RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/18588888http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18588888http://www.w3.org/2000/01/rdf-schema#comment"Microtubule (MT) dynamic instability is tightly regulated by stabilizing and destabilizing proteins, the latter being exemplified by stathmin/Op18, a protein known to destabilize MTs. Studies in cells have indicated that the level of stathmin expression modifies the cytotoxicity of antimicrotubule drugs, such as vinblastine (VLB). Using isothermal titration calorimetry and analytical ultracentrifugation, we show that VLB increases the affinity of stathmin for tubulin 50-fold (and vice versa). These results are the first biochemical evidence of the direct relationship between stathmin and an antimitotic drug, and reveal a new mechanism of action for VLB."xsd:string
http://purl.uniprot.org/citations/18588888http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2008.06.035"xsd:string
http://purl.uniprot.org/citations/18588888http://purl.uniprot.org/core/author"Barbier P."xsd:string
http://purl.uniprot.org/citations/18588888http://purl.uniprot.org/core/author"Makarov A.A."xsd:string
http://purl.uniprot.org/citations/18588888http://purl.uniprot.org/core/author"Tsvetkov P.O."xsd:string
http://purl.uniprot.org/citations/18588888http://purl.uniprot.org/core/author"Horwitz S.B."xsd:string
http://purl.uniprot.org/citations/18588888http://purl.uniprot.org/core/author"Allegro D."xsd:string
http://purl.uniprot.org/citations/18588888http://purl.uniprot.org/core/author"Devred F."xsd:string
http://purl.uniprot.org/citations/18588888http://purl.uniprot.org/core/author"Peyrot V."xsd:string
http://purl.uniprot.org/citations/18588888http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18588888http://purl.uniprot.org/core/name"FEBS Lett"xsd:string
http://purl.uniprot.org/citations/18588888http://purl.uniprot.org/core/pages"2484-2488"xsd:string
http://purl.uniprot.org/citations/18588888http://purl.uniprot.org/core/title"Stathmin/Op18 is a novel mediator of vinblastine activity."xsd:string
http://purl.uniprot.org/citations/18588888http://purl.uniprot.org/core/volume"582"xsd:string
http://purl.uniprot.org/citations/18588888http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18588888
http://purl.uniprot.org/citations/18588888http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18588888
http://purl.uniprot.org/uniprot/#_P16949-mappedCitation-18588888http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18588888
http://purl.uniprot.org/uniprot/#_Q6B856-mappedCitation-18588888http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18588888
http://purl.uniprot.org/uniprot/#_P81948-mappedCitation-18588888http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18588888
http://purl.uniprot.org/uniprot/Q6B856http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18588888
http://purl.uniprot.org/uniprot/P81948http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18588888
http://purl.uniprot.org/uniprot/P16949http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18588888