ArticleChemometrics and intelligent laboratory systems : an international journal sponsored by the Chemometrics Society2020
Chemometric Outlier Classification of 2D-NMR Spectra to Enable Higher Order Structure Characterization of Protein Therapeutics.
Article in Chemometrics and intelligent laboratory systems : an international journal sponsored by the Chemometrics Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
9 citing papers in PubMed, 10 citations in OpenAlex.
- Recent Advances in Atomic-Resolution NMR Investigations of Monoclonal Antibodies.Biomolecules · 2026Review
- From Cloudy to Clear: A Strategy to Resolve the Complex Structural Elucidation of Bicycle Drug Conjugate Zelenectide Pevedotin by NMR.Bioconjugate chemistry · 2026Article
- Article
- Assessment of ADC Higher Order Structure Through 2D NMR Analysis.Molecules (Basel, Switzerland) · 2025Article
- Structural Relationships to Efficacy for Prazole-Derived Antivirals.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Structural Fingerprinting of siRNA Therapeutics by Solution NMR Spectroscopy.Nucleic acid therapeutics · 2022Article
- Analytical Similarity Assessment of Biosimilars: Global Regulatory Landscape, Recent Studies and Major Advancements in Orthogonal Platforms.Frontiers in bioengineering and biotechnology · 2022Review
- Interlaboratory Studies Using the NISTmAb to Advance Biopharmaceutical Structural Analytics.Frontiers in molecular biosciences · 2022Review
- Principal component analysis for automated classification of 2D spectra and interferograms of protein therapeutics: influence of noise, reconstruction details, and data preparation.Journal of biomolecular NMR · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Protein therapeutics are vitally important clinically and commercially, with monoclonal antibody (mAb) therapeutic sales alone accounting for $115 billion in revenue for 2018.[1] In order for these therapeutics to be safe and efficacious, their protein components must maintain their high order structure (HOS), which includes retaining their three-dimensional fold and not forming aggregates. As demonstrated in the recent NISTmAb Interlaboratory nuclear magnetic resonance (NMR) Study[2], NMR spectroscopy is a robust and precise approach to address this HOS measurement need. Using the NISTmAb study data, we benchmark a procedure for automated outlier detection used to identify spectra that are not of sufficient quality for further automated analysis. When applied to a diverse collection of all 252
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.