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http://purl.uniprot.org/citations/10481176http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10481176http://www.w3.org/2000/01/rdf-schema#comment"Septins are a family of conserved proteins that have been implicated in a variety of cellular functions involving specialized regions of the cell cortex and changes in cell shape. The biochemistry and localization of septins suggest that they form a novel cytoskeletal system or that they function as scaffolds for the assembly of signalling complexes. This article discusses septin biochemistry and septin-interacting proteins, focusing on the missing link between the structure and biochemical properties of septin proteins, and on how they function at a molecular level in processes such as cytokinesis and yeast budding."xsd:string
http://purl.uniprot.org/citations/10481176http://purl.org/dc/terms/identifier"doi:10.1016/s0962-8924(99)01632-3"xsd:string
http://purl.uniprot.org/citations/10481176http://purl.uniprot.org/core/author"Field C.M."xsd:string
http://purl.uniprot.org/citations/10481176http://purl.uniprot.org/core/author"Kellogg D."xsd:string
http://purl.uniprot.org/citations/10481176http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10481176http://purl.uniprot.org/core/name"Trends Cell Biol"xsd:string
http://purl.uniprot.org/citations/10481176http://purl.uniprot.org/core/pages"387-394"xsd:string
http://purl.uniprot.org/citations/10481176http://purl.uniprot.org/core/title"Septins: cytoskeletal polymers or signalling GTPases?"xsd:string
http://purl.uniprot.org/citations/10481176http://purl.uniprot.org/core/volume"9"xsd:string
http://purl.uniprot.org/citations/10481176http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10481176
http://purl.uniprot.org/citations/10481176http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10481176
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http://purl.uniprot.org/uniprot/Q07657http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/10481176