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

Characterization of a mutation in a family with saposin B deficiency: a glycosylation site defect.

Proceedings of the National Academy of Sciences of the United States of America - 1 Apr 1990

Kretz K A, Carson G S, Morimoto S, Kishimoto Y, Fluharty A L, O'Brien J S

Abstract excerpt

Saposins are small, heat-stable glycoproteins required for the hydrolysis of sphingolipids by specific lysosomal hydrolases. Saposins A, B, C, and D are derived by proteolytic processing from a single precursor protein named prosaposin. Saposin B, previously known as SAP-1 and sulfatide activator, stimulates the hydrolysis of a wide variety of substrates including cerebroside sulfate, GM1 ganglioside, and...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Base Sequence

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cloning, Molecular

Share to Molecular Sequence Data

Share to Mutation

Share to Polymerase Chain Reaction

Share to Reference Values

Source

Open in PubMed Open full text

Identifiers

PMID: 2320574
DOI: 10.1073/pnas.87.7.2541
PMCID: PMC53725

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization of a mutation in a family with saposin B deficiency: a glycosylation site defect.PMID 2320574Read ↗

A non-glycosylated and functionally deficient mutant (N215H) of the sphingolipid activator protein B (SAP-B) in a novel case of metachromatic leukodystrophy (MLD).Semantic proximity Read ↗

Prosaposin deficiency and saposin B deficiency (activator-deficient metachromatic leukodystrophy): report on two patients detected by analysis of urinary sphingolipids and carrying novel PSAP gene mutations.Semantic proximity Read ↗

Neurological deficits and glycosphingolipid accumulation in saposin B deficient mice.Semantic proximity Read ↗

Saposins: structure, function, distribution, and molecular genetics.Semantic proximity Read ↗

Detection of a point mutation in sphingolipid activator protein-1 mRNA in patients with a variant form of metachromatic leukodystrophy.Semantic proximity Read ↗

Molecular genetics of metachromatic leukodystrophy.Semantic proximity Read ↗

A mutation in the saposin A domain of the sphingolipid activator protein (prosaposin) gene results in a late-onset, chronic form of globoid cell leukodystrophy in the mouse.Semantic proximity Read ↗

A novel mutation in the coding region of the prosaposin gene leads to a complete deficiency of prosaposin and saposins, and is associated with a complex sphingolipidosis dominated by lactosylceramide accumulation.Semantic proximity Read ↗

A mutation in the saposin C domain of the sphingolipid activator protein (Prosaposin) gene causes neurodegenerative disease in mice.Semantic proximity Read ↗

Non-neuronopathic Gaucher disease due to saposin C deficiency.Semantic proximity Read ↗

Saposin A mobilizes lipids from low cholesterol and high bis(monoacylglycerol)phosphate-containing membranes: patient variant Saposin A lacks lipid extraction capacity.Semantic proximity Read ↗

Sulfatide activator protein. Alternative splicing that generates three mRNAs and a newly found mutation responsible for a clinical disease.Semantic proximity Read ↗

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