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dc.contributor.authorYanachkov, Ivan
dc.contributor.authorPan, Julie Y.
dc.contributor.authorWessling-Resnick, Marianne
dc.contributor.authorWright, George E.
dc.date2022-08-11T08:09:33.000
dc.date.accessioned2022-08-23T16:35:40Z
dc.date.available2022-08-23T16:35:40Z
dc.date.issued1997-01-01
dc.date.submitted2009-03-24
dc.identifier.citation<p>Mol Pharmacol. 1997 Jan;51(1):47-51.</p>
dc.identifier.issn0026-895X (Print)
dc.identifier.doi10.1124/mol.51.1.47
dc.identifier.pmid9016345
dc.identifier.urihttp://hdl.handle.net/20.500.14038/38611
dc.description.abstractA novel and convenient method for nucleoside triphosphate synthesis was applied to the preparation of potentially nonhydrolyzable xanthosine triphosphate derivatives. The N-methylimidazolide of xanthosine 5'-monophosphate reacted rapidly with methylenediphosphonic acid and imidodiphosphonic acid to give xanthosine 5'-(beta, gamma-methylene)triphosphate and xanthosine 5'-(beta, gamma-imido)triphosphate, respectively, in good yields. Both compounds inhibited the xanthosine-diphosphate-dependent prenylation of a mutant of Rab5, Rab5D136N, the nucleotide specificity of which had been converted from GTP to xanthosine triphosphate. The results indicate that xanthosine 5'-(beta, gamma-methylene)triphosphate and xanthosine 5'-(beta, gamma-imido)triphosphate bound to the mutant protein with similar affinities and were not hydrolyzed under the assay conditions. These novel derivatives may be useful tools for the study of the role of individual GTPases mutated to xanthosine triphosphate specificity in the background of other GTP-binding proteins.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=9016345&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1124/mol.51.1.47
dc.subjectGTP Phosphohydrolases
dc.subjectGTP-Binding Proteins
dc.subjectHydrolysis
dc.subjectProtein Prenylation
dc.subjectRibonucleotides
dc.subjectrab5 GTP-Binding Proteins
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleSynthesis and effect of nonhydrolyzable xanthosine triphosphate derivatives on prenylation of Rab5D136N
dc.typeJournal Article
dc.source.journaltitleMolecular pharmacology
dc.source.volume51
dc.source.issue1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/1474
dc.identifier.contextkey794971
html.description.abstract<p>A novel and convenient method for nucleoside triphosphate synthesis was applied to the preparation of potentially nonhydrolyzable xanthosine triphosphate derivatives. The N-methylimidazolide of xanthosine 5'-monophosphate reacted rapidly with methylenediphosphonic acid and imidodiphosphonic acid to give xanthosine 5'-(beta, gamma-methylene)triphosphate and xanthosine 5'-(beta, gamma-imido)triphosphate, respectively, in good yields. Both compounds inhibited the xanthosine-diphosphate-dependent prenylation of a mutant of Rab5, Rab5D136N, the nucleotide specificity of which had been converted from GTP to xanthosine triphosphate. The results indicate that xanthosine 5'-(beta, gamma-methylene)triphosphate and xanthosine 5'-(beta, gamma-imido)triphosphate bound to the mutant protein with similar affinities and were not hydrolyzed under the assay conditions. These novel derivatives may be useful tools for the study of the role of individual GTPases mutated to xanthosine triphosphate specificity in the background of other GTP-binding proteins.</p>
dc.identifier.submissionpathoapubs/1474
dc.contributor.departmentDepartment of Pharmacology and Molecular Toxicology
dc.source.pages47-51


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