Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Functional characterization of zebrafish orthologs of the human Beta 3-Glucosyltransferase B3GLCT gene mutated in Peters Plus Syndrome.

PloS one - 1 Jan 2017

Weh Eric, Takeuchi Hideyuki, Muheisen Sanaa, Haltiwanger Robert S, Semina Elena V

Abstract excerpt

Peters Plus Syndrome (PPS) is a rare autosomal recessive disease characterized by ocular defects, short stature, brachydactyly, characteristic facial features, developmental delay and other highly variable systemic defects. Classic PPS is caused by loss-of-function mutations in the B3GLCT gene encoding for a β3-glucosyltransferase that catalyzes the attachment of glucose via a β1-3 glycosidic linkage to O-linked...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cleft Lip
Share to Cornea
Share to Gene Editing

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Knockout Techniques

Share to Glucosyltransferases

Share to Growth Disorders

Share to Limb Deformities, Congenital

Share to Transcription Activator-Like Effector Nucleases

Source

Open in PubMed Open full text

Identifiers

PMID: 28926587
DOI: 10.1371/journal.pone.0184903
PMCID: PMC5604996

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional characterization of zebrafish orthologs of the human Beta 3-Glucosyltransferase B3GLCT gene mutated in Peters Plus Syndrome.PMID 28926587Read ↗

Peters plus syndrome mutations affect the function and stability of human β1,3-glucosyltransferase.Semantic proximity Read ↗

ADAMTS9 and ADAMTS20 are differentially affected by loss of B3GLCT in mouse model of Peters plus syndromeSemantic proximity Read ↗

Peters'-plus syndrome is a congenital disorder of glycosylation caused by a defect in the beta1,3-glucosyltransferase that modifies thrombospondin type 1 repeats.Semantic proximity Read ↗

Peters Plus syndrome is caused by mutations in B3GALTL, a putative glycosyltransferase.Semantic proximity Read ↗

Genetic Diseases of Fucosylation: Insights from Model OrganismsSemantic proximity Read ↗

<i>b3galt6</i> knock-out zebrafish recapitulate β3GalT6-deficiency disorders in human and reveal a trisaccharide proteoglycan linkage regionSemantic proximity Read ↗

Mutations in B3GALNT2 cause congenital muscular dystrophy and hypoglycosylation of α-dystroglycan.Semantic proximity Read ↗

A patient-based medaka alg2 mutant as a model for hypo-N-glycosylation.Semantic proximity Read ↗

Peters plus syndrome mutations disrupt a noncanonical ER quality-control mechanism.Semantic proximity Read ↗

High-throughput analysis of B3GLCT regulation predicts phenotype of Peters’ Plus Syndrome in line with the miRNA Proxy HypothesisSemantic proximity Read ↗

Biallelic Mutations in FUT8 Cause a Congenital Disorder of Glycosylation with Defective Fucosylation.Semantic proximity Read ↗

Hydrocephalus in mouse B3glct mutants is likely caused by defects in multiple B3GLCT substrates in ependymal cells and subcommissural organSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.