Evidence map›Paper›PMID 40427548›Full record

ReviewBiomolecules2025

Enzymatic Glycosylation of

Te-Sheng Chang, Jiumn-Yih Wu, Hsiou-Yu Ding, Tzi-Yuan Wang

Abstract readReview
In one paragraph

Review in Biomolecules, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
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  5. Article
  6. Review
  7. Review
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.

Te-Sheng ChangDepartment of Biological Sciences and Technology, National University of Tainan, Tainan 70005, Taiwan.ORCID 0000-0002-4205-2912
Jiumn-Yih WuDepartment of Food Science, National Quemoy University, Kinmen 89250, Taiwan.ORCID 0000-0002-0681-5505
Hsiou-Yu DingDepartment of Cosmetic Science, Chia Nan University of Pharmacy and Science, Tainan 717301, Taiwan.
Tzi-Yuan WangBiodiversity Research Center, Academia Sinica, Taipei 11529, Taiwan.ORCID 0000-0002-1562-0144

Funding

This research was funded by the National Science and Technology Council of Taiwan 386 MOST 111-2221-E-024 -001-MY3
6 · The paper itself

Abstract

Glycosylation is a critical enzymatic modification that involves the attachment of sugar moieties to target compounds, considerably influencing their physicochemical and biological characteristics. This review explored the role of two primary enzyme classes-glycosyltransferases (GTs) and glycoside hydrolases (GHs, glycosidases)-in catalyzing the glycosylation of natural products, with a specific focus on

Indexed as

GanodermaGlycoside HydrolasesGlycosyltransferasesTerpenesGlycosidesGlycosylationSubstrate SpecificityGlycoside HydrolasesGlycosidesGlycosyltransferasesTerpenesbiotransformationenzymatic synthesisGHglucosideglycoside hydrolaseglycosylationglycosyltransferaseGT1phenolicstriterpenoids

Identifiers

PMID40427548
PMCPMC12109177

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.