|Author||Ntoukakis, Vardis ♦ Schwessinger, Benjamin ♦ Segonzac, Cécile ♦ Zipfel, Cyril|
|Source||World Health Organization (WHO)-Global Index Medicus|
|Publisher||American Society of Plant Biologists|
|File Format||HTM / HTML|
|Subject Domain (in DDC)||Natural sciences & mathematics ♦ Chemistry & allied sciences ♦ Life sciences; biology ♦ Physiology & related subjects ♦ Biochemistry ♦ Genetics and evolution ♦ Natural history of organisms ♦ Technology ♦ Medicine & health ♦ Human physiology ♦ Pharmacology and therapeutics|
|Subject Domain (in MeSH)||Eukaryota ♦ Organisms ♦ Polycyclic Compounds ♦ Enzymes and Coenzymes ♦ Amino Acids, Peptides, and Proteins ♦ Chemicals and Drugs ♦ Chemical Phenomena ♦ Genetic Phenomena ♦ Biological Sciences|
|Subject Keyword||Discipline Botany ♦ Arabidopsis Proteins ♦ Genetics ♦ Metabolism ♦ Brassinosteroids ♦ Protein-serine-threonine Kinases ♦ Recombinant Fusion Proteins ♦ Arabidopsis ♦ Drug Effects ♦ Flagellin ♦ Pharmacology ♦ Mutation ♦ Peptide Elongation Factor Tu ♦ Plants, Genetically Modified ♦ Protein Kinases ♦ Signal Transduction ♦ Journal Article ♦ Research Support, Non-u.s. Gov't|
|Abstract||Detailed phenotypic characterization reveals that several BAK1 fusion proteins with C-terminal tags strongly impair complementation of bak1 null mutants with respect to responsiveness to the bacterial pathogen-associated molecular patterns flagellin and EF-Tu. This raises concerns about the widespread use of such protein variants of this important regulatory Leu-rich repeat receptor-like kinase (RLK) for functional analyses of RLK-based signaling.|
|Description||Country affiliation: United kingdom
Author Affiliation: Ntoukakis V ( The Sainsbury Laboratory, Norwich NR4 7UH, United Kingdom.)
|Educational Role||Student ♦ Teacher|
|Age Range||above 22 year|
|Educational Use||Reading ♦ Research ♦ Self Learning|
|Education Level||UG and PG|
|Learning Resource Type||Article|
|Publisher Place||United States|
|Journal||THE PLANT CELL ONLINE|
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