutations and deletion during aggregate/oligomer/fibril formation" @default.
- W1547850596 cites W1559704329 @default.
- W1547850596 cites W1797763128 @default.
- W1547850596 cites W1968995509 @default.
- W1547850596 cites W1969099023 @default.
- W1547850596 cites W1987583742 @default.
- W1547850596 cites W1996155206 @default.
- W1547850596 cites W1998915407 @default.
- W1547850596 cites W2001121129 @default.
- W1547850596 cites W2002898580 @default.
- W1547850596 cites W2024559246 @default.
- W1547850596 cites W2029695041 @default.
- W1547850596 cites W2038518713 @default.
- W1547850596 cites W2063272219 @default.
- W1547850596 cites W2066912813 @default.
- W1547850596 cites W2081990092 @default.
- W1547850596 cites W2092249030 @default.
- W1547850596 cites W2095031277 @default.
- W1547850596 cites W2110031429 @default.
- W1547850596 cites W2118241214 @default.
- W1547850596 cites W2142186280 @default.
- W1547850596 cites W2152222652 @default.
- W1547850596 cites W2154755614 @default.
- W1547850596 doi "https://doi.org/10.1002/jnr.23507" @default.
- W1547850596 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25377128" @default.
- W1547850596 hasPublicationYear "2014" @default.
- W1547850596 type Work @default.
- W1547850596 sameAs 1547850596 @default.
- W1547850596 citedByCount "8" @default.
- W1547850596 countsByYear W15478505962015 @default.
- W1547850596 countsByYear W15478505962019 @default.
- W1547850596 countsByYear W15478505962020 @default.
- W1547850596 countsByYear W15478505962023 @default.
- W1547850596 crossrefType "journal-article" @default.
- W1547850596 hasAuthorship W1547850596A5033609567 @default.
- W1547850596 hasAuthorship W1547850596A5080381270 @default.
- W1547850596 hasConcept C12554922 @default.
- W1547850596 hasConcept C166940927 @default.
- W1547850596 hasConcept C178790620 @default.
- W1547850596 hasConcept C179104552 @default.
- W1547850596 hasConcept C185592680 @default.
- W1547850596 hasConcept C27523624 @default.
- W1547850596 hasConcept C2777633098 @default.
- W1547850596 hasConcept C2779281246 @default.
- W1547850596 hasConcept C2780642029 @default.
- W1547850596 hasConcept C521977710 @default.
- W1547850596 hasConcept C55493867 @default.
- W1547850596 hasConcept C86803240 @default.
- W1547850596 hasConceptScore W1547850596C12554922 @default.
- W1547850596 hasConceptScore W1547850596C166940927 @default.
- W1547850596 hasConceptScore W1547850596C178790620 @default.
- W1547850596 hasConceptScore W1547850596C179104552 @default.
- W1547850596 hasConceptScore W1547850596C185592680 @default.
- W1547850596 hasConceptScore W1547850596C27523624 @default.
- W1547850596 hasConceptScore W1547850596C2777633098 @default.
- W1547850596 hasConceptScore W1547850596C2779281246 @default.
- W1547850596 hasConceptScore W1547850596C2780642029 @default.
- W1547850596 hasConceptScore W1547850596C521977710 @default.
- W1547850596 hasConceptScore W1547850596C55493867 @default.
- W1547850596 hasConceptScore W1547850596C86803240 @default.
- W1547850596 hasIssue "3" @default.
- W1547850596 hasLocation W15478505961 @default.
- W1547850596 hasLocation W15478505962 @default.
- W1547850596 hasOpenAccess W1547850596 @default.
- W1547850596 hasPrimaryLocation W15478505961 @default.
- W1547850596 hasRelatedWork W1538630004 @default.
- W1547850596 hasRelatedWork W1969967781 @default.
- W1547850596 hasRelatedWork W1990479827 @default.
- W1547850596 hasRelatedWork W1997713676 @default.
- W1547850596 hasRelatedWork W2040412257 @default.
- W1547850596 hasRelatedWork W2306350765 @default.
- W1547850596 hasRelatedWork W2952029520 @default.
- W1547850596 hasRelatedWork W3013285207 @default.
- W1547850596 hasRelatedWork W4249078792 @default.
- W1547850596 hasRelatedWork W4379987770 @default.
- W1547850596 hasVolume "93" @default.
- W1547850596 isParatext "false" @default.
- W1547850596 isRetracted "false" @default.
- W1547850596 magId "1547850596" @default.
- W1547850596 workType "article" @default.