ArticleResearch square2026
Discovery of a Functional Sequon for Chondroitin Sulfate Glycosylation.
Article in Research square, 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
16 authors.
Funding
Abstract
The amino acid sequence requirements that instruct the modification of proteins with chondroitin sulfate (CS) have been unknown, precluding predictions or opportunities for precise protein engineering. This study identified an essential amino acid motif for CS addition, the "CS-sequon" (EDQDDKDGGDFSGWGG), by comparing the secreted sulfatases SULF1 and SULF2, where only SULF2 is CS-modified. A cluster of seven amino acids plus a nearby tryptophan are critical for CS attachment; inserting the CS-sequon into SULF1 enabled it to gain CS modification. This sequon recruits the activity of the CS-initiating xylosyltransferase to the peptide modification site and CS addition enhances SULF1/2 extracellular abundance and enzymatic activity. These findings were validated across human and non-human cells and in Drosophila, providing a foundational resource for engineering CS modifications into proteins.
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.