Evidence map›Paper›PMID 42542536›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2026

Mass Spectrometry Analysis of Biotherapeutic Monoclonal Antibody Glycosylation.

Min Fang, Timothy R Rudd, Gail C Whiting

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Min FangMolecular Analysis, Medicines and Healthcare Products Regulatory Agency, Blanche Lane, South Mimms, EN6 3QG, UK.
Timothy R RuddMolecular Analysis, Medicines and Healthcare Products Regulatory Agency, Blanche Lane, South Mimms, EN6 3QG, UK.
Gail C WhitingMolecular Analysis, Medicines and Healthcare Products Regulatory Agency, Blanche Lane, South Mimms, EN6 3QG, UK. Gail.Whiting@mhra.gov.uk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosylation plays a critical role in the efficacy of therapeutic monoclonal antibodies (mAbs), the major category of glycoprotein-based therapeutic medicines. It is claimed that glycosylation of therapeutic mAbs has implications on their half-life, immunogenicity, and pharmacokinetics. Comprehensive characterization of glycosylation enables a deeper understanding of the complexity of therapeutic mAbs. The method presented here describes an integrated approach that incorporates filtered-aided sample preparation, mass spectrometry with different ion activation techniques, and a software that enables intact glycopeptide database search and de novo sequencing, to provide both N- and O-linked glycan profiling with structural resolution, without performing pre-glycoprotein/glycopeptide enrichment.

Indexed as

Antibodies, MonoclonalMass SpectrometryAnimalsGlycopeptidesGlycoproteinsGlycosylationHumansPolysaccharidesSoftwareAntibodies, MonoclonalGlycopeptidesGlycoproteinsPolysaccharidesDe-glycosylationFASPGlycosylationMass spectrometryPEAKS glycan searchTherapeutic monoclonal antibodyUnenriched intact glycopeptide

Identifiers

PMID42542536

What Socratic holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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 Socratic graph.