Evidence map›Paper›PMID 31427814›Full record

ReviewNature chemical biology2019

Emerging structural insights into glycosyltransferase-mediated synthesis of glycans.

Kelley W Moremen, Robert S Haltiwanger

Abstract readReview
In one paragraph

Review in Nature chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.

0numbers the graph read from it
0cells of the map it votes in
113citing papers in PubMed
7.4field-weighted citation impact, top 2% 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

113 citing papers in PubMed, 204 citations in OpenAlex.

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  15. WrtF fromProceedings of the National Academy of Sciences of the United States of America · 2025
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53 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Kelley W MoremenComplex Carbohydrate Research Center, University of Georgia, Athens, GA, USA. moremen@uga.edu.ORCID http://orcid.org/0000-0003-1768-582X
Robert S HaltiwangerComplex Carbohydrate Research Center, University of Georgia, Athens, GA, USA. halti@uga.edu.ORCID http://orcid.org/0000-0001-7439-9577
University of Georgia · US

Funding

TR&D3. Approaches to Proteoglycan Function at Biochemical and Cellular LevelsP41GM103390 · NIGMS · UNIVERSITY OF GEORGIA · PI MOREMEN, KELLEY W. · 2012 to 2019
$14.5M
O-Glycosylation of Epidermal Growth Factor-like MotifsR01GM061126 · NIGMS · UNIVERSITY OF GEORGIA · PI HALTIWANGER, ROBERT S. · 2001 to 2021
$9.1M
Recombinant Production of Glycosylation Enzymes for Biochem/Structural StudiesP01GM107012 · NIGMS · UNIVERSITY OF GEORGIA · PI MOREMEN, KELLEY · 2013 to 2017
$7.5M
Origin of N-Glycan Site-Specific HeterogeneityR01GM130915 · NIGMS · UNIVERSITY OF GEORGIA · PI KANNAN, NATARAJAN, MOREMEN, KELLEY W. · 2019 to 2022
$3.4M
Streamlining the chemoenzymatic synthesis of asymmetrical glycans of biological importanceU01GM120408 · NIGMS · UNIVERSITY OF GEORGIA · PI BOONS, GEERT-JAN · 2016 to 2019
$3.0M
Role of Beta3-Glucosyltransferase in a non-canonical quality control pathwayR01HD096030 · NICHD · UNIVERSITY OF GEORGIA · PI HALTIWANGER, ROBERT S., HOLDENER, BERNADETTE C · 2018 to 2022
$2.9M
Characterization of the role of POFUT2-mediated O-fucosylation in folding Thrombospondin Type 1 Repeats and Development R01HD090156 · NICHD · UNIVERSITY OF GEORGIA · PI HALTIWANGER, ROBERT S., HOLDENER, BERNADETTE C · 2017 to 2021
$2.4M
NICHD NIH HHS R01 HD090156NICHD NIH HHS R01 HD096030NIGMS NIH HHS P01 GM107012NIGMS NIH HHS P41 GM103390NIGMS NIH HHS R01 GM061126NIGMS NIH HHS R01 GM130915NIGMS NIH HHS U01 GM120408
6 · The paper itself

Abstract

Glycans linked to proteins and lipids play key roles in biology; thus, accurate replication of cellular glycans is crucial for maintaining function following cell division. The fact that glycans are not copied from genomic templates suggests that fidelity is provided by the catalytic templates of glycosyltransferases that accurately add sugars to specific locations on growing oligosaccharides. To form new glycosidic bonds, glycosyltransferases bind acceptor substrates and orient a specific hydroxyl group, frequently one of many, for attack of the donor sugar anomeric carbon. Several recent crystal structures of glycosyltransferases with bound acceptor substrates reveal that these enzymes have common core structures that function as scaffolds upon which variable loops are inserted to confer substrate specificity and correctly orient the nucleophilic hydroxyl group. The varied approaches for acceptor binding site assembly suggest an ongoing evolution of these loop regions provides templates for assembly of the diverse glycan structures observed in biology.

Indexed as

AnimalsCarbohydrate ConformationDatabases, ProteinGene Expression Regulation, EnzymologicGlycosyltransferasesPolysaccharidesGlycosyltransferasesPolysaccharides

Identifiers

PMID31427814
PMCPMC6820136
OpenAlexW2968256998

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.