Evidence map›Paper›PMID 25279697›Full record

ArticleeLife2014

B4GAT1 is the priming enzyme for the LARGE-dependent functional glycosylation of α-dystroglycan.

Jeremy L Praissman, David H Live, Shuo Wang, Annapoorani Ramiah, Zoeisha S Chinoy, Geert-Jan Boons, Kelley W Moremen, Lance Wells

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

59 citing papers in PubMed, 97 citations in OpenAlex.

  1. [Association between umbilical cord blood proteome and early infant neurodevelopmental risk].Beijing da xue xue bao. Yi xue ban = Journal of Peking University. Health sciences · 2026
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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

8 authors at 1 institution in 1 country.

Jeremy L PraissmanComplex Carbohydrate Research Center, University of Georgia, Athens, United States.
David H LiveComplex Carbohydrate Research Center, University of Georgia, Athens, United States.
Shuo WangComplex Carbohydrate Research Center, University of Georgia, Athens, United States.
Annapoorani RamiahComplex Carbohydrate Research Center, University of Georgia, Athens, United States.
Zoeisha S ChinoyComplex Carbohydrate Research Center, University of Georgia, Athens, United States.
Geert-Jan BoonsComplex Carbohydrate Research Center, University of Georgia, Athens, United States.
Kelley W MoremenComplex Carbohydrate Research Center, University of Georgia, Athens, United States.
Lance WellsComplex Carbohydrate Research Center, University of Georgia, Athens, United States.
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
TR&D1: Stem Cell and Induced Pluripotent Stem Cell Resources (Pages 116-134)P41GM103490 · NIGMS · UNIVERSITY OF GEORGIA · PI PIERCE, J. MICHAEL · 2012 to 2018
$13.7M
Recombinant Production of Glycosylation Enzymes for Biochem/Structural StudiesP01GM107012 · NIGMS · UNIVERSITY OF GEORGIA · PI PRESTEGARD, JAMES H. · 2013 to 2017
$7.5M
Structure and Function in alpha-Dystroglycan GlycosylationR01GM111939 · NIGMS · UNIVERSITY OF GEORGIA · PI Lance Wells · 2014 to 2026
$4.0M
NIGMS NIH HHS P01 GM107012NIGMS NIH HHS P01GM107012NIGMS NIH HHS P41 GM103390NIGMS NIH HHS P41GM103390NIGMS NIH HHS P41 GM103490NIGMS NIH HHS P41GM103490NIGMS NIH HHS R01 GM111939NIGMS NIH HHS R01GM111939
6 · The paper itself

Abstract

Recent studies demonstrated that mutations in B3GNT1, an enzyme proposed to be involved in poly-N-acetyllactosamine synthesis, were causal for congenital muscular dystrophy with hypoglycosylation of α-dystroglycan (secondary dystroglycanopathies). Since defects in the O-mannosylation protein glycosylation pathway are primarily responsible for dystroglycanopathies and with no established O-mannose initiated structures containing a β3 linked GlcNAc known, we biochemically interrogated this human enzyme. Here we report this enzyme is not a β-1,3-N-acetylglucosaminyltransferase with catalytic activity towards β-galactose but rather a β-1,4-glucuronyltransferase, designated B4GAT1, towards both α- and β-anomers of xylose. The dual-activity LARGE enzyme is capable of extending products of B4GAT1 and we provide experimental evidence that B4GAT1 is the priming enzyme for LARGE. Our results further define the functional O-mannosylated glycan structure and indicate that B4GAT1 is involved in the initiation of the LARGE-dependent repeating disaccharide that is necessary for extracellular matrix protein binding to O-mannosylated α-dystroglycan that is lacking in secondary dystroglycanopathies.

Indexed as

Amino Acid SequenceBiocatalysisDisaccharidesDystroglycansGlycosylationHEK293 CellsHumansKineticsModels, BiologicalMolecular Sequence DataN-AcetylglucosaminyltransferasesPentosyltransferasesSolubilityStereoisomerismSubstrate SpecificityTrisaccharidesB4GAT1 protein, humanDisaccharidesDystroglycansLARGE1 protein, humanN-AcetylglucosaminyltransferasesPentosyltransferasesTrisaccharidesUDP Xylose-Protein XylosyltransferaseUridine Diphosphate Glucuronic AcidXylosealpha-dystroglycanB3GNT1B4GAT1biochemistrycongenital muscular dystrophyglycosylationhumanhuman biologymedicineO-mannosylation

Identifiers

PMID25279697
PMCPMC4227051
OpenAlexW2134377460

What OpenQuestion holds

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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 OpenQuestion graph.