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The proteasome acts as a hub for local and systemic plant immunity in Arabidopsis thaliana and constitutes a virulence target of Pseudomonas syringae type-III effector proteins

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inferredcites →https://doi.org/10.1016/j.biochi.2007.07.019openalex-snapshot
Structure, function and regulation of plant proteasomes
inferredcites →https://doi.org/10.1016/j.cell.2006.02.047openalex-snapshot
Specific Bacterial Suppressors of MAMP Signaling Upstream of MAPKKK in Arabidopsis Innate Immunity
inferredcites →https://doi.org/10.1016/j.cell.2009.03.038openalex-snapshot
Proteasome-Mediated Turnover of the Transcription Coactivator NPR1 Plays Dual Roles in Regulating Plant Immunity
inferredcites →https://doi.org/10.1016/j.chom.2014.10.007openalex-snapshot
The Calcium-Dependent Protein Kinase CPK28 Buffers Plant Immunity and Regulates BIK1 Turnover
inferredcites →https://doi.org/10.1016/j.cub.2007.02.028openalex-snapshot
A J Domain Virulence Effector of Pseudomonas syringae Remodels Host Chloroplasts and Suppresses Defenses
inferredcites →https://doi.org/10.1016/j.cub.2008.07.085openalex-snapshot
Negative Regulation of PAMP-Triggered Immunity by an E3 Ubiquitin Ligase Triplet in Arabidopsis
inferredcites →https://doi.org/10.1016/j.febslet.2005.07.073openalex-snapshot
Proteasome comprising a β1 inducible subunit acts as a negative regulator of NADPH oxidase during elicitation of plant defense reactions
inferredcites →https://doi.org/10.1016/j.molcel.2014.02.021openalex-snapshot
Direct Regulation of the NADPH Oxidase RBOHD by the PRR-Associated Kinase BIK1 during Plant Immunity
inferredcites →https://doi.org/10.1016/j.semcancer.2006.12.001openalex-snapshot
Inducible cell death in plant immunity
inferredcites →https://doi.org/10.1016/s0092-8674(00)81858-9openalex-snapshot
The Arabidopsis NPR1 Gene That Controls Systemic Acquired Resistance Encodes a Novel Protein Containing Ankyrin Repeats
inferredcites →https://doi.org/10.1016/s1097-2765(00)80265-8openalex-snapshot
FLS2
inferredcites →https://doi.org/10.1016/s1357-2725(02)00386-2openalex-snapshot
Preferential induction of 20S proteasome subunits during elicitation of plant defense reactions: towards the characterization of “plant defense proteasomes”
inferredcites →https://doi.org/10.1021/bi001815nopenalex-snapshot
Assembly of the 26S Proteasome Is Regulated by Phosphorylation of the p45/Rpt6 ATPase Subunit
inferredcites →https://doi.org/10.1021/pr400630wopenalex-snapshot
Proteomics Analysis Reveals a Highly Heterogeneous Proteasome Composition and the Post-translational Regulation of Peptidase Activity under Pathogen Signaling in Plants
inferredcites →https://doi.org/10.1038/nature05286openalex-snapshot
The plant immune system
inferredcites →https://doi.org/10.1038/nature06782openalex-snapshot
A plant pathogen virulence factor inhibits the eukaryotic proteasome by a novel mechanism
inferredcites →https://doi.org/10.1038/nrm2688openalex-snapshot
The ubiquitin–26S proteasome system at the nexus of plant biology
inferredcites →https://doi.org/10.1073/pnas.0401601101openalex-snapshot
A family of conserved bacterial effectors inhibits salicylic acid-mediated basal immunity and promotes disease necrosis in plants
inferredcites →https://doi.org/10.1073/pnas.0910943107openalex-snapshot
Pseudomonas syringae hijacks plant stress chaperone machinery for virulence
inferredcites →https://doi.org/10.1073/pnas.1013031108openalex-snapshot
Genetic disassembly and combinatorial reassembly identify a minimal functional repertoire of type III effectors in Pseudomonas syringae
inferredcites →https://doi.org/10.1073/pnas.1103338108openalex-snapshot
Effector-triggered immunity blocks pathogen degradation of an immunity-associated vesicle traffic regulator in Arabidopsis
inferredcites →https://doi.org/10.1073/pnas.97.9.4856openalex-snapshot
The Pseudomonas syringae Hrp pathogenicity island has a tripartite mosaic structure composed of a cluster of type III secretion genes bounded by exchangeable effector and conserved effector loci that contribute to parasitic fitness and pathogenicity in plants
inferredcites →https://doi.org/10.1074/jbc.m110.136622openalex-snapshot
Affinity Purification of the Arabidopsis 26 S Proteasome Reveals a Diverse Array of Plant Proteolytic Complexes
inferredcites →https://doi.org/10.1074/jbc.m113.491662openalex-snapshot
The Proteasome-associated Protein Ecm29 Inhibits Proteasomal ATPase Activity and in Vivo Protein Degradation by the Proteasome
inferredcites →https://doi.org/10.1093/jexbot/52.362.1947openalex-snapshot
Cryptogein affects expression of α3, α6 and β1 20S proteasome subunits encoding genes in tobacco
inferredcites →https://doi.org/10.1093/pcp/pcr099openalex-snapshot
RPT2a, a 26S proteasome AAA-ATPase, is Directly Involved in Arabidopsis CC-NBS-LRR Protein uni-1D-Induced Signaling Pathways
inferredcites →https://doi.org/10.1094/mpmi-04-10-0094openalex-snapshot
Pseudomonas syringae Virulence Factor Syringolin A Counteracts Stomatal Immunity by Proteasome Inhibition
inferredcites →https://doi.org/10.1094/mpmi-12-13-0363-ropenalex-snapshot
HopZ4 from Pseudomonas syringae, a Member of the HopZ Type III Effector Family from the YopJ Superfamily, Inhibits the Proteasome in Plants
inferredcites →https://doi.org/10.1101/gad.1825209openalex-snapshot
A novel membrane fusion-mediated plant immunity against bacterial pathogens
inferredcites →https://doi.org/10.1104/pp.106.081257openalex-snapshot
The Arabidopsis Flavin-Dependent Monooxygenase FMO1 Is an Essential Component of Biologically Induced Systemic Acquired Resistance
inferredcites →https://doi.org/10.1104/pp.109.139709openalex-snapshot
Recent Advances in PAMP-Triggered Immunity against Bacteria: Pattern Recognition Receptors Watch over and Raise the Alarm
inferredcites →https://doi.org/10.1104/pp.112.199281openalex-snapshot
Ubiquitination during Plant Immune Signaling
inferredcites →https://doi.org/10.1104/pp.15.00132openalex-snapshot
The Xanthomonas campestris Type III Effector XopJ Proteolytically Degrades Proteasome Subunit RPT6
inferredcites →https://doi.org/10.1105/tpc.010381openalex-snapshot
Cytokinin Growth Responses in Arabidopsis Involve the 26S Proteasome Subunit RPN12
inferredcites →https://doi.org/10.1105/tpc.111.089482openalex-snapshot
The RPT2 Subunit of the 26S Proteasome Directs Complex Assembly, Histone Dynamics, and Gametophyte and Sporophyte Development inArabidopsis
inferredcites →https://doi.org/10.1105/tpc.112.103564openalex-snapshot
Pipecolic Acid, an Endogenous Mediator of Defense Amplification and Priming, Is a Critical Regulator of Inducible Plant Immunity
inferredcites →https://doi.org/10.1105/tpc.112.104463openalex-snapshot
The Ubiquitin Ligase PUB22 Targets a Subunit of the Exocyst Complex Required for PAMP-Triggered Responses in Arabidopsis
inferredcites →https://doi.org/10.1105/tpc.114.125419openalex-snapshot
Intervention of Phytohormone Pathways by Pathogen Effectors
inferredcites →https://doi.org/10.1105/tpc.15.00496openalex-snapshot
Pipecolic Acid Orchestrates Plant Systemic Acquired Resistance and Defense Priming via Salicylic Acid-Dependent and -Independent Pathways
inferredcites →https://doi.org/10.1111/cmi.12385openalex-snapshot
Perturbation of host ubiquitin systems by plant pathogen/pest effector proteins
inferredcites →https://doi.org/10.1111/j.1364-3703.2011.00719.xopenalex-snapshot
The YopJ superfamily in plant‐associated bacteria
inferredcites →https://doi.org/10.1111/j.1365-313x.2008.03466.xopenalex-snapshot
Constitutive activation of a CC‐NB‐LRR protein alters morphogenesis through the cytokinin pathway in Arabidopsis
inferredcites →https://doi.org/10.1111/j.1365-313x.2009.04122.xopenalex-snapshot
Proteasome activity profiling: a simple, robust and versatile method revealing subunit-selective inhibitors and cytoplasmic, defense-induced proteasome activities
inferredcites →https://doi.org/10.1111/j.1365-313x.2012.05048.xopenalex-snapshot
RPN1a, a 26S proteasome subunit, is required for innate immunity in Arabidopsis
inferredcites →https://doi.org/10.1111/j.1462-5822.2009.01396.xopenalex-snapshot
The Pseudomonas syringae type III effector HopG1 targets mitochondria, alters plant development and suppresses plant innate immunity
inferredcites →https://doi.org/10.1111/j.1469-8137.2012.04266.xopenalex-snapshot
The ubiquitin–proteasome system: central modifier of plant signalling
inferredcites →https://doi.org/10.1111/nph.12651openalex-snapshot
The bacterial effector H op M 1 suppresses PAMP ‐triggered oxidative burst and stomatal immunity
inferredcites →https://doi.org/10.1111/nph.13605openalex-snapshot
Subversion of plant cellular functions by bacterial type‐ III effectors: beyond suppression of immunity
inferredcites →https://doi.org/10.1111/tpj.12035openalex-snapshot
Nuclear ubiquitin proteasome degradation affects WRKY 45 function in the rice defense program
inferredcites →https://doi.org/10.1126/science.1129523openalex-snapshot
A Bacterial Virulence Protein Suppresses Host Innate Immunity to Cause Plant Disease
inferredcites →https://doi.org/10.1126/science.1204903openalex-snapshot
Direct Ubiquitination of Pattern Recognition Receptor FLS2 Attenuates Plant Innate Immunity
inferredcites →https://doi.org/10.1126/science.1211592openalex-snapshot
Pathogen Effectors Target Arabidopsis EDS1 and Alter Its Interactions with Immune Regulators
inferredcites →https://doi.org/10.1126/science.1248849openalex-snapshot
A Bacterial Tyrosine Phosphatase Inhibits Plant Pattern Recognition Receptor Activation
inferredcites →https://doi.org/10.1146/annurev-arplant-042811-105606openalex-snapshot
Systemic Acquired Resistance: Turning Local Infection into Global Defense
inferredcites →https://doi.org/10.1146/annurev-phyto-080614-120132openalex-snapshot
Priming for Enhanced Defense
inferredcites →https://doi.org/10.1146/annurev-phyto-082712-102312openalex-snapshot
Manipulation of Host Proteasomes as a Virulence Mechanism of Plant Pathogens
inferredcites →https://doi.org/10.1146/annurev.arplant.55.031903.141801openalex-snapshot
THE UBIQUITIN 26S PROTEASOME PROTEOLYTIC PATHWAY
inferredcites →https://doi.org/10.1146/annurev.arplant.57.032905.105346openalex-snapshot
A Renaissance of Elicitors: Perception of Microbe-Associated Molecular Patterns and Danger Signals by Pattern-Recognition Receptors
inferredcites →https://doi.org/10.1371/journal.ppat.1000388openalex-snapshot
Deletions in the Repertoire of Pseudomonas syringae pv. tomato DC3000 Type III Secretion Effector Genes Reveal Functional Overlap among Effectors
inferredcites →https://doi.org/10.1371/journal.ppat.1002132openalex-snapshot
Dynamic Evolution of Pathogenicity Revealed by Sequencing and Comparative Genomics of 19 Pseudomonas syringae Isolates
inferredcites →https://doi.org/10.1371/journal.ppat.1003121openalex-snapshot
A Pathogen Type III Effector with a Novel E3 Ubiquitin Ligase Architecture
inferredcites →https://doi.org/10.1371/journal.ppat.1003281openalex-snapshot
Pseudomonas syringae pv. syringae Uses Proteasome Inhibitor Syringolin A to Colonize from Wound Infection Sites
inferredcites →https://doi.org/10.1371/journal.ppat.1003427openalex-snapshot
The Xanthomonas campestris Type III Effector XopJ Targets the Host Cell Proteasome to Suppress Salicylic-Acid Mediated Plant Defence
inferredcites →https://doi.org/10.3389/fpls.2013.00252openalex-snapshot
Reprogramming of plants during systemic acquired resistance
inferredcites →https://doi.org/10.3389/fpls.2014.00295openalex-snapshot
Preparing to fight back: generation and storage of priming compounds
inferredcites →https://doi.org/10.3389/fpls.2014.00736openalex-snapshot
Interactions of Xanthomonas type-III effector proteins with the plant ubiquitin and ubiquitin-like pathways
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