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

Activity of partially inhibited serine palmitoyltransferase is sufficient for normal sphingolipid metabolism and viability of HSN1 patient cells.

Biochimica et biophysica acta - 2 Mar 2004

Dedov Vadim N, Dedova Irina V, Merrill Alfred H, Nicholson Garth A

Abstract excerpt

Hereditary sensory neuropathy type I (HSN1) is a common degenerative disorder of peripheral sensory neurons. HSN1 is caused by mutations in the gene, encoding the long chain base 1 of serine palmitoyltransferase (SPT) [Nat. Genet. 27 (2001) 309]. Here, we show a 44% reduction of SPT activity in transformed lymphocytes from HSN1 patients with mutation T399G in the SPTLC1 gene. However, the decrease in SPT activity...

Read the complete abstract on PubMed

Topics

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

Share to Acyltransferases
Share to Blood Cell Count

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cell Membrane Permeability

Share to Cell Transformation, Viral

Share to Hereditary Sensory and Autonomic Neuropathies

Share to Lymphocytes

Share to Serine C-Palmitoyltransferase

Share to Sphingolipids

Source

Identifiers

PMID: 14990347
DOI: 10.1016/j.bbadis.2003.12.005

Genes

SPTLC1

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

Activity of partially inhibited serine palmitoyltransferase is sufficient for normal sphingolipid metabolism and viability of HSN1 patient cells.PMID 14990347Read ↗

Hereditary sensory neuropathy type 1 is caused by the accumulation of two neurotoxic sphingolipids.Semantic proximity Read ↗

Characterization of two mutations in the SPTLC1 subunit of serine palmitoyltransferase associated with hereditary sensory and autonomic neuropathy type I.Semantic proximity Read ↗

Hereditary sensory neuropathy type 1 mutations confer dominant negative effects on serine palmitoyltransferase, critical for sphingolipid synthesis.Semantic proximity Read ↗

HSAN1 mutations in serine palmitoyltransferase reveal a close structure-function-phenotype relationship.Semantic proximity Read ↗

Serine Palmitoyltransferase (SPT)-related Neurodegenerative and Neurodevelopmental DisordersSemantic proximity Read ↗

Overexpression of the wild-type SPT1 subunit lowers desoxysphingolipid levels and rescues the phenotype of HSAN1.Semantic proximity Read ↗

A systematic comparison of all mutations in hereditary sensory neuropathy type I (HSAN I) reveals that the G387A mutation is not disease associated.Semantic proximity Read ↗

Oral l-serine supplementation reduces production of neurotoxic deoxysphingolipids in mice and humans with hereditary sensory autonomic neuropathy type 1Semantic proximity Read ↗

Exclusion of serine palmitoyltransferase long chain base subunit 2 (SPTLC2) as a common cause for hereditary sensory neuropathy.Semantic proximity Read ↗

Mutant SPTLC1 dominantly inhibits serine palmitoyltransferase activity in vivo and confers an age-dependent neuropathy.Semantic proximity Read ↗

SPTLC1 is mutated in hereditary sensory neuropathy, type 1.Semantic proximity Read ↗

New Insights into the Neuromyogenic Spectrum of a Gain of Function Mutation in SPTLC1.Semantic proximity Read ↗

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