Evidence map›Paper›PMID 42757430›Full record

ReviewThe Biochemical journal2026

Design rules for bioorthogonal glycan-based tools.

Freya Hoddle, Sophie Dela Schmidt, Sandhya Sridhar, Benjamin Schumann

Abstract readReview
In one paragraph

Review in The Biochemical journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Freya Hoddle *Department of Chemistry, Imperial College London, W12 0BZ London, U.K.
Sophie Dela Schmidt *Department of Chemistry, Imperial College London, W12 0BZ London, U.K.ORCID 0009-0009-9349-4997
Sandhya Sridhar *Department of Chemistry, Imperial College London, W12 0BZ London, U.K.ORCID 0009-0009-2856-8275
Benjamin SchumannDepartment of Chemistry, Imperial College London, W12 0BZ London, U.K.ORCID 0000-0001-5504-0147

Funding

Cancer Research UK (CRUK) CC2127Cancer Research UK (CRUK) DRCMDP-Nov22/100011UKRI | Engineering and Physical Sciences Research Council (SRC) UKRI3602UKRI | Medical Research Council (MRC) CC2127Wellcome Trust CC2127Wellcome Trust (WT) CC2127
6 · The paper itself

Abstract

As one of the most abundant and diverse post-translational modifications in biology, glycosylation has a significant influence on the functions of proteins in health and disease. To untangle the complexity of glycan biosynthetic pathways, the process of studying glycosylation has been expedited by specialised, chemical labelling techniques. In the present review, we explore the development of metabolic glycan labelling from early biochemical methods to current approaches that use interdisciplinary techniques. We highlight work that has informed our understanding of glycan biosynthesis through pioneering chemical biology approaches. Moreover, we provide guidance for experimental design that can be tailored to the specific needs of those investigating glycosylation in the context of their own work. Our 'Design Rules' consolidate the findings of several groups in a simple roadmap to make metabolic glycan labelling as effective as possible.

Indexed as

PolysaccharidesStaining and LabelingGlycosylationHumansProtein Processing, Post-TranslationalPolysaccharidesBioorthogonalcarbon metabolismGlycosylationGlycosyltransferase

Identifiers

PMID42757430
PMCPMC13591258

What Socratic holds

Textmetadata
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.