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

Mutation of the glycosylated asparagine residue 286 in human CLN2 protein results in loss of enzymatic activity.

Glycobiology - 1 Apr 2004

Tsiakas Kostas, Steinfeld Robert, Storch Stephan, Ezaki Junji, Lukacs Zoltan, Kominami Eiki, Kohlschütter Alfried, Ullrich Kurt, Braulke Thomas

Abstract excerpt

Late infantile neuronal ceroid lipofuscinosis (LINCL) is caused by the deficiency of the lysosomal tripeptidyl peptidase-I encoded by CLN2. We previously detected in two LINCL patients a homozygous missense mutation, p.Asn286Ser, that affects a potential N-glycosylation site. We introduced the p.Asn286Ser mutation into the wild-type CLN2 cDNA and performed transient expression analysis to determine the effect on...

Read the complete abstract on PubMed

Topics

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

Share to Aminopeptidases
Share to Asparagine

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

Share to Dipeptidyl-Peptidases and Tripeptidyl-Peptidases

Share to Endopeptidases

Share to Neuronal Ceroid-Lipofuscinoses

Share to Peptide Hydrolases

Share to Serine Proteases

Share to Tripeptidyl-Peptidase 1

Source

Identifiers

PMID: 14736728
DOI: 10.1093/glycob/cwh054

Variants

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

Mutation of the glycosylated asparagine residue 286 in human CLN2 protein results in loss of enzymatic activity.PMID 14736728Read ↗

Expression and analysis of CLN2 variants in CHO cells: Q100R represents a polymorphism, and G389E and R447H represent loss-of-function mutations.Semantic proximity Read ↗

Mutational analysis of the defective protease in classic late-infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.Semantic proximity Read ↗

Two common mutations in the CLN2 gene underlie late infantile neuronal ceroid lipofuscinosis.Semantic proximity Read ↗

Defective endoplasmic reticulum-resident membrane protein CLN6 affects lysosomal degradation of endocytosed arylsulfatase A.Semantic proximity Read ↗

N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I.Semantic proximity Read ↗

CLN2/TPP1 deficiency: the novel mutation IVS7-10A>G causes intron retention and is associated with a mild disease phenotype.Semantic proximity Read ↗

The role of N-glycosylation in folding, trafficking, and functionality of lysosomal protein CLN5.Semantic proximity Read ↗

Retention of lysosomal protein CLN5 in the endoplasmic reticulum causes neuronal ceroid lipofuscinosis in Asian sibship.Semantic proximity Read ↗

Cln6 mutants associated with neuronal ceroid lipofuscinosis are degraded in a proteasome-dependent manner.Semantic proximity Read ↗

Role of N-glycosylation of human lysosomal phospholipase A2 for the formation of catalytically active enzyme.Semantic proximity Read ↗

Pathogenic mutations cause rapid degradation of lysosomal storage disease-related membrane protein CLN6.Semantic proximity Read ↗

Biosynthesis, glycosylation, and enzymatic processing in vivo of human tripeptidyl-peptidase I.Semantic proximity Read ↗

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