Matches in SemOpenAlex for { <https://semopenalex.org/work/W4247392209> ?p ?o ?g. }
Showing items 1 to 84 of
84
with 100 items per page.
- W4247392209 endingPage "334" @default.
- W4247392209 startingPage "323" @default.
- W4247392209 abstract "Amyloid formation is an ordered aggregation process, where β-sheet rich polymers are assembled from unstructured or partially folded monomers. We examined how two Escherichia coli cytosolic chaperones, DnaK and Hsp33, and a more recently characterized periplasmic chaperone, Spy, modulate the aggregation of a functional amyloid protein, CsgA. We found that DnaK, the Hsp70 homolog in E. coli, and Hsp33, a redox-regulated holdase, potently inhibited CsgA amyloidogenesis. The Hsp33 anti-amyloidogenesis activity was oxidation dependent, as oxidized Hsp33 was significantly more efficient than reduced Hsp33 at preventing CsgA aggregation. When soluble CsgA was seeded with preformed amyloid fibers, neither Hsp33 nor DnaK were able to efficiently prevent soluble CsgA from adopting the amyloid conformation. Moreover, both DnaK and Hsp33 increased the time that CsgA was reactive with the amyloid oligomer conformation-specific A11 antibody. Since CsgA must also pass through the periplasm during secretion, we assessed the ability of the periplasmic chaperone Spy to inhibit CsgA polymerization. Like DnaK and Hsp33, Spy also inhibited CsgA polymerization in vitro. Overexpression of Spy resulted in increased chaperone activity in periplasmic extracts and in reduced curli biogenesis in vivo. We propose that DnaK, Hsp33 and Spy exert their effects during the nucleation stages of CsgA fibrillation. Thus, both housekeeping and stress induced cytosolic and periplasmic chaperones may be involved in discouraging premature CsgA interactions during curli biogenesis." @default.
- W4247392209 created "2022-05-12" @default.
- W4247392209 creator A5012242924 @default.
- W4247392209 creator A5024846442 @default.
- W4247392209 creator A5046177432 @default.
- W4247392209 creator A5046842963 @default.
- W4247392209 creator A5049775174 @default.
- W4247392209 creator A5071536449 @default.
- W4247392209 creator A5076867367 @default.
- W4247392209 creator A5078438907 @default.
- W4247392209 creator A5080901411 @default.
- W4247392209 date "2011-10-01" @default.
- W4247392209 modified "2023-09-25" @default.
- W4247392209 title "E. coli chaperones DnaK, Hsp33 and Spy inhibit bacterial functional amyloid assembly" @default.
- W4247392209 doi "https://doi.org/10.4161/pri.5.4.18555" @default.
- W4247392209 hasPublicationYear "2011" @default.
- W4247392209 type Work @default.
- W4247392209 citedByCount "2" @default.
- W4247392209 countsByYear W42473922092021 @default.
- W4247392209 crossrefType "journal-article" @default.
- W4247392209 hasAuthorship W4247392209A5012242924 @default.
- W4247392209 hasAuthorship W4247392209A5024846442 @default.
- W4247392209 hasAuthorship W4247392209A5046177432 @default.
- W4247392209 hasAuthorship W4247392209A5046842963 @default.
- W4247392209 hasAuthorship W4247392209A5049775174 @default.
- W4247392209 hasAuthorship W4247392209A5071536449 @default.
- W4247392209 hasAuthorship W4247392209A5076867367 @default.
- W4247392209 hasAuthorship W4247392209A5078438907 @default.
- W4247392209 hasAuthorship W4247392209A5080901411 @default.
- W4247392209 hasBestOaLocation W42473922092 @default.
- W4247392209 hasConcept C104317684 @default.
- W4247392209 hasConcept C131934819 @default.
- W4247392209 hasConcept C142724271 @default.
- W4247392209 hasConcept C179104552 @default.
- W4247392209 hasConcept C181199279 @default.
- W4247392209 hasConcept C185592680 @default.
- W4247392209 hasConcept C201663137 @default.
- W4247392209 hasConcept C204328495 @default.
- W4247392209 hasConcept C2775962898 @default.
- W4247392209 hasConcept C2777633098 @default.
- W4247392209 hasConcept C547475151 @default.
- W4247392209 hasConcept C55493867 @default.
- W4247392209 hasConcept C71924100 @default.
- W4247392209 hasConcept C86803240 @default.
- W4247392209 hasConcept C95444343 @default.
- W4247392209 hasConcept C98539663 @default.
- W4247392209 hasConceptScore W4247392209C104317684 @default.
- W4247392209 hasConceptScore W4247392209C131934819 @default.
- W4247392209 hasConceptScore W4247392209C142724271 @default.
- W4247392209 hasConceptScore W4247392209C179104552 @default.
- W4247392209 hasConceptScore W4247392209C181199279 @default.
- W4247392209 hasConceptScore W4247392209C185592680 @default.
- W4247392209 hasConceptScore W4247392209C201663137 @default.
- W4247392209 hasConceptScore W4247392209C204328495 @default.
- W4247392209 hasConceptScore W4247392209C2775962898 @default.
- W4247392209 hasConceptScore W4247392209C2777633098 @default.
- W4247392209 hasConceptScore W4247392209C547475151 @default.
- W4247392209 hasConceptScore W4247392209C55493867 @default.
- W4247392209 hasConceptScore W4247392209C71924100 @default.
- W4247392209 hasConceptScore W4247392209C86803240 @default.
- W4247392209 hasConceptScore W4247392209C95444343 @default.
- W4247392209 hasConceptScore W4247392209C98539663 @default.
- W4247392209 hasIssue "4" @default.
- W4247392209 hasLocation W42473922091 @default.
- W4247392209 hasLocation W42473922092 @default.
- W4247392209 hasLocation W42473922093 @default.
- W4247392209 hasOpenAccess W4247392209 @default.
- W4247392209 hasPrimaryLocation W42473922091 @default.
- W4247392209 hasRelatedWork W1766330086 @default.
- W4247392209 hasRelatedWork W2040711560 @default.
- W4247392209 hasRelatedWork W2417423829 @default.
- W4247392209 hasRelatedWork W2584560985 @default.
- W4247392209 hasRelatedWork W2815495857 @default.
- W4247392209 hasRelatedWork W2944015260 @default.
- W4247392209 hasRelatedWork W4308274720 @default.
- W4247392209 hasRelatedWork W4319931934 @default.
- W4247392209 hasRelatedWork W4319936700 @default.
- W4247392209 hasRelatedWork W4320490313 @default.
- W4247392209 hasVolume "5" @default.
- W4247392209 isParatext "false" @default.
- W4247392209 isRetracted "false" @default.
- W4247392209 workType "article" @default.