On the public citation graph

Identification of Novel PAMP-Triggered Phosphorylation and Dephosphorylation Events in Arabidopsis thaliana by Quantitative Phosphoproteomic Analysis

0 signed · 117 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/mas.20278openalex-snapshot
Linking the proteins—Elucidation of proteome‐scale networks using mass spectrometry
inferredcites →https://doi.org/10.1002/pmic.200402040openalex-snapshot
Comparative proteomic analysis of extracellular matrix proteins secreted by two types of skin fibroblasts
inferredcites →https://doi.org/10.1002/pmic.200900788openalex-snapshot
Integrating titania enrichment, iTRAQ labeling, and Orbitrap CID‐HCD for global identification and quantitative analysis of phosphopeptides
inferredcites →https://doi.org/10.1002/pmic.201090112openalex-snapshot
PROTEOMICS: Into the next decade
inferredcites →https://doi.org/10.1002/pmic.201100120openalex-snapshot
MassChroQ: A versatile tool for mass spectrometry quantification
inferredcites →https://doi.org/10.1002/pmic.201200555openalex-snapshot
Depletion of abundant plant R u B is CO protein using the protamine sulfate precipitation method
inferredcites →https://doi.org/10.1007/s00299-011-1064-4openalex-snapshot
Arabidopsis MAP kinase phosphatase 1 is phosphorylated and activated by its substrate AtMPK6
inferredcites →https://doi.org/10.1016/j.cellsig.2005.10.020openalex-snapshot
Phosphorylation of the Pro-X-Thr-Pro site in phosphatase inhibitor-2 by cyclin-dependent protein kinase during M-phase of the cell cycle
inferredcites →https://doi.org/10.1016/j.febslet.2007.05.066openalex-snapshot
Identification and characterization of RED120: A conserved PWI domain protein with links to splicing and 3′‐end formation
inferredcites →https://doi.org/10.1016/j.tplants.2013.05.004openalex-snapshot
Arabidopsis PPP family of serine/threonine protein phosphatases: many targets but few engines
inferredcites →https://doi.org/10.1021/ac061457fopenalex-snapshot
Supplemental Activation Method for High-Efficiency Electron-Transfer Dissociation of Doubly Protonated Peptide Precursors
inferredcites →https://doi.org/10.1021/ac302364ropenalex-snapshot
Automated and High Confidence Protein Phosphorylation Site Localization Using Complementary Collision-Activated Dissociation and Electron Transfer Dissociation Tandem Mass Spectrometry
inferredcites →https://doi.org/10.1021/ac9018582openalex-snapshot
Statistical Analysis of Peptide Electron Transfer Dissociation Fragmentation Mass Spectrometry
inferredcites →https://doi.org/10.1021/pr1003888openalex-snapshot
Quantitative Analysis of Protein Complex Constituents and Their Phosphorylation States on a LTQ-Orbitrap Instrument
inferredcites →https://doi.org/10.1021/pr300507jopenalex-snapshot
Automated Phosphopeptide Identification Using Multiple MS/MS Fragmentation Modes
inferredcites →https://doi.org/10.1021/pr8000173openalex-snapshot
Site-Specific Phosphorylation Profiling of Arabidopsis Proteins by Mass Spectrometry and Peptide Chip Analysis
inferredcites →https://doi.org/10.1021/pr800834eopenalex-snapshot
Electron Transfer Dissociation in Conjunction with Collision Activation To Investigate the Drosophila melanogaster Phosphoproteome
inferredcites →https://doi.org/10.1021/pr900451uopenalex-snapshot
High Precision Quantitative Proteomics Using iTRAQ on an LTQ Orbitrap: A New Mass Spectrometric Method Combining the Benefits of All
inferredcites →https://doi.org/10.1021/pr9004647openalex-snapshot
Proteome Analysis of Sorangium cellulosum Employing 2D-HPLC-MS/MS and Improved Database Searching Strategies for CID and ETD Fragment Spectra
inferredcites →https://doi.org/10.1038/415977aopenalex-snapshot
MAP kinase signalling cascade in Arabidopsis innate immunity
inferredcites →https://doi.org/10.1038/cr.2008.300openalex-snapshot
MEKK1, MKK1/MKK2 and MPK4 function together in a mitogen-activated protein kinase cascade to regulate innate immunity in plants
inferredcites →https://doi.org/10.1038/nature02485openalex-snapshot
Bacterial disease resistance in Arabidopsis through flagellin perception
inferredcites →https://doi.org/10.1038/nature05286openalex-snapshot
The plant immune system
inferredcites →https://doi.org/10.1038/nature08794openalex-snapshot
Differential innate immune signalling via Ca2+ sensor protein kinases
inferredcites →https://doi.org/10.1038/nature08854openalex-snapshot
NINJA connects the co-repressor TOPLESS to jasmonate signalling
inferredcites →https://doi.org/10.1038/nbt.2585openalex-snapshot
A large synthetic peptide and phosphopeptide reference library for mass spectrometry–based proteomics
inferredcites →https://doi.org/10.1038/nbt1240openalex-snapshot
A probability-based approach for high-throughput protein phosphorylation analysis and site localization
inferredcites →https://doi.org/10.1038/nmeth.1260openalex-snapshot
Decision tree–driven tandem mass spectrometry for shotgun proteomics
inferredcites →https://doi.org/10.1038/nrm1679openalex-snapshot
Plants, symbiosis and parasites: a calcium signalling connection
inferredcites →https://doi.org/10.1038/sj.emboj.7600737openalex-snapshot
The MAP kinase substrate MKS1 is a regulator of plant defense responses
inferredcites →https://doi.org/10.1046/j.1365-313x.1999.00451.xopenalex-snapshot
A single locus determines sensitivity to bacterial flagellin in Arabidopsis thaliana
inferredcites →https://doi.org/10.1073/pnas.0611217104openalex-snapshot
Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry
inferredcites →https://doi.org/10.1073/pnas.0811964106openalex-snapshot
Human embryonic stem cell phosphoproteome revealed by electron transfer dissociation tandem mass spectrometry
inferredcites →https://doi.org/10.1073/pnas.1104734108openalex-snapshot
Comparative phosphoproteome profiling reveals a function of the STN8 kinase in fine-tuning of cyclic electron flow (CEF)
inferredcites →https://doi.org/10.1073/pnas.1214287110openalex-snapshot
Arabidopsis Pumilio protein APUM5 suppresses Cucumber mosaic virus infection via direct binding of viral RNAs
inferredcites →https://doi.org/10.1074/jbc.m112.434654openalex-snapshot
Phosphorylation and Stabilization of Arabidopsis MAP Kinase Phosphatase 1 in Response to UV-B Stress
inferredcites →https://doi.org/10.1074/mcp.m110.003830openalex-snapshot
Confident Phosphorylation Site Localization Using the Mascot Delta Score
inferredcites →https://doi.org/10.1074/mcp.m111.015867openalex-snapshot
Phosphoproteome Dynamics Upon Changes in Plant Water Status Reveal Early Events Associated With Rapid Growth Adjustment in Maize Leaves
inferredcites →https://doi.org/10.1074/mcp.m112.020560openalex-snapshot
Identification of Novel in vivo MAP Kinase Substrates in Arabidopsis thaliana Through Use of Tandem Metal Oxide Affinity Chromatography
inferredcites →https://doi.org/10.1074/mcp.m600429-mcp200openalex-snapshot
Quantitative Phosphoproteomics of Early Elicitor Signaling in Arabidopsis
inferredcites →https://doi.org/10.1074/mcp.m700073-mcp200openalex-snapshot
Performance Characteristics of Electron Transfer Dissociation Mass Spectrometry
inferredcites →https://doi.org/10.1074/mcp.m700282-mcp200openalex-snapshot
Quantitative Proteomic Analysis of Protein Complexes
inferredcites →https://doi.org/10.1094/mpmi-11-11-0281openalex-snapshot
Activation of the Arabidopsis thaliana Mitogen-Activated Protein Kinase MPK11 by the Flagellin-Derived Elicitor Peptide, flg22
inferredcites →https://doi.org/10.1104/pp.109.138677openalex-snapshot
Large-Scale Arabidopsis Phosphoproteome Profiling Reveals Novel Chloroplast Kinase Substrates and Phosphorylation Networks
inferredcites →https://doi.org/10.1104/pp.109.149625openalex-snapshot
Large-Scale Phosphoprotein Analysis inMedicago truncatulaRoots Provides Insight into in Vivo Kinase Activity in Legumes
inferredcites →https://doi.org/10.1104/pp.111.192385openalex-snapshot
Arabidopsis VILLIN2 and VILLIN3 Are Required for the Generation of Thick Actin Filament Bundles and for Directional Organ Growth
inferredcites →https://doi.org/10.1104/pp.112.196816openalex-snapshot
Structural and Functional Analysis of VQ Motif-Containing Proteins in Arabidopsis as Interacting Proteins of WRKY Transcription Factors
inferredcites →https://doi.org/10.1105/tpc.107.056796openalex-snapshot
The Plant TPX2 Protein Regulates Prospindle Assembly before Nuclear Envelope Breakdown
inferredcites →https://doi.org/10.1105/tpc.108.058891openalex-snapshot
Arabidopsis DDB1-CUL4 ASSOCIATED FACTOR1 Forms a Nuclear E3 Ubiquitin Ligase with DDB1 and CUL4 That Is Involved in Multiple Plant Developmental Processes
inferredcites →https://doi.org/10.1105/tpc.112.101253openalex-snapshot
Constitutively Active Mitogen-Activated Protein Kinase Versions Reveal Functions of Arabidopsis MPK4 in Pathogen Defense Signaling
inferredcites →https://doi.org/10.1111/j.1365-313x.2007.03192.xopenalex-snapshot
Quantitative phosphoproteomic analysis of plasma membrane proteins reveals regulatory mechanisms of plant innate immune responses
inferredcites →https://doi.org/10.1111/j.1365-313x.2008.03556.xopenalex-snapshot
A novel nucleocytoplasmic traffic GTPase identified as a functional target of the bipartite geminivirus nuclear shuttle protein
inferredcites →https://doi.org/10.1111/j.1365-313x.2011.04671.xopenalex-snapshot
Interplay between calcium signalling and early signalling elements during defence responses to microbe‐ or damage‐associated molecular patterns
inferredcites →https://doi.org/10.1111/j.1365-313x.2012.05044.xopenalex-snapshot
Arabidopsis VILLIN2 and VILLIN3 act redundantly in sclerenchyma development via bundling of actin filaments
inferredcites →https://doi.org/10.1126/science.1123841openalex-snapshot
TOPLESS Regulates Apical Embryonic Fate in Arabidopsis
inferredcites →https://doi.org/10.1126/science.1151461openalex-snapshot
TOPLESS Mediates Auxin-Dependent Transcriptional Repression During Arabidopsis Embryogenesis
inferredcites →https://doi.org/10.1146/annurev.arplant.53.100301.135233openalex-snapshot
R UBISCO : Structure, Regulatory Interactions, and Possibilities for a Better Enzyme
inferredcites →https://doi.org/10.1210/edrv.22.2.0428openalex-snapshot
Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions*
inferredcites →https://doi.org/10.1255/ejms.555openalex-snapshot
Letter: The Diagnostic Value of Amino Acid Side-Chain Losses in Electron Capture Dissociation of Polypeptides. Comment on: “Can the (M . −X) Region in Electron Capture Dissociation Provide Reliable Information on Amino Acid Composition of Polypeptides?”, Eur. J. Mass Spectrom. 8, 461–469 (2002)
inferredcites →https://doi.org/10.1371/journal.ppat.1002911openalex-snapshot
The Cyclase-Associated Protein Cap1 Is Important for Proper Regulation of Infection-Related Morphogenesis in Magnaporthe oryzae
inferredcites →https://doi.org/10.1385/1-59745-227-0:1openalex-snapshot
Total Protein Extraction with TCA-Acetone
inferredcites →https://doi.org/10.4161/psb.23975openalex-snapshot
Role ofArabidopsisPumilio RNA binding protein 5 in virus infection
inferredcites →https://doi.org/10.4161/psb.6.5.15146openalex-snapshot
Arabidopsis thaliana MAP65-1 and MAP65-2 function redundantly with MAP65-3/PLEIADE in cytokinesis downstream of MPK4

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4837604openalex-extracted
Dynamic Changes and Transcriptome Analyses Reveal the Microfilament Skeleton Response to Water Stress in Thalli of Neopyropia Yezoensis Inhabiting the Intertidal Zone
inferred← citeshttps://doi.org/10.1002/9781119541578.ch16openalex-snapshot
A Network View of MAP Kinase Pathways in Plant Defense Regulation
inferred← citeshttps://doi.org/10.1002/elps.201400154openalex-snapshot
Phosphoproteomics in photosynthetic organisms
inferred← citeshttps://doi.org/10.1002/fes3.70276openalex-snapshot
Pathogen‐Induced Shifts in Alternative Splicing Shaping Plant Defense
inferred← citeshttps://doi.org/10.1016/j.aca.2016.11.001openalex-snapshot
Toward a suitable structural analysis of gene delivery carrier based on polycationic carbohydrates by electron transfer dissociation tandem mass spectrometry
inferred← citeshttps://doi.org/10.1016/j.jplph.2016.03.007openalex-snapshot
Phosphoproteomic analysis of induced resistance reveals activation of signal transduction processes by beneficial and pathogenic interaction in grapevine
inferred← citeshttps://doi.org/10.1016/j.mcpro.2023.100705openalex-snapshot
Phosphorylation Dynamics in a flg22-Induced, G Protein–Dependent Network Reveals the AtRGS1 Phosphatase
inferred← citeshttps://doi.org/10.1016/j.meegid.2015.04.015openalex-snapshot
Cross-talk in host–parasite associations: What do past and recent proteomics approaches tell us?
inferred← citeshttps://doi.org/10.1016/j.molp.2014.12.022openalex-snapshot
Signaling Mechanisms in Pattern-Triggered Immunity (PTI)
inferred← citeshttps://doi.org/10.1016/j.plantsci.2021.111121openalex-snapshot
In vivo identification of putative CPK5 substrates in Arabidopsis thaliana
inferred← citeshttps://doi.org/10.1016/j.plantsci.2025.112514openalex-snapshot
Decoding the signaling triad: Molecular interactions of G-proteins, MAP kinases, and helicases in environmental stress responses
inferred← citeshttps://doi.org/10.1016/j.plaphy.2023.108003openalex-snapshot
Role of myristoylation in modulating PCaP1 interaction with calmodulin
inferred← citeshttps://doi.org/10.1016/j.stress.2025.100762openalex-snapshot
Dynamic changes and transcriptome analyses reveal the microfilament skeleton response to water stress in thalli of Neopyropia yezoensis inhabiting the intertidal zone
inferred← citeshttps://doi.org/10.1016/j.tplants.2022.02.007openalex-snapshot
Guiding the guards: MPK3/6–VLN3 module regulating stomatal defense
inferred← citeshttps://doi.org/10.1016/j.tplants.2024.11.010openalex-snapshot
Pathogen-responsive alternative splicing in plant immunity
inferred← citeshttps://doi.org/10.1016/j.tplants.2025.07.013openalex-snapshot
Phosphorylation-regulated SEC14-GOLD PATELLIN lipid transfer proteins
inferred← citeshttps://doi.org/10.1021/acs.analchem.5b04123openalex-snapshot
Phosphoproteomics in the Age of Rapid and Deep Proteome Profiling
inferred← citeshttps://doi.org/10.1021/acs.analchem.7b04810openalex-snapshot
The Role of Electron Transfer Dissociation in Modern Proteomics
inferred← citeshttps://doi.org/10.1038/s41467-021-26827-2openalex-snapshot
MPK3- and MPK6-mediated VLN3 phosphorylation regulates actin dynamics during stomatal immunity in Arabidopsis
inferred← citeshttps://doi.org/10.1073/pnas.2024272118openalex-snapshot
Phosphorylation-dependent subfunctionalization of the calcium-dependent protein kinase CPK28
inferred← citeshttps://doi.org/10.1074/mcp.ra117.000135openalex-snapshot
Quantitative Phosphoproteomic Analysis Reveals Shared and Specific Targets of Arabidopsis Mitogen-Activated Protein Kinases (MAPKs) MPK3, MPK4, and MPK6
inferred← citeshttps://doi.org/10.1080/15476286.2020.1774987openalex-snapshot
Utilization of microRNAs and their regulatory functions for improving biotic stress tolerance in tea plant [Camellia sinensis (L.) O. Kuntze]
inferred← citeshttps://doi.org/10.1080/15592324.2019.1642037openalex-snapshot
Phosphorylation regulates the activity of INDETERMINATE-DOMAIN (IDD/BIRD) proteins in response to diverse environmental conditions
inferred← citeshttps://doi.org/10.1089/omi.2021.0192openalex-snapshot
Plant Phosphoproteomics: Known Knowns, Known Unknowns, and Unknown Unknowns of an Emerging Systems Science Frontier
inferred← citeshttps://doi.org/10.1093/aobpla/plad053openalex-snapshot
Integrating multiple regulations on enzyme activity: the case of phosphoenolpyruvate carboxykinases
inferred← citeshttps://doi.org/10.1093/jxb/eraf509openalex-snapshot
Novel effector proteins of the plant heteromeric acetyl-CoA carboxylase
inferred← citeshttps://doi.org/10.1093/nar/gkad827openalex-snapshot
Dynamics of ribosome composition and ribosomal protein phosphorylation in immune signaling in Arabidopsis thaliana
inferred← citeshttps://doi.org/10.1093/pcp/pcz086openalex-snapshot
Alternative Splicing in the Regulation of Plant–Microbe Interactions
inferred← citeshttps://doi.org/10.1094/mpmi-09-18-0267-fiopenalex-snapshot
Regulation of Plant Immune Signaling by Calcium-Dependent Protein Kinases
inferred← citeshttps://doi.org/10.1101/2021.12.06.471472openalex-snapshot
Phosphorylation dynamics in a flg22-induced, heterotrimeric G-protein dependent signaling network in Arabidopsis thaliana reveals a candidate PP2A phosphatase involved in AtRGS1 trafficking
inferred← citeshttps://doi.org/10.1101/2021.12.07.471565openalex-snapshot
Phosphorylation dynamics in a flg22-induced, heterotrimeric G-protein dependent signaling network in Arabidopsis thaliana reveals a candidate PP2A phosphatase involved in AtRGS1 trafficking
inferred← citeshttps://doi.org/10.1104/pp.20.00795openalex-snapshot
Phosphorylation of the CAMTA3 Transcription Factor Triggers Its Destabilization and Nuclear Export
inferred← citeshttps://doi.org/10.1111/nph.15523openalex-snapshot
Quantitative phosphoproteomic analysis reveals common regulatory mechanisms between effector‐ and PAMP‐triggered immunity in plants
inferred← citeshttps://doi.org/10.1111/nph.18989openalex-snapshot
Essential role of the CD docking motif of MPK4 in plant immunity, growth, and development
inferred← citeshttps://doi.org/10.1111/pce.14118openalex-snapshot
The plasma membrane–associated Ca 2+ ‐binding protein, PCaP1, is required for oligogalacturonide and flagellin‐induced priming and immunity
inferred← citeshttps://doi.org/10.1111/ppl.12619openalex-snapshot
Trans‐methylation reactions in plants: focus on the activated methyl cycle
inferred← citeshttps://doi.org/10.1111/ppl.70128openalex-snapshot
Role of aconitase in plant stress response and signaling
inferred← citeshttps://doi.org/10.1111/tpj.15395openalex-snapshot
Arabidopsis thaliana 2,3‐bisphosphoglycerate‐independent phosphoglycerate mutase 2 activity requires serine 82 phosphorylation
inferred← citeshttps://doi.org/10.1126/sciadv.aee6303openalex-snapshot
A rice calmodulin-like protein OsCML27 participates in drought tolerance by fine-tuning OsRbohB-mediated ROS signaling
inferred← citeshttps://doi.org/10.1186/gb-2014-15-6-r87openalex-snapshot
Functional analysis of Arabidopsisimmune-related MAPKs uncovers a role for MPK3 as negative regulator of inducible defences
inferred← citeshttps://doi.org/10.1371/journal.ppat.1008401openalex-snapshot
Role of MPK4 in pathogen-associated molecular pattern-triggered alternative splicing in Arabidopsis
inferred← citeshttps://doi.org/10.15252/embr.201947965openalex-snapshot
MAP4K4 associates with BIK1 to regulate plant innate immunity
inferred← citeshttps://doi.org/10.18632/oncotarget.17280openalex-snapshot
Hepatitis C virus core protein targets 4E-BP1 expression and phosphorylation and potentiates Myc-induced liver carcinogenesis in transgenic mice
inferred← citeshttps://doi.org/10.2139/ssrn.4253568openalex-snapshot
The Plasma Membrane-Associated Cation-Binding Protein Pcap1 of Arabidopsis Thaliana is a Uranyl-Binding Protein
inferred← citeshttps://doi.org/10.31083/fbl40847openalex-snapshot
Revealing the Molecular Network of Pattern-Triggered Immunity (PTI) Signal Transduction
inferred← citeshttps://doi.org/10.3389/fimmu.2026.1820993openalex-snapshot
Metabolic and post-translational modifications in sepsis-associated immune dysfunction: a conceptual framework
inferred← citeshttps://doi.org/10.3389/fpls.2016.00812openalex-snapshot
Protein Phosphatase 2A in the Regulatory Network Underlying Biotic Stress Resistance in Plants
inferred← citeshttps://doi.org/10.3389/fpls.2016.01107openalex-snapshot
Comprehensive Analysis of the Membrane Phosphoproteome Regulated by Oligogalacturonides in Arabidopsis thaliana
inferred← citeshttps://doi.org/10.3389/fpls.2020.618835openalex-snapshot
Signaling Toward Reactive Oxygen Species-Scavenging Enzymes in Plants
inferred← citeshttps://doi.org/10.3389/fpls.2021.666229openalex-snapshot
TALEN-Based HvMPK3 Knock-Out Attenuates Proteome and Root Hair Phenotypic Responses to flg22 in Barley
inferred← citeshttps://doi.org/10.3389/fpls.2021.768693openalex-snapshot
Integrative Proteomic and Phosphoproteomic Analyses of Pattern- and Effector-Triggered Immunity in Tomato
inferred← citeshttps://doi.org/10.3390/ijms22147440openalex-snapshot
HopA1 Effector from Pseudomonas syringae pv syringae Strain 61 Affects NMD Processes and Elicits Effector-Triggered Immunity
inferred← citeshttps://doi.org/10.70675/80f3b6dazbf8cz4713zabb9z69270ea8f24aopenalex-snapshot
Modélisation mathématique du réseau transcriptionnel contrôlé par MYB30 et MYB96, deux facteurs de transcription impliqués dans la réponse de la plante modèle arabidopsis thaliana
inferred← citeshttps://doi.org/10.70675/c2844cd4z4c3az4a6azb70czbaf852dc8504openalex-snapshot
Role of the NSR-ASCO ribonucleoprotein complex in the regulation of plant development
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.