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

A model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidases.

BMC structural biology - 11 Nov 2003

Wlodawer Alexander, Durell Stewart R, Li Mi, Oyama Hiroshi, Oda Kohei, Dunn Ben M

Abstract excerpt

BACKGROUND: Tripeptidyl-peptidase I, also known as CLN2, is a member of the family of sedolisins (serine-carboxyl peptidases). In humans, defects in expression of this enzyme lead to a fatal neurodegenerative disease, classical late-infantile neuronal ceroid lipofuscinosis. Similar enzymes have been found in the genomic sequences of several species, but neither systematic analyses of their distribution nor...

Read the complete abstract on PubMed

Topics

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

Share to Aminopeptidases
Share to Carboxypeptidases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dipeptidyl-Peptidases and Tripeptidyl-Peptidases

Share to Macaca

Share to Peptide Hydrolases

Share to Pseudomonas

Share to Serine Proteases

Share to Tripeptidyl-Peptidase 1

Source

Open in PubMed Open full text

Identifiers

PMID: 14609438
DOI: 10.1186/1472-6807-3-8
PMCID: PMC280685

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

A model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidases.PMID 14609438Read ↗

New families of carboxyl peptidases: serine-carboxyl peptidases and glutamic peptidases.Semantic proximity Read ↗

Prosegment of tripeptidyl peptidase I is a potent, slow-binding inhibitor of its cognate enzyme.Semantic proximity Read ↗

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

Ser475, Glu272, Asp276, Asp327, and Asp360 are involved in catalytic activity of human tripeptidyl-peptidase I.Semantic proximity Read ↗

The Degradome database: expanding roles of mammalian proteases in life and disease.Semantic proximity Read ↗

The Human Asparaginase-like Protein 1 hASRGL1 Is an Ntn Hydrolase with β-Aspartyl Peptidase ActivitySemantic proximity Read ↗

The Degradome database: mammalian proteases and diseases of proteolysis.Semantic proximity Read ↗

New Structural Insights into the Function of the Catalytically Active Human Taspase1Semantic proximity Read ↗

MEROPS: the peptidase databaseSemantic proximity Read ↗

Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.Semantic proximity Read ↗

Identification and classification of papain-like cysteine proteinasesSemantic proximity Read ↗

MEROPS: the peptidase databaseSemantic proximity Read ↗

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