Evidence map›Paper›PMID 23125099›Full record

ArticleGlycobiology2013

Xylosyl- and glucuronyltransferase functions of LARGE in α-dystroglycan modification are conserved in LARGE2.

Kei-ichiro Inamori, Yuji Hara, Tobias Willer, Mary E Anderson, Zihan Zhu, Takako Yoshida-Moriguchi, Kevin P Campbell

Open access · hybridAbstract read
In one paragraph

Article in Glycobiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

38 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Review
  3. UDP-glucose dehydrogenase variants cause dystroglycanopathy.Annals of clinical and translational neurology · 2025
    Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Post-translational Modification in Muscular Dystrophies.Advances in experimental medicine and biology · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Mammalian O-mannosyl glycans: Biochemistry and glycopathology.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019
    Article
  18. Molecules (Basel, Switzerland) · 2018
    Article
  19. Article
  20. 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

7 authors at 2 institutions in 1 country.

Kei-ichiro InamoriHoward Hughes Medical Institute, University of Iowa Roy J. and Lucille A. Carver College of Medicine, Iowa City, IA 52242-1101, USA.
Yuji Hara
Tobias Willer
Mary E Anderson
Zihan Zhu
Takako Yoshida-Moriguchi
Kevin P Campbell
Howard Hughes Medical Institute · USUniversity of Iowa · US

Funding

Therapeutic Potential of ESC-Derived Myogenic PrecursorsU54NS053672 · NINDS · UNIVERSITY OF IOWA · PI CAMPBELL, KEVIN P. · 2005 to 2019
$22.0M
Howard Hughes Medical InstituteNINDS NIH HHS 1U54NS053672
6 · The paper itself

Abstract

LARGE-dependent modification enables α-dystroglycan (α-DG) to bind to its extracellular matrix ligands. Mutations in the LARGE gene and several others involved in O-mannosyl glycan synthesis have been identified in congenital and limb-girdle muscular dystrophies that are characterized by perturbed glycosylation and reduced ligand-binding affinity of α-DG. LARGE is a bifunctional glycosyltransferase that alternately transfers xylose and glucuronic acid, thereby generating the heteropolysaccharides on α-DG that confer its ligand binding. Although the LARGE paralog LARGE2 (also referred to as GYLTL1B) has likewise been shown to enhance the functional modification of α-DG in cultured cells, its enzymatic activities have not been identified. Here, we report that LARGE2 is also a bifunctional glycosyltransferase and compare its properties with those of LARGE. By means of a high-performance liquid chromatography-based enzymatic assay, we demonstrate that like LARGE, LARGE2 has xylosyltransferase (Xyl-T) and glucuronyltransferase (GlcA-T) activities, as well as polymerizing activity. Notably, however, the pH optima of the Xyl-T and GlcA-T of LARGE2 are distinct from one another and also from those of LARGE. Our results suggest that LARGE and LARGE2 catalyze the same glycosylation reactions for the functional modification of α-DG, but that they have different biochemical properties.

Indexed as

AnimalsCatalytic DomainCHO CellsCricetinaeCricetulusDystroglycansGlucuronic AcidGlycosyltransferasesHydrogen-Ion ConcentrationKineticsMiceN-AcetylglucosaminyltransferasesProtein MultimerizationXyloseDystroglycansGlucuronic AcidGlycosyltransferasesLarge1 protein, mouseLarge2 protein, mouseN-AcetylglucosaminyltransferasesXylose

Identifiers

PMID23125099
PMCPMC3555503
OpenAlexW2156396820

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.