| http://purl.uniprot.org/citations/18408008 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18408008 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18408008 | http://www.w3.org/2000/01/rdf-schema#comment | "AAK-2 is one of two alpha isoforms of the AMP-activated protein kinase in Caenorhabditis elegans and is involved in life span maintenance, stress responses, and germ cell cycle arrest upon dauer entry. We found that AAK-2 was phosphorylated at threonine 243 in response to paraquat treatment and that this phosphorylation depends on PAR-4, the C. elegans LKB1 homologue. Both aak-2 mutation and par-4 knockdown increased the sensitivity of C. elegans worms to paraquat, and the double deficiency did not further increase sensitivity, indicating that aak-2 and par-4 act in a linear pathway. Both mutations also slowed body bending during locomotion and failed to reduce head oscillation in response to anterior touch. Consistent with this abnormal motility and behavioral response, expression of the AAK-2::green fluorescent protein fusion protein was observed in the ventral cord, some neurons, body wall muscle, pharynx, vulva, somatic gonad, and excretory cell. Our study suggests that AMPK can influence the behavior of C. elegans worms in addition to its well known function in metabolic control."xsd:string |
| http://purl.uniprot.org/citations/18408008 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m709115200"xsd:string |
| http://purl.uniprot.org/citations/18408008 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m709115200"xsd:string |
| http://purl.uniprot.org/citations/18408008 | http://purl.uniprot.org/core/author | "Lee H."xsd:string |
| http://purl.uniprot.org/citations/18408008 | http://purl.uniprot.org/core/author | "Lee H."xsd:string |
| http://purl.uniprot.org/citations/18408008 | http://purl.uniprot.org/core/author | "Lee J."xsd:string |
| http://purl.uniprot.org/citations/18408008 | http://purl.uniprot.org/core/author | "Lee J."xsd:string |
| http://purl.uniprot.org/citations/18408008 | http://purl.uniprot.org/core/author | "Lee S.J."xsd:string |
| http://purl.uniprot.org/citations/18408008 | http://purl.uniprot.org/core/author | "Lee S.J."xsd:string |
| http://purl.uniprot.org/citations/18408008 | http://purl.uniprot.org/core/author | "Cho J.S."xsd:string |
| http://purl.uniprot.org/citations/18408008 | http://purl.uniprot.org/core/author | "Cho J.S."xsd:string |
| http://purl.uniprot.org/citations/18408008 | http://purl.uniprot.org/core/author | "Gartner A."xsd:string |
| http://purl.uniprot.org/citations/18408008 | http://purl.uniprot.org/core/author | "Gartner A."xsd:string |
| http://purl.uniprot.org/citations/18408008 | http://purl.uniprot.org/core/author | "Koo H.S."xsd:string |
| http://purl.uniprot.org/citations/18408008 | http://purl.uniprot.org/core/author | "Koo H.S."xsd:string |
| http://purl.uniprot.org/citations/18408008 | http://purl.uniprot.org/core/author | "Lambacher N."xsd:string |
| http://purl.uniprot.org/citations/18408008 | http://purl.uniprot.org/core/author | "Lambacher N."xsd:string |
| http://purl.uniprot.org/citations/18408008 | http://purl.uniprot.org/core/author | "Lee T.H."xsd:string |
| http://purl.uniprot.org/citations/18408008 | http://purl.uniprot.org/core/author | "Lee T.H."xsd:string |
| http://purl.uniprot.org/citations/18408008 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18408008 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18408008 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/18408008 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |