FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2624481446> ?p ?o ?g. }

• W2624481446 endingPage "2026" @default.
• W2624481446 startingPage "2019" @default.
• W2624481446 abstract "Cu/Zn superoxide dismutase (SOD1) forms intracellular aggregates that are pathological indicators of amyotrophic lateral sclerosis. A large body of research indicates that the entry point to aggregate formation is a monomeric, metal-ion free (apo), and disulfide-reduced species. Fibril formation by SOD1 in vitro has typically been reported only for harsh solvent conditions or mechanical agitation. Here we show that monomeric apo-SOD1 in the disulfide-reduced state forms fibrillar aggregates under near-physiological quiescent conditions. Monomeric apo-SOD1 with an intact intramolecular disulfide bond is highly resistant to aggregation under the same conditions. A cysteine-free variant of SOD1 exhibits fibrillization behavior and fibril morphology identical to those of disulfide-reduced SOD1, firmly establishing that intermolecular disulfide bonds or intramolecular disulfide shuffling are not required for aggregation and fibril formation. The decreased lag time for fibril formation resulting from reduction of the intramolecular disulfide bond thus primarily reflects the decreased stability of the folded state relative to partially unfolded states, rather than an active role of free sulfhydryl groups in mediating aggregation. Addition of urea to increase the amount of fully unfolded SOD1 increases the lag time for fibril formation, indicating that the population of this species does not dominate over other factors in determining the onset of aggregation. Our results contrast with previous results obtained for agitated samples, in which case amyloid formation was accelerated by denaturant. We reconcile these observations by suggesting that denaturants destabilize monomeric and aggregated species to different extents and thus affect nucleation and growth." @default.
• W2624481446 created "2017-06-15" @default.
• W2624481446 creator A5004631122 @default.
• W2624481446 creator A5006358400 @default.
• W2624481446 creator A5063659458 @default.
• W2624481446 creator A5068883180 @default.
• W2624481446 creator A5070625264 @default.
• W2624481446 creator A5082863839 @default.
• W2624481446 date "2017-06-20" @default.
• W2624481446 modified "2023-10-14" @default.
• W2624481446 title "Cu/Zn Superoxide Dismutase Forms Amyloid Fibrils under Near-Physiological Quiescent Conditions: The Roles of Disulfide Bonds and Effects of Denaturant" @default.
• W2624481446 cites W1488155304 @default.
• W2624481446 cites W1744659906 @default.
• W2624481446 cites W1865863333 @default.
• W2624481446 cites W1963767682 @default.
• W2624481446 cites W1970577444 @default.
• W2624481446 cites W1972463563 @default.
• W2624481446 cites W1981020468 @default.
• W2624481446 cites W1982967923 @default.
• W2624481446 cites W1988287851 @default.
• W2624481446 cites W1991493368 @default.
• W2624481446 cites W1991659188 @default.
• W2624481446 cites W1993689524 @default.
• W2624481446 cites W2004950164 @default.
• W2624481446 cites W2004978936 @default.
• W2624481446 cites W2008452978 @default.
• W2624481446 cites W2017062988 @default.
• W2624481446 cites W2017848780 @default.
• W2624481446 cites W2022721388 @default.
• W2624481446 cites W2022933182 @default.
• W2624481446 cites W2026634322 @default.
• W2624481446 cites W2036946816 @default.
• W2624481446 cites W2038665076 @default.
• W2624481446 cites W2043517717 @default.
• W2624481446 cites W2046002256 @default.
• W2624481446 cites W2047991384 @default.
• W2624481446 cites W2048401333 @default.
• W2624481446 cites W2049919805 @default.
• W2624481446 cites W2051401615 @default.
• W2624481446 cites W2052630549 @default.
• W2624481446 cites W2056447311 @default.
• W2624481446 cites W2057170892 @default.
• W2624481446 cites W2060433067 @default.
• W2624481446 cites W2067930756 @default.
• W2624481446 cites W2071242789 @default.
• W2624481446 cites W2074542471 @default.
• W2624481446 cites W2079048346 @default.
• W2624481446 cites W2082114591 @default.
• W2624481446 cites W2087323681 @default.
• W2624481446 cites W2088577455 @default.
• W2624481446 cites W2094520151 @default.
• W2624481446 cites W2094881767 @default.
• W2624481446 cites W2096678032 @default.
• W2624481446 cites W2099071260 @default.
• W2624481446 cites W2101571804 @default.
• W2624481446 cites W2105442888 @default.
• W2624481446 cites W2106297709 @default.
• W2624481446 cites W2112552649 @default.
• W2624481446 cites W2112761293 @default.
• W2624481446 cites W2115923704 @default.
• W2624481446 cites W2124084307 @default.
• W2624481446 cites W2127769185 @default.
• W2624481446 cites W2131268816 @default.
• W2624481446 cites W2145869597 @default.
• W2624481446 cites W2149428117 @default.
• W2624481446 cites W2157076525 @default.
• W2624481446 cites W2160704231 @default.
• W2624481446 cites W2165186407 @default.
• W2624481446 cites W2169707043 @default.
• W2624481446 cites W2169821755 @default.
• W2624481446 cites W2256271877 @default.
• W2624481446 doi "https://doi.org/10.1021/acschemneuro.7b00162" @default.
• W2624481446 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28585802" @default.
• W2624481446 hasPublicationYear "2017" @default.
• W2624481446 type Work @default.
• W2624481446 sameAs 2624481446 @default.
• W2624481446 citedByCount "23" @default.
• W2624481446 countsByYear W26244814462018 @default.
• W2624481446 countsByYear W26244814462019 @default.
• W2624481446 countsByYear W26244814462020 @default.
• W2624481446 countsByYear W26244814462021 @default.
• W2624481446 countsByYear W26244814462022 @default.
• W2624481446 countsByYear W26244814462023 @default.
• W2624481446 crossrefType "journal-article" @default.
• W2624481446 hasAuthorship W2624481446A5004631122 @default.
• W2624481446 hasAuthorship W2624481446A5006358400 @default.
• W2624481446 hasAuthorship W2624481446A5063659458 @default.
• W2624481446 hasAuthorship W2624481446A5068883180 @default.
• W2624481446 hasAuthorship W2624481446A5070625264 @default.
• W2624481446 hasAuthorship W2624481446A5082863839 @default.
• W2624481446 hasBestOaLocation W26244814461 @default.
• W2624481446 hasConcept C12554922 @default.
• W2624481446 hasConcept C136238340 @default.
• W2624481446 hasConcept C166940927 @default.
• W2624481446 hasConcept C178790620 @default.
• W2624481446 hasConcept C181199279 @default.
• W2624481446 hasConcept C185592680 @default.
• W2624481446 hasConcept C204328495 @default.

• next