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Separation of mAbs molecular variants by analytical hydrophobic interaction chromatography HPLC: overview and applications
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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Developability Index: A Rapid In Silico Tool for the Screening of Antibody Aggregation Propensity
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High-performance hydrophobic-interaction chromatography of proteins on a series of poly(alkyl aspart-amide)-silicas
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Microheterogeneity of a purified IgG1, due to asymmetric fab glycosylation
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Single-step purification of F(ab′)2μ fragments of mouse monoclonal antibodies (immunoglobulins M) by hydrophobic interaction high-performance liquid chromatography using TSKgel Ether-5PW
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Separation of populations of antibody variants by fine tuning of hydrophobic-interaction chromatography operating conditions
inferredcites →https://doi.org/10.1016/j.chroma.2010.10.107openalex-snapshot
Separation of oxidized variants of a monoclonal antibody by anion-exchange
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Impact of short range hydrophobic interactions and long range electrostatic forces on the aggregation kinetics of a monoclonal antibody and a dual-variable domain immunoglobulin at low and high concentrations
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Liquid chromatography of recombinant proteins and protein drugs
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HIC resolution of an IgG1 with an oxidized Trp in a complementarity determining region
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Aggregation-Prone Motifs in Human Immunoglobulin G
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The effects of arginine on protein binding and elution in hydrophobic interaction and ion-exchange chromatography
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Hydrophobic interaction chromatography of proteins
inferredcites →https://doi.org/10.1016/s0731-7085(97)00153-2openalex-snapshot
An adaptation of hydrophobic interaction chromatography for estimation of protein solubility optima
inferredcites →https://doi.org/10.1021/ac702245copenalex-snapshot
Separation and Characterization of an IgG2 Antibody Containing a Cyclic Imide in CDR1 of Light Chain by Hydrophobic Interaction Chromatography and Mass Spectrometry
inferredcites →https://doi.org/10.1021/bi061500topenalex-snapshot
Aspartate Isomerization in the Complementarity-Determining Regions of Two Closely Related Monoclonal Antibodies
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Structure-Immunogenicity Relationships of Therapeutic Proteins
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Characterizing biological products and assessing comparability following manufacturing changes
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Natural expansion of the genetic code
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Design of therapeutic proteins with enhanced stability
inferredcites →https://doi.org/10.1074/jbc.m110.160457openalex-snapshot
Classification and Characterization of Therapeutic Antibody Aggregates
inferredcites →https://doi.org/10.1093/glycob/cwn116openalex-snapshot
O-Fucosylation of an antibody light chain: Characterization of a modification occurring on an IgG1 molecule
inferredcites →https://doi.org/10.1093/protein/gzq037openalex-snapshot
Structure-based engineering of a monoclonal antibody for improved solubility
inferredcites →https://doi.org/10.1093/protein/gzs042openalex-snapshot
Aggregation-resistant domain antibodies engineered with charged mutations near the edges of the complementarity-determining regions
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Effects of Drug Loading on the Antitumor Activity of a Monoclonal Antibody Drug Conjugate
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Fast identification of folded human protein domains expressed in E. coli suitable for structural analysis
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Biosimilar monoclonal antibodies: a science-based regulatory challenge
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Soluble tumor necrosis factor (TNF) receptors are effective therapeutic agents in lethal endotoxemia and function simultaneously as both TNF carriers and TNF antagonists.
inferredcites →https://doi.org/10.4161/mabs.21328openalex-snapshot
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Comparison of the in vitro and in vivo stability of a succinimide intermediate observed on a therapeutic IgG1 molecule
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Developability studies before initiation of process development
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Analytical methods for physicochemical characterization of antibody drug conjugates
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Conformational stability and aggregation of therapeutic monoclonal antibodies studied with ANS and Thioflavin T binding
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Oxidation in the complementarity-determining regions differentially influences the properties of therapeutic antibodies
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Blueprint for antibody biologics developability
inferred← citeshttps://doi.org/10.1080/19420862.2023.2215887openalex-snapshot
Design of antibody variable fragments with reduced reactivity to preexisting anti-drug antibodies
inferred← citeshttps://doi.org/10.1080/19420862.2023.2256745openalex-snapshot
Development of in silico models to predict viscosity and mouse clearance using a comprehensive analytical data set collected on 83 scaffold-consistent monoclonal antibodies
inferred← citeshttps://doi.org/10.1080/19420862.2024.2362788openalex-snapshot
Molecular surface descriptors to predict antibody developability: sensitivity to parameters, structure models, and conformational sampling
inferred← citeshttps://doi.org/10.1080/19420862.2025.2474521openalex-snapshot
PROPERMAB: an integrative framework for in silico prediction of antibody developability using machine learning
inferred← citeshttps://doi.org/10.1080/21645515.2022.2122507openalex-snapshot
Advancing humanized monoclonal antibody for counteracting fentanyl toxicity towards clinical development
inferred← citeshttps://doi.org/10.1093/protein/gzag003openalex-snapshot
VIF-Ig: a novel fc framework for ADCC by incorporation of VHH unit
inferred← citeshttps://doi.org/10.1101/2023.07.18.549448openalex-snapshot
Molecular Surface Descriptors to Predict Antibody Developability
inferred← citeshttps://doi.org/10.1248/cpb.c21-00258openalex-snapshot
Recent Advances in Drug–Antibody Ratio Determination of Antibody–Drug Conjugates
inferred← citeshttps://doi.org/10.1371/journal.pone.0210712openalex-snapshot
Therapeutic Fc fusion protein misfolding: A three-phasic cultivation experimental design
inferred← citeshttps://doi.org/10.1371/journal.pone.0336791openalex-snapshot
Multispecific antibodies: Bioanalytics for early-stage screening and characterization of mispairing profiles
inferred← citeshttps://doi.org/10.1586/14789450.2016.1132167openalex-snapshot
Cutting-edge mass spectrometry methods for the multi-level structural characterization of antibody-drug conjugates
inferred← citeshttps://doi.org/10.17760/d20259955openalex-snapshot
Top-down proteomic analysis of protein pharmaceuticals, mixtures of protein complexes, and ribosomal protein extracts by capillary zone electrophoresis-mass spectrometry
inferred← citeshttps://doi.org/10.33612/diss.603403111openalex-snapshot
Bioanalytical methodology to study the in vivo biotransformation of therapeutic proteins
inferred← citeshttps://doi.org/10.3389/fmolb.2022.960194openalex-snapshot
Comparison of hydrophobicity scales for predicting biophysical properties of antibodies
inferred← citeshttps://doi.org/10.3390/biom14080999openalex-snapshot
Charge Variants Characterization of Co-Formulated Antibodies by Three-Dimensional Liquid Chromatography–Mass Spectrometry
inferred← citeshttps://doi.org/10.3390/ijms21218037openalex-snapshot
QSAR Implementation for HIC Retention Time Prediction of mAbs Using Fab Structure: A Comparison between Structural Representations
inferred← citeshttps://doi.org/10.5282/edoc.17528openalex-snapshot
Influence of the antibody variable domain on FcRn-dependent pharmacokinetics
inferred← citeshttps://doi.org/10.5772/intechopen.89644openalex-snapshot
Preparing Proteoforms of Therapeutic Proteins for Top-Down Mass Spectrometry
inferred← citeshttps://doi.org/10.70675/94501199z1059z4dbez9356za0cd21ee3d9copenalex-snapshot
Hyphenation of non-denaturing liquid chromatography to native mass spectrometry for therapeutic protein characterization
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