Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A novel method for in silico assessment of Methionine oxidation risk in monoclonal antibodies: Improvement over the 2-shell model

29 Dec 2022

Abstract excerpt

Over the past decade, therapeutic monoclonal antibodies (mAbs) have established their role as valuable agents in the treatment of various diseases ranging from cancers to infectious, cardiovascular and autoimmune diseases. Reactive groups of the amino acids within these proteins make them susceptible to many kinds of chemical modifications during manufacturing, storage and in vivo circulation. Among these...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Monoclonal and Polyclonal Antibodies Research
Share to Protein purification and stability
Share to Viral Infectious Diseases and Gene Expression in Insects

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 36580468
DOI: 10.1371/journal.pone.0279689

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A novel method for in silico assessment of Methionine oxidation risk in monoclonal antibodies: Improvement over the 2-shell modelPMID 36580468Read ↗

Understanding the impacts of dual methionine oxidations in complementarity-determining regions on the structure of monoclonal antibodiesSemantic proximity Read ↗

Rational design of oxidation-resistant antibodies through local electrostatic modulationSemantic proximity Read ↗

Structure-Based Prediction of Asparagine and Aspartate Degradation Sites in Antibody Variable RegionsSemantic proximity Read ↗

Prediction of Aggregation Prone Regions of Therapeutic ProteinsSemantic proximity Read ↗

Complementary MS methods assist conformational characterization of antibodies with altered S-S bonding networks.Semantic proximity Read ↗

Structure and stability changes of human IgG1 Fc as a consequence of methionine oxidation.Semantic proximity Read ↗

Machine Learning Enables Accurate Prediction of Asparagine Deamidation Probability and RateSemantic proximity Read ↗

In silico methods for immunogenicity risk assessment and human homology screening for therapeutic antibodiesSemantic proximity Read ↗

Increasing the melting temperature of VHH with the in silico free energy score.Semantic proximity Read ↗

Mass spectrometry-based multi-attribute method for mutation analysis in the early development of therapeutic proteins.Semantic proximity Read ↗

Mitigation of reversible self-association and viscosity in a human IgG1 monoclonal antibody by rational, structure-guided Fv engineeringSemantic proximity Read ↗

Predictive tools for stabilization of therapeutic proteinsSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.