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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5475
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pubmed:dateCreated |
2000-7-24
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pubmed:abstractText |
An assay was developed to study plant receptor kinase activation and signaling mechanisms. The extracellular leucine-rich repeat (LRR) and transmembrane domains of the Arabidopsis receptor kinase BRI1, which is implicated in brassinosteroid signaling, were fused to the serine/threonine kinase domain of XA21, the rice disease resistance receptor. The chimeric receptor initiates plant defense responses in rice cells upon treatment with brassinosteroids. These results, which indicate that the extracellular domain of BRI1 perceives brassinosteroids, suggest a general signaling mechanism for the LRR receptor kinases of plants. This system should allow the discovery of ligands for the LRR kinases, the largest group of plant receptor kinases.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/BRI1 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Brassinosteroids,
http://linkedlifedata.com/resource/pubmed/chemical/Chitinase,
http://linkedlifedata.com/resource/pubmed/chemical/Cholestanols,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylalanine Ammonia-Lyase,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Steroids, Heterocyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Xa21 protein, Oryza sativa,
http://linkedlifedata.com/resource/pubmed/chemical/brassinolide
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
288
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2360-3
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:10875920-Arabidopsis,
pubmed-meshheading:10875920-Arabidopsis Proteins,
pubmed-meshheading:10875920-Brassinosteroids,
pubmed-meshheading:10875920-Cell Death,
pubmed-meshheading:10875920-Cell Line,
pubmed-meshheading:10875920-Chitinase,
pubmed-meshheading:10875920-Cholestanols,
pubmed-meshheading:10875920-Gene Expression Regulation, Plant,
pubmed-meshheading:10875920-Ligands,
pubmed-meshheading:10875920-Oryza sativa,
pubmed-meshheading:10875920-Phenylalanine Ammonia-Lyase,
pubmed-meshheading:10875920-Plant Proteins,
pubmed-meshheading:10875920-Plants, Genetically Modified,
pubmed-meshheading:10875920-Protein Kinases,
pubmed-meshheading:10875920-Protein Structure, Tertiary,
pubmed-meshheading:10875920-Protein-Serine-Threonine Kinases,
pubmed-meshheading:10875920-Recombinant Fusion Proteins,
pubmed-meshheading:10875920-Respiratory Burst,
pubmed-meshheading:10875920-Signal Transduction,
pubmed-meshheading:10875920-Steroids, Heterocyclic,
pubmed-meshheading:10875920-Xanthomonas
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pubmed:year |
2000
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pubmed:articleTitle |
Perception of brassinosteroids by the extracellular domain of the receptor kinase BRI1.
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pubmed:affiliation |
Plant Biology Laboratory, The Howard Hughes Medical Institute, The Salk Institute for Biological Studies, La Jolla, CA 92037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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