Evidence map›Paper›PMID 35037700›Full record

ArticleProteins2022

Crystal structure of a human MUC16 SEA domain reveals insight into the nature of the CA125 tumor marker.

Brandy White, Michelle Patterson, Saloni Karnwal, Cory L Brooks

Open access · greenAbstract read
In one paragraph

Article in Proteins, 2022. 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
2.3field-weighted citation impact, top 11% 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, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Personalizing CA125 Levels Using Tumor Marker Variants: A Case-Control Analysis of Diagnostic Performance for Pancreatic Cancer.Cancer epidemiology, biomarkers & prevention : a publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Critical Roles of SEA Domains.Advances in experimental medicine and biology · 2025
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  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

4 authors at 1 institution in 1 country.

Brandy WhiteDepartment of Chemistry and Biochemistry, California State University Fresno, Fresno, California, USA.
Michelle PattersonDepartment of Chemistry and Biochemistry, California State University Fresno, Fresno, California, USA.
Saloni KarnwalDepartment of Chemistry and Biochemistry, California State University Fresno, Fresno, California, USA.
Cory L BrooksDepartment of Chemistry and Biochemistry, California State University Fresno, Fresno, California, USA.ORCID 0000-0002-6745-6526
California State University, Fresno · US

Funding

Role of Antigen Glycosylation in Mucin Binding by Monoclonal AntibodiesR15CA242349 · NCI · CALIFORNIA STATE UNIVERSITY FRESNO · PI BROOKS, CORY · 2020 to 2020
$415k
CIHRNCI NIH HHS R15 CA242349
6 · The paper itself

Abstract

MUC16 is a membrane bound glycoprotein involved in the progression and metastasis of pancreatic and ovarian cancer. The protein is shed into the serum and the resulting cancer antigen 125 (CA125) can be detected by immunoassays. The CA125 epitope is used for monitoring ovarian cancer treatment progression, and has emerged as a potential target for antibody mediated immunotherapy. The extracellular tandem repeat domain of the protein is composed of repeating segments of heavily glycosylated sequence intermixed with homologous SEA (Sperm protein, Enterokinase and Agrin) domains. Here we report the purification and the first X-ray structure of a human MUC16 SEA domain. The structure was solved by molecular replacement using a Rosetta generated structure as a search model. The SEA domain reacted with three different MUC16 therapeutic antibodies, confirming that the CA125 epitope is localized to the SEA domain. The structure revealed a canonical ferredoxin-like fold, and contained a conserved disulfide bond. Analysis of the relative solvent accessibility of side chains within the SEA domain clarified the assignment of N-linked and O-linked glycosylation sites within the domain. A model of the glycosylated SEA domain revealed two major accessible faces, which likely represent the binding sites of CA125 specific antibodies. The results presented here will serve to accelerate future work to understand the functional role of MUC16 SEA domains and antibody recognition of the CA125 epitope.

Indexed as

CA-125 AntigenMembrane ProteinsOvarian NeoplasmsAntibodiesBiomarkers, TumorEpitopesFemaleHumansAntibodiesBiomarkers, TumorCA-125 AntigenEpitopesMembrane ProteinsMUC16 protein, humanCA125mucinovarian cancerpancreatic cancerunknown function

Identifiers

PMID35037700
PMCPMC9007846
OpenAlexW4206784414

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.