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

Tripeptidyl-peptidase I in neuronal ceroid lipofuscinoses and other lysosomal storage disorders.

European journal of paediatric neurology : EJPN : official journal of the European Paediatric Neurology Society - 1 Jan 2001

Wisniewski K E, Kida E, Walus M, Wujek P, Kaczmarski W, Golabek A A

Abstract excerpt

The classic late infantile form of neuronal ceroid lipofuscinosis (CLN2, cLINCL) is associated with mutations in the gene encoding tripeptidyl-peptidase I (TPP-I), a lysosomal aminopeptidase that cleaves off tripeptides from the free N-termini of oligopeptides. To date over 30 different mutations and 14 polymorphisms associated with CLN2 disease process have been identified. In the present study, we analysed the...

Read the complete abstract on PubMed

Topics

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

Share to Aminopeptidases
Share to Dipeptidyl-Peptidases and Tripeptidyl-Peptidases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endopeptidases

Share to Lysosomal Storage Diseases

Share to Neuronal Ceroid-Lipofuscinoses

Share to Peptide Hydrolases

Share to Serine Proteases

Share to Tripeptidyl-Peptidase 1

Source

Identifiers

PMID: 11589013
DOI: 10.1053/ejpn.2000.0439

Genes

CLN3

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

Tripeptidyl-peptidase I in neuronal ceroid lipofuscinoses and other lysosomal storage disorders.PMID 11589013Read ↗

A mouse model of classical late-infantile neuronal ceroid lipofuscinosis based on targeted disruption of the CLN2 gene results in a loss of tripeptidyl-peptidase I activity and progressive neurodegeneration.Semantic proximity Read ↗

[Tripeptidyl-peptidase I--distribution, biogenesis, and mechanisms of activation].Semantic proximity Read ↗

Clinical study in Chinese patients with late-infantile form neuronal ceroid lipofuscinoses.Semantic proximity Read ↗

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

Neuronal ceroid lipofuscinosis type CLN2: a new rationale for the construction of phenotypic subgroups based on a survey of 25 cases in South America.Semantic proximity Read ↗

The neuronal ceroid lipofuscinoses: mutations in different proteins result in similar disease.Semantic proximity Read ↗

Neuronal ceroid lipofuscinoses caused by defects in soluble lysosomal enzymes (CLN1 and CLN2).Semantic proximity Read ↗

Cln1 gene disruption in mice reveals a common pathogenic link between two of the most lethal childhood neurodegenerative lysosomal storage disorders.Semantic proximity Read ↗

Mutation update: Review of TPP1 gene variants associated with neuronal ceroid lipofuscinosis CLN2 diseaseSemantic 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 ↗

Diagnosis of neuronal ceroid lipofuscinosis type 2 (CLN2 disease): Expert recommendations for early detection and laboratory diagnosis.Semantic proximity Read ↗

R208X mutation in CLN2 gene associated with reduced cerebrospinal fluid pterins in a girl with classic late infantile neuronal ceroid lipofuscinosis.Semantic proximity Read ↗

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