ReviewGlycobiology2025
Decoding the complex substrate specificities of GalNAc-Ts.
Review in Glycobiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
- Design rules for bioorthogonal glycan-based tools.The Biochemical journal · 2026Review
- A single catalytic domain residue regulates the substrate specificity of a mucin-type O-glycosyltransferase in salivary gland function.bioRxiv : the preprint server for biology · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
Abstract
GalNAc-Ts are a large family of glycosyltransferases that regulate numerous cellular processes by initiating the post-translational modification mucin-type O-glycosylation. Disruptions in GalNAc-T expression and function are associated with congenital diseases, metabolic disorders, and cancer. The substrates and acceptor sites affected by the inactivation or over-activation of each specific family member are often not known due to acceptor site and substrate redundancies among the isoenzymes that are present within a cell type. However, substantial progress has been made in disentangling the enzyme-substrate conundrum by showing that each isoenzyme follows a unique set of substrate recognition rules. This review summarizes biochemical and structural findings that have advanced our understanding of the distinct substrate specificities of individual GalNAc-Ts.
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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.