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http://purl.uniprot.org/citations/15200958http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15200958http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15200958http://www.w3.org/2000/01/rdf-schema#comment"Protein-protein interactions are required for most cellular functions, yet little is known about the relationship between protein-protein interaction affinity and biological activity. To investigate this issue, we engineered a series of mutants that incrementally reduced the affinity of the yeast Sho1p SH3 domain for its in vivo target, the MAP kinase kinase Pbs2p. We demonstrate a strong linear correlation between the binding energy of these mutants and quantitative in vivo outputs from the HOG high-osmolarity response pathway controlled by Sho1p. In addition, we find that reduction in binding affinity for the correct target within this pathway causes a proportional increase in misactivation of the related mating pheromone response pathway and that strong binding affinity alone does not guarantee efficient biological activity. Our experiments also indicate that a second binding surface on the Sho1p SH3 domain is required for its proper in vivo function."xsd:string
http://purl.uniprot.org/citations/15200958http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2004.05.024"xsd:string
http://purl.uniprot.org/citations/15200958http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2004.05.024"xsd:string
http://purl.uniprot.org/citations/15200958http://purl.uniprot.org/core/author"Davidson A.R."xsd:string
http://purl.uniprot.org/citations/15200958http://purl.uniprot.org/core/author"Davidson A.R."xsd:string
http://purl.uniprot.org/citations/15200958http://purl.uniprot.org/core/author"Andrews B.J."xsd:string
http://purl.uniprot.org/citations/15200958http://purl.uniprot.org/core/author"Andrews B.J."xsd:string
http://purl.uniprot.org/citations/15200958http://purl.uniprot.org/core/author"Haynes J."xsd:string
http://purl.uniprot.org/citations/15200958http://purl.uniprot.org/core/author"Haynes J."xsd:string
http://purl.uniprot.org/citations/15200958http://purl.uniprot.org/core/author"Dahesh S."xsd:string
http://purl.uniprot.org/citations/15200958http://purl.uniprot.org/core/author"Dahesh S."xsd:string
http://purl.uniprot.org/citations/15200958http://purl.uniprot.org/core/author"Marles J.A."xsd:string
http://purl.uniprot.org/citations/15200958http://purl.uniprot.org/core/author"Marles J.A."xsd:string
http://purl.uniprot.org/citations/15200958http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15200958http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15200958http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/15200958http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/15200958http://purl.uniprot.org/core/pages"813-823"xsd:string
http://purl.uniprot.org/citations/15200958http://purl.uniprot.org/core/pages"813-823"xsd:string
http://purl.uniprot.org/citations/15200958http://purl.uniprot.org/core/title"Protein-protein interaction affinity plays a crucial role in controlling the Sho1p-mediated signal transduction pathway in yeast."xsd:string
http://purl.uniprot.org/citations/15200958http://purl.uniprot.org/core/title"Protein-protein interaction affinity plays a crucial role in controlling the Sho1p-mediated signal transduction pathway in yeast."xsd:string
http://purl.uniprot.org/citations/15200958http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/15200958http://purl.uniprot.org/core/volume"14"xsd:string