FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2012893809> ?p ?o ?g. }

• W2012893809 endingPage "217" @default.
• W2012893809 startingPage "209" @default.
• W2012893809 abstract "Molinate is a thiocarbamate herbicide used in the rice industry for over 25 years, and regulatory reports have shown that administration of molinate results in reproductive toxicity in male rats. Previous in vitro studies indicate that molinate undergoes oxidative metabolism, forming reactive electrophilic intermediates capable of undergoing nucleophilic addition by protein nucleophiles. On the basis of in vitro studies, carbamylation of an active site serine residue in Hydrolase A has been proposed to be the mechanism responsible for the observed testicular toxicity. The experiments presented here utilize hemoglobin to characterize covalent protein modifications produced in vivo by molinate. Rats were dosed intraperitoneally with molinate as a function of exposure duration. Examination of globin from molinate-treated rats by HPLC demonstrated a new peak in the isolated samples and, when collected and analyzed using MALDI-TOF MS, revealed a 126 Da increase in mass relative to the native beta(3) chain. Digestion of the globin using Glu-C and analysis by MALDI-TOF MS revealed two modified peptide fragments at m/z 2743 and 4985 consistent with a 126 Da increase to peptide fragments [122-146] and [102-146] in the unmodified beta(2) and beta(3) chains of globin. Using selected reaction monitoring LC/MS/MS, S-hexahydro-1H-azepine-1-carbonyl cysteine (HHAC-Cys) was identified in the globin hydrolysates isolated from the molinate-treated rats, but not in the control samples, and the quantity of adduct exhibited a cumulative dose response. These experiments demonstrate the ability of molinate to covalently modify proteins in vivo in a dose dependent manner. For hemoglobin this modification was a carbamylation at Cys-125 similar to the modification produced by disulfiram and N,N-diethyldithiocarbamate. The ability of molinate to covalently modify cysteine residues provides a potential mechanism to account for enzyme inhibition following molinate exposure and suggests that enzymes with cysteine residues in their active site may be inhibited by molinate." @default.
• W2012893809 created "2016-06-24" @default.
• W2012893809 creator A5001111463 @default.
• W2012893809 creator A5038117623 @default.
• W2012893809 creator A5044424041 @default.
• W2012893809 creator A5044621021 @default.
• W2012893809 date "2002-01-23" @default.
• W2012893809 modified "2023-10-18" @default.
• W2012893809 title "Identification of a <i>S</i>-Hexahydro-1<i>H</i>-azepine-1-carbonyl Adduct Produced by Molinate on Rat Hemoglobin β₂ and β₃ Chains in Vivo" @default.
• W2012893809 cites W2007256917 @default.
• W2012893809 cites W2011209216 @default.
• W2012893809 cites W2044294240 @default.
• W2012893809 cites W2044434841 @default.
• W2012893809 cites W2302267746 @default.
• W2012893809 doi "https://doi.org/10.1021/tx015564a" @default.
• W2012893809 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11849047" @default.
• W2012893809 hasPublicationYear "2002" @default.
• W2012893809 type Work @default.
• W2012893809 sameAs 2012893809 @default.
• W2012893809 citedByCount "8" @default.
• W2012893809 countsByYear W20128938092013 @default.
• W2012893809 countsByYear W20128938092020 @default.
• W2012893809 crossrefType "journal-article" @default.
• W2012893809 hasAuthorship W2012893809A5001111463 @default.
• W2012893809 hasAuthorship W2012893809A5038117623 @default.
• W2012893809 hasAuthorship W2012893809A5044424041 @default.
• W2012893809 hasAuthorship W2012893809A5044621021 @default.
• W2012893809 hasConcept C108204754 @default.
• W2012893809 hasConcept C125996951 @default.
• W2012893809 hasConcept C150903083 @default.
• W2012893809 hasConcept C178790620 @default.
• W2012893809 hasConcept C180577832 @default.
• W2012893809 hasConcept C181199279 @default.
• W2012893809 hasConcept C185592680 @default.
• W2012893809 hasConcept C207001950 @default.
• W2012893809 hasConcept C2778917026 @default.
• W2012893809 hasConcept C2779201268 @default.
• W2012893809 hasConcept C2779281246 @default.
• W2012893809 hasConcept C55493867 @default.
• W2012893809 hasConcept C71240020 @default.
• W2012893809 hasConcept C86803240 @default.
• W2012893809 hasConceptScore W2012893809C108204754 @default.
• W2012893809 hasConceptScore W2012893809C125996951 @default.
• W2012893809 hasConceptScore W2012893809C150903083 @default.
• W2012893809 hasConceptScore W2012893809C178790620 @default.
• W2012893809 hasConceptScore W2012893809C180577832 @default.
• W2012893809 hasConceptScore W2012893809C181199279 @default.
• W2012893809 hasConceptScore W2012893809C185592680 @default.
• W2012893809 hasConceptScore W2012893809C207001950 @default.
• W2012893809 hasConceptScore W2012893809C2778917026 @default.
• W2012893809 hasConceptScore W2012893809C2779201268 @default.
• W2012893809 hasConceptScore W2012893809C2779281246 @default.
• W2012893809 hasConceptScore W2012893809C55493867 @default.
• W2012893809 hasConceptScore W2012893809C71240020 @default.
• W2012893809 hasConceptScore W2012893809C86803240 @default.
• W2012893809 hasIssue "2" @default.
• W2012893809 hasLocation W20128938091 @default.
• W2012893809 hasLocation W20128938092 @default.
• W2012893809 hasOpenAccess W2012893809 @default.
• W2012893809 hasPrimaryLocation W20128938091 @default.
• W2012893809 hasRelatedWork W137251115 @default.
• W2012893809 hasRelatedWork W1983250406 @default.
• W2012893809 hasRelatedWork W2000687060 @default.
• W2012893809 hasRelatedWork W2039537532 @default.
• W2012893809 hasRelatedWork W2054859731 @default.
• W2012893809 hasRelatedWork W2101400584 @default.
• W2012893809 hasRelatedWork W2942876461 @default.
• W2012893809 hasRelatedWork W4307722706 @default.
• W2012893809 hasRelatedWork W1865001985 @default.
• W2012893809 hasRelatedWork W301674984 @default.
• W2012893809 hasVolume "15" @default.
• W2012893809 isParatext "false" @default.
• W2012893809 isRetracted "false" @default.
• W2012893809 magId "2012893809" @default.
• W2012893809 workType "article" @default.