Bockorny B. et.al. (2023). A Large-Scale Proteomics Resource of Circulating Extracellular Vesicles for Biomarker Discovery in Pancreatic Cancer. eLife. https://doi.org/10.7554/eLife.87369.1

Clemens Z. et.al. (2023). Arsenic disrupts extracellular vesicle-mediated signaling in regenerating myofibers. Toxicological Sciences. https://doi.org/10.1093/toxsci/kfad075

Songbai Z. et.al. (2023). A viral protein activates MAPKs pathway to promote viral infection by downregulating callose deposition in plants. Research Square. https://www.researchsquare.com/article/rs-3247000/v1

Casu A. et.al. (2023). The proteome and phosphoproteome of circulating extracellular vesicle-enriched preparations are associated with characteristic clinical features in type 1 diabetes. Front Endocrinol. https://doi.org/10.3389/fendo.2023.1219293

Deng Y. et.al. (2023). Phosphoproteome analysis of cerebrospinal fluid extracellular vesicles in primary central nervous system lymphoma. Analyst. https://pubmed.ncbi.nlm.nih.gov/37403840/

Cheng X. et.al. (2023). Breast cancer mutations HER2 V777L and PIK3CA H1047R activate the p21-CDK4/6 -Cyclin D1 axis driving tumorigenesis and drug resistance. Cancer Res. https://pubmed.ncbi.nlm.nih.gov/37272756/

Reyes A. et.al. (2023). Proteomic Profiling of Extracellular Vesicles Isolated from Plasma and Peritoneal Exudate in Mice Induced by Crotalus scutulatus scutulatus Crude Venom and Its Purified Cysteine-Rich Secretory Protein (Css-CRiSP). Toxins. https://www.mdpi.com/2072-6651/15/7/434

Hadisurya M. et.al. (2023). Quantitative proteomics and phosphoproteomics of urinary extracellular vesicles define putative diagnostic biosignatures for Parkinson’s disease. Nature Communications Medicine. https://www.nature.com/articles/s43856-023-00294-w

Hadisurya M. et.al. (2023). Data-independent acquisition phosphoproteomics of urinary extracellular vesicles enables renal cell carcinoma grade differentiation. Mol Cell Proteomics. https://www.mcponline.org/article/S1535-9476(23)00046-4/fulltext

Eitan E. et.al. (2023). Synaptic proteins in neuron-derived extracellular vesicles as biomarkers for Alzheimer’s disease: novel methodology and clinical proof of concept. Extracellular Vesicles and Circulating Nucleic Acids. http://dx.doi.org/10.20517/evcna.2023.13

Lihon M. et.al. (2023). Isolation and Identification of Plasma Extracellular Vesicles Protein Biomarkers. Methods in Mol Biology. https://link.springer.com/protocol/10.1007/978-1-0716-3163-8_14

Garcia Coronado P. et.al. (2023). Putative Wound Healing Induction Functions of Exosomes Isolated from IMMUNEPOTENT. Int J Mol Sciences. https://doi.org/10.3390/ijms24108971

Hein J. et.al. (2023). Global substrate identification and high throughput in vitro dephosphorylation reactions uncover PP1 and PP2A-B55 specificity principles. bioRxiv. https://www.biorxiv.org/content/10.1101/2023.05.14.540683v1.abstract

McDonald N. et.al. (2023). SAD-1 kinase controls presynaptic phase separation by relieving SYD-2/Liprin-α autoinhibition. bioRxiv. https://doi.org/10.1101/2023.06.12.544643

Bockorny B. et.al. (2023). A Large-Scale Proteomics Resource of Circulating Extracellular Vesicles for Biomarker Discovery in Pancreatic Cancer. medRxiv. https://pubmed.ncbi.nlm.nih.gov/36993200/

Nunez Lopez Y. et.al. (2023). Extracellular vesicle proteomics and phosphoproteomics identify pathways for increased risk in patients hospitalized with COVID-19 and type 2 diabetes mellitus. Diabetes Research and Clinical Practice. https://doi.org/10.1016/j.diabres.2023.110565

Wu X. et.al. (2023). Chapter Three – Translational proteomics and phosphoproteomics: Tissue to extracellular vesicles. Advances in Clinical Chemistry. https://doi.org/10.1016/bs.acc.2022.09.003

Onyedibe K. et.al. (2023). Proteomic and phosphoproteomic analyses of Jurkat T-cell treated with 2′3′ cGAMP reveals various signaling axes impacted by cyclic dinucleotides. Journal of Proteomics. https://doi.org/10.1016/j.jprot.2023.104869

Jankowska M. et.al. (2023). Sublethal biochemical, behavioral, and physiological toxicity of extremely low dose of bendiocarb insecticide in Periplaneta americana. Environ Sci Pollut Res Int. https://pubmed.ncbi.nlm.nih.gov/36745351/

Li D. et.al. (2023). Glycoproteomic Analysis of Urinary Extracellular Vesicles for Biomarkers of Hepatocellular Carcinoma. Molecules. https://doi.org/10.3390/molecules28031293

Bao Y. et.al. (2023). A pair of G-type lectin receptor-like kinases modulate nlp20-mediated immune responses by coupling to RLP23 receptor complex. Journal of Integrative Plant Biology. https://doi.org/10.1111/jipb.13449

Maloney M. et.al. (2022). LRRK2 Kinase Activity Regulates Parkinson’s Disease-Relevant Lipids at the Lysosome. BioRxiv. https://www.biorxiv.org/content/10.1101/2022.12.19.521070v1.full

Signorelli R. et.al. (2022). ALCAM: A Novel Surface Marker on EpCAMlow Circulating Tumor Cells. Biomedicines. https://www.mdpi.com/2227-9059/10/8/1983

Zeid F. et.al. (2022). Characterization of cardiac extracellular vesicles in heart failure. Archives of Cardiovascular Diseases. https://www.sciencedirect.com/science/article/pii/S1878648022000647

Jacob H.K. et.al. (2022). Identification of novel early pancreatic cancer biomarkers KIF5B and SFRP2 from “first contact” interactions in the tumor microenvironment. J Exp Clin Cancer Res. https://jeccr.biomedcentral.com/articles/10.1186/s13046-022-02425-y

Zhu P. et.al. (2022). An Integrated Proteomic Strategy to Identify SHP2 Substrates. J Proteome Res. https://pubs.acs.org/doi/abs/10.1021/acs.jproteome.2c00481

Zhao Y. et.al. (2022). Temporal Proteomic and Phosphoproteomic Analysis of EV-A71-Infected Human Cells. J Proteome Res. https://pubs.acs.org/doi/abs/10.1021/acs.jproteome.2c00237

Vujic T. et.al. (2022). Oxidative Stress and Extracellular Matrix Remodeling Are Signature Pathways of Extracellular Vesicles Released upon Morphine Exposure on Human Brain Microvascular Endothelial Cells. Cells. https://doi.org/10.3390/cells11233926

Zhang T. et.al. (2022). CDK7/GRP78 signaling axis contributes to tumor growth and metastasis in osteosarcoma. Oncogene. https://pubmed.ncbi.nlm.nih.gov/36042349/

Kim S. et.al. (2022). Multi-Omics Approach Reveals Dysregulation of Protein Phosphorylation Correlated with Lipid Metabolism in Mouse Non-Alcoholic Fatty Liver. Cells. https://doi.org/10.3390/cells11071172

Kao D. et.al. (2022). Identification of Novel Kinases of Tau Using Fluorescence Complementation Mass Spectrometry (FCMS). Mol Cell Proteomics. https://doi.org/10.1016/j.mcpro.2022.100441

Hadisurya M. et.al. (2022). Data-independent acquisition phosphoproteomics of urinary extracellular vesicles enables renal cell carcinoma grade differentiation. medRxiv. https://www.medrxiv.org/content/10.1101/2022.08.15.22278799v1

Chong L. et.al. (2022). Updating mass spectrometry-based phosphoproteomics for elucidating abscisic acid signaling and plant response to abiotic stress. J Exp Bot. https://pubmed.ncbi.nlm.nih.gov/35959917/

Zhang H. et.al. (2022). Proteomics, Phosphoproteomics and Mirna Analysis of Circulating Extracellular Vesicles through Automated and High-Throughput Isolation. Cells. https://pubmed.ncbi.nlm.nih.gov/35805153/

Hinzman C. et.al. (2022). A multi-omics approach identifies pancreatic cancer cell extracellular vesicles as mediators of the unfolded protein response in normal pancreatic epithelial cells. J Extracell Vesicles. https://pubmed.ncbi.nlm.nih.gov/35656858/

Nunez Lopez YO. et.al. (2022). Proteomics and Phosphoproteomics of Circulating Extracellular Vesicles Provide New Insights into Diabetes Pathobiology. Int J Mol Sci. https://pubmed.ncbi.nlm.nih.gov/35628588/

Tathe P. et.al. (2022). SHP-1 dephosphorylates histone H2B to facilitate its ubiquitination during transcription. EMBO J. https://www.embopress.org/doi/abs/10.15252/embj.2021109720

Hinzman C. et.al. (2022). An optimized method for the isolation of urinary extracellular vesicles for molecular phenotyping: detection of biomarkers for radiation exposure. J Transl Med. https://pubmed.ncbi.nlm.nih.gov/35538547/

Shuen, T. et.al. (2022). Extracellular vesicles may predict response to radioembolization and sorafenib treatment in advanced hepatocellular carcinoma. Clin Cancer Res. https://pubmed.ncbi.nlm.nih.gov/35763041/

Hernandez-Rojas, R. et.al. (2022). The interplay between estrogen receptor beta and protein kinase C, a crucial collaboration for medulloblastoma cell proliferation and invasion. Cell Signaling. https://pubmed.ncbi.nlm.nih.gov/35033667/

Zeid F. et.al. (2022). Lim Domain Binding 3 (Ldb3) Identified as a Potential Marker of Cardiac Extracellular Vesicles. Int J Mol Sci. https://doi.org/10.3390/ijms23137374

Zhang H. et.al. (2022). High Throughput Isolation and Data Independent Acquisition Mass Spectrometry (DIA-MS) of Urinary Extracellular Vesicles to Improve Prostate Cancer Diagnosis. Molecules. https://doi.org/10.3390/molecules27238155

Zhou M. et.al. (2022). Open Access Dose-dependent phosphorylation and activation of Hh pathway transcription factors. Life Science Alliance. https://www.life-science-alliance.org/content/5/11/e202201570.abstract

Casu, A. et.al. (2022). Correlates of circulating extracellular vesicle cargo with key clinical features of type 1 diabetes. MedRxiv. https://www.medrxiv.org/content/10.1101/2022.03.10.22272207v1

Gong C. et.al. (2022). PKR Protects the Major Catalytic Subunit of PKA Cpk1 from FgBlm10-Mediated Proteasome Degradation in Fusarium graminearum. Int. J. Mol. Sci. https://doi.org/10.3390/ijms231810208

Rui X. et.al. (2022). Extracellular phosphoprotein regulation is affected by culture system scale-down. Biochimica et Biophysica Acta. https://www.sciencedirect.com/science/article/abs/pii/S0304416522000836#f0030

Tombesi G. et.al. (2022). LRRK2 regulates dendritic spine dynamics through interaction with post-synaptic actin cytoskeleton. bioRxiv. https://www.biorxiv.org/content/10.1101/2022.10.31.514622v2.abstract

Kilburn R. et.al. (2022). Autophosphorylation Inhibits RcCDPK1, A Dual-Specificity Kinase that Phosphorylates Bacterial-Type Phosphoenolpyruvate Carboxylase in Castor Oil Seeds. Plant and Cell Physiology. https://doi.org/10.1093/pcp/pcac030

Jacob HK. et.al. (2022). Rapid and Multifaceted Characterization of the Effects of the Secreted EVome in Pancreatic Cancer: A Global Omics Approach for Screening Putative Biomarkers. Research Square. https://www.researchsquare.com/article/rs-1489466/v1

Kim S. et.al. (2022). Multi-omics approach reveals dysregulation of protein phosphorylation correlated with lipid metabolism in mouse fatty liver. bioRxiv. https://www.biorxiv.org/content/10.1101/2022.02.16.480672v1.full

Iliuk A. (2022). Purification and Phosphoproteomic Analysis of Plasma-Derived Extracellular Vesicles. Methods Mol Biol. https://pubmed.ncbi.nlm.nih.gov/35467285/

Hawkins L. et.al. (2022). Novel CRK-Cyclin Complex Controls Spindle Assembly Checkpoint in Toxoplasma Endodyogeny. mBio. https://pubmed.ncbi.nlm.nih.gov/35130726/

Hadisurya M. et.al. (2022). Quantitative proteomics and phosphoproteomics of urinary extracellular vesicles define diagnostic and prognostic biosignatures for Parkinson’s Disease. medRxiv. https://www.medrxiv.org/content/10.1101/2022.01.18.22269096v1

Li J. et.al. (2022). Highly efficient enrichment of intact phosphoproteins by a cadmium ion-based co-precipitation strategy. J Sep Sci. https://pubmed.ncbi.nlm.nih.gov/35108751/

Feldman H. et.al. (2021). ATP-competitive partial antagonists of the IRE1α RNase segregate outputs of the UPR. Nature Chem Biol. https://www.nature.com/articles/s41589-021-00852-0

Hinzman C. et.al. (2021). A multi-omics approach identifies pancreatic cancer cell extracellular vesicles as mediators of the unfolded protein response in normal pancreatic epithelial cells. bioRxiv. https://www.biorxiv.org/content/10.1101/2021.10.12.464079v1

Chen F. et.al. (2021). Transcriptomic, proteomic, and phosphoproteomic analyses reveal dynamic signaling networks influencing long-grain rice development. The Crop Journal. https://doi.org/10.1016/j.cj.2021.11.007

Nunez Lopez Y. et.al. (2021). Defining the Proteomic and Phosphoproteomic Landscape of Circulating Extracellular Vesicles in the Diabetes Spectrum. medRxiv. https://www.medrxiv.org/content/10.1101/2021.10.31.21265724v1.full.pdf

Gu H. et.al. (2021). A previously uncharacterized two-component signaling system in uropathogenic Escherichia coli coordinates protection against host-derived oxidative stress with activation of hemolysin-mediated host cell pyroptosis. PLOS Pathogens. https://pubmed.ncbi.nlm.nih.gov/34653218/

Willard N. et.al. (2021). Proteomic Identification and Quantification of Snake Venom Biomarkers in Venom and Plasma Extracellular Vesicles. Toxins. https://www.mdpi.com/2072-6651/13/9/654

Li W-J.. et.al. (2021). Insulin signaling regulates longevity through protein phosphorylation in Caenorhabditis elegans. Nature Commun. https://pubmed.ncbi.nlm.nih.gov/34315882/

Bredow M. et.al. (2021). Phosphorylation-dependent subfunctionalization of the calcium-dependent protein kinase CPK28. PNAS. https://pubmed.ncbi.nlm.nih.gov/33941701/

Han Y. et.al. (2021). Ci/Gli Phosphorylation by the Fused/Ulk Family Kinases. Methods Mol Biol. https://link.springer.com/protocol/10.1007/978-1-0716-1701-4_19

Hinzman C. et.al. (2021). A multi-omics approach identifies pancreatic cancer cell extracellular vesicles as mediators of the unfolded protein response in normal pancreatic epithelial cells. biRxiv. https://www.biorxiv.org/content/10.1101/2021.10.12.464079v1.abstract

Hsu CC. et.al. (2021). Universal Sample Preparation Workflow for Plant Phosphoproteomic Profiling. Methods Mol Biol. https://link.springer.com/protocol/10.1007/978-1-0716-1625-3_6

Jacob H. et.al. (2021). Modulation of Early Neutrophil Granulation: The Circulating Tumor Cell-Extravesicular Connection in Pancreatic Ductal Adenocarcinoma. Cancers (Basel). https://pubmed.ncbi.nlm.nih.gov/34072942/

Rossman P. et.al. (2021). Phase I/II Trial of Vemurafenib in Dogs with Naturally Occurring, BRAF-mutated Urothelial Carcinoma. Mol Cancer Ther. https://pubmed.ncbi.nlm.nih.gov/34433660/

Mohallem R. et.al. (2021). Quantitative Proteomics and Phosphoproteomics Reveal TNF-α-Mediated Protein Functions in Hepatocytes. Molecules. https://www.mdpi.com/1420-3049/26/18/5472

Zeid F. et.al. (2021). Characterization of cardiac extracellular vesicles upon thiamet G treatment in a rat model of acute decompensated heart failure. Archives of Cardiovascular Diseases. https://www.sciencedirect.com/science/article/pii/S1878648021001646

Vujic T. et.al. (2021). Ubiquinone Metabolism and Transcription HIF-1 Targets Pathway Are Toxicity Signature Pathways Present in Extracellular Vesicles of Paraquat-Exposed Human Brain Microvascular Endothelial Cells. Int J Mol Sci. https://pubmed.ncbi.nlm.nih.gov/34064677/

Yang M. et.al. (2021). MYLK4 promotes tumor progression through the activation of epidermal growth factor receptor signaling in osteosarcoma. J Exp Clin Cancer Res. https://pubmed.ncbi.nlm.nih.gov/33980265/

Gu H. et.al. (2021). A bacterial “shield and sword”: A previously uncharacterized two-component system protects uropathogenic Escherichia coli from host-derived oxidative insults and promotes hemolysin-mediated host cell pyroptosis. BioRxiv. https://www.biorxiv.org/content/10.1101/2021.04.19.440293v1.abstract

Bredow M. et.al. (2021). Differential regulation of the calcium-dependent protein kinase CPK28 by site-specific modification. Plant Physiology. https://academic.oup.com/plphys/advance-article/doi/10.1093/plphys/kiab216/6270795

Si J. et.al. (2021). Phytophthora sojae LRR-RLKs: Diverse and essential roles in Development and Pathogenicity. iScience. https://www.sciencedirect.com/science/article/pii/S2589004221006933

Wu C. et.al. (2021). The apple MdPTI1L kinase is phosphorylated by MdOXI1 during S-RNase-induced reactive oxygen species signaling in pollen tubes. Plant Science. https://pubmed.ncbi.nlm.nih.gov/33691959/

Zhou X. et.al. (2021). A Bacterial Toxin Perturbs Intracellular Amino Acid Balance To Induce Persistence. Am Soc for Microbiology. https://pubmed.ncbi.nlm.nih.gov/33622732/

Min K. et.al. (2021). Integrative multi-omics profiling reveals cAMP-independent mechanisms regulating hyphal morphogenesis in Candida albicans. bioRxiv. https://www.biorxiv.org/content/biorxiv/early/2021/03/08/2021.03.08.433668.full.pdf

Zembroski A. et.al. (2021). Proteome and phosphoproteome characterization of liver in the postprandial state from diet-induced obese and lean mice. J Proteomics. https://www.sciencedirect.com/science/article/abs/pii/S1874391920304401

Zhang Y. et.al. (2021). Profiling Glycoproteins on Functionalized Reverse Phase Protein Array. Antibody Arrays. https://link.springer.com/protocol/10.1007/978-1-0716-1064-0_17

Pandey S. et.al. (2021). Intrinsic bias at non-canonical, β-arrestin-coupled seven transmembrane receptors. bioRxiv. https://www.biorxiv.org/content/10.1101/2021.02.02.429298v1.abstract

Han Y. et.al. (2021). Expression and purification of fused kinase from insect cells for in vitro kinase assay. STAR Protoc. https://pubmed.ncbi.nlm.nih.gov/33681825/

Sun J. et.al. (2021). Synergistically Bifunctional Paramagnetic Separation Enables Efficient Isolation of Urine Extracellular Vesicles and Downstream Phosphoproteomic Analysis. ACS Appl Mater Interfaces. https://pubmed.ncbi.nlm.nih.gov/33443402/

Mohallem R. et.al. (2020). Regulators of TNFα mediated insulin resistance elucidated by quantitative proteomics. Sci Rep. https://pubmed.ncbi.nlm.nih.gov/33257747/

Zhang H. et.al. (2020). Glass Fiber-Supported Hybrid Monolithic Spin Tip for Enrichment of Phosphopeptides from Urinary Extracellular Vesicles. Analytical Chemistry. https://pubmed.ncbi.nlm.nih.gov/33074658/

Christensen B. et.al. (2020). FAM20C‐Mediated Phosphorylation of MEPE and Its Acidic Serine‐ and Aspartate‐Rich Motif. JBMRPlus. https://asbmr.onlinelibrary.wiley.com/doi/full/10.1002/jbm4.10378

Iliuk A. et.al. (2020). Plasma-Derived Extracellular Vesicle Phosphoproteomics through Chemical Affinity Purification. J Proteome Res. https://pubmed.ncbi.nlm.nih.gov/32396726/

Mohallem R. et.al. (2020). Regulators of TNFα Mediated Insulin Resistance Elucidated by Quantitative Proteomics. BioRxiv. https://www.biorxiv.org/content/10.1101/2020.06.22.165472v1.abstract

Justilien V. et.al. (2020). Protein kinase Cι promotes UBF1–ECT2 binding on ribosomal DNA to drive rRNA synthesis and transformed growth of non-small-cell lung cancer cells. J Biol Chem. https://pubmed.ncbi.nlm.nih.gov/32350115/

Andaluz Aguilar H. et.al. (2020). Sequential phosphoproteomics and N-glycoproteomics of plasma-derived extracellular vesicles. Nat Protoc. https://pubmed.ncbi.nlm.nih.gov/31863077/

Pal D. et.al. (2020). Chk1-mediated phosphorylation of Cdh1 promotes the SCFβTRCP-dependent degradation of Cdh1 during S-phase and efficient cell-cycle progression. Cell Death & Disease. https://www.nature.com/articles/s41419-020-2493-1

Wang P. et.al. (2020). Mapping proteome-wide targets of protein kinases in plant stress responses. PNAS. https://doi.org/10.1073/pnas.1919901117

Cho Y. et.al. (2020). CDK7 regulates organ size and tumor growth by safeguarding the Hippo pathway effector Yki/Yap/Taz in the nucleus. Genes Dev. https://www.ncbi.nlm.nih.gov/pubmed/31857346

Li S. et.al. (2020). Gilgamesh (Gish)/CK1γ regulates tissue homeostasis and aging in adult Drosophila midgut. J of Cell Biology. https://doi.org/10.1083/jcb.201909103

Yamazaki H. et.al. (2020). Quantitative proteomics indicate a strong correlation of mitotic phospho-/dephosphorylation with non-structured regions of substrates. Biochimica et Biophysica Acta. https://www.ncbi.nlm.nih.gov/pubmed/31676455

Sen A. et.al. (2020). Ubiquitination and Phosphorylation are Independently Required for Epsin-Mediated Internalization of Cargo in S. cerevisiae. BioRxiv. https://doi.org/10.1101/2020.02.07.939082

Mullis B. et.al. (2019). Automating Complex, Multistep Processes on a Single Robotic Platform to Generate Reproducible Phosphoproteomic Data. SLAS Discov. doi: 10.1177/2472555219878152. https://www.ncbi.nlm.nih.gov/pubmed/31556780

Park J. et.al. (2019). Identification of Protein Phosphatase 4 Inhibitory Protein That Plays an Indispensable Role in DNA Damage Response. Mol Cells. doi: 10.14348/molcells.2019.0014.  https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6681864/

Han Y. et.al. (2019). Phosphorylation of Ci/Gli by Fused Family Kinases Promotes Hedgehog Signaling. Developmental Cell. doi: 10.1016/j.devcel.2019.06.008. https://www.ncbi.nlm.nih.gov/pubmed/31279575

Lee IY. et.al. (2019). MST1 Negatively Regulates TNFα-Induced NF-κB Signaling through Modulating LUBAC Activity. Molecular Cell. 73(6): 1138. https://www.ncbi.nlm.nih.gov/pubmed/30901564

Zhong Z. et.al. (2019). Phosphoproteomics Reveals the Biosynthesis of Secondary Metabolites in Catharanthus roseus under Ultraviolet-B Radiation. J Proteome Res. https://www.ncbi.nlm.nih.gov/pubmed/31356092

Yu Y. et.al. (2019). Spleen tyrosine kinase activity regulates epidermal growth factor receptor signaling pathway in ovarian cancer. EBioMedicine. https://www.ncbi.nlm.nih.gov/pubmed/31492560

Li X. et.al. (2019). Spontaneous mutations in FgSAD1 suppress the growth defect of the Fgprp4 mutant by affecting tri‐snRNP stability and its docking in Fusarium graminearum. Environ. Microbiol. doi: 10.1111/1462-2920.14736. https://www.ncbi.nlm.nih.gov/pubmed/31291045

Weber T. et.al. (2019). Stable Acinar Progenitor Cell Model Identifies Treacle-Dependent Radioresistance. Radiat. Res. doi: 10.1667/RR15342.1. https://www.ncbi.nlm.nih.gov/pubmed/31141469

Yamazaki H. et.al. (2019). Quantitative proteomics revealed a tight correlation between mitotic phosphorylation/dephosphorylation and structural properties of substrate domains. BioRxiv. doi: https://doi.org/10.1101/636407

Perez M. et.al. (2019). High-throughput Identification of FLT3 Wild-type and Mutant Kinase Substrate Preferences and Application to Design of Sensitive In Vitro Kinase Assay Substrates. Mol Cell Proteomics. 18(3): 477. https://www.ncbi.nlm.nih.gov/pubmed/30541869

Arrington J. et.al. (2019). Identification of the Direct Substrates of the ABL Kinase via Kinase Assay Linked Phosphoproteomics with Multiple Drug Treatments. J Proteome Res. 18(4): 1679. https://www.ncbi.nlm.nih.gov/pubmed/30869898

Pal D. et.al. (2019). Chk1 Phosphorylates Cdh1 to Promote SCFβTRCP-Dependent Degradation of Cdh1 During S-Phase. bioRxiv. https://www.biorxiv.org/content/10.1101/535799v4.abstract

Hong NH, Tak YJ. et.al. (2019). Hip2 ubiquitin-conjugating enzyme has a role in UV-induced G1/S arrest and re-entry. Genes Genomics. 41(2): 159. https://www.ncbi.nlm.nih.gov/pubmed/30264212

Wu X, Li L. et.al. (2018). Highly efficient phosphoproteome capture and analysis from urinary extracellular vesicles. J Proteome Res. 17(9): 3308. https://www.ncbi.nlm.nih.gov/pubmed/30080416   Original EVtrap publication.

Zhang Y, Zhao C. et.al. (2018). High-throughput phosphorylation screening and validation through Ti(IV)-nanopolymer functionalized reverse phase phosphoprotein array. Anal Chem. 90(17): 10263. https://www.ncbi.nlm.nih.gov/pubmed/30103608

Hsu CC, Zhu Y. et.al. (2018). Universal plant phosphoproteomics workflow and its application to tomato signaling in response to cold stress. Mol Cell Proteomics. Epub ahead of print. https://www.ncbi.nlm.nih.gov/pubmed/30006488

Sroga GE, Vashishth D Y. et.al. (2018). Phosphorylation of extracellular bone matrix proteins and its contribution to bone fragility. J Bone Miner Res. Epub ahead of print. https://www.ncbi.nlm.nih.gov/pubmed/30001467

Sun M, Zhang Y. et.al. (2018). The tri-snRPN specific protein FgSnu66 is functionally related to PgPrp4 kinase in Fusarium graminearum. Mol Microbiol. Epub ahead of print. https://www.ncbi.nlm.nih.gov/pubmed/29923654

Iliuk A. (2018). Identification of phosphorylated proteins on a global scale. Curr Protoc Chem Biol. 10(3): e48. https://www.ncbi.nlm.nih.gov/pubmed/29927094

Yin X, Wang X. et.al. (2018). Phosphoproteomics: protein phosphorylation in regulation of seed germination and plant growth. Curr Protein Pept Sci. 19(4): 401. https://www.ncbi.nlm.nih.gov/pubmed/28190389

Gao X, Zhang J. et.al. (2018). Phosphorylation by Prp4 kinase releases the self-inhibition of FgPrp31 in Fusarium graminearum. Current Genetics. Epub ahead of print. https://www.ncbi.nlm.nih.gov/pubmed/29671102

Chen IH, Aguilar H. et.al. (2018). Analytical pipeline for discovery and verification of glycoproteins from plasma-derived extracellular vesicles as breast cancer biomarkers. Anal Chem. 90: 6307. https://www.ncbi.nlm.nih.gov/pubmed/29629753

Dong M. et.al. (2018). The divide and conquer strategies for deep phosphoproteomics analysis. TrAC Trends in Anal Chem. 105: 282. https://www.sciencedirect.com/science/article/abs/pii/S0165993617304922

Nunez C. et.al. (2018). Novel functionalized nanomaterials for the effective enrichment of proteins and peptides with post-translational modifications. J Proteomics. 181: 170. https://www.ncbi.nlm.nih.gov/pubmed/29674016

Butterfield A. (2018). Phosphoproteomics of Alzheimer disease brain: insights into altered brain protein regulation of critical neuronal functions and their contributions to subsequent cognitive loss. Biochimica et Biophysica Acta. https://www.sciencedirect.com/science/article/abs/pii/S0925443918303284

Dong M, Yao Y. et.al. (2018). The divide and conquer strategies for deep phosphoproteomics analysis. TrAC Trends Anal Chem. 105: 282. https://www.sciencedirect.com/science/article/pii/S0165993617304922

Ni W, Xu SL. et.al. (2017). PPKs mediate direct signal transfer from phytochrome photoreceptors to transcription factor PIF3. Nature Communications. 8: 15236. https://www.ncbi.nlm.nih.gov/pubmed/28492231

Chen IH, Xue L. et.al. (2017). Phosphoproteins in extracellular vesicles as candidate markers for breast cancer. 114: 3175. https://www.ncbi.nlm.nih.gov/pubmed/28270605

Adelaiye-Ogala R., Budka J. et.al. (2017). EZH2 modifies sunitinib resistance in renal cell carcinoma by kinome reprogramming. Cancer Research. 77: 6651. https://www.ncbi.nlm.nih.gov/pubmed/28978636

Zhao C., Wang P. et.al. (2017). MAP kinase cascades regulate the cold response by modulating ICE1 protein stability. Developmental Cell. S1534-5807(17): 30783-9. https://www.ncbi.nlm.nih.gov/pubmed/29056551

Gangula NR, Maddika S. (2017). Interplay between the phosphatase PHLPP1 and E3 ligase RNF41 stimulates proper kinetochore assembly via the outer-kinetochore protein SGT1. J Biol Chem. 292: 13947-13958. https://www.ncbi.nlm.nih.gov/pubmed/28696259

Bender K, Blackburn R, et.al. (2017). Autophosphorylation-based calcium sensitivity priming of Ca2+/Calmodulin inhibition of Arabidopsis thaliana Ca2+-dependent Protein Kinase 28. J Biol Chem. 292: 3988-4002. https://www.ncbi.nlm.nih.gov/pubmed/28154194

Hsu C-C, Arrington J, et.al. (2017). Identification of plant kinase substrates based on kinase assay-linked phosphoproteomics. Kinase Signaling Pathways. Methods in Molecular Biology. 1636: 327-335. https://www.ncbi.nlm.nih.gov/pubmed/28730489

Hardy J, Tellier M, et.al. (2017). The RS domain of human CFlm68 plays a key role in selection between alternative sites of pre-mRNA cleavage and polyadenylation. BioRxiv. doi: https://doi.org/10.1101/177980

Kuzmina A, Krasnopolski S, et.al. (2017). Super elongation complex promotes early HIV transcliption and its function is modulated by P-TEFb. Transcription. 8: 133-149. https://www.ncbi.nlm.nih.gov/pubmed/28340332

Hsu C-C, Xue L, et.al. (2017). Estimating the efficiency of phosphopeptide identification by tandem mass spectrometry. J Am Soc Mass Spectrom. 28: 1127-1135. https://www.ncbi.nlm.nih.gov/pubmed/28283928

Hatfield S. (2017). Establishing methods for protein purification and activity analysis Pkn1 and Pkn5 from Chlamydia Trachomatis.  https://search.proquest.com/docview/1803609691

Chang Y-Y., Li H, et.al. (2017). Immobilized metal affinity chromatography (IMAC) for metalloproteomics and phosphoproteomics. Chapter 9, p. 329. www.elsevier.com

Pan L, Aguilar H, et.al. (2016). Three-dimensionally functionalized reverse-phase glycoprotein array for cancer biomarker discovery and validation. JACS. 138: 15311. https://www.ncbi.nlm.nih.gov/pubmed/27933927

Li L, Kim P, et.al. (2016). Activation dependent destruction of a co-receptor by a pseudomonas syringae effector dampens plant immunity. Cell Host Microbe. 20(4): 504-14. https://www.ncbi.nlm.nih.gov/pubmed/27736646

Zhao H, Pflug B, et.al. (2016). Pyruvate dehydrogenase alpha 1 as a target of omega-3 polyunsaturated fatty acids in human prostate cancer through a global phosphoproteomic analysis. Proteomics. 16(17): 2419-31.  https://www.ncbi.nlm.nih.gov/pubmed/27357730

Chaput D, PKirouac L, et.al. (2016). Potential role of PCTAIRE-2, PCTAIRE-3 and P-Histone H4 in amyloid precursor protein-dependent Alzheimer pathology. Oncotarget. 7(8): 8481-97.  https://www.ncbi.nlm.nih.gov/pubmed/26885753

Gao X, Jin Q, et.al. (2016). FgPrp4 kinase is important for spliceosome B-complex activation and splicing efficiency in Fusarium graminearum. PLoS Genet. 12(4): e1005973.  https://www.ncbi.nlm.nih.gov/pubmed/27058959

Sroga GE, Vashishth D. (2016). A strategy to quantitate global phosphorylation of bone matrix proteins. Anal Biochem. 499:85-89. http://www.ncbi.nlm.nih.gov/pubmed/26851341

Modak S, Kumar V. (2016). Influence of phosphorylation on the foamability and stability of bovine serum albumin and citrus peel pectin mixed foams. J Disp Sci Technology. 38:1266-1275.  http://www.tandfonline.com/doi/full/10.1080/01932691.2016.1234382?scroll=top&needAccess=true

Batalha I, Roque A. (2016). Phosphopeptide enrichment using various magnetic nanocomposits: an overview. Phosphoproteomics. Methods in Molecular Biology. 1355:193-209. https://www.ncbi.nlm.nih.gov/pubmed/26584927

Xue L, Arrington J, et.al. (2016). Identification of direct kinase substrates via kinase assay-linked phosphoproteomics. Methods Mol Biol. 1355: 263-73. https://www.ncbi.nlm.nih.gov/pubmed/26584932

Iliuk A, Li L, et.al. (2016). Multiplexed imaging of protein phosphorylation on membranes based on Ti(IV) functionalized nanopolymers. Chembiochem. 17(10):900-03. http://www.ncbi.nlm.nih.gov/pubmed/27037847

Niimori Kita K, Nakamura F, et.al. (2016). Nuclear phosphoproteomics features the novel smoking markers in mouse lung tissue following subacute phase exposure to tobacco smoke. J Bioanal Biomed. 8: 09.  DOI: 10.4172/1948-593X.1000146

Zhao H. (2016). The effects of dietary polyunsaturated fatty acids on prostate cancer – proteomics and phosphoproteomics studies.  https://scholarworks.iupui.edu/handle/1805/9790

Pelech S, Yue L. (2016). Profiling signaling protein expression, modifications and interactions with multi-dimensional antibody microarrays. FASEB J. http://www.fasebj.org/content/30/1_Supplement/lb190.short

Baxter D. (2016). Regulation of Ciz1 by Cyclin A-Cyclin Dependent Kinase 2 (CDK2) mediated phosphorylation.  http://eprints.lancs.ac.uk/78800/

Li M, Yin X, et.al. (2015). Proteomic analysis of phosphoproteins in the rice nucleus during the early stage of seed germination. Journal of Proteome Research. 14(17): 2884-96.  https://www.ncbi.nlm.nih.gov/pubmed/26035336

Muschter S, Berthold T, et.al. (2015). Mass spectrometric phosphoproteome analysis of small-sized samples of human neutrophils. Clinica Chimica Acta. 451:199-207.  https://www.ncbi.nlm.nih.gov/pubmed/26434552

Yin X, Komatsu S. (2015). Quantitative proteomics of nuclear phosphoproteins in the root tip of soybean during the initial stages of flooding stress. J Proteome. 119:183–195. https://www.ncbi.nlm.nih.gov/pubmed/25724727

Gendrin C, Lembo A, Whidbey C, Burnside K, Berry J, Ngo L, Banerjee A, Xue L, Arrington J, Doran KS, Tao WA, Rajagopal L. (2015). The sensor histidine kinase RgfC affects group B streptococcal virulence factor expression independent of its response regulator RgfA. Infect Immun. 2015 Mar;83(3):1078-88. http://www.ncbi.nlm.nih.gov/pubmed/25561709

Iliuk A, Jayasundera K, Wang WH, Schluttenhofer R, Geahlen RL, Tao WA. (2015). In-Depth Analyses of B Cell Signaling Through Tandem Mass Spectrometry of Phosphopeptides Enriched by PolyMAC. Int J Mass Spectrom. 2015 Feb 1;377:744-753. http://www.ncbi.nlm.nih.gov/pubmed/25954137

Johnson H. (2015). Uncovering dynamic phosphorylation signaling using mass spectrometry. Int. J. Mass Spectrometry. 391:123-138. http://www.sciencedirect.com/science/article/pii/S1387380615002511

Pan L, Wang L, Hsu CC, Zhang J, Iliuk A, Tao WA. (2015). Sensitive measurement of total protein phosphorylation level in complex protein samples. Analyst. 2015 May 21;140(10):3390-6. http://www.ncbi.nlm.nih.gov/pubmed/25857711

Yin X, Sakata K, et.al. (2014). Phosphoproteomics reveals the effect of ethylene in soybean root under flooding stress. Journal of Proteome Research. 2014 13(12):5618-34. https://www.ncbi.nlm.nih.gov/pubmed/25316100

Han C, Yang P et.al. (2014). Quantitative proteomics reveals the role of protein phosphorylation in rice embryos during early stages of germination. Journal of Proteome Research. 2014 13(3):1766-82. http://pubs.acs.org/doi/abs/10.1021/pr401295c

Yang C, Zhong X, Li L. (2014). Recent advances in enrichment and separation strategies for mass spectrometry-based phosphoproteomics. Electrophoresis. 2014 Dec;35(24):3418-29. http://www.ncbi.nlm.nih.gov/pubmed/24687451

X Liu, Y Li, X Xu, P Li, Z Nie, Y Huang, S Yao. (2014). Nanomaterial based tools for protein kinase bioanalysis. TrAC Trends in Analytical Chemistry. 58:40-53. http://www.sciencedirect.com/science/article/pii/S0165993614000533

Arrington JV, Xue L, Tao WA. (2014). Quantitation of the phosphoproteome using the library-assisted extracted ion chromatogram (LAXIC) strategy. Methods Mol Biol. 2014;1156:407-16. http://www.ncbi.nlm.nih.gov/pubmed/24792004

Xue L, Wang P, Cao P, Zhu JK, Tao WA. (2014). Identification of extracellular signal-regulated kinase 1 (ERK1) direct substrates using stable isotope labeled kinase assay-linked phosphoproteomics. Mol Cell Proteomics. 2014 Nov;13(11):3199-210. http://www.ncbi.nlm.nih.gov/pubmed/25022875

Jayasundera KB, Iliuk AB, Nguyen A, Higgins R, Geahlen RL, Tao WA. (2014). Global phosphoproteomics of activated B cells using complementary metal ion functionalized soluble nanopolymers. Anal Chem. 2014 Jul 1;86(13):6363-71. http://www.ncbi.nlm.nih.gov/pubmed/24905233

Searleman AC, Iliuk AB, Collier TS, Chodosh LA, Tao WA, Bose R. (2014). Tissue phosphoproteomics with PolyMAC identifies potential therapeutic targets in a transgenic mouse model of HER2 positive breast cancer. Electrophoresis. 2014 Dec;35(24):3463-9. http://www.ncbi.nlm.nih.gov/pubmed/24723360

Walls C., Iliuk A., Bai Y., Wang M., Tao WA, Zhang ZY. (2013). Phosphatase of regenerating liver 3 (PRL3) provokes a tyrosine phosphoproteome to drive prometastatic signal transduction. Mol. Cell. Proteomics. 12(12): 3759-77, http://www.ncbi.nlm.nih.gov/pubmed/24030100

Wang P, Xue L, Batelli G, Lee S, Hou YJ, Van Oosten MJ, Zhang H, Tao WA, Zhu JK. (2013). Quantitative phosphoproteomics identifies SnRK2 protein kinase substrates and reveals the effectors of abscisic acid action. Proc Natl Acad Sci U S A. 2013 Jul 2;110(27):11205-10. http://www.ncbi.nlm.nih.gov/pubmed/23776212

Radu M., Rawat S., Beeser A., Iliuk A., Tao WA., Chernoff J. (2013). ArhGAP15, a Rac-specific GTPase activating protein, plays a dual role in inhibiting small GTPase signaling. Journal of Biological Chemistry. 288(29): 21117-25, http://www.ncbi.nlm.nih.gov/pubmed/23760270

Yu S., Huang H., Iliuk A., Wang W-H., Tao WA., Post C., Geahlen R. (2013). Syk Inhibits the Activity of Protein Kinase A by Phosphorylating Tyrosine 330 of the Catalytic Subunit. Journal of Biological Chemistry. 288(15): 10870-10881, http://www.ncbi.nlm.nih.gov/pubmed/23447535

Xue L, Wang P, Wang L, Renzi E, Radivojac P, Tang H, Arnold R, Zhu JK, Tao WA. (2013). Quantitative measurement of phosphoproteome response to osmotic stress in arabidopsis based on Library-Assisted eXtracted Ion Chromatogram (LAXIC). Mol Cell Proteomics. 2013 Aug;12(8):2354-69. http://www.ncbi.nlm.nih.gov/pubmed/23660473

Chu H et.al. (2012). Identification of cytoskeletal elements enclosing the ATP pools that fuel human red blood cell membrane cation pumps. PNAS. 109(31): 12794-99.  https://www.ncbi.nlm.nih.gov/pubmed/22745158

Pan L, Iliuk A, Yu S, Geahlen RL, Tao WA. (2012). Multiplexed quantitation of protein expression and phosphorylation based on functionalized soluble nanopolymers. J Am Chem Soc. 134(44): 18201-4, http://www.ncbi.nlm.nih.gov/pubmed/23088311   Original pIMAGO-Fluor detection on microplate publication.

Iliuk A, Liu XS, Xue L, Liu X, Tao WA. (2012). Chemical visualization of phosphoproteomes on membrane. Mol. Cell. Proteomics. 11(9): 629-39, http://www.ncbi.nlm.nih.gov/pubmed/22593177   Original pIMAGO-biotin detection on Western Blot publication.

Xue L, Wang WH, Iliuk A, Hu L, Galan JA, Yu S, Hans M, Geahlen RL, Tao WA (2012). Sensitive kinase assay linked with phosphoproteomics for identifying direct kinase substrates. PNAS. 109(15): 5615-20, http://www.ncbi.nlm.nih.gov/pubmed/22451900

Iliuk A, Jayasundera K, Schluttenhofer R, Tao WA (2011). Functional soluble nanopolymers for phosphoproteome analysis. Methods Mol. Biol. 790: 277-85, http://www.ncbi.nlm.nih.gov/pubmed/21948422

Iliuk A, Martinez J, Hall MC, Tao WA (2011). Phosphorylation assay based on functionalized soluble nanopolymer. Anal. Chem. 83(7): 2767-74, http://www.ncbi.nlm.nih.gov/pubmed/21395237  Original pIMAGO-biotin detection on microplate publication.