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Protein digestion priority is independent of protein abundances

https://doi.org/10.1038/nmeth.2850
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What this work says

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

inferredcites →https://doi.org/10.1021/pr060507uopenalex-snapshot
Prediction of Missed Cleavage Sites in Tryptic Peptides Aids Protein Identification in Proteomics
inferredcites →https://doi.org/10.1021/pr0705035openalex-snapshot
Does Trypsin Cut Before Proline?
inferredcites →https://doi.org/10.1038/nmeth.2250openalex-snapshot
Digestion and depletion of abundant proteins improves proteomic coverage
inferredcites →https://doi.org/10.1038/nmeth0314-347openalex-snapshot
Addendum: Digestion and depletion of abundant proteins improves proteomic coverage
inferredcites →https://doi.org/10.1073/pnas.1117158109openalex-snapshot
Global kinetic analysis of proteolysis via quantitative targeted proteomics
inferredcites →https://doi.org/10.1101/gr.849004openalex-snapshot
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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.4779102openalex-extracted
Discrimination and Quantification of Protein Species in Processed Meat Products Using High Resolution Mass Spectrometry
inferred← citeshttps://doi.org/10.1002/pmic.201400498openalex-snapshot
The proteomic analysis improved by cleavage kinetics‐based fractionation of tryptic peptides
inferred← citeshttps://doi.org/10.1002/pmic.201700432openalex-snapshot
Systematic Evaluation of Immobilized Trypsin‐Based Fast Protein Digestion for Deep and High‐Throughput Bottom‐Up Proteomics
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/s00604-015-1642-1openalex-snapshot
A fluorescent turn-on detection scheme for α-fetoprotein using quantum dots placed in a boronate-modified molecularly imprinted polymer with high affinity for glycoproteins
inferred← citeshttps://doi.org/10.1016/j.aca.2015.11.042openalex-snapshot
Trypsin immobilization in ordered porous polymer membranes for effective protein digestion
inferred← citeshttps://doi.org/10.1016/j.aca.2017.10.023openalex-snapshot
Integrated platform with combination of on-line protein digestion, isotope dimethyl labeling and multidimensional peptide separation for high-throughput proteome quantification
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.ijbiomac.2022.06.125openalex-snapshot
Novel biohybrid spongy scaffolds for fabrication of suturable intraoral graft substitutes
inferred← citeshttps://doi.org/10.1016/j.jprot.2018.11.002openalex-snapshot
Determination of food allergens by LC-MS: Impacts of sample preparation, food matrix, and thermal processing on peptide detectability and quantification
inferred← citeshttps://doi.org/10.1016/j.jprot.2024.105109openalex-snapshot
Optimal conditions for carrying out trypsin digestions on complex proteomes: From bulk samples to single cells
inferred← citeshttps://doi.org/10.1016/j.tifs.2018.04.008openalex-snapshot
Mass spectrometry based proteomics as foodomics tool in research and assurance of food quality and safety
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/acs.analchem.1c00965openalex-snapshot
Enhancing Comprehensive Analysis of Newly Synthesized Proteins Based on Cleavable Bioorthogonal Tagging
inferred← citeshttps://doi.org/10.1021/acs.analchem.5b00331openalex-snapshot
Quantitative Performance of Internal Standard Platforms for Absolute Protein Quantification Using Multiple Reaction Monitoring-Mass Spectrometry
inferred← citeshttps://doi.org/10.1021/acs.analchem.6b05071openalex-snapshot
Fluorous Solid-Phase Extraction Technique Based on Nanographite Fluoride
inferred← citeshttps://doi.org/10.1021/acs.analchem.7b03616openalex-snapshot
Investigating the Relationship between the Substrates’ Consumption and Their Abundances in a Complex Enzymatic System
inferred← citeshttps://doi.org/10.1021/acs.jproteome.6b00797openalex-snapshot
Thermal Shock Induces Host Proteostasis Disruption and Endoplasmic Reticulum Stress in the Model Symbiotic CnidarianAiptasia
inferred← citeshttps://doi.org/10.1021/acs.jproteome.8b00197openalex-snapshot
Surfactant and Chaotropic Agent Assisted Sequential Extraction/On-Pellet Digestion (SCAD) for Enhanced Proteomics
inferred← citeshttps://doi.org/10.1038/nmeth0314-347openalex-snapshot
Addendum: Digestion and depletion of abundant proteins improves proteomic coverage
inferred← citeshttps://doi.org/10.1039/c8an01330fopenalex-snapshot
Multi-lumen capillary based trypsin micro-reactor for the rapid digestion of proteins
inferred← citeshttps://doi.org/10.1039/d1fo00413aopenalex-snapshot
Protein acidification and hydrolysis by pepsin ensure efficient trypsin-catalyzed hydrolysis
inferred← citeshttps://doi.org/10.1039/d5cc02378eopenalex-snapshot
Beyond the known cuts: trypsin specificity in native proteins
inferred← citeshttps://doi.org/10.1074/mcp.m116.062869openalex-snapshot
Enzyme Kinetics for Complex System Enables Accurate Determination of Specificity Constants of Numerous Substrates in a Mixture by Proteomics Platform
inferred← citeshttps://doi.org/10.18174/564000openalex-snapshot
Plant proteins: from processing to digestion
inferred← citeshttps://doi.org/10.4155/fso.15.32openalex-snapshot
Ms for Investigation of Time-Dependent Protein Adsorption On Surfaces in Complex Biological Samples
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