Evidence map›Paper›PMID 28301937›Full record

ReviewACS chemical biology2017

Tools for Studying Glycans: Recent Advances in Chemoenzymatic Glycan Labeling.

Aime Lopez Aguilar, Jennie Grace Briard, Linette Yang, Ben Ovryn, Matthew Scott Macauley, Peng Wu

Open access · greenAbstract readReview
In one paragraph

Review in ACS chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
5.5field-weighted citation impact, top 3% of its field
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

60 citing papers in PubMed, 127 citations in OpenAlex.

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  7. Photoionization of pyrenemethylamine-labeled oligosaccharides: a new MALDI-TOF precursor ion-type for efficient fragmentation.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2025
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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

6 authors at 2 institutions in 1 country.

Aime Lopez AguilarDepartment of Chemical Physiology, The Scripps Research Institute , La Jolla, California 92037, United States.
Jennie Grace BriardDepartment of Chemical Physiology, The Scripps Research Institute , La Jolla, California 92037, United States.
Linette YangVassar College , 124 Raymond Ave, Poughkeepsie, New York 12604, United States.
Ben OvrynDepartment of Chemical Physiology, The Scripps Research Institute , La Jolla, California 92037, United States.
Matthew Scott MacauleyDepartment of Chemical Physiology, The Scripps Research Institute , La Jolla, California 92037, United States.
Peng WuDepartment of Chemical Physiology, The Scripps Research Institute , La Jolla, California 92037, United States.ORCID 0000-0002-5204-0229
Scripps Research Institute · USVassar College · US

Funding

REGULATION OF SIALOSIDE EXPRESSION IN LEUKOCYTESR01AI050143 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI PAULSON, JAMES C · 2003 to 2018
$7.0M
Chemical Tools for Studying Fucosylated GlycansR01GM093282 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI WU, PENG · 2010 to 2019
$3.4M
Inducing antigen specific B cell toleranceR01AI099141 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI PAULSON, JAMES C · 2012 to 2016
$2.3M
Chemoenzymatic methods for the detection of cellsurface glycansR01GM113046 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI WU, PENG · 2015 to 2018
$1.9M
Chemical tools for studying membrane protein glycosylationR01GM111938 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI OVRYN, BEN, WU, PENG · 2015 to 2018
$1.4M
Role of Siglec-10/G as a tumor suppressor in B-cellsR21AI128598 · NIAID · UNIVERSITY OF ALBERTA · PI MACAULEY, MATTHEW SCOTT · 2017 to 2018
$354k
NIAID NIH HHS R01 AI050143NIAID NIH HHS R01 AI099141NIAID NIH HHS R21 AI128598NIGMS NIH HHS R01 GM093282NIGMS NIH HHS R01 GM111938NIGMS NIH HHS R01 GM113046
6 · The paper itself

Abstract

The study of cellular glycosylation presents many challenges due, in large part, to the nontemplated nature of glycan biosynthesis and glycans' structural complexity. Chemoenzymatic glycan labeling (CeGL) has emerged as a new technique to address the limitations of existing methods for glycan detection. CeGL combines glycosyltransferases and unnatural nucleotide sugar donors equipped with a bioorthogonal chemical tag to directly label specific glycan acceptor substrates in situ within biological samples. This article reviews the current CeGL strategies that are available to characterize cell-surface and intracellular glycans. Applications include imaging glycan expression status in live cells and tissue samples, proteomic analysis of glycoproteins, and target validation. Combined with genetic and biochemical tools, CeGL provides new opportunities to elucidate the functional roles of glycans in human health and disease.

Indexed as

AnimalsCell MembraneGlycosylationMolecular ProbesPolysaccharidesMolecular ProbesPolysaccharides

Identifiers

PMID28301937
PMCPMC5469623
OpenAlexW2589017504

What OpenQuestion holds

Textmetadata
LicenceTDM
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 OpenQuestion graph.