ArticleJACS Au2026
A Chemoenzymatic Labeling Strategy for Site-Specific Analysis of Tumor-Associated Sialyl Thomsen-Friedenreich Antigen.
Article in JACS Au, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sialyl Thomsen-Friedenreich (ST) antigen, the attachment of trisaccharide Neu5Acα2-3Galβ1-3GalNAc on a serine or threonine residue, is a well-known tumor-associated carbohydrate antigen. There is a growing body of studies indicating that aberrant expression of ST antigen has a strong relationship with tumor invasion and metastasis. However, details about the biological functions of ST antigen are still poorly understood, as there is a lack of an effective method for glycosylation site analysis of the ST antigen. In this study, we developed a chemoenzymatic labeling strategy for the efficient site-specific analysis of ST antigen. A temperature-sensitive probe carried by the CMP-Neu5Ac derivative was designed and synthesized. The probe could be specifically introduced to ST antigen through a one-pot reaction mediated by sialyltransferase ST6GalNAc4. Controlled increase-reduction temperature cycling enabled the effective enrichment of the labeled glycopeptides from complex biological samples. Subsequently, the enriched glycopeptides were released via UV356 irradiation for mass spectrometry analysis, providing the details of where ST antigen attaches to proteins. Finally, this approach was successfully applied to globally profile ST antigen-modified proteins in three breast cancer cell lines: MCF7, MDA-MB-231, and MDA-MB-468.
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.