FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W4281678563> ?p ?o ?g. }

• W4281678563 abstract "Abstract Background The molecular heterogeneity of Alzheimer’s amyloid-β (Aβ) deposits extends well beyond the classic Aβ1-40/Aβ1-42 dichotomy, substantially expanded by multiple post-translational modifications that increase the proteome diversity. Numerous truncated fragments consistently populate the brain Aβ peptidome, and their homeostatic regulation and potential contribution to disease pathogenesis are largely unknown. Aβ4-x peptides have been reported as major components of plaque cores and the limited studies available indicate their relative abundance in Alzheimer’s disease (AD). Methods Immunohistochemistry was used to assess the topographic distribution of Aβ4-x species in well-characterized AD cases using custom-generated monoclonal antibody 18H6—specific for Aβ4-x species and blind for full-length Aβ1-40/Aβ1-42—in conjunction with thioflavin-S and antibodies recognizing Aβx-40 and Aβx-42 proteoforms. Circular dichroism, thioflavin-T binding, and electron microscopy evaluated the biophysical and aggregation/oligomerization properties of full-length and truncated synthetic homologues, whereas stereotaxic intracerebral injections of monomeric and oligomeric radiolabeled homologues in wild-type mice were used to evaluate their brain clearance characteristics. Results All types of amyloid deposits contained the probed Aβ epitopes, albeit expressed in different proportions. Aβ4-x species showed preferential localization within thioflavin-S-positive cerebral amyloid angiopathy and cored plaques, strongly suggesting poor clearance characteristics and consistent with the reduced solubility and enhanced oligomerization of their synthetic homologues. In vivo clearance studies demonstrated a fast brain efflux of N-terminally truncated and full-length monomeric forms whereas their oligomeric counterparts—particularly of Aβ4-40 and Aβ4-42—consistently exhibited enhanced brain retention. Conclusions The persistence of aggregation-prone Aβ4-x proteoforms likely contributes to the process of amyloid formation, self-perpetuating the amyloidogenic loop and exacerbating amyloid-mediated pathogenic pathways." @default.
• W4281678563 created "2022-06-13" @default.
• W4281678563 creator A5031100058 @default.
• W4281678563 creator A5050946548 @default.
• W4281678563 creator A5081547926 @default.
• W4281678563 creator A5083614755 @default.
• W4281678563 date "2022-06-01" @default.
• W4281678563 modified "2023-10-18" @default.
• W4281678563 title "N-terminally truncated Aβ4-x proteoforms and their relevance for Alzheimer’s pathophysiology" @default.
• W4281678563 cites W143061144 @default.
• W4281678563 cites W1495429911 @default.
• W4281678563 cites W1514539285 @default.
• W4281678563 cites W1519536920 @default.
• W4281678563 cites W1577742100 @default.
• W4281678563 cites W1580479524 @default.
• W4281678563 cites W1629460796 @default.
• W4281678563 cites W1729585270 @default.
• W4281678563 cites W1758831574 @default.
• W4281678563 cites W1965080574 @default.
• W4281678563 cites W1967823816 @default.
• W4281678563 cites W1974072353 @default.
• W4281678563 cites W1974145718 @default.
• W4281678563 cites W1977128117 @default.
• W4281678563 cites W1977384524 @default.
• W4281678563 cites W1980046421 @default.
• W4281678563 cites W1980825524 @default.
• W4281678563 cites W1981458288 @default.
• W4281678563 cites W1992758695 @default.
• W4281678563 cites W1997822484 @default.
• W4281678563 cites W2002614840 @default.
• W4281678563 cites W2002755165 @default.
• W4281678563 cites W2005483591 @default.
• W4281678563 cites W2006035554 @default.
• W4281678563 cites W2008917014 @default.
• W4281678563 cites W2012288880 @default.
• W4281678563 cites W2020068741 @default.
• W4281678563 cites W2028161249 @default.
• W4281678563 cites W2028379029 @default.
• W4281678563 cites W2030260517 @default.
• W4281678563 cites W2035514833 @default.
• W4281678563 cites W2037904566 @default.
• W4281678563 cites W2038012168 @default.
• W4281678563 cites W2040641201 @default.
• W4281678563 cites W2045197448 @default.
• W4281678563 cites W2046288613 @default.
• W4281678563 cites W2046847750 @default.
• W4281678563 cites W2052742260 @default.
• W4281678563 cites W2058729222 @default.
• W4281678563 cites W2062647232 @default.
• W4281678563 cites W2064566310 @default.
• W4281678563 cites W2067766876 @default.
• W4281678563 cites W2072435649 @default.
• W4281678563 cites W2073516240 @default.
• W4281678563 cites W2076742349 @default.
• W4281678563 cites W2080705044 @default.
• W4281678563 cites W2081598046 @default.
• W4281678563 cites W2082151254 @default.
• W4281678563 cites W2082429191 @default.
• W4281678563 cites W2086499847 @default.
• W4281678563 cites W2087255758 @default.
• W4281678563 cites W2087932565 @default.
• W4281678563 cites W2089765958 @default.
• W4281678563 cites W2093356656 @default.
• W4281678563 cites W2093910429 @default.
• W4281678563 cites W2096410114 @default.
• W4281678563 cites W2097033620 @default.
• W4281678563 cites W2097338951 @default.
• W4281678563 cites W2097965815 @default.
• W4281678563 cites W2098022922 @default.
• W4281678563 cites W2107233754 @default.
• W4281678563 cites W2107363753 @default.
• W4281678563 cites W2111605497 @default.
• W4281678563 cites W2113154138 @default.
• W4281678563 cites W2122093493 @default.
• W4281678563 cites W2125368074 @default.
• W4281678563 cites W2127458156 @default.
• W4281678563 cites W2128823466 @default.
• W4281678563 cites W2130270031 @default.
• W4281678563 cites W2133631618 @default.
• W4281678563 cites W2134755663 @default.
• W4281678563 cites W2135617975 @default.
• W4281678563 cites W2137649439 @default.
• W4281678563 cites W2140323904 @default.
• W4281678563 cites W2142807222 @default.
• W4281678563 cites W2143238511 @default.
• W4281678563 cites W2143461767 @default.
• W4281678563 cites W2149438499 @default.
• W4281678563 cites W2159081021 @default.
• W4281678563 cites W2159719455 @default.
• W4281678563 cites W2161420960 @default.
• W4281678563 cites W2162124438 @default.
• W4281678563 cites W2162681653 @default.
• W4281678563 cites W2165503155 @default.
• W4281678563 cites W2167183660 @default.
• W4281678563 cites W2169152986 @default.
• W4281678563 cites W2171495114 @default.
• W4281678563 cites W2298163613 @default.
• W4281678563 cites W2298591538 @default.
• W4281678563 cites W2345680808 @default.
• W4281678563 cites W2402622870 @default.

• next