Evidence map›Paper›PMID 42324012›Full record

ArticleInternational journal of biological macromolecules2026

Mass spectrometry-based mapping of conformational epitopes on SARS-CoV-2 antigens targeted by monoclonal antibodies.

Phumrapee Pianpaktr, Parawan Ramanandana, Saharat Nanthawong, Tossapon Wongtangprasert, Pijitra Saelao, Phijitra Muanwien, Chatikorn Boonkrai, Hasan Cicek, Dorota Focht, Raymond Kimbung and 6 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of biological macromolecules, 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

16 authors.

Phumrapee PianpaktrDepartment of Food and Pharmaceutical Chemistry, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Pathumwan, Bangkok, 10330, Thailand; Pharmaceutical Sciences and Technology (PST) Graduate Program, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Pathumwan, Bangkok, 10330, Thailand; Center of Excellence in Systems Biology (CUSB), Faculty of Medicine, Chulalongkorn University, Pathumwan, Bangkok, 10330, Thailand. Electronic address: p.pianpaktr@gmail.com.
Parawan RamanandanaDepartment of Food and Pharmaceutical Chemistry, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Pathumwan, Bangkok, 10330, Thailand; Pharmaceutical Sciences and Technology (PST) Graduate Program, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Pathumwan, Bangkok, 10330, Thailand; Center of Excellence in Systems Biology (CUSB), Faculty of Medicine, Chulalongkorn University, Pathumwan, Bangkok, 10330, Thailand; Department of Pharmaceutical Chemistry, Faculty of Pharmaceutical Sciences, Huachiew Chalermprakiet University, Bang Phli, Samut Prakan, 10540, Thailand. Electronic address: waew2.pr@gmail.com.
Saharat NanthawongCenter of Excellence in Systems Biology (CUSB), Faculty of Medicine, Chulalongkorn University, Pathumwan, Bangkok, 10330, Thailand. Electronic address: saharat.nanthawongb@gmail.com.
Tossapon WongtangprasertCenter of Excellence in Systems Biology (CUSB), Faculty of Medicine, Chulalongkorn University, Pathumwan, Bangkok, 10330, Thailand; The Excellence Chulalongkorn Comprehensive Cancer Center, King Chulalongkorn Memorial Hospital, Pathumwan, Bangkok, 10330, Thailand. Electronic address: cassavara@gmail.com.
Pijitra SaelaoCenter of Excellence in Systems Biology (CUSB), Faculty of Medicine, Chulalongkorn University, Pathumwan, Bangkok, 10330, Thailand. Electronic address: p.saelao11@gmail.com.
Phijitra MuanwienCenter of Excellence in Systems Biology (CUSB), Faculty of Medicine, Chulalongkorn University, Pathumwan, Bangkok, 10330, Thailand. Electronic address: phijitra.jame7@gmail.com.
Chatikorn BoonkraiCenter of Excellence in Systems Biology (CUSB), Faculty of Medicine, Chulalongkorn University, Pathumwan, Bangkok, 10330, Thailand. Electronic address: ctkorn@gmail.com.
Hasan CicekSARomics Biostructures AB, Medicon Village, Lund, 223 81, Sweden. Electronic address: hasan.cicek@saromics.com.
Dorota FochtSARomics Biostructures AB, Medicon Village, Lund, 223 81, Sweden. Electronic address: dorota.focht@saromics.com.
Raymond KimbungSARomics Biostructures AB, Medicon Village, Lund, 223 81, Sweden. Electronic address: Raymond.kimbung@saromics.com.
Martin WelinSARomics Biostructures AB, Medicon Village, Lund, 223 81, Sweden. Electronic address: martin.welin@saromics.com.
Vanessa L StahlDepartment of Chemistry, University of Massachusetts Amherst, Amherst, MA, 01003, United States. Electronic address: vstahl@umass.edu.
Eric M GrabanQuarryBio Inc., Bloomington, IN, 47404, United States. Electronic address: eric.graban@reclaim-rx.com.
Richard W VachetDepartment of Chemistry, University of Massachusetts Amherst, Amherst, MA, 01003, United States. Electronic address: rwvachet@chem.umass.edu.
Trairak PisitkunCenter of Excellence in Systems Biology (CUSB), Faculty of Medicine, Chulalongkorn University, Pathumwan, Bangkok, 10330, Thailand; Division of Research Affairs, Faculty of Medicine, Chulalongkorn University, Pathumwan, Bangkok, 10330, Thailand. Electronic address: trairak@gmail.com.
Patanachai K LimpikiratiDepartment of Food and Pharmaceutical Chemistry, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Pathumwan, Bangkok, 10330, Thailand; Pharmaceutical Sciences and Technology (PST) Graduate Program, Faculty of Pharmaceutical Sciences, Chulalongkorn University, Pathumwan, Bangkok, 10330, Thailand; Center of Excellence in Systems Biology (CUSB), Faculty of Medicine, Chulalongkorn University, Pathumwan, Bangkok, 10330, Thailand. Electronic address: patanachai.l@pharm.chula.ac.th.

Funding

Protein Amyloid Formation and Inhibition Studied by Mass SpectrometryR35GM145272 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI RICHARD W VACHET · 2022 to 2026
$2.0M
NIGMS NIH HHS R35 GM145272
6 · The paper itself

Abstract

The spike glycoprotein of SARS-CoV-2, particularly its receptor-binding domain (RBD), is a key target for therapeutic monoclonal antibodies (mAbs). Epitope mapping is therefore critical for the development of effective antiviral therapeutics. In this study, diethylpyrocarbonate covalent labeling mass spectrometry (DEPC CL-MS) was applied to map epitopes on the beta (B.1.351) and omicron (B.1.1.529) variants of the SARS-CoV-2 RBD, as well as on the original SARS-CoV-2 spike S

Indexed as

Antibodies, MonoclonalAntibodies, ViralAntigens, ViralEpitope MappingEpitopesSARS-CoV-2Spike Glycoprotein, CoronavirusHumansMass SpectrometryModels, MolecularTandem Mass SpectrometryAntibodies, MonoclonalAntibodies, ViralAntigens, ViralEpitopesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2Covalent labeling mass spectrometryEpitope mappingSARS-CoV-2 spike protein

Identifiers

PMID42324012
PMCPMC13359033

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.