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

Structural and mechanistic insight into the basis of mucopolysaccharidosis IIIB.

Proceedings of the National Academy of Sciences of the United States of America - 6 May 2008

Ficko-Blean Elizabeth, Stubbs Keith A, Nemirovsky Oksana, Vocadlo David J, Boraston Alisdair B

Abstract excerpt

Mucopolysaccharidosis III (MPS III) has four forms (A-D) that result from buildup of an improperly degraded glycosaminoglycan in lysosomes. MPS IIIB is attributable to the decreased activity of a lysosomal alpha-N-acetylglucosaminidase (NAGLU). Here, we describe the structure, catalytic mechanism, and inhibition of CpGH89 from Clostridium perfringens, a close bacterial homolog of NAGLU. The structure enables the...

Read the complete abstract on PubMed

Topics

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

Share to Acetylglucosaminidase
Share to Catalysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Clostridium perfringens

Share to Drug Design

Share to Glycoside Hydrolases

Share to Molecular Chaperones

Share to Mucopolysaccharidosis III

Share to Protein Structure, Secondary

Source

Open in PubMed Open full text

Identifiers

PMID: 18443291
DOI: 10.1073/pnas.0711491105
PMCID: PMC2373330

Genes

NAGLU

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and mechanistic insight into the basis of mucopolysaccharidosis IIIB.PMID 18443291Read ↗

Bioinformatics classification of mutations in patients with Mucopolysaccharidosis IIIASemantic proximity Read ↗

Structural and mechanistic insights into a lysosomal membrane enzyme HGSNAT involved in Sanfilippo syndrome.Semantic proximity Read ↗

Biochemical and structural analysis of missense mutations in N-acetylgalactosamine-6-sulfate sulfatase causing mucopolysaccharidosis IVA phenotypes.Semantic proximity Read ↗

Structure of sulfamidase provides insight into the molecular pathology of mucopolysaccharidosis IIIASemantic proximity Read ↗

Portrait of an Enzyme, a Complete Structural Analysis of a Multimodular β-N-Acetylglucosaminidase from Clostridium perfringensSemantic proximity Read ↗

Structural and biochemical analyses of β-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila involved in mucin degradation.Semantic proximity Read ↗

Molecular Modeling of N-Acetylglucosamine Binding to the I154R Mutant of NAGLU: Pathogenic Insights into Sanfilippo Syndrome Type B.Semantic proximity Read ↗

Structure of the human heparan-α-glucosaminide N-acetyltransferase (HGSNAT).Semantic proximity Read ↗

Mucopolysaccharidosis type VI: Structural and clinical implications of mutations in N-acetylgalactosamine-4-sulfatase.Semantic proximity Read ↗

Structure of the human heparan-α-glucosaminide <i>N</i> -acetyltransferase (HGSNAT)Semantic proximity Read ↗

The 1.9 A structure of alpha-N-acetylgalactosaminidase: molecular basis of glycosidase deficiency diseases.Semantic proximity Read ↗

N-acetylgalactosamine-4-sulfatase: identification of four new mutations within the conserved sulfatase region causing mucopolysaccharidosis type VI.Semantic proximity Read ↗

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