FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W4308129318> ?p ?o ?g. }

• W4308129318 abstract "The stress induced protein NQO1 can participate in a wide range of biological pathways which are dependent upon the interaction of NQO1 with protein targets. Many of the protein-protein interactions involving NQO1 have been shown to be regulated by the pyridine nucleotide redox balance. NQO1 can modify its conformation as a result of redox changes in pyridine nucleotides and sites on the C-terminal and helix seven regions of NQO1 have been identified as potential areas that may be involved in redox-dependent protein-protein interactions. Since post-translational modifications can modify the functionality of proteins, we examined whether redox-dependent conformational changes induced in NQO1 would alter lysine acetylation. Recombinant NQO1 was incubated with and without NADH then acetylated non-enzymatically by acetic anhydride or S-acetylglutathione (Ac-GSH). NQO1 acetylation was determined by immunoblot and site-specific lysine acetylation was quantified by mass spectrometry (MS). NQO1 was readily acetylated by acetic anhydride and Ac-GSH. Interestingly, despite a large number of lysine residues (9%) in NQO1 only a small subset of lysines were acetylated and the majority of these were located in or near the functional C-terminal or helix seven regions. Reduction of NQO1 by NADH prior to acetylation resulted in almost complete protection of NQO1 from lysine acetylation as confirmed by immunoblot analysis and MS. Lysines located within the redox-active C-terminus and helix seven regions were readily acetylated when NQO1 was in an oxidized conformation but were protected from acetylation when NQO1 was in the reduced conformation. To investigate regulatory mechanisms of enzymatic deacetylation, NQO1 was acetylated by Ac-GSH then exposed to purified sirtuins (SIRT 1-3) or histone deacetylase 6 (HDAC6). NQO1 could be deacetylated by all sirtuin isoforms and quantitative MS analysis performed using SIRT2 revealed very robust deacetylation of NQO1, specifically at K262 and K271 in the C-terminal region. No deacetylation of NQO1 by HDAC6 was detected. These data demonstrate that the same subset of key lysine residues in the C-terminal and helix seven regions of NQO1 undergo redox dependent acetylation and are regulated by sirtuin-mediated deacetylation." @default.
• W4308129318 created "2022-11-08" @default.
• W4308129318 creator A5001448342 @default.
• W4308129318 creator A5006856018 @default.
• W4308129318 creator A5024622700 @default.
• W4308129318 creator A5038923785 @default.
• W4308129318 creator A5040985981 @default.
• W4308129318 creator A5045433486 @default.
• W4308129318 date "2022-11-02" @default.
• W4308129318 modified "2023-10-06" @default.
• W4308129318 title "Redox state and the sirtuin deacetylases are major factors that regulate the acetylation status of the stress protein NQO1" @default.
• W4308129318 cites W1417333514 @default.
• W4308129318 cites W1943243678 @default.
• W4308129318 cites W1959721425 @default.
• W4308129318 cites W1985824499 @default.
• W4308129318 cites W1990927292 @default.
• W4308129318 cites W2001326517 @default.
• W4308129318 cites W2002314190 @default.
• W4308129318 cites W2016055538 @default.
• W4308129318 cites W2035471676 @default.
• W4308129318 cites W2041440237 @default.
• W4308129318 cites W2043274355 @default.
• W4308129318 cites W2052080274 @default.
• W4308129318 cites W2059190026 @default.
• W4308129318 cites W2078683837 @default.
• W4308129318 cites W2094294128 @default.
• W4308129318 cites W2099952208 @default.
• W4308129318 cites W2150408345 @default.
• W4308129318 cites W2181797758 @default.
• W4308129318 cites W2256771672 @default.
• W4308129318 cites W2313910402 @default.
• W4308129318 cites W2345900051 @default.
• W4308129318 cites W2436282489 @default.
• W4308129318 cites W2518264493 @default.
• W4308129318 cites W2562940458 @default.
• W4308129318 cites W2592360697 @default.
• W4308129318 cites W2612243116 @default.
• W4308129318 cites W2748512916 @default.
• W4308129318 cites W2782178515 @default.
• W4308129318 cites W2885804421 @default.
• W4308129318 cites W2886979358 @default.
• W4308129318 cites W2895507983 @default.
• W4308129318 cites W2901164269 @default.
• W4308129318 cites W2995728771 @default.
• W4308129318 cites W3037844642 @default.
• W4308129318 cites W3112822293 @default.
• W4308129318 cites W3137878085 @default.
• W4308129318 cites W3176688350 @default.
• W4308129318 cites W3215378256 @default.
• W4308129318 cites W4210317027 @default.
• W4308129318 cites W4229023075 @default.
• W4308129318 cites W4238224725 @default.
• W4308129318 doi "https://doi.org/10.3389/fphar.2022.1015642" @default.
• W4308129318 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36408211" @default.
• W4308129318 hasPublicationYear "2022" @default.
• W4308129318 type Work @default.
• W4308129318 citedByCount "2" @default.
• W4308129318 countsByYear W43081293182023 @default.
• W4308129318 crossrefType "journal-article" @default.
• W4308129318 hasAuthorship W4308129318A5001448342 @default.
• W4308129318 hasAuthorship W4308129318A5006856018 @default.
• W4308129318 hasAuthorship W4308129318A5024622700 @default.
• W4308129318 hasAuthorship W4308129318A5038923785 @default.
• W4308129318 hasAuthorship W4308129318A5040985981 @default.
• W4308129318 hasAuthorship W4308129318A5045433486 @default.
• W4308129318 hasBestOaLocation W43081293181 @default.
• W4308129318 hasConcept C104317684 @default.
• W4308129318 hasConcept C119157956 @default.
• W4308129318 hasConcept C161790260 @default.
• W4308129318 hasConcept C178790620 @default.
• W4308129318 hasConcept C185592680 @default.
• W4308129318 hasConcept C2776016237 @default.
• W4308129318 hasConcept C2779854550 @default.
• W4308129318 hasConcept C2780561631 @default.
• W4308129318 hasConcept C515207424 @default.
• W4308129318 hasConcept C55493867 @default.
• W4308129318 hasConcept C55904794 @default.
• W4308129318 hasConceptScore W4308129318C104317684 @default.
• W4308129318 hasConceptScore W4308129318C119157956 @default.
• W4308129318 hasConceptScore W4308129318C161790260 @default.
• W4308129318 hasConceptScore W4308129318C178790620 @default.
• W4308129318 hasConceptScore W4308129318C185592680 @default.
• W4308129318 hasConceptScore W4308129318C2776016237 @default.
• W4308129318 hasConceptScore W4308129318C2779854550 @default.
• W4308129318 hasConceptScore W4308129318C2780561631 @default.
• W4308129318 hasConceptScore W4308129318C515207424 @default.
• W4308129318 hasConceptScore W4308129318C55493867 @default.
• W4308129318 hasConceptScore W4308129318C55904794 @default.
• W4308129318 hasFunder F4320332161 @default.
• W4308129318 hasLocation W43081293181 @default.
• W4308129318 hasLocation W43081293182 @default.
• W4308129318 hasLocation W43081293183 @default.
• W4308129318 hasLocation W43081293184 @default.
• W4308129318 hasOpenAccess W4308129318 @default.
• W4308129318 hasPrimaryLocation W43081293181 @default.
• W4308129318 hasRelatedWork W2030620740 @default.
• W4308129318 hasRelatedWork W2083078738 @default.
• W4308129318 hasRelatedWork W2327853242 @default.
• W4308129318 hasRelatedWork W2945798114 @default.
• W4308129318 hasRelatedWork W2985810429 @default.

• next