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http://purl.uniprot.org/citations/22270398http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22270398http://www.w3.org/2000/01/rdf-schema#comment"Cofilin promotes actin filament turnover by severing and depolymerizing actin filaments. Cofilin is inactivated by phosphorylation on Ser-3 by LIM-kinase1 (LIMK1) and is activated when protein phosphatase Slingshot-1L (SSH1L) dephosphorylates this residue. The authors have shown that Ca-induced cofilin dephosphorylation is mediated by calcineurin (Cn)-dependent activation of SSH1L. In this study, Ca/calmodulin-dependent protein kinase II (CaMKII) is shown to negatively regulate SSH1L activity and bind to SSH1L in a complex with 14-3-3. Phosphorylation of LIMK1 by CaMKII and its subsequent activation regulates the subcellular localization of SSH1L. Based on these findings, the authors suggest that CaMKII and Cn provide a switch-like mechanism that controls Ca-dependent LIMK1, SSH1L and cofilin activation, and subsequently actin cytoskeletal reorganization."xsd:string
http://purl.uniprot.org/citations/22270398http://purl.org/dc/terms/identifier"doi:10.1097/maj.0b013e318244745b"xsd:string
http://purl.uniprot.org/citations/22270398http://purl.uniprot.org/core/author"Wang Y."xsd:string
http://purl.uniprot.org/citations/22270398http://purl.uniprot.org/core/author"Wang H."xsd:string
http://purl.uniprot.org/citations/22270398http://purl.uniprot.org/core/author"Zhang H.Y."xsd:string
http://purl.uniprot.org/citations/22270398http://purl.uniprot.org/core/author"Yang Y.D."xsd:string
http://purl.uniprot.org/citations/22270398http://purl.uniprot.org/core/author"Gao Z.L."xsd:string
http://purl.uniprot.org/citations/22270398http://purl.uniprot.org/core/author"Meng L.J."xsd:string
http://purl.uniprot.org/citations/22270398http://purl.uniprot.org/core/author"Zhao J.W."xsd:string
http://purl.uniprot.org/citations/22270398http://purl.uniprot.org/core/author"Ji Q.Y."xsd:string
http://purl.uniprot.org/citations/22270398http://purl.uniprot.org/core/author"Xing F.J."xsd:string
http://purl.uniprot.org/citations/22270398http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22270398http://purl.uniprot.org/core/name"Am J Med Sci"xsd:string
http://purl.uniprot.org/citations/22270398http://purl.uniprot.org/core/pages"462-472"xsd:string
http://purl.uniprot.org/citations/22270398http://purl.uniprot.org/core/title"Regulation of cofilin activity by CaMKII and calcineurin."xsd:string
http://purl.uniprot.org/citations/22270398http://purl.uniprot.org/core/volume"344"xsd:string
http://purl.uniprot.org/citations/22270398http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22270398
http://purl.uniprot.org/citations/22270398http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22270398
http://purl.uniprot.org/uniprot/#_E9PBG7-mappedCitation-22270398http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22270398
http://purl.uniprot.org/uniprot/#_E9PF82-mappedCitation-22270398http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22270398
http://purl.uniprot.org/uniprot/#_A0A0S2Z4B5-mappedCitation-22270398http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22270398
http://purl.uniprot.org/uniprot/#_A0A0S2Z4C6-mappedCitation-22270398http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22270398
http://purl.uniprot.org/uniprot/#_A0A8V8TPJ8-mappedCitation-22270398http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22270398
http://purl.uniprot.org/uniprot/#_A0A8V8TPY4-mappedCitation-22270398http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22270398