Evidence map›Paper›PMID 29712889›Full record

ArticleNature communications2018

Native mass spectrometry combined with enzymatic dissection unravels glycoform heterogeneity of biopharmaceuticals.

Therese Wohlschlager, Kai Scheffler, Ines C Forstenlehner, Wolfgang Skala, Stefan Senn, Eugen Damoc, Johann Holzmann, Christian G Huber

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
6.1field-weighted citation impact, top 3% of its field
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

43 citing papers in PubMed, 116 citations in OpenAlex.

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  7. AsymmetricJournal of the American Chemical Society · 2024
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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

8 authors at 2 institutions in 2 countries.

Therese WohlschlagerDepartment of Biosciences, Bioanalytical Research Labs, University of Salzburg, Hellbrunner Strasse 34, 5020, Salzburg, Austria.ORCID http://orcid.org/0000-0001-9359-6744
Kai SchefflerChristian Doppler Laboratory for Innovative Tools for Biosimilar Characterization, University of Salzburg, Hellbrunner Strasse 34, 5020, Salzburg, Austria.
Ines C ForstenlehnerDepartment of Biosciences, Bioanalytical Research Labs, University of Salzburg, Hellbrunner Strasse 34, 5020, Salzburg, Austria.
Wolfgang SkalaDepartment of Biosciences, Bioanalytical Research Labs, University of Salzburg, Hellbrunner Strasse 34, 5020, Salzburg, Austria.
Stefan SennDepartment of Biosciences, Bioanalytical Research Labs, University of Salzburg, Hellbrunner Strasse 34, 5020, Salzburg, Austria.
Eugen DamocThermo Fisher Scientific GmbH, Hanna-Kunath-Strasse 11, 28199, Bremen, Germany.
Johann HolzmannChristian Doppler Laboratory for Innovative Tools for Biosimilar Characterization, University of Salzburg, Hellbrunner Strasse 34, 5020, Salzburg, Austria.
Christian G HuberDepartment of Biosciences, Bioanalytical Research Labs, University of Salzburg, Hellbrunner Strasse 34, 5020, Salzburg, Austria. c.huber@sbg.ac.at.ORCID http://orcid.org/0000-0001-8358-1880
University of Salzburg · ATThermo Fisher Scientific (Germany) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Robust manufacturing processes resulting in consistent glycosylation are critical for the efficacy and safety of biopharmaceuticals. Information on glycosylation can be obtained by conventional bottom-up methods but is often limited to the glycan or glycopeptide level. Here, we apply high-resolution native mass spectrometry (MS) for the characterization of the therapeutic fusion protein Etanercept to unravel glycoform heterogeneity in conditions of hitherto unmatched mass spectral complexity. Higher spatial resolution at lower charge states, an inherent characteristic of native MS, represents a key component for the successful revelation of glycan heterogeneity. Combined with enzymatic dissection using a set of proteases and glycosidases, assignment of specific glycoforms is achieved by transferring information from subunit to whole protein level. The application of native mass spectrometric analysis of intact Etanercept as a fingerprinting tool for the assessment of batch-to-batch variability is exemplified and may be extended to demonstrate comparability after changes in the biologic manufacturing process.

Identifiers

PMID29712889
PMCPMC5928108
OpenAlexW2805894928

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.