Evidence map›Paper›PMID 23483515›Full record

ArticleJournal of the American Society for Mass Spectrometry2013

Complementary MS methods assist conformational characterization of antibodies with altered S-S bonding networks.

Lisa M Jones, Hao Zhang, Weidong Cui, Sandeep Kumar, Justin B Sperry, James A Carroll, Michael L Gross

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

21 citing papers in PubMed, 61 citations in OpenAlex.

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  12. Variation in FPOP Measurements Is Primarily Caused by Poor Peptide Signal Intensity.Journal of the American Society for Mass Spectrometry · 2018
    Article
  13. Article
  14. Intact Transition Epitope Mapping (ITEM).Journal of the American Society for Mass Spectrometry · 2017
    Article
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  19. Probing the paramyxovirus fusion (F) protein-refolding event from pre- to postfusion by oxidative footprinting.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  20. Article
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

7 authors at 2 institutions in 1 country.

Lisa M JonesDepartment of Chemistry, Washington University in St. Louis, One Brookings Drive, St. Louis, MO 63130, USA.
Hao Zhang
Weidong Cui
Sandeep Kumar
Justin B Sperry
James A Carroll
Michael L Gross
Washington University in St. Louis · USPfizer (United States) · US

Funding

TrainingP41GM103422 · NIGMS · WASHINGTON UNIVERSITY · PI YARASHESKI, KEVIN E · 2012 to 2019
$12.0M
High Field Fourier Transform Mass Spectrometer for Biomedical ApplicationsS10RR025101 · NCRR · WASHINGTON UNIVERSITY · PI GROSS, MICHAEL L · 2008 to 2008
$1.9M
NCRR NIH HHS S10 RR025101NIGMS NIH HHS 8 P41 GM103422-35NIGMS NIH HHS P41 GM103422
6 · The paper itself

Abstract

As therapeutic monoclonal antibodies (mAbs) become a major focus in biotechnology and a source of the next-generation drugs, new analytical methods or combination methods are needed for monitoring changes in higher order structure and effects of post-translational modifications. The complexity of these molecules and their vulnerability to structural change provide a serious challenge. We describe here the use of complementary mass spectrometry methods that not only characterize mutant mAbs but also may provide a general framework for characterizing higher order structure of other protein therapeutics and biosimilars. To frame the challenge, we selected members of the IgG2 subclass that have distinct disulfide isomeric structures as a model to evaluate an overall approach that uses ion mobility, top-down MS sequencing, and protein footprinting in the form of fast photochemical oxidation of proteins (FPOP). These three methods are rapid, sensitive, respond to subtle changes in conformation of Cys → Ser mutants of an IgG2, each representing a single disulfide isoform, and may be used in series to probe higher order structure. The outcome suggests that this approach of using various methods in combination can assist the development and quality control of protein therapeutics.

Indexed as

Amino Acid SequenceAnimalsAntibodies, MonoclonalDisulfidesHumansImmunoglobulin GIsomerismMass SpectrometryMiceModels, MolecularMolecular Sequence DataMutationOxidation-ReductionRecombinant ProteinsAntibodies, MonoclonalDisulfidesImmunoglobulin GRecombinant Proteins

Identifiers

PMID23483515
PMCPMC3651811
OpenAlexW2045138572

What OpenQuestion holds

Textmetadata
LicenceTDM
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 OpenQuestion graph.