FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2003405967> ?p ?o ?g. }

• W2003405967 endingPage "13670" @default.
• W2003405967 startingPage "13665" @default.
• W2003405967 abstract "Organisms encode multiple homologous heat shock protein (Hsp)-70s, which are essential protein chaperones that play the major role in cellular protein “quality control.” Although Hsp70s are functionally redundant and highly homologous, many possess distinct functions. A regulatory motif underlying such distinctions, however, is unknown. The 98% identical cytoplasmic Hsp70s Ssa1p and Ssa2p function differently with regard to propagation of yeast [URE3] prions and in the vacuolar-mediated degradation of gluconeogenesis enzymes, such as FBPase. Here, we show that the Hsp70 nucleotide binding domain (NBD) regulates these functional specificities. We find little difference in ATPase, protein refolding, and amyloid inhibiting activities of purified Ssa1p and Ssa2p, but show that interchanging NBD residue alanine 83 (Ssa1p) and glycine 83 (Ssa2p) switched functions of Ssa1p and Ssa2p in [URE3] propagation and FBPase degradation. Disrupting the degradation pathway did not affect prion propagation, however, indicating these are two distinct processes where Ssa1/2p chaperones function differently. Our results suggest that the primary evolutionary pressure for Hsp70 functional distinctions is not to specify interactions of Hsp70 with substrate, but to specify the regulation of this activity. Our data suggest a rationale for maintaining multiple Hsp70s and suggest that subtle differences among Hsp70s evolved to provide functional specificity without affecting overall enzymatic activity." @default.
• W2003405967 created "2016-06-24" @default.
• W2003405967 creator A5001586772 @default.
• W2003405967 creator A5009751245 @default.
• W2003405967 date "2011-08-01" @default.
• W2003405967 modified "2023-10-17" @default.
• W2003405967 title "Single methyl group determines prion propagation and protein degradation activities of yeast heat shock protein (Hsp)-70 chaperones Ssa1p and Ssa2p" @default.
• W2003405967 cites W1558079148 @default.
• W2003405967 cites W1903209843 @default.
• W2003405967 cites W1965384335 @default.
• W2003405967 cites W1969006061 @default.
• W2003405967 cites W1969875733 @default.
• W2003405967 cites W1972121275 @default.
• W2003405967 cites W1979701744 @default.
• W2003405967 cites W1982260690 @default.
• W2003405967 cites W1988784180 @default.
• W2003405967 cites W1990839192 @default.
• W2003405967 cites W1991526269 @default.
• W2003405967 cites W2000204824 @default.
• W2003405967 cites W2013112316 @default.
• W2003405967 cites W2020528675 @default.
• W2003405967 cites W2020646160 @default.
• W2003405967 cites W2025743107 @default.
• W2003405967 cites W2028705478 @default.
• W2003405967 cites W2031652657 @default.
• W2003405967 cites W2038177768 @default.
• W2003405967 cites W2043433277 @default.
• W2003405967 cites W2046445620 @default.
• W2003405967 cites W2046603119 @default.
• W2003405967 cites W2058993984 @default.
• W2003405967 cites W2068960164 @default.
• W2003405967 cites W2075609989 @default.
• W2003405967 cites W2103725642 @default.
• W2003405967 cites W2103884669 @default.
• W2003405967 cites W2114880077 @default.
• W2003405967 cites W2120396047 @default.
• W2003405967 cites W2126406409 @default.
• W2003405967 cites W2127076278 @default.
• W2003405967 cites W2128352699 @default.
• W2003405967 cites W2133865059 @default.
• W2003405967 cites W2137530170 @default.
• W2003405967 cites W2138871985 @default.
• W2003405967 cites W2147770635 @default.
• W2003405967 cites W2148823498 @default.
• W2003405967 cites W2168905327 @default.
• W2003405967 doi "https://doi.org/10.1073/pnas.1107421108" @default.
• W2003405967 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3158190" @default.
• W2003405967 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21808014" @default.
• W2003405967 hasPublicationYear "2011" @default.
• W2003405967 type Work @default.
• W2003405967 sameAs 2003405967 @default.
• W2003405967 citedByCount "52" @default.
• W2003405967 countsByYear W20034059672012 @default.
• W2003405967 countsByYear W20034059672013 @default.
• W2003405967 countsByYear W20034059672014 @default.
• W2003405967 countsByYear W20034059672015 @default.
• W2003405967 countsByYear W20034059672016 @default.
• W2003405967 countsByYear W20034059672018 @default.
• W2003405967 countsByYear W20034059672019 @default.
• W2003405967 countsByYear W20034059672020 @default.
• W2003405967 countsByYear W20034059672021 @default.
• W2003405967 countsByYear W20034059672022 @default.
• W2003405967 countsByYear W20034059672023 @default.
• W2003405967 crossrefType "journal-article" @default.
• W2003405967 hasAuthorship W2003405967A5001586772 @default.
• W2003405967 hasAuthorship W2003405967A5009751245 @default.
• W2003405967 hasBestOaLocation W20034059671 @default.
• W2003405967 hasConcept C104317684 @default.
• W2003405967 hasConcept C142724271 @default.
• W2003405967 hasConcept C178180057 @default.
• W2003405967 hasConcept C205260736 @default.
• W2003405967 hasConcept C2775962898 @default.
• W2003405967 hasConcept C2779222958 @default.
• W2003405967 hasConcept C55493867 @default.
• W2003405967 hasConcept C68991219 @default.
• W2003405967 hasConcept C71924100 @default.
• W2003405967 hasConcept C86803240 @default.
• W2003405967 hasConcept C95444343 @default.
• W2003405967 hasConceptScore W2003405967C104317684 @default.
• W2003405967 hasConceptScore W2003405967C142724271 @default.
• W2003405967 hasConceptScore W2003405967C178180057 @default.
• W2003405967 hasConceptScore W2003405967C205260736 @default.
• W2003405967 hasConceptScore W2003405967C2775962898 @default.
• W2003405967 hasConceptScore W2003405967C2779222958 @default.
• W2003405967 hasConceptScore W2003405967C55493867 @default.
• W2003405967 hasConceptScore W2003405967C68991219 @default.
• W2003405967 hasConceptScore W2003405967C71924100 @default.
• W2003405967 hasConceptScore W2003405967C86803240 @default.
• W2003405967 hasConceptScore W2003405967C95444343 @default.
• W2003405967 hasIssue "33" @default.
• W2003405967 hasLocation W20034059671 @default.
• W2003405967 hasLocation W20034059672 @default.
• W2003405967 hasLocation W20034059673 @default.
• W2003405967 hasLocation W20034059674 @default.
• W2003405967 hasOpenAccess W2003405967 @default.
• W2003405967 hasPrimaryLocation W20034059671 @default.
• W2003405967 hasRelatedWork W160183570 @default.
• W2003405967 hasRelatedWork W1990308695 @default.

• next