Faculty Opinions recommendation of Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase.
By G. Ingram. 2005
406 citations recorded by the source corpus.
View Paper: https://www.semanticscholar.org/paper/5fa0804c6df7ea21277c22f3a118ff61f39486b5
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- Cyril Zipfel
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Citations in the corpus
- Brassinosteroids: Multidimensional Regulators of Plant Growth, Development, and Stress Responses[OPEN] (2019, background): “This protein was previously characterized as a BRI1-interacting protein (Li and Nam, 2002; Nam and Li, 2002; Russinova et al., 2004; Wang et al., 2005b, 2008), a genetic componentofBRsignaling (Li et al., 2002;NamandLi, 2002), and a BRI1 phosphorylation target (Li et al., 2002; Nam and Li, 2002).”
- PhosPhAt: a database of phosphorylation sites in Arabidopsis thaliana and a plant-specific phosphorylation site predictor (2007, background): “In the field of plant biology, the focus so far has been on the analysis of phosphorylation of specific proteins and protein families (5,6) and the study of very specific signaling pathways ( 7 ,8), mainly using genetic tools.”
- Brassinosteroid signal transduction from receptor kinases to transcription factors. (2010, methodology): “These include a chimeric receptor of BRI1-XA21 conferring BR-induced defense responses (29), binding of BRI1 immunoprecipitated from Arabidopsis plants (94) or expressed and purified in Escherichia coli (43) to tritium-labeled BL (3H-BL), and BRinduced BRI1 auto-phosphorylation (90, 91, 94).”
- Ligand-induced endocytosis of the pattern recognition receptor FLS2 in Arabidopsis. (2006, background): “Although this motif can be found in plant RLKs and PRRs (Ron and Avni 2004), it is not present in FLS2.”
- The Arabidopsis Leucine-Rich Repeat Receptor–Like Kinases BAK1/SERK3 and BKK1/SERK4 Are Required for Innate Immunity to Hemibiotrophic and Biotrophic Pathogens[W] (2011, background): “In addition, SERK3/BAK1 silencing in tomato led to loss ofVerticillium resistancemediated by the LRR receptor-like protein Ve1 (Fradin et al., 2009).”