Matches in SemOpenAlex for { <https://semopenalex.org/work/W1980169916> ?p ?o ?g. }
Showing items 1 to 86 of
86
with 100 items per page.
- W1980169916 endingPage "1528" @default.
- W1980169916 startingPage "1520" @default.
- W1980169916 abstract "Formamidopyrimidine-DNA-glycosylase of Escherichia coli (Fpg protein) repairs oxidative DNA damage by removing formamidopyrimidine lesions and 8-oxoguanine residues from DNA. This enzyme possesses three types of activities resulting in the excision of oxidized residue from DNA: hydrolysis of the N-glycosidic bond (DNA glycosylase), beta-elimination (AP-lyase), and delta-elimination. In our work, the kinetic mechanism for 8-oxoguanine excision from DNA substrate with Fpg protein has been determined from stopped-flow measurements of changes in the tryptophan fluorescence. The 12-nucleotide duplex d(CTCTC(oxo)GCCTTCC)*d(GGAAGGCGAGAG) containing the 8-oxoG nucleotide in the sixth position of one strand was used as the specific substrate. Four distinct phases in the time traces were detected. These four-phase transition changes in the Fpg protein fluorescence curves were analyzed by global fitting to determine the intrinsic rate constants. We propose that the first two phases represent the equilibrium steps. The first of them describes the bimolecular binding step and the second, formation of the apurinic site. The third, irreversible step is believed to describe the beta-elimination process. The fourth step reflects the delta-elimination and decomposition of complex between enzyme and the product of 8-oxoG nucleotide excision. The results obtained provide direct evidence of conformational transitions of the Fpg protein during the catalytic process. The significance of these results for the functioning of Fpg protein is discussed." @default.
- W1980169916 created "2016-06-24" @default.
- W1980169916 creator A5003204998 @default.
- W1980169916 creator A5047066214 @default.
- W1980169916 creator A5055746584 @default.
- W1980169916 creator A5081504559 @default.
- W1980169916 creator A5088944638 @default.
- W1980169916 creator A5091637118 @default.
- W1980169916 date "2002-01-10" @default.
- W1980169916 modified "2023-09-26" @default.
- W1980169916 title "Stopped-Flow Kinetic Studies of the Interaction between <i>Escherichia coli </i>Fpg Protein and DNA Substrates" @default.
- W1980169916 cites W1494022099 @default.
- W1980169916 cites W1510358641 @default.
- W1980169916 cites W194968609 @default.
- W1980169916 cites W1967825316 @default.
- W1980169916 cites W1994626352 @default.
- W1980169916 cites W2052419615 @default.
- W1980169916 cites W2113104146 @default.
- W1980169916 cites W2146899351 @default.
- W1980169916 cites W2765354461 @default.
- W1980169916 cites W4232534952 @default.
- W1980169916 doi "https://doi.org/10.1021/bi011524u" @default.
- W1980169916 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11814345" @default.
- W1980169916 hasPublicationYear "2002" @default.
- W1980169916 type Work @default.
- W1980169916 sameAs 1980169916 @default.
- W1980169916 citedByCount "53" @default.
- W1980169916 countsByYear W19801699162012 @default.
- W1980169916 countsByYear W19801699162013 @default.
- W1980169916 countsByYear W19801699162014 @default.
- W1980169916 countsByYear W19801699162015 @default.
- W1980169916 countsByYear W19801699162016 @default.
- W1980169916 countsByYear W19801699162018 @default.
- W1980169916 countsByYear W19801699162019 @default.
- W1980169916 countsByYear W19801699162020 @default.
- W1980169916 crossrefType "journal-article" @default.
- W1980169916 hasAuthorship W1980169916A5003204998 @default.
- W1980169916 hasAuthorship W1980169916A5047066214 @default.
- W1980169916 hasAuthorship W1980169916A5055746584 @default.
- W1980169916 hasAuthorship W1980169916A5081504559 @default.
- W1980169916 hasAuthorship W1980169916A5088944638 @default.
- W1980169916 hasAuthorship W1980169916A5091637118 @default.
- W1980169916 hasConcept C104317684 @default.
- W1980169916 hasConcept C134935766 @default.
- W1980169916 hasConcept C150777479 @default.
- W1980169916 hasConcept C185592680 @default.
- W1980169916 hasConcept C187206112 @default.
- W1980169916 hasConcept C192396546 @default.
- W1980169916 hasConcept C512185932 @default.
- W1980169916 hasConcept C547475151 @default.
- W1980169916 hasConcept C552990157 @default.
- W1980169916 hasConcept C55493867 @default.
- W1980169916 hasConcept C71240020 @default.
- W1980169916 hasConceptScore W1980169916C104317684 @default.
- W1980169916 hasConceptScore W1980169916C134935766 @default.
- W1980169916 hasConceptScore W1980169916C150777479 @default.
- W1980169916 hasConceptScore W1980169916C185592680 @default.
- W1980169916 hasConceptScore W1980169916C187206112 @default.
- W1980169916 hasConceptScore W1980169916C192396546 @default.
- W1980169916 hasConceptScore W1980169916C512185932 @default.
- W1980169916 hasConceptScore W1980169916C547475151 @default.
- W1980169916 hasConceptScore W1980169916C552990157 @default.
- W1980169916 hasConceptScore W1980169916C55493867 @default.
- W1980169916 hasConceptScore W1980169916C71240020 @default.
- W1980169916 hasIssue "5" @default.
- W1980169916 hasLocation W19801699161 @default.
- W1980169916 hasLocation W19801699162 @default.
- W1980169916 hasOpenAccess W1980169916 @default.
- W1980169916 hasPrimaryLocation W19801699161 @default.
- W1980169916 hasRelatedWork W1970566518 @default.
- W1980169916 hasRelatedWork W1991985168 @default.
- W1980169916 hasRelatedWork W2030475136 @default.
- W1980169916 hasRelatedWork W2031101499 @default.
- W1980169916 hasRelatedWork W2037838723 @default.
- W1980169916 hasRelatedWork W2082586163 @default.
- W1980169916 hasRelatedWork W2148033272 @default.
- W1980169916 hasRelatedWork W2799543090 @default.
- W1980169916 hasRelatedWork W3031599833 @default.
- W1980169916 hasRelatedWork W3141399017 @default.
- W1980169916 hasVolume "41" @default.
- W1980169916 isParatext "false" @default.
- W1980169916 isRetracted "false" @default.
- W1980169916 magId "1980169916" @default.
- W1980169916 workType "article" @default.