ArticleJournal of proteome research2016
Protein-Specific Differential Glycosylation of Immunoglobulins in Serum of Ovarian Cancer Patients.
Article in Journal of proteome research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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.
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.
Who cites it
38 citing papers in PubMed, 74 citations in OpenAlex.
- N-Glycosylation of Antibodies: Biological Effects During Infections and Therapeutic Applications.Antibodies (Basel, Switzerland) · 2025Review
- Diagnosing and staging epithelial ovarian cancer by serum glycoproteomic profiling.British journal of cancer · 2024Article
- The effects of immortalization on the N-glycome and proteome of CDK4-transformed lung cancer cells.Glycobiology · 2024Article
- Decoding the glycoproteome: a new frontier for biomarker discovery in cancer.Journal of hematology & oncology · 2024Review
- Noninvasive serum N-glycans associated with ovarian cancer diagnosis and precancerous lesion prediction.Journal of ovarian research · 2024Article
- Article
- IgM N-glycosylation correlates with COVID-19 severity and rate of complement deposition.Nature communications · 2024Article
- Regulation of ovarian cancer by protein post-translational modifications.Frontiers in oncology · 2024Review
- Recent Developments and Application of Mass Spectrometry Imaging in N-Glycosylation Studies: An Overview.Mass spectrometry (Tokyo, Japan) · 2024Review
- 6-PlexAnalytical chemistry · 2023Article
- Development and validation of a method for analyzing the sialylated glycopeptides of recombinant erythropoietin in urine using LC-HRMS.Scientific reports · 2023Article
- In-Depth Analysis of theInternational journal of molecular sciences · 2023Article
- Article
- Polyfunctional antibodies: a path towards precision vaccines for vulnerable populations.Frontiers in immunology · 2023Review
- Quantitative clinical glycomics strategies: A guide for selecting the best analysis approach.Mass spectrometry reviews · 2022Review
- Glycosylation and its research progress in endometrial cancer.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2022Review
- Review
- In SituCancers · 2022Article
- Sialic acids in gynecological cancer development and progression: Impact on diagnosis and treatment.International journal of cancer · 2022Review
- Glycosylation alterations in serum of Alzheimer's disease patients show widespread changes inAlzheimer's & dementia (Amsterdam, Netherlands) · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Previous studies indicated that glycans in serum may serve as biomarkers for diagnosis of ovarian cancer; however, it was unclear to which proteins these glycans belong. We hypothesize that protein-specific glycosylation profiles of the glycans may be more informative of ovarian cancer and can provide insight into biological mechanisms underlying glycan aberration in serum of diseased individuals. Serum samples from women diagnosed with epithelial ovarian cancer (EOC, n = 84) and matched healthy controls (n = 84) were obtained from the Gynecologic Oncology Group. Immunoglobulin (IgG, IgA, and IgM) concentrations and glycosylation profiles were quantified using multiple reaction monitoring mass spectrometry. Differential and classification analyses were performed to identify aberrant protein-specific glycopeptides using a training set. All findings were validated in an independent test set. Multiple glycopeptides from immunoglubins IgA, IgG, and IgM were found to be differentially expressed in serum of EOC patients compared with controls. The protein-specific glycosylation profiles showed their potential in the diagnosis of EOC. In particular, IgG-specific glycosylation profiles are the most powerful in discriminating between EOC case and controls. Additional studies of protein- and site-specific glycosylation profiles of immunoglobulins and other proteins will allow further elaboration on the characteristics of biological functionality and causality of the differential glycosylation in ovarian cancer and thus ultimately lead to increased sensitivity and specificity of diagnosis.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.