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Improve the Coverage for the Analysis of Phosphoproteome of HeLa Cells by a Tandem Digestion Approach

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What this work says

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

inferredcites →https://doi.org/10.1002/elps.200600718openalex-snapshot

Highly specific enrichment of phosphopeptides by zirconium dioxide nanoparticles for phosphoproteome analysis

inferredcites →https://doi.org/10.1002/elps.200900637openalex-snapshot

Mapping of phosphorylation sites in human MSK1 activated by a novel interaction with MRK‐β

inferredcites →https://doi.org/10.1002/pmic.200700884openalex-snapshot

Large‐scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography

inferredcites →https://doi.org/10.1007/s00216-011-5466-5openalex-snapshot

Increasing phosphoproteomic coverage through sequential digestion by complementary proteases

inferredcites →https://doi.org/10.1016/j.aca.2009.01.033openalex-snapshot

Preparation of monodisperse immobilized Ti4+ affinity chromatography microspheres for specific enrichment of phosphopeptides

inferredcites →https://doi.org/10.1016/j.cell.2006.09.026openalex-snapshot

Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks

inferredcites →https://doi.org/10.1016/j.molcel.2008.07.007openalex-snapshot

Kinase-Selective Enrichment Enables Quantitative Phosphoproteomics of the Kinome across the Cell Cycle

inferredcites →https://doi.org/10.1016/s0092-8674(00)81688-8openalex-snapshot

Signaling—2000 and Beyond

inferredcites →https://doi.org/10.1021/ac000826jopenalex-snapshot

Analysis of Protein Phosphorylation by a Combination of Elastase Digestion and Neutral Loss Tandem Mass Spectrometry

inferredcites →https://doi.org/10.1021/ac050232mopenalex-snapshot

Mapping of Phosphorylation Sites by a Multi-Protease Approach with Specific Phosphopeptide Enrichment and NanoLC−MS/MS Analysis

inferredcites →https://doi.org/10.1021/ac100075yopenalex-snapshot

A Fully Automated System with Online Sample Loading, Isotope Dimethyl Labeling and Multidimensional Separation for High-Throughput Quantitative Proteome Analysis

inferredcites →https://doi.org/10.1021/ac801708popenalex-snapshot

Evaluation of the Low-Specificity Protease Elastase for Large-Scale Phosphoproteome Analysis

inferredcites →https://doi.org/10.1021/ac9004309openalex-snapshot

Lys-N and Trypsin Cover Complementary Parts of the Phosphoproteome in a Refined SCX-Based Approach

inferredcites →https://doi.org/10.1021/ac9023044openalex-snapshot

Reversed-Phase-Reversed-Phase Liquid Chromatography Approach with High Orthogonality for Multidimensional Separation of Phosphopeptides

inferredcites →https://doi.org/10.1021/pr060559jopenalex-snapshot

Large-Scale Phosphorylation Analysis of α-Factor-Arrested Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1021/pr100075xopenalex-snapshot

Optimized IMAC−IMAC Protocol for Phosphopeptide Recovery from Complex Biological Samples

inferredcites →https://doi.org/10.1021/pr7006335openalex-snapshot

Phosphoproteome Analysis of Fission Yeast

inferredcites →https://doi.org/10.1021/pr700675jopenalex-snapshot

Automatic Validation of Phosphopeptide Identifications by the MS2/MS3 Target-Decoy Search Strategy

inferredcites →https://doi.org/10.1021/pr800223mopenalex-snapshot

Specific Phosphopeptide Enrichment with Immobilized Titanium Ion Affinity Chromatography Adsorbent for Phosphoproteome Analysis

inferredcites →https://doi.org/10.1021/pr900863uopenalex-snapshot

Value of Using Multiple Proteases for Large-Scale Mass Spectrometry-Based Proteomics

inferredcites →https://doi.org/10.1021/pr9009904openalex-snapshot

ArMone: A Software Suite Specially Designed for Processing and Analysis of Phosphoproteome Data

inferredcites →https://doi.org/10.1038/nbt1146openalex-snapshot

An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets

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/ncb0502-e127openalex-snapshot

The origins of protein phosphorylation

inferredcites →https://doi.org/10.1038/nmeth1100openalex-snapshot

Mapping protein post-translational modifications with mass spectrometry

inferredcites →https://doi.org/10.1038/nprot.2008.150openalex-snapshot

The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry

inferredcites →https://doi.org/10.1073/pnas.0609836104openalex-snapshot

Large-scale phosphorylation analysis of mouse liver

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.0805139105openalex-snapshot

A quantitative atlas of mitotic phosphorylation

inferredcites →https://doi.org/10.1074/mcp.m500135-mcp200openalex-snapshot

Phosphorylation Analysis by Mass Spectrometry

inferredcites →https://doi.org/10.1074/mcp.m700362-mcp200openalex-snapshot

SIMAC (Sequential Elution from IMAC), a Phosphoproteomics Strategy for the Rapid Separation of Monophosphorylated from Multiply Phosphorylated Peptides

inferredcites →https://doi.org/10.1074/mcp.m700468-mcp200openalex-snapshot

A Multidimensional Chromatography Technology for In-depth Phosphoproteome Analysis

inferredcites →https://doi.org/10.1093/nar/gkh070openalex-snapshot

Human protein reference database as a discovery resource for proteomics

inferredcites →https://doi.org/10.1101/gr.849004openalex-snapshot

WebLogo: A Sequence Logo Generator: Figure 1

inferredcites →https://doi.org/10.1126/scisignal.2000475openalex-snapshot

Quantitative Phosphoproteomics Reveals Widespread Full Phosphorylation Site Occupancy During Mitosis

inferredcites →https://doi.org/10.1186/gb-2006-7-11-r106openalex-snapshot

Analysis of the Saccharomyces cerevisiae proteome with PeptideAtlas

What points at this work

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

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Discrimination and Quantification of Protein Species in Processed Meat Products Using High Resolution Mass Spectrometry

inferred← citeshttps://doi.org/10.1002/9781119250906.ch2openalex-snapshot

Identification and Analysis of Protein Phosphorylation by Mass Spectrometry

inferred← citeshttps://doi.org/10.1002/elps.201400017openalex-snapshot

Recent advances in enrichment and separation strategies for mass spectrometry‐based phosphoproteomics

inferred← citeshttps://doi.org/10.1002/med.21889openalex-snapshot

Dual roles of drug or its metabolite−protein conjugate: Cutting‐edge strategy of drug discovery using shotgun proteomics

inferred← citeshttps://doi.org/10.1002/pmic.201200484openalex-snapshot

Technologies and challenges in large‐scale phosphoproteomics

inferred← citeshttps://doi.org/10.1002/pmic.201400268openalex-snapshot

Identification of phosphopeptides with unknown cleavage specificity by a de novo sequencing assisted database search strategy

inferred← citeshttps://doi.org/10.1002/rcm.70051openalex-snapshot

TCEP‐Mediated Protein Hydrolysis: Highly Selective Cleavage C‐Terminal to Aspartic Acid

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Maximizing Depth of PTM Coverage: Generating Robust MS Datasets for Computational Prediction Modeling

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Proteomic Strategies to Characterize Signaling Pathways

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Sample Preparation for Mass Spectrometry-Based Proteomics; from Proteomes to Peptides

inferred← citeshttps://doi.org/10.1007/s00216-014-8071-6openalex-snapshot

Quantitative proteomics reveals the kinetics of trypsin-catalyzed protein digestion

inferred← citeshttps://doi.org/10.1007/s11427-014-4714-2openalex-snapshot

Rapid development of proteomics in China: from the perspective of the Human Liver Proteome Project and technology development

inferred← citeshttps://doi.org/10.1016/j.afres.2026.102404openalex-snapshot

Pseudo-MRM-QTOF mass spectrometry for identification and quantification of livestock and poultry meat adulteration in beef balls

inferred← citeshttps://doi.org/10.1016/j.celrep.2015.05.029openalex-snapshot

An Augmented Multiple-Protease-Based Human Phosphopeptide Atlas

inferred← citeshttps://doi.org/10.1016/j.chroma.2014.10.107openalex-snapshot

Enrichment and separation techniques for large-scale proteomics analysis of the protein post-translational modifications

inferred← citeshttps://doi.org/10.1016/j.chroma.2016.11.027openalex-snapshot

Preparation and application of immobilized enzymatic reactors for consecutive digestion with two enzymes

inferred← citeshttps://doi.org/10.1016/j.colsurfb.2020.111422openalex-snapshot

A dual enzyme-containing microreactor for consecutive digestion based on hydrophilic ZIF-90 with size-selective sheltering

inferred← citeshttps://doi.org/10.1016/j.ijms.2015.08.002openalex-snapshot

Uncovering dynamic phosphorylation signaling using mass spectrometry

inferred← citeshttps://doi.org/10.1016/j.jchromb.2017.04.026openalex-snapshot

Targeted mass spectrometry: An emerging powerful approach to unblock the bottleneck in phosphoproteomics

inferred← citeshttps://doi.org/10.1016/j.jprot.2012.10.018openalex-snapshot

A large-scale protein phosphorylation analysis reveals novel phosphorylation motifs and phosphoregulatory networks in Arabidopsis

inferred← citeshttps://doi.org/10.1016/j.jprot.2013.11.014openalex-snapshot

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome

inferred← citeshttps://doi.org/10.1016/j.mcpro.2024.100819openalex-snapshot

Molecular Signatures of Neurodegenerative Diseases Identified by Proteomic and Phosphoproteomic Analyses in Aging Mouse Brain

inferred← citeshttps://doi.org/10.1016/j.mcpro.2025.101019openalex-snapshot

A Methanolic Urea-Enhanced Protein Extraction Enabling the Largest Bacterial Phosphorylation Resource

inferred← citeshttps://doi.org/10.1016/j.semcdb.2012.05.005openalex-snapshot

Sample preparation and analytical strategies for large-scale phosphoproteomics experiments

inferred← citeshttps://doi.org/10.1016/j.talanta.2018.03.047openalex-snapshot

A fast sample processing strategy for large-scale profiling of human urine phosphoproteome by mass spectrometry

inferred← citeshttps://doi.org/10.1016/s1872-2040(15)60864-7openalex-snapshot

High Concentration Trypsin Assisted Fast In-Gel Digestion for Phosphoproteome Analysis

inferred← citeshttps://doi.org/10.1021/ac402696bopenalex-snapshot

Dual Matrix-Based Immobilized Trypsin for Complementary Proteolytic Digestion and Fast Proteomics Analysis with Higher Protein Sequence Coverage

inferred← citeshttps://doi.org/10.1021/ac5002146openalex-snapshot

Integration of Cell Lysis, Protein Extraction, and Digestion into One Step for Ultrafast Sample Preparation for Phosphoproteome Analysis

inferred← citeshttps://doi.org/10.1021/acs.analchem.0c00906openalex-snapshot

Multi-in-One: Multiple-Proteases, One-Hour-Shot Strategy for Fast and High-Coverage Phosphoproteomic Investigation

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.8b02448openalex-snapshot

Lys-C/Arg-C, a More Specific and Efficient Digestion Approach for Proteomics Studies

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Application of a Pseudotargeted MS Method for the Quantification of Glycated Hemoglobin for the Improved Diagnosis of Diabetes Mellitus

inferred← citeshttps://doi.org/10.1021/acs.jproteome.5b01122openalex-snapshot

Extraction, Enrichment, Solubilization, and Digestion Techniques for Membrane Proteomics

inferred← citeshttps://doi.org/10.1021/acs.jproteome.5c00220openalex-snapshot

An Optimized SP3 Sample Processing Workflow for In-Depth and Reproducible Phosphoproteomics

inferred← citeshttps://doi.org/10.1021/cr3003533openalex-snapshot

Protein Analysis by Shotgun/Bottom-up Proteomics

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Six alternative proteases for mass spectrometry–based proteomics beyond trypsin

inferred← citeshttps://doi.org/10.1038/s41598-017-01915-wopenalex-snapshot

Protein Phosphatase 2A (PP2A) Regulates EG5 to Control Mitotic Progression

inferred← citeshttps://doi.org/10.1039/c7an00985bopenalex-snapshot

Recent advances in phosphoproteomics and application to neurological diseases

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Phosphoproteomic strategies in cancer research: a minireview

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Enzyme Kinetics for Complex System Enables Accurate Determination of Specificity Constants of Numerous Substrates in a Mixture by Proteomics Platform

inferred← citeshttps://doi.org/10.1074/mcp.r113.032862openalex-snapshot

The Coming of Age of Phosphoproteomics—from Large Data Sets to Inference of Protein Functions

inferred← citeshttps://doi.org/10.1111/febs.12380openalex-snapshot

Phosphoproteomics‐based network medicine

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Differential analysis of N-glycoproteome between hepatocellular carcinoma and normal human liver tissues by combination of multiple protease digestion and solid phase based labeling

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中国蛋白质组学研究进展—以人类肝脏蛋白质组计划和蛋白质组学技术发展为主题

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Current strategies and findings in clinically relevant post-translational modification-specific proteomics

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The current state of the art of quantitative phosphoproteomics and its applications to diabetes research

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S100A4+ Macrophages Are Necessary for Pulmonary Fibrosis by Activating Lung Fibroblasts

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