http://purl.uniprot.org/citations/20801873 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/20801873 | http://www.w3.org/2000/01/rdf-schema#comment | "Cells are responding to hypoxia via prolyl-4-hydroxylase domain (PHD) enzymes, which are responsible for oxygen-dependent hydroxylation of the hypoxia-inducible factor (HIF)-1α subunit. To gain further insight into PHD function, we generated knockdown cell models for the PHD2 isoform, which is the main isoform regulating HIF-1α hydroxylation and thus stability in normoxia. Induction of a PHD2 knockdown in tetracycline-inducible HeLa PHD2 knockdown cells resulted in increased F-actin formation as detected by phalloidin staining. A similar effect could be observed in the stably transfected PHD2 knockdown cell clones 1B6 and 3B7. F-actin is at least in part responsible for shaping cell morphology as well as regulating cell migration. Cell migration was impaired significantly as a consequence of PHD2 knockdown in a scratch assay. Mechanistically, PHD2 knockdown resulted in activation of the RhoA (Ras homolog gene family member A)/Rho-associated kinase pathway with subsequent phosphorylation of cofilin. Because cofilin phosphorylation impairs its actin-severing function, this may explain the F-actin phenotype, thereby providing a functional link between PHD2-dependent signaling and cell motility."xsd:string |
http://purl.uniprot.org/citations/20801873 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.132985"xsd:string |
http://purl.uniprot.org/citations/20801873 | http://purl.uniprot.org/core/author | "Camenisch G."xsd:string |
http://purl.uniprot.org/citations/20801873 | http://purl.uniprot.org/core/author | "Vogel S."xsd:string |
http://purl.uniprot.org/citations/20801873 | http://purl.uniprot.org/core/author | "Katschinski D.M."xsd:string |
http://purl.uniprot.org/citations/20801873 | http://purl.uniprot.org/core/author | "Wottawa M."xsd:string |
http://purl.uniprot.org/citations/20801873 | http://purl.uniprot.org/core/author | "Zieseniss A."xsd:string |
http://purl.uniprot.org/citations/20801873 | http://purl.uniprot.org/core/author | "Farhat K."xsd:string |
http://purl.uniprot.org/citations/20801873 | http://purl.uniprot.org/core/author | "Le-Huu S."xsd:string |
http://purl.uniprot.org/citations/20801873 | http://purl.uniprot.org/core/author | "Malz C."xsd:string |
http://purl.uniprot.org/citations/20801873 | http://purl.uniprot.org/core/author | "Schnelle M."xsd:string |
http://purl.uniprot.org/citations/20801873 | http://purl.uniprot.org/core/author | "von Ahlen M."xsd:string |
http://purl.uniprot.org/citations/20801873 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
http://purl.uniprot.org/citations/20801873 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
http://purl.uniprot.org/citations/20801873 | http://purl.uniprot.org/core/pages | "33756-33763"xsd:string |
http://purl.uniprot.org/citations/20801873 | http://purl.uniprot.org/core/title | "Prolyl hydroxylase domain (PHD) 2 affects cell migration and F-actin formation via RhoA/rho-associated kinase-dependent cofilin phosphorylation."xsd:string |
http://purl.uniprot.org/citations/20801873 | http://purl.uniprot.org/core/volume | "285"xsd:string |
http://purl.uniprot.org/citations/20801873 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20801873 |
http://purl.uniprot.org/citations/20801873 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/20801873 |
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http://purl.uniprot.org/uniprot/#_P61586-mappedCitation-20801873 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/20801873 |
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http://purl.uniprot.org/uniprot/#_A0A7I2YQV1-mappedCitation-20801873 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/20801873 |
http://purl.uniprot.org/uniprot/#_B4DKN9-mappedCitation-20801873 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/20801873 |