| http://purl.uniprot.org/citations/14766016 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/14766016 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/14766016 | http://www.w3.org/2000/01/rdf-schema#comment | "Inosine 5'-monophosphate dehydrogenase (IMPDH) is the rate-limiting enzyme in the de novo biosynthesis of guanine nucleotides. In addition to the catalytic domain, IMPDH contains a subdomain of unknown function composed of two cystathione beta-synthase domains. Our results, using three different assays, show that IMPDHs from Tritrichomonas foetus, Escherichia coli, and both human isoforms bind single-stranded nucleic acids with nanomolar affinity via the subdomain. Approx. 100 nucleotides are bound per IMPDH tetramer. Deletion of the subdomain decreases affinity 10-fold and decreases site size to 60 nucleotides, whereas substitution of conserved Arg/Lys residues in the subdomain with Glu decreases affinity by 20-fold. IMPDH is found in the nucleus of human cells, as might be expected for a nucleic-acid-binding protein. Lastly, immunoprecipitation experiments show that IMPDH binds both RNA and DNA in vivo. These experiments indicate that IMPDH has a previously unappreciated role in replication, transcription or translation that is mediated by the subdomain."xsd:string |
| http://purl.uniprot.org/citations/14766016 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj20031585"xsd:string |
| http://purl.uniprot.org/citations/14766016 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj20031585"xsd:string |
| http://purl.uniprot.org/citations/14766016 | http://purl.uniprot.org/core/author | "Hedstrom L."xsd:string |
| http://purl.uniprot.org/citations/14766016 | http://purl.uniprot.org/core/author | "Hedstrom L."xsd:string |
| http://purl.uniprot.org/citations/14766016 | http://purl.uniprot.org/core/author | "Belenky P."xsd:string |
| http://purl.uniprot.org/citations/14766016 | http://purl.uniprot.org/core/author | "Belenky P."xsd:string |
| http://purl.uniprot.org/citations/14766016 | http://purl.uniprot.org/core/author | "Hamaguchi N."xsd:string |
| http://purl.uniprot.org/citations/14766016 | http://purl.uniprot.org/core/author | "Hamaguchi N."xsd:string |
| http://purl.uniprot.org/citations/14766016 | http://purl.uniprot.org/core/author | "McLean J.E."xsd:string |
| http://purl.uniprot.org/citations/14766016 | http://purl.uniprot.org/core/author | "McLean J.E."xsd:string |
| http://purl.uniprot.org/citations/14766016 | http://purl.uniprot.org/core/author | "Mortimer S.E."xsd:string |
| http://purl.uniprot.org/citations/14766016 | http://purl.uniprot.org/core/author | "Mortimer S.E."xsd:string |
| http://purl.uniprot.org/citations/14766016 | http://purl.uniprot.org/core/author | "Stanton M."xsd:string |
| http://purl.uniprot.org/citations/14766016 | http://purl.uniprot.org/core/author | "Stanton M."xsd:string |
| http://purl.uniprot.org/citations/14766016 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/14766016 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/14766016 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |
| http://purl.uniprot.org/citations/14766016 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |
| http://purl.uniprot.org/citations/14766016 | http://purl.uniprot.org/core/pages | "243-251"xsd:string |
| http://purl.uniprot.org/citations/14766016 | http://purl.uniprot.org/core/pages | "243-251"xsd:string |
| http://purl.uniprot.org/citations/14766016 | http://purl.uniprot.org/core/title | "Inosine 5'-monophosphate dehydrogenase binds nucleic acids in vitro and in vivo."xsd:string |
| http://purl.uniprot.org/citations/14766016 | http://purl.uniprot.org/core/title | "Inosine 5'-monophosphate dehydrogenase binds nucleic acids in vitro and in vivo."xsd:string |