RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/9294177http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9294177http://www.w3.org/2000/01/rdf-schema#comment"The level and fate of hMSH3 (human MutS homolog 3) were examined in the promyelocytic leukemia cell line HL-60 and its methotrexate-resistant derivative HL-60R, which is drug resistant by virtue of an amplification event that spans the dihydrofolate reductase (DHFR) and MSH3 genes. Nuclear extracts from HL-60 and HL-60R cells were subjected to an identical, rapid purification protocol that efficiently captures heterodimeric hMutSalpha (hMSH2. hMSH6) and hMutSbeta (hMSH2.hMSH3). In HL-60 extracts the hMutSalpha to hMutSbeta ratio is roughly 6:1, whereas in methotrexate-resistant HL-60R cells the ratio is less than 1:100, due to overproduction of hMSH3 and heterodimer formation of this protein with virtually all the nuclear hMSH2. This shift is associated with marked reduction in the efficiency of base-base mismatch and hypermutability at the hypoxanthine phosphoribosyltransferase (HPRT) locus. Purified hMutSalpha and hMutSbeta display partial overlap in mismatch repair specificity: both participate in repair of a dinucleotide insertion-deletion heterology, but only hMutSalpha restores base-base mismatch repair to extracts of HL-60R cells or hMSH2-deficient LoVo colorectal tumor cells."xsd:string
http://purl.uniprot.org/citations/9294177http://purl.org/dc/terms/identifier"doi:10.1073/pnas.94.19.10144"xsd:string
http://purl.uniprot.org/citations/9294177http://purl.uniprot.org/core/author"Wolf E."xsd:string
http://purl.uniprot.org/citations/9294177http://purl.uniprot.org/core/author"Genschel J."xsd:string
http://purl.uniprot.org/citations/9294177http://purl.uniprot.org/core/author"Modrich P."xsd:string
http://purl.uniprot.org/citations/9294177http://purl.uniprot.org/core/author"Drummond J.T."xsd:string
http://purl.uniprot.org/citations/9294177http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9294177http://purl.uniprot.org/core/name"Proc Natl Acad Sci U S A"xsd:string
http://purl.uniprot.org/citations/9294177http://purl.uniprot.org/core/pages"10144-10149"xsd:string
http://purl.uniprot.org/citations/9294177http://purl.uniprot.org/core/title"DHFR/MSH3 amplification in methotrexate-resistant cells alters the hMutSalpha/hMutSbeta ratio and reduces the efficiency of base-base mismatch repair."xsd:string
http://purl.uniprot.org/citations/9294177http://purl.uniprot.org/core/volume"94"xsd:string
http://purl.uniprot.org/citations/9294177http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9294177
http://purl.uniprot.org/citations/9294177http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9294177
http://purl.uniprot.org/uniprot/#_P52701-mappedCitation-9294177http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9294177
http://purl.uniprot.org/uniprot/#_P20585-mappedCitation-9294177http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9294177
http://purl.uniprot.org/uniprot/#_P43246-mappedCitation-9294177http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9294177
http://purl.uniprot.org/uniprot/P20585http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/9294177
http://purl.uniprot.org/uniprot/P52701http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/9294177
http://purl.uniprot.org/uniprot/P43246http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/9294177