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Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues

https://doi.org/10.1038/ncomms1871
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What this work says

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

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Cell Signaling by Receptor Tyrosine Kinases
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A Tissue-Specific Atlas of Mouse Protein Phosphorylation and Expression
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Kinase-Selective Enrichment Enables Quantitative Phosphoproteomics of the Kinome across the Cell Cycle
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Mislocalized Activation of Oncogenic RTKs Switches Downstream Signaling Outcomes
inferredcites →https://doi.org/10.1016/j.molcel.2011.10.015openalex-snapshot
Tyrosine Phosphorylation of Mitochondrial Pyruvate Dehydrogenase Kinase 1 Is Important for Cancer Metabolism
inferredcites →https://doi.org/10.1016/s0955-0674(96)80067-6openalex-snapshot
Regulation of transcription by MAP kinase cascades
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Selective Isolation at the Femtomole Level of Phosphopeptides from Proteolytic Digests Using 2D-NanoLC-ESI-MS/MS and Titanium Oxide Precolumns
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Performance Evaluation of a Hybrid Linear Ion Trap/Orbitrap Mass Spectrometer
inferredcites →https://doi.org/10.1021/ac981409yopenalex-snapshot
Immobilized Gallium(III) Affinity Chromatography of Phosphopeptides
inferredcites →https://doi.org/10.1021/pr1002214openalex-snapshot
Brain Phosphoproteome Obtained by a FASP-Based Method Reveals Plasma Membrane Protein Topology
inferredcites →https://doi.org/10.1021/pr100637qopenalex-snapshot
Feasibility of Large-Scale Phosphoproteomics with Higher Energy Collisional Dissociation Fragmentation
inferredcites →https://doi.org/10.1021/pr101065jopenalex-snapshot
Andromeda: A Peptide Search Engine Integrated into the MaxQuant Environment
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inferredcites →https://doi.org/10.1074/mcp.m400129-mcp200openalex-snapshot
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inferredcites →https://doi.org/10.1074/mcp.m700458-mcp200openalex-snapshot
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inferredcites →https://doi.org/10.1074/mcp.m900375-mcp200openalex-snapshot
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inferredcites →https://doi.org/10.1074/mcp.t600060-mcp200openalex-snapshot
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inferredcites →https://doi.org/10.1080/00365516209075148openalex-snapshot
The Ether Soluble Porphyrins Found in the Urine of Normal Man and Rabbit
inferredcites →https://doi.org/10.1126/science.1062538openalex-snapshot
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inferredcites →https://doi.org/10.1126/science.1104345openalex-snapshot
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inferredcites →https://doi.org/10.1126/science.1140321openalex-snapshot
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inferredcites →https://doi.org/10.1126/scisignal.2000475openalex-snapshot
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inferredcites →https://doi.org/10.1126/scisignal.2001570openalex-snapshot
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inferredcites →https://doi.org/10.1126/scisignal.287re6openalex-snapshot
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inferredcites →https://doi.org/10.1128/mcb.06120-11openalex-snapshot
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inferredcites →https://doi.org/10.1146/annurev.pharmtox.011008.145606openalex-snapshot
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inferredcites →https://doi.org/10.1182/blood.v97.8.2434openalex-snapshot
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inferredcites →https://doi.org/10.1186/gb-2007-8-11-r253openalex-snapshot
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inferredcites →https://doi.org/10.1371/journal.pgen.1001090openalex-snapshot
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inferredcites →https://doi.org/10.1371/journal.pgen.1001273openalex-snapshot
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inferredcites →https://doi.org/10.2337/db06-0148openalex-snapshot
Temporal Dynamics of Tyrosine Phosphorylation in Insulin Signaling

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Quantitative phosphoproteomics reveals novel phosphorylation events in insulin signaling regulated by protein phosphatase 1 regulatory subunit 12A
inferred← citeshttps://doi.org/10.1016/j.jprot.2015.03.019openalex-snapshot
Feasibility of label-free phosphoproteomics and application to base-line signaling of colorectal cancer cell lines
inferred← citeshttps://doi.org/10.1016/j.jprot.2016.12.011openalex-snapshot
The MAP kinase MAPKLK1 is essential to Trypanosoma brucei proliferation and regulates proteins involved in mRNA metabolism
inferred← citeshttps://doi.org/10.1016/j.jprot.2019.103556openalex-snapshot
Human muscle pathology is associated with altered phosphoprotein profile of mitochondrial proteins in the skeletal muscle
inferred← citeshttps://doi.org/10.1016/j.jprot.2022.104768openalex-snapshot
Quantitative phosphoproteomic analysis of mice with liver fibrosis by DIA mass spectrometry analysis with PRM verification
inferred← citeshttps://doi.org/10.1016/j.jsb.2015.06.001openalex-snapshot
Tissue-specific sequence and structural environments of lysine acetylation sites
inferred← citeshttps://doi.org/10.1016/j.lwt.2016.06.025openalex-snapshot
Optimal computational comparison of mass spectrometric peptide profiles of alternative hydrolysates from the same starting material
inferred← citeshttps://doi.org/10.1016/j.lwt.2026.119567openalex-snapshot
Proteomics reveals the potential effects of protein phosphorylation on muscle softening of Esox lucius during cold storage
inferred← citeshttps://doi.org/10.1016/j.mito.2016.08.004openalex-snapshot
Mitochondrial phosphoproteomics of mammalian tissues
inferred← citeshttps://doi.org/10.1016/j.molcel.2017.05.030openalex-snapshot
mTORC2 Regulates Amino Acid Metabolism in Cancer by Phosphorylation of the Cystine-Glutamate Antiporter xCT
inferred← citeshttps://doi.org/10.1016/j.molcel.2018.09.023openalex-snapshot
Phosphorylation of Histone H4T80 Triggers DNA Damage Checkpoint Recovery
inferred← citeshttps://doi.org/10.1016/j.nbd.2014.01.019openalex-snapshot
GABAA receptor dephosphorylation followed by internalization is coupled to neuronal death in in vitro ischemia
inferred← citeshttps://doi.org/10.1016/j.pep.2018.10.002openalex-snapshot
Production of Phosphorylated Ric-8A proteins using protein kinase CK2
inferred← citeshttps://doi.org/10.1016/j.plaphy.2022.12.003openalex-snapshot
Phosphorylation of aldose-6-phosphate reductase from Prunus persica leaves
inferred← citeshttps://doi.org/10.1016/j.plipres.2015.04.001openalex-snapshot
Long-chain acyl-CoA esters in metabolism and signaling: Role of acyl-CoA binding proteins
inferred← citeshttps://doi.org/10.1016/j.redox.2024.103426openalex-snapshot
Regulation of mitochondrial oxidative phosphorylation through tight control of cytochrome c oxidase in health and disease – Implications for ischemia/reperfusion injury, inflammatory diseases, diabetes, and cancer
inferred← citeshttps://doi.org/10.1016/j.redox.2025.103584openalex-snapshot
A high-resolution N-glycoproteome landscape of aging mouse ovary
inferred← citeshttps://doi.org/10.1016/j.sbi.2019.01.003openalex-snapshot
Regulatory mechanisms in postsynaptic phosphorylation networks
inferred← citeshttps://doi.org/10.1016/j.semcdb.2017.05.027openalex-snapshot
Functional roles of p120ctn family of proteins in central neurons
inferred← citeshttps://doi.org/10.1016/j.talo.2025.100399openalex-snapshot
A novel strategy for biomarker discovery: Neutral loss-dependent acquisition of circulating extracellular vesicles for the detection of phosphopeptides
inferred← citeshttps://doi.org/10.1016/j.tcb.2022.04.004openalex-snapshot
Where protein structure and cell diversity meet
inferred← citeshttps://doi.org/10.1016/j.tem.2015.09.013openalex-snapshot
Protein Phosphorylation: A Major Switch Mechanism for Metabolic Regulation
inferred← citeshttps://doi.org/10.1016/j.ttbdis.2024.102379openalex-snapshot
A multi-omics approach for understanding blood digestion dynamics in Ixodes scapularis and identification of anti-tick vaccine targets
inferred← citeshttps://doi.org/10.1016/j.xpro.2021.101089openalex-snapshot
Unraveling virus-induced cellular signaling cascades by label-free quantitative phosphoproteomics
inferred← citeshttps://doi.org/10.1016/j.yjmcc.2013.12.032openalex-snapshot
Monoamine oxidases as sources of oxidants in the heart
inferred← citeshttps://doi.org/10.1016/j.yjmcc.2014.09.013openalex-snapshot
Cardiac troponin I tyrosine 26 phosphorylation decreases myofilament Ca2+ sensitivity and accelerates deactivation
inferred← citeshttps://doi.org/10.1016/j.ymeth.2013.04.008openalex-snapshot
Recent advances in quantitative neuroproteomics
inferred← citeshttps://doi.org/10.1016/j.ymeth.2024.08.004openalex-snapshot
PhosBERT: A self-supervised learning model for identifying phosphorylation sites in SARS-CoV-2-infected human cells
inferred← citeshttps://doi.org/10.1016/s1872-2040(13)60742-2openalex-snapshot
Data Acquisition Strategy for Mass Spectrometers Applied to Bottom-up-Based Protein Identification
inferred← citeshttps://doi.org/10.1021/ac403551fopenalex-snapshot
Fine Tuning of Proteomic Technologies to Improve Biological Findings: Advancements in 2011–2013
inferred← citeshttps://doi.org/10.1021/ac503934fopenalex-snapshot
Evaluating Multiplexed Quantitative Phosphopeptide Analysis on a Hybrid Quadrupole Mass Filter/Linear Ion Trap/Orbitrap Mass Spectrometer
inferred← citeshttps://doi.org/10.1021/acs.analchem.0c03415openalex-snapshot
Global Phosphoproteome Analysis Using High-Field Asymmetric Waveform Ion Mobility Spectrometry on a Hybrid Orbitrap Mass Spectrometer
inferred← citeshttps://doi.org/10.1021/acs.analchem.1c04070openalex-snapshot
Molecularly Imprinted and Cladded Nanoparticles Provide Better Phosphorylation Recognition
inferred← citeshttps://doi.org/10.1021/acs.analchem.4c06727openalex-snapshot
Top-Down Proteomic Analysis of Limited Samples Using Porous Layer Open Tubular Columns and High-Field Asymmetric Ion Mobility Spectrometry Coupled to Mass Spectrometry
inferred← citeshttps://doi.org/10.1021/acs.analchem.5b01216openalex-snapshot
Extended Coverage of Singly and Multiply Phosphorylated Peptides from a Single Titanium Dioxide Microcolumn
inferred← citeshttps://doi.org/10.1021/acs.analchem.5b03040openalex-snapshot
Triomics Analysis of Imatinib-Treated Myeloma Cells Connects Kinase Inhibition to RNA Processing and Decreased Lipid Biosynthesis
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.7b00212openalex-snapshot
Phosphoproteomics with Activated Ion Electron Transfer Dissociation
inferred← citeshttps://doi.org/10.1021/acs.analchem.7b02078openalex-snapshot
Sensitive, Robust, and Cost-Effective Approach for Tyrosine Phosphoproteome Analysis
inferred← citeshttps://doi.org/10.1021/acs.analchem.8b01843openalex-snapshot
High-Throughput Phosphorylation Screening and Validation through Ti(IV)-Nanopolymer Functionalized Reverse Phase Phosphoprotein Array
inferred← citeshttps://doi.org/10.1021/acs.analchem.8b03022openalex-snapshot
Selective Enrichment of Phosphopeptides and Phospholipids from Biological Matrixes on TiO2 Nanowire Arrays for Direct Molecular Characterization by Internal Extractive Electrospray Ionization Mass Spectrometry
inferred← citeshttps://doi.org/10.1021/acs.analchem.9b01930openalex-snapshot
A Fully Integrated Spintip-Based Approach for Sensitive and Quantitative Profiling of Region-Resolved in Vivo Brain Glycoproteome
inferred← citeshttps://doi.org/10.1021/acs.biochem.8b00007openalex-snapshot
Structural Regulation of a Neurofilament-Inspired Intrinsically Disordered Protein Brush by Multisite Phosphorylation
inferred← citeshttps://doi.org/10.1021/acs.chemrev.1c00937openalex-snapshot
In-Cell Structural Biology by NMR: The Benefits of the Atomic Scale
inferred← citeshttps://doi.org/10.1021/acs.jpcb.5c07407openalex-snapshot
Phosphorylation-Dependent Charge Transport in Biomolecular Junctions of Major Histocompatibility Complex Phosphopeptides
inferred← citeshttps://doi.org/10.1021/acs.jproteome.2c00164openalex-snapshot
Panoramic Perspective on Human Phosphosites
inferred← citeshttps://doi.org/10.1021/acs.jproteome.4c00978openalex-snapshot
Protein Sequencing with Single Amino Acid Resolution Discerns Peptides That Discriminate Tropomyosin Proteoforms
inferred← citeshttps://doi.org/10.1021/acs.jproteome.6b00753openalex-snapshot
Robust, Sensitive, and Automated Phosphopeptide Enrichment Optimized for Low Sample Amounts Applied to Primary Hippocampal Neurons
inferred← citeshttps://doi.org/10.1021/acs.jproteome.6b01016openalex-snapshot
Phosphoproteomic Analysis of Paper Mulberry Reveals Phosphorylation Functions in Chilling Tolerance
inferred← citeshttps://doi.org/10.1021/acs.jproteome.6c00570openalex-snapshot
onsite: An Integrated Framework for Phosphosite Localization and False Localization Rate Estimation
inferred← citeshttps://doi.org/10.1021/acs.jproteome.7b00364openalex-snapshot
Combining Genomics To Identify the Pathways of Post-Transcriptional Nongenotoxic Signaling and Energy Homeostasis in Livers of Rats Treated with the Pregnane X Receptor Agonist, Pregnenolone Carbonitrile
inferred← citeshttps://doi.org/10.1021/acs.jproteome.7b00520openalex-snapshot
TiO2 with Tandem Fractionation (TAFT): An Approach for Rapid, Deep, Reproducible, and High-Throughput Phosphoproteome Analysis
inferred← citeshttps://doi.org/10.1021/acs.jproteome.7b00610openalex-snapshot
Sensitive and Accurate Quantitation of Phosphopeptides Using TMT Isobaric Labeling Technique
inferred← citeshttps://doi.org/10.1021/acsami.0c02572openalex-snapshot
Preorganization Increases the Self-Assembling Ability and Antitumor Efficacy of Peptide Nanomedicine
inferred← citeshttps://doi.org/10.1021/acschembio.7b00361openalex-snapshot
Site-Specific Phosphorylation of PSD-95 PDZ Domains Reveals Fine-Tuned Regulation of Protein–Protein Interactions
inferred← citeshttps://doi.org/10.1021/acschemneuro.5c00779openalex-snapshot
Phosphoproteomic Analysis of Cortical Tissue from Mice Lacking Both CaMKIIα and CaMKIIβ Identifies Novel In Vivo Substrates
inferred← citeshttps://doi.org/10.1021/acsnano.3c00674openalex-snapshot
Dual Tumor Exosome Biomarker Co-recognitions Based Nanoliquid Biopsy for the Accurate Early Diagnosis of Pancreatic Cancer
inferred← citeshttps://doi.org/10.1021/pr301061qopenalex-snapshot
Citric Acid-Assisted Two-Step Enrichment with TiO2 Enhances the Separation of Multi- and Monophosphorylated Peptides and Increases Phosphoprotein Profiling
inferred← citeshttps://doi.org/10.1021/pr400281ropenalex-snapshot
Tissue Specific Phosphorylation of Mitochondrial Proteins Isolated from Rat Liver, Heart Muscle, and Skeletal Muscle
inferred← citeshttps://doi.org/10.1021/pr400960ropenalex-snapshot
Phosphoproteome Analysis of Formalin-Fixed and Paraffin-Embedded Tissue Sections Mounted on Microscope Slides
inferred← citeshttps://doi.org/10.1021/pr500549hopenalex-snapshot
StUbEx: Stable Tagged Ubiquitin Exchange System for the Global Investigation of Cellular Ubiquitination
inferred← citeshttps://doi.org/10.1021/pr500985wopenalex-snapshot
Rapid and Deep Proteomes by Faster Sequencing on a Benchtop Quadrupole Ultra-High-Field Orbitrap Mass Spectrometer
inferred← citeshttps://doi.org/10.1021/pr501025eopenalex-snapshot
An Optimized Platform for Hydrophilic Interaction Chromatography–Immobilized Metal Affinity Chromatography Enables Deep Coverage of the Rat Liver Phosphoproteome
inferred← citeshttps://doi.org/10.1038/cr.2016.39openalex-snapshot
Ubiquitin modifications
inferred← citeshttps://doi.org/10.1038/nbt.3327openalex-snapshot
High-throughput phosphoproteomics reveals in vivo insulin signaling dynamics
inferred← citeshttps://doi.org/10.1038/ng.2610openalex-snapshot
Identification of heart rate–associated loci and their effects on cardiac conduction and rhythm disorders
inferred← citeshttps://doi.org/10.1038/nmeth.2997openalex-snapshot
Annotation of loci from genome-wide association studies using tissue-specific quantitative interaction proteomics
inferred← citeshttps://doi.org/10.1038/nmeth.3811openalex-snapshot
Plug-and-play analysis of the human phosphoproteome by targeted high-resolution mass spectrometry
inferred← citeshttps://doi.org/10.1038/nprot.2013.010openalex-snapshot
Robust phosphoproteome enrichment using monodisperse microsphere–based immobilized titanium (IV) ion affinity chromatography
inferred← citeshttps://doi.org/10.1038/nrg3356openalex-snapshot
Next-generation proteomics: towards an integrative view of proteome dynamics
inferred← citeshttps://doi.org/10.1038/nrn3729openalex-snapshot
Nuclear and cytosolic JNK signalling in neurons
inferred← citeshttps://doi.org/10.1038/nsmb.3366openalex-snapshot
Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation
inferred← citeshttps://doi.org/10.1038/onc.2014.206openalex-snapshot
In vivo quantitative phosphoproteomic profiling identifies novel regulators of castration-resistant prostate cancer growth
inferred← citeshttps://doi.org/10.1038/s41467-018-03309-6openalex-snapshot
Benchmarking common quantification strategies for large-scale phosphoproteomics
inferred← citeshttps://doi.org/10.1038/s41467-020-17647-xopenalex-snapshot
Functional 3D architecture in an intrinsically disordered E3 ligase domain facilitates ubiquitin transfer
inferred← citeshttps://doi.org/10.1038/s41467-022-30235-5openalex-snapshot
Cryo-EM structure of human glucose transporter GLUT4
inferred← citeshttps://doi.org/10.1038/s41467-023-38035-1openalex-snapshot
DeepFLR facilitates false localization rate control in phosphoproteomics
inferred← citeshttps://doi.org/10.1038/s41467-023-42227-0openalex-snapshot
O-GlcNAcylation regulates neurofilament-light assembly and function and is perturbed by Charcot-Marie-Tooth disease mutations
inferred← citeshttps://doi.org/10.1038/s41467-024-46392-8openalex-snapshot
Structural basis for the modulation of MRP2 activity by phosphorylation and drugs
inferred← citeshttps://doi.org/10.1038/s41589-019-0404-5openalex-snapshot
Global targeting of functional tyrosines using sulfur-triazole exchange chemistry
inferred← citeshttps://doi.org/10.1038/s41596-018-0014-9openalex-snapshot
High-throughput and high-sensitivity phosphoproteomics with the EasyPhos platform
inferred← citeshttps://doi.org/10.1038/s41598-017-13440-xopenalex-snapshot
MCM2-regulated functional networks in lung cancer by multi-dimensional proteomic approach
inferred← citeshttps://doi.org/10.1038/s41598-017-15739-1openalex-snapshot
Molecular architecture of potassium chloride co-transporter KCC2
inferred← citeshttps://doi.org/10.1038/s41598-017-18299-6openalex-snapshot
Sample handling of gastric tissue and O-glycan alterations in paired gastric cancer and non-tumorigenic tissues
inferred← citeshttps://doi.org/10.1038/s41598-018-25064-wopenalex-snapshot
Inferring a nonlinear biochemical network model from a heterogeneous single-cell time course data
inferred← citeshttps://doi.org/10.1038/s41598-021-81986-yopenalex-snapshot
Proteome-wide profiling and mapping of post translational modifications in human hearts
inferred← citeshttps://doi.org/10.1038/s41598-023-29116-8openalex-snapshot
Pien Tze Huang regulates phosphorylation of metabolic enzymes in mice of hepatocellular carcinoma
inferred← citeshttps://doi.org/10.1038/s42003-022-04021-4openalex-snapshot
Alteration in tyrosine phosphorylation of cardiac proteome and EGFR pathway contribute to hypertrophic cardiomyopathy
inferred← citeshttps://doi.org/10.1038/s42003-022-04400-xopenalex-snapshot
A streamlined tandem tip-based workflow for sensitive nanoscale phosphoproteomics
inferred← citeshttps://doi.org/10.1038/srep03460openalex-snapshot
Global Screening of CK2 Kinase Substrates by an Integrated Phosphoproteomics Workflow
inferred← citeshttps://doi.org/10.1038/srep13099openalex-snapshot
Label-free quantitative phosphoproteomics with novel pairwise abundance normalization reveals synergistic RAS and CIP2A signaling
inferred← citeshttps://doi.org/10.1038/srep23534openalex-snapshot
dbPAF: an integrative database of protein phosphorylation in animals and fungi
inferred← citeshttps://doi.org/10.1038/srep25801openalex-snapshot
A homology-based pipeline for global prediction of post-translational modification sites
inferred← citeshttps://doi.org/10.1039/c3ra41332bopenalex-snapshot
Pore size-optimized periodic mesoporous organosilicas for the enrichment of peptides and polymers
inferred← citeshttps://doi.org/10.1039/c5sc00560dopenalex-snapshot
Integrating proteomics with electrochemistry for identifying kinase biomarkers
inferred← citeshttps://doi.org/10.1039/c7an00985bopenalex-snapshot
Recent advances in phosphoproteomics and application to neurological diseases
inferred← citeshttps://doi.org/10.1039/c8cc01082jopenalex-snapshot
Narrowing the diversification of supramolecular assemblies by preorganization
inferred← citeshttps://doi.org/10.1039/d0cb00180eopenalex-snapshot
Development and biological applications of sulfur–triazole exchange (SuTEx) chemistry
inferred← citeshttps://doi.org/10.1042/bcj20160819openalex-snapshot
G protein subunit phosphorylation as a regulatory mechanism in heterotrimeric G protein signaling in mammals, yeast, and plants
inferred← citeshttps://doi.org/10.1042/bcj20220510openalex-snapshot
Identification of ester-linked ubiquitylation sites during TLR7 signalling increases the number of inter-ubiquitin linkages from 8 to 12
inferred← citeshttps://doi.org/10.1042/bj20150238openalex-snapshot
The NHERF2 sequence adjacent and upstream of the ERM-binding domain affects NHERF2–ezrin binding and dexamethasone stimulated NHE3 activity
inferred← citeshttps://doi.org/10.1042/bsr20180721openalex-snapshot
Obesity-mediated regulation of cardiac protein acetylation: parallel analysis of total and acetylated proteins via TMT-tagged mass spectrometry
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