http://purl.uniprot.org/citations/29361797 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/29361797 | http://www.w3.org/2000/01/rdf-schema#comment | "Protein post-translational modification by phosphorylation is essential for the activity and stability of proteins in higher plants and underlies their responses to diverse stimuli. There are more than 300 leucine-rich repeat receptor-like kinases (LRR-RLKs), a major group of receptor-like kinases (RLKs) that plays an important role in growth, development, and biotic stress responses in higher plants. To analyze auto- and transphosphorylation patterns and kinase activities in vitro, 43 full-length complementary DNA (cDNA) sequences were cloned from genes encoding LRR-RLKs. Autophosphorylation activity was found in the cytoplasmic domains (CDs) of 18 LRR-RLKs; 13 of these LRR-RLKs with autophosphorylation activity showed transphosphorylation in Escherichiacoli. BRI1-Associated Receptor Kinase (BAK1), which is critically involved in the brassinosteroid and plant innate immunity signal transduction pathways, showed strong auto- and transphosphorylation with multi-specific kinase activity within 2 h of induction of Brassica oleraceae BAK1-CD (BoBAK1-CD) in E. coli; moreover, the carboxy-terminus of LRR-RLKs regulated phosphorylation and kinase activity in Arabidopsis thaliana and vegetative crops."xsd:string |
http://purl.uniprot.org/citations/29361797 | http://purl.org/dc/terms/identifier | "doi:10.3390/molecules23010236"xsd:string |
http://purl.uniprot.org/citations/29361797 | http://purl.uniprot.org/core/author | "Lee Y."xsd:string |
http://purl.uniprot.org/citations/29361797 | http://purl.uniprot.org/core/author | "Park Y.S."xsd:string |
http://purl.uniprot.org/citations/29361797 | http://purl.uniprot.org/core/author | "Lim Y.P."xsd:string |
http://purl.uniprot.org/citations/29361797 | http://purl.uniprot.org/core/author | "Oh M.H."xsd:string |
http://purl.uniprot.org/citations/29361797 | http://purl.uniprot.org/core/author | "Oh E.S."xsd:string |
http://purl.uniprot.org/citations/29361797 | http://purl.uniprot.org/core/author | "Chae W.B."xsd:string |
http://purl.uniprot.org/citations/29361797 | http://purl.uniprot.org/core/author | "Rameneni J.J."xsd:string |
http://purl.uniprot.org/citations/29361797 | http://purl.uniprot.org/core/date | "2018"xsd:gYear |
http://purl.uniprot.org/citations/29361797 | http://purl.uniprot.org/core/name | "Molecules"xsd:string |
http://purl.uniprot.org/citations/29361797 | http://purl.uniprot.org/core/pages | "E236"xsd:string |
http://purl.uniprot.org/citations/29361797 | http://purl.uniprot.org/core/title | "Biochemical Analysis of the Role of Leucine-Rich Repeat Receptor-Like Kinases and the Carboxy-Terminus of Receptor Kinases in Regulating Kinase Activity in Arabidopsis thaliana and Brassica oleracea."xsd:string |
http://purl.uniprot.org/citations/29361797 | http://purl.uniprot.org/core/volume | "23"xsd:string |
http://purl.uniprot.org/citations/29361797 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/29361797 |
http://purl.uniprot.org/citations/29361797 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/29361797 |
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