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Biopharmaceutical Quality Control with Mass Spectrometry
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Outgoing claims: the papers this work cites, builds on, or argues with.
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Exploring an Orbitrap Analyzer for the Characterization of Intact Antibodies by Native Mass Spectrometry
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Progress in biopharmaceutical development
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Host cell protein testing by ELISAs and the use of orthogonal methods
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Enzymatic removal of N‐glycans by PNGase F coated magnetic microparticles
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Adding a new separation dimension to MS and LC–MS: What is the utility of ion mobility spectrometry?
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Methods to improve quantitative glycoprotein coverage from bottom‐up LC‐MS data
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MS‐based glycomics and glycoproteomics methods enabling isomeric characterization
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Quantification of proteins using data‐independent analysis (MSE) in simple andcomplex samples: A systematic evaluation
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The top‐down, middle‐down, and bottom‐up mass spectrometry approaches for characterization of histone variants and their post‐translational modifications
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Automated measurement of site‐specific N‐glycosylation occupancy with SWATH‐MS
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Improved detection of host cell proteins (HCPs) in a mammalian cell‐derived antibody drug using liquid chromatography/mass spectrometry in conjunction with an HCP‐enrichment strategy
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Comparison of gas chromatography/quadrupole time‐of‐flight and quadrupole Orbitrap mass spectrometry in anti‐doping analysis: I. Detection of anabolic‐androgenic steroids
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Quantitative Methods in Proteomics
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Automated Workflow for Peptide-Level Quantitation from DIA/SWATH-MS Data
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Spectral Counting Label-Free Proteomics
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Separation and Purification of Amino Acids
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Application of amide hydrogen/deuterium exchange mass spectrometry for epitope mapping in human cystatin C
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Modifications of therapeutic proteins: challenges and prospects
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Liquid chromatography-tandem mass spectrometry-based fragmentation analysis of glycopeptides
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Post-translational Modifications of Recombinant Proteins: Significance for Biopharmaceuticals
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Posttranslational Modifications: Key Players in Health and Disease
inferredcites →https://doi.org/10.1016/b978-0-12-821618-7.00067-5openalex-snapshot
Posttranslational Modifications: Key Players in Health and Disease
inferredcites →https://doi.org/10.1016/j.ab.2020.113972openalex-snapshot
Improved host cell protein analysis in monoclonal antibody products through ProteoMiner
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Hydrogen/deuterium exchange mass spectrometry with improved electrochemical reduction enables comprehensive epitope mapping of a therapeutic antibody to the cysteine-knot containing vascular endothelial growth factor
inferredcites →https://doi.org/10.1016/j.bbapap.2016.08.013openalex-snapshot
Comparative higher-order structure analysis of antibody biosimilars using combined bottom-up and top-down hydrogen-deuterium exchange mass spectrometry
inferredcites →https://doi.org/10.1016/j.bjm.2016.10.007openalex-snapshot
Biopharmaceuticals from microorganisms: from production to purification
inferredcites →https://doi.org/10.1016/j.cbpa.2017.11.010openalex-snapshot
Collision induced unfolding of isolated proteins in the gas phase: past, present, and future
inferredcites →https://doi.org/10.1016/j.copbio.2014.06.017openalex-snapshot
Measurement and control of host cell proteins (HCPs) in CHO cell bioprocesses
inferredcites →https://doi.org/10.1016/j.jasms.2008.09.005openalex-snapshot
A versatile microfluidic chip for millisecond time-scale kinetic studies by electrospray mass spectrometry
inferredcites →https://doi.org/10.1016/j.jchromb.2018.04.010openalex-snapshot
Hyphenation of size exclusion chromatography to native ion mobility mass spectrometry for the analytical characterization of therapeutic antibodies and related products
inferredcites →https://doi.org/10.1016/j.jconrel.2018.01.018openalex-snapshot
Bioorthogonal strategies for site-directed decoration of biomaterials with therapeutic proteins
inferredcites →https://doi.org/10.1016/j.jpba.2020.113256openalex-snapshot
Improved identification of host cell proteins in a protein biopharmaceutical by LC–MS/MS using the ProteoMiner™ Enrichment Kit
inferredcites →https://doi.org/10.1016/j.jpba.2020.113395openalex-snapshot
Development of a targeted nanoLC-MS/MS method for quantitation of residual toxins from Bordetella pertussis
inferredcites →https://doi.org/10.1016/j.jpba.2021.114069openalex-snapshot
Toward unbiased identification and comparative quantification of host cell protein impurities by automated iterative LC–MS/MS (HCP-AIMS) for therapeutic protein development
inferredcites →https://doi.org/10.1016/j.jprot.2019.03.005openalex-snapshot
Label-free absolute protein quantification with data-independent acquisition
inferredcites →https://doi.org/10.1016/j.micpath.2018.09.006openalex-snapshot
Stable isotope labelling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Edwardsiella tarda ATCC 15947 under prolonged cold stress
inferredcites →https://doi.org/10.1016/j.nbt.2011.03.015openalex-snapshot
Advances in the production and downstream processing of antibodies
inferredcites →https://doi.org/10.1016/j.trac.2018.06.008openalex-snapshot
Conformational analysis of complex protein states by hydrogen/deuterium exchange mass spectrometry (HDX-MS): Challenges and emerging solutions
inferredcites →https://doi.org/10.1016/s1387-2656(03)09008-2openalex-snapshot
The state of biopharmaceutical manufacturing
inferredcites →https://doi.org/10.1021/ac010617eopenalex-snapshot
An Automated Multidimensional Protein Identification Technology for Shotgun Proteomics
inferredcites →https://doi.org/10.1021/ac0341261openalex-snapshot
A Statistical Model for Identifying Proteins by Tandem Mass Spectrometry
inferredcites →https://doi.org/10.1021/ac501789eopenalex-snapshot
Approach to Characterization of the Higher Order Structure of Disulfide-Containing Proteins Using Hydrogen/Deuterium Exchange and Top-Down Mass Spectrometry
inferredcites →https://doi.org/10.1021/ac901366nopenalex-snapshot
H/D Exchange and Mass Spectrometry in the Studies of Protein Conformation and Dynamics: Is There a Need for a Top-Down Approach?
inferredcites →https://doi.org/10.1021/acs.analchem.0c00293openalex-snapshot
Middle Level IM–MS and CIU Experiments for Improved Therapeutic Immunoglobulin Subclass Fingerprinting
inferredcites →https://doi.org/10.1021/acs.analchem.0c00360openalex-snapshot
Enhancing Host-Cell Protein Detection in Protein Therapeutics Using HILIC Enrichment and Proteomic Analysis
inferredcites →https://doi.org/10.1021/acs.analchem.0c00772openalex-snapshot
Collision-Induced Unfolding Studies of Proteins and Protein Complexes using Drift Tube Ion Mobility-Mass Spectrometer
inferredcites →https://doi.org/10.1021/acs.analchem.0c01175openalex-snapshot
Combination of FAIMS, Protein A Depletion, and Native Digest Conditions Enables Deep Proteomic Profiling of Host Cell Proteins in Monoclonal Antibodies
inferredcites →https://doi.org/10.1021/acs.analchem.0c01954openalex-snapshot
Utility of Ion-Mobility Spectrometry for Deducing Branching of Multiply Charged Glycans and Glycopeptides in a High-Throughput Positive ion LC-FLR-IMS-MS Workflow
inferredcites →https://doi.org/10.1021/acs.analchem.0c02258openalex-snapshot
Fast, Robust, and Sensitive Identification of Residual Host Cell Proteins in Recombinant Monoclonal Antibodies Using Sodium Deoxycholate Assisted Digestion
inferredcites →https://doi.org/10.1021/acs.analchem.5b01377openalex-snapshot
Quantitative Host Cell Protein Analysis Using Two Dimensional Data Independent LC–MSE
inferredcites →https://doi.org/10.1021/acs.analchem.8b01865openalex-snapshot
Online Hydrophobic Interaction Chromatography–Mass Spectrometry for the Analysis of Intact Monoclonal Antibodies
inferredcites →https://doi.org/10.1021/acs.analchem.9b03952openalex-snapshot
Targeted Host Cell Protein Quantification by LC–MRM Enables Biologics Processing and Product Characterization
inferredcites →https://doi.org/10.1021/acs.analchem.9b05081openalex-snapshot
Improved Host Cell Protein Analysis in Monoclonal Antibody Products through Molecular Weight Cutoff Enrichment
inferredcites →https://doi.org/10.1021/acs.biochem.0c00308openalex-snapshot
Epitope Mapping for a Preclinical Bevacizumab (Avastin) Biosimilar on an Extended Construct of Vascular Endothelial Growth Factor A Using Millisecond Hydrogen–Deuterium Exchange Mass Spectrometry
inferredcites →https://doi.org/10.1021/acs.jproteome.0c00218openalex-snapshot
Optimal Dissociation Methods Differ for N - and O -Glycopeptides
inferredcites →https://doi.org/10.1021/acs.jproteome.0c00252openalex-snapshot
Sensitive, Rapid, Robust, and Reproducible Workflow for Host Cell Protein Profiling in Biopharmaceutical Process Development
inferredcites →https://doi.org/10.1021/acs.jproteome.0c00664openalex-snapshot
Optimized Sample Preparation and Data Processing of Data-Independent Acquisition Methods for the Robust Quantification of Trace-Level Host Cell Protein Impurities in Antibody Drug Products
inferredcites →https://doi.org/10.1021/acs.jproteome.5b00997openalex-snapshot
Quantitation and Identification of Thousands of Human Proteoforms below 30 kDa
inferredcites →https://doi.org/10.1021/acs.molpharmaceut.8b00941openalex-snapshot
Quantification of Proteins Involved in Drug Metabolism and Disposition in the Human Liver Using Label-Free Global Proteomics
inferredcites →https://doi.org/10.1021/bm700540popenalex-snapshot
Delivery of Large Biopharmaceuticals from Cardiovascular Stents: A Review
inferredcites →https://doi.org/10.1021/cr3003533openalex-snapshot
Protein Analysis by Shotgun/Bottom-up Proteomics
inferredcites →https://doi.org/10.1021/ja507880wopenalex-snapshot
Subzero Temperature Chromatography and Top-Down Mass Spectrometry for Protein Higher-Order Structure Characterization: Method Validation and Application to Therapeutic Antibodies
inferredcites →https://doi.org/10.1021/ja805573hopenalex-snapshot
Electron Transfer Dissociation Facilitates the Measurement of Deuterium Incorporation into Selectively Labeled Peptides with Single Residue Resolution
inferredcites →https://doi.org/10.1021/pr3003722openalex-snapshot
Methylation of γ-Carboxylated Glu (Gla) Allows Detection by Liquid Chromatography–Mass Spectrometry and the Identification of Gla Residues in the γ-Glutamyl Carboxylase
inferredcites →https://doi.org/10.1038/85686openalex-snapshot
Large-scale analysis of the yeast proteome by multidimensional protein identification technology
inferredcites →https://doi.org/10.1038/nature10575openalex-snapshot
Mapping intact protein isoforms in discovery mode using top-down proteomics
inferredcites →https://doi.org/10.1038/ncomms13397openalex-snapshot
Hybrid mass spectrometry approaches in glycoprotein analysis and their usage in scoring biosimilarity
inferredcites →https://doi.org/10.1038/nprot.2016.042openalex-snapshot
Label-free quantification in ion mobility–enhanced data-independent acquisition proteomics
inferredcites →https://doi.org/10.1038/s42003-021-01903-xopenalex-snapshot
Coagulation factor IX analysis in bioreactor cell culture supernatant predicts quality of the purified product
inferredcites →https://doi.org/10.1038/srep25289openalex-snapshot
Combination of ESI and MALDI mass spectrometry for qualitative, semi-quantitative and in situ analysis of gangliosides in brain
inferredcites →https://doi.org/10.1039/c3lc00007aopenalex-snapshot
An electrospray ms-coupled microfluidic device for sub-second hydrogen/deuterium exchange pulse-labelling reveals allosteric effects in enzyme inhibition
inferredcites →https://doi.org/10.1039/c8sc05029eopenalex-snapshot
Hybrid mass spectrometry methods reveal lot-to-lot differences and delineate the effects of glycosylation on the tertiary structure of Herceptin®
inferredcites →https://doi.org/10.1039/c8sm00919hopenalex-snapshot
Characterisation of protein aggregation with the Smoluchowski coagulation approach for use in biopharmaceuticals
inferredcites →https://doi.org/10.1039/c9an02081kopenalex-snapshot
N -Glycosylation profiling of intact target proteins by high-resolution mass spectrometry (MS) and glycan analysis using ion mobility-MS/MS
inferredcites →https://doi.org/10.1073/pnas.0832254100openalex-snapshot
Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
inferredcites →https://doi.org/10.1074/jbc.m114.595454openalex-snapshot
Changes in Signal Transducer and Activator of Transcription 3 (STAT3) Dynamics Induced by Complexation with Pharmacological Inhibitors of Src Homology 2 (SH2) Domain Dimerization
inferredcites →https://doi.org/10.1074/mcp.o115.057638openalex-snapshot
Maturing Glycoproteomics Technologies Provide Unique Structural Insights into the N-glycoproteome and Its Regulation in Health and Disease
inferredcites →https://doi.org/10.1074/mcp.r120.002204openalex-snapshot
The Role of Data-Independent Acquisition for Glycoproteomics
inferredcites →https://doi.org/10.1074/mcp.r120.002263openalex-snapshot
Glycomics, Glycoproteomics, and Glycogenomics: An Inter-Taxa Evolutionary Perspective
inferredcites →https://doi.org/10.1080/19420862.2017.1379641openalex-snapshot
Suppressing allostery in epitope mapping experiments using millisecond hydrogen / deuterium exchange mass spectrometry
inferredcites →https://doi.org/10.1080/21655979.2016.1229718openalex-snapshot
The evolution of recombinant thrombolytics: Current status and future directions
inferredcites →https://doi.org/10.1101/2021.03.14.435332openalex-snapshot
Community Evaluation of Glycoproteomics Informatics Solutions Reveals High-Performance Search Strategies of Serum N - and O -Glycopeptide Data
inferredcites →https://doi.org/10.1111/febs.12332openalex-snapshot
Characterizing rapid, activity‐linked conformational transitions in proteins via sub‐second hydrogen deuterium exchange mass spectrometry
inferredcites →https://doi.org/10.1111/jcmm.14459openalex-snapshot
Isobaric tag for relative and absolute quantitation based quantitative proteomics reveals unique urinary protein profiles in patients with preeclampsia
inferredcites →https://doi.org/10.1126/science.abb9983openalex-snapshot
Site-specific glycan analysis of the SARS-CoV-2 spike
inferredcites →https://doi.org/10.1128/cmr.00072-12openalex-snapshot
Matrix-Assisted Laser Desorption Ionization–Time of Flight Mass Spectrometry: a Fundamental Shift in the Routine Practice of Clinical Microbiology
inferredcites →https://doi.org/10.1155/2016/5358272openalex-snapshot
Posttranslational Modifications and the Immunogenicity of Biotherapeutics
inferredcites →https://doi.org/10.1186/s12934-014-0141-0openalex-snapshot
Cell factories for insulin production
inferredcites →https://doi.org/10.1371/journal.pone.0241310openalex-snapshot
Comparative proteomic analysis of silica-induced pulmonary fibrosis in rats based on tandem mass tag (TMT) quantitation technology
inferredcites →https://doi.org/10.2144/000112201openalex-snapshot
Analysis of Posttranslational Modifications of Proteins by Tandem Mass Spectrometry
inferredcites →https://doi.org/10.3109/09546634.2015.1054782openalex-snapshot
Biologics and biosimilars
inferredcites →https://doi.org/10.3389/fbioe.2019.00420openalex-snapshot
Recent Developments in Bioprocessing of Recombinant Proteins: Expression Hosts and Process Development
inferredcites →https://doi.org/10.3389/fpls.2019.00261openalex-snapshot
Critical Evaluation of Strategies for the Production of Blood Coagulation Factors in Plant-Based Systems
inferredcites →https://doi.org/10.3390/biomedicines8070224openalex-snapshot
HDX-MS: An Analytical Tool to Capture Protein Motion in Action
inferredcites →https://doi.org/10.3390/molecules23102557openalex-snapshot
Applications of Ion Mobility-Mass Spectrometry in Carbohydrate Chemistry and Glycobiology
inferredcites →https://doi.org/10.4137/cin.s385openalex-snapshot
Comparison of a Label-Free Quantitative Proteomic Method Based on Peptide Ion Current Area to the Isotope Coded Affinity Tag Method
inferredcites →https://doi.org/10.4161/mabs.2.5.12720openalex-snapshot
Cell culture processes for monoclonal antibody production
inferredcites →https://doi.org/10.4310/sii.2012.v5.n1.a7openalex-snapshot
Analyzing LC-MS/MS data by spectral count and ion abundance: two case studies
inferredcites →https://doi.org/10.5772/intechopen.79194openalex-snapshot
Introductory Chapter: Biopharmaceuticals
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Stochastic Dynamics Mass Spectrometry of Caffeine Metabolites
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Machine Learning Meets Mass Spectrometry: a Focused Perspective
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Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2021–2022
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Proteomics and glycoproteomics of beer and wine
inferred← citeshttps://doi.org/10.1002/pro.4612openalex-snapshot
Dissecting the structural heterogeneity of proteins by native mass spectrometry
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Purification and separation of bioproducts from yeast cells cultivated on lignocellulosic hydrolysates
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Stochastic dynamic quantitative and 3D structural matrix assisted laser desorption/ionization mass spectrometric analyses of mixture of nucleosides
inferred← citeshttps://doi.org/10.1016/j.steroids.2022.109001openalex-snapshot
Mass spectrometric stochastic dynamic 3D structural analysis of mixture of steroids in solution – Experimental and theoretical study
inferred← citeshttps://doi.org/10.1016/j.tibtech.2025.07.026openalex-snapshot
Advanced mass spectrometry techniques for monitoring biopharmaceutical host cell proteins
inferred← citeshttps://doi.org/10.1016/j.xphs.2026.104302openalex-snapshot
Divergent host cell protein profiles during special purification of biologics from prokaryotic versus eukaryotic systems dictate the need for tailored ELISA assay development
inferred← citeshttps://doi.org/10.1021/acs.analchem.2c03820openalex-snapshot
Optimized Multi-Attribute Method Workflow Addressing Missed Cleavages and Chromatographic Tailing/Carry-Over of Hydrophobic Peptides
inferred← citeshttps://doi.org/10.1021/acs.analchem.3c02609openalex-snapshot
Addressing Acid-Catalyzed Deamidation and the Solubility of Hydrophobic Peptides in Multi-Attribute Method Workflows
inferred← citeshttps://doi.org/10.1021/acs.jproteome.6c00097openalex-snapshot
Integrated Effects of Digestion Strategy and LC Gradient Architecture Define Host Cell Protein Detectability in CHO Null Harvests
inferred← citeshttps://doi.org/10.1038/s41598-024-70914-5openalex-snapshot
Rapid identification of antibody impurities in size-based electrophoresis via CZE-MS generated spectral library
inferred← citeshttps://doi.org/10.1080/28378083.2025.2512237openalex-snapshot
Advanced site-specific analysis of insulin-PEG conjugates using MALDI-MS
inferred← citeshttps://doi.org/10.3389/fphar.2023.1110900openalex-snapshot
Extractive electrospray ionization mass spectrometry for analytical evaluation and synthetic preparation of pharmaceutical chemicals
inferred← citeshttps://doi.org/10.3390/antib13030066openalex-snapshot
Enhanced N-Glycan Profiling of Therapeutic Monoclonal Antibodies through the Application of Upper-Hinge Middle-Up Level LC-HRMS Analysis
inferred← citeshttps://doi.org/10.64898/2026.05.21.727034openalex-snapshot
Systematic characterization of the yeast secretome under diverse proteosynthetic stress conditions reveals secretion of functional ER chaperone BiP
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