Binding of brassinosteroids to the extracellular domain of plant receptor kinase BRI1. - Wikidata - awgldk - TriplyDB

Binding of brassinosteroids to the extracellular domain of plant receptor kinase BRI1.

Binding of brassinosteroids to the extracellular domain of plant receptor kinase BRI1.

http://www.wikidata.org/entity/Q45224133

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Evolutionary proteomics identifies amino acids essential for ligand-binding of the cytokinin receptor CHASE domain Tomato BRASSINOSTEROID INSENSITIVE1 is required for systemin-induced root elongation in Solanum pimpinellifolium but is not essential for wound signaling Brassinosteroid-mediated regulation of agronomic traits in rice Brassinosteroid signalling Structural basis of steroid hormone perception by the receptor kinase BRI1 Structural insight into brassinosteroid perception by BRI1 Crystal structure of an LRR protein with two solenoids Structural basis for differential recognition of brassinolide by its receptors Crystal structures of the phosphorylated BRI1 kinase domain and implications for brassinosteroid signal initiation Molecular mechanism for plant steroid receptor activation by somatic embryogenesis co-receptor kinases The molecular circuitry of brassinosteroid signaling Tomato BRI1 and systemin wound signalling Genetic evidence for an indispensable role of somatic embryogenesis receptor kinases in brassinosteroid signaling Complex evolutionary events at a tandem cluster of Arabidopsis thaliana genes resulting in a single-locus genetic incompatibility Bacterial effectors target the common signaling partner BAK1 to disrupt multiple MAMP receptor-signaling complexes and impede plant immunity Structure-function analysis of STRUBBELIG, an Arabidopsis atypical receptor-like kinase involved in tissue morphogenesis Leucine-Rich Repeat (LRR) Domains Containing Intervening Motifs in Plants.The EVERSHED receptor-like kinase modulates floral organ shedding in Arabidopsis.Identification of ligand binding site of phytosulfokine receptor by on-column photoaffinity labeling.Molecular characterisation of the STRUBBELIG-RECEPTOR FAMILY of genes encoding putative leucine-rich repeat receptor-like kinases in Arabidopsis thaliana.The Arabidopsis thaliana brassinosteroid receptor (AtBRI1) contains a domain that functions as a guanylyl cyclase in vitro.The role of OsBRI1 and its homologous genes, OsBRL1 and OsBRL3, in rice.A genome-wide functional investigation into the roles of receptor-like proteins in Arabidopsis.Functional analyses of the CLAVATA2-like proteins and their domains that contribute to CLAVATA2 specificity.The Arabidopsis cell cycle F-box protein SKP2A binds to auxin.Somatic embryogenesis receptor kinases control root development mainly via brassinosteroid-independent actions in Arabidopsis thaliana.Fluorescent castasterone reveals BRI1 signaling from the plasma membrane.Genome-wide identification, characterization and expression analysis of populus leucine-rich repeat receptor-like protein kinase genes.Activity of the brassinosteroid transcription factors BRASSINAZOLE RESISTANT1 and BRASSINOSTEROID INSENSITIVE1-ETHYL METHANESULFONATE-SUPPRESSOR1/BRASSINAZOLE RESISTANT2 blocks developmental reprogramming in response to low phosphate availability.BAM 1 and RECEPTOR-LIKE PROTEIN KINASE 2 constitute a signaling pathway and modulate CLE peptide-triggered growth inhibition in Arabidopsis root.Arabidopsis MAKR5 is a positive effector of BAM3-dependent CLE45 signaling BES1 regulates the localization of the brassinosteroid receptor BRL3 within the provascular tissue of the Arabidopsis primary root Chemical genetic dissection of brassinosteroid-ethylene interaction Characterization of receptor proteins using affinity cross-linking with biotinylated ligands.A receptor-like cytoplasmic kinase, BIK1, associates with a flagellin receptor complex to initiate plant innate immunity.Activation-tagged suppressors of a weak brassinosteroid receptor mutant.Mechanisms of brassinosteroids interacting with multiple hormones Tyrosine phosphorylation in brassinosteroid signaling.Overproduction of the membrane-bound receptor-like protein kinase 1, RPK1, enhances abiotic stress tolerance in Arabidopsis.Rapid heteromerization and phosphorylation of ligand-activated plant transmembrane receptors and their associated kinase BAK1.

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P2860

Binding of brassinosteroids to the extracellular domain of plant receptor kinase BRI1.

http://www.wikidata.org/entity/Q45224133

description

2005 nî lūn-bûn

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年學術文章

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2005年學術文章

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name

Binding of brassinosteroids to the extracellular domain of plant receptor kinase BRI1.

@en

Binding of brassinosteroids to the extracellular domain of plant receptor kinase BRI1.

@nl

type

label

Binding of brassinosteroids to the extracellular domain of plant receptor kinase BRI1.

@en

Binding of brassinosteroids to the extracellular domain of plant receptor kinase BRI1.

@nl

prefLabel

Binding of brassinosteroids to the extracellular domain of plant receptor kinase BRI1.

@en

Binding of brassinosteroids to the extracellular domain of plant receptor kinase BRI1.

@nl

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Binding of brassinosteroids to the extracellular domain of plant receptor kinase BRI1.

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Ana Caño-Delgado

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Hideharu Seto

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Sayoko Hiranuma

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Shigeo Yoshida

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Shozo Fujioka

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Toshinori Kinoshita

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167-171

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scholarly article

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10.1038/NATURE03227

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1006682530

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15650741

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