Extracellular leucine-rich repeats as a platform for receptor/coreceptor complex formation. - Wikidata - awgldk - TriplyDB

Extracellular leucine-rich repeats as a platform for receptor/coreceptor complex formation.

Extracellular leucine-rich repeats as a platform for receptor/coreceptor complex formation.

http://www.wikidata.org/entity/Q35002696

about

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 Brassinosteroid signaling and BRI1 dynamics went underground The molecular circuitry of brassinosteroid signaling The growth-defense pivot: crisis management in plants mediated by LRR-RK surface receptors Brassinosteroids modulate the efficiency of plant immune responses to microbe-associated molecular patterns Leucine-Rich Repeat (LRR) Domains Containing Intervening Motifs in Plants.Fine mapping and identification of candidate genes for a QTL affecting Meloidogyne incognita reproduction in Upland cotton Nod factor receptors form heteromeric complexes and are essential for intracellular infection in medicago nodules.Growth-defense tradeoffs in plants: a balancing act to optimize fitness.The yeast three-hybrid system as an experimental platform to identify proteins interacting with small signaling molecules in plant cells: potential and limitations Structural insights into the negative regulation of BRI1 signaling by BRI1-interacting protein BKI1.Structure of the OsSERK2 leucine-rich repeat extracellular domain Direct involvement of leucine-rich repeats in assembling ligand-triggered receptor-coreceptor complexes Functional analysis of the tomato immune receptor Ve1 through domain swaps with its non-functional homolog Ve2 Mutational analysis of the Ve1 immune receptor that mediates Verticillium resistance in tomato.SRC2-1 is required in PcINF1-induced pepper immunity by acting as an interacting partner of PcINF1.Evolutionary, Comparative and Functional Analyses of the Brassinosteroid Receptor Gene, BRI1, in Wheat and Its Relation to Other Plant Genomes Brassinosteroids inhibit pathogen-associated molecular pattern-triggered immune signaling independent of the receptor kinase BAK1 De Novo Assembled Wheat Transcriptomes Delineate Differentially Expressed Host Genes in Response to Leaf Rust Infection.Internalization and vacuolar targeting of the brassinosteroid hormone receptor BRI1 are regulated by ubiquitination Assessing the diverse functions of BAK1 and its homologs in arabidopsis, beyond BR signaling and PTI responses.Protein kinase signaling networks in plant innate immunity.Latest news on Arabidopsis brassinosteroid perception and signaling.Mapping FLS2 function to structure: LRRs, kinase and its working bits.The brassinosteroid signaling pathway-new key players and interconnections with other signaling networks crucial for plant development and stress tolerance.Structure-function aspects of extracellular leucine-rich repeat-containing cell surface receptors in plants.Ligand perception, activation, and early signaling of plant steroid receptor brassinosteroid insensitive 1.BAK1 directly regulates brassinosteroid perception and BRI1 activation.A sweet story: Bean pod mottle virus transmission dynamics by Mexican bean beetles (Epilachna varivestis)Functional roles of the pepper leucine-rich repeat protein and its interactions with pathogenesis-related and hypersensitive-induced proteins in plant cell death and immunity.Plant immune and growth receptors share common signalling components but localise to distinct plasma membrane nanodomains.Probing Activation and Deactivation of the BRASSINOSTEROID INSENSITIVE1 Receptor Kinase by Immunoprecipitation.ERECTA and BAK1 Receptor Like Kinases Interact to Regulate Immune Responses in Arabidopsis.Structure reveals that BAK1 as a co-receptor recognizes the BRI1-bound brassinolide.Brassinosteroids antagonize gibberellin- and salicylate-mediated root immunity in rice.BAK1 is involved in AtRALF1-induced inhibition of root cell expansion.Constitutive activation of brassinosteroid signaling in the Arabidopsis elongated-D/bak1 mutant.Structure-oriented bioinformatic approach exploring histidine-rich clusters in proteins.

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Extracellular leucine-rich repeats as a platform for receptor/coreceptor complex formation.

http://www.wikidata.org/entity/Q35002696

description

2011 nî lūn-bûn

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2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2011 թվականի ապրիլին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Extracellular leucine-rich rep ...... /coreceptor complex formation.

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Extracellular leucine-rich rep ...... /coreceptor complex formation.

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Extracellular leucine-rich rep ...... /coreceptor complex formation.

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Extracellular leucine-rich rep ...... /coreceptor complex formation.

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Extracellular leucine-rich rep ...... /coreceptor complex formation.

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Proceedings of the National Academy of Sciences of the United States of America

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Extracellular leucine-rich rep ...... /coreceptor complex formation.

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Emilia Balsemão-Pires

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Jeffery L Dangl

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Youssef Belkhadir

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Yvon Jaillais

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P2860

Cell signaling by receptor tyrosine kinases

Bacterial disease resistance in Arabidopsis through flagellin perception

A renaissance of elicitors: perception of microbe-associated molecular patterns and danger signals by pattern-recognition receptors

Brassinosteroids regulate dissociation of BKI1, a negative regulator of BRI1 signaling, from the plasma membrane.

The retromer protein VPS29 links cell polarity and organ initiation in plants.

Rapid heteromerization and phosphorylation of ligand-activated plant transmembrane receptors and their associated kinase BAK1.

Receptor-like kinases from Arabidopsis form a monophyletic gene family related to animal receptor kinases.

Brassinosteroid signal transduction from cell-surface receptor kinases to nuclear transcription factors.

Intragenic suppression of a trafficking-defective brassinosteroid receptor mutant in Arabidopsis

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