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

Glycosaminoglycans modulate activation, activity, and stability of tripeptidyl-peptidase I in vitro and in vivo.

The Journal of biological chemistry - 4 Mar 2005

Golabek Adam A, Walus Marius, Wisniewski Krystyna E, Kida Elizabeth

Abstract excerpt

Tripeptidyl-peptidase I (TPP I, CLN2 protein) is a lysosomal exopeptidase that sequentially removes tripeptides from the N termini of polypeptides and shows a minor endoprotease activity. Mutations in TPP I lead to classic late-infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disease. TPP I proenzyme is converted in lysosomes into a mature enzyme with the assistance of another...

Read the complete abstract on PubMed

Topics

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

Share to Anions
Share to Detergents
Share to Dextran Sulfate

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dipeptidyl-Peptidases and Tripeptidyl-Peptidases

Share to Glycosaminoglycans

Share to Octoxynol

Share to Serine Proteases

Share to Tripeptidyl-Peptidase 1

Source

Identifiers

PMID: 15582991
DOI: 10.1074/jbc.M412047200

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

Glycosaminoglycans modulate activation, activity, and stability of tripeptidyl-peptidase I in vitro and in vivo.PMID 15582991Read ↗

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

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

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

Lysosomal protein thermal stability does not correlate with cellular half-life: global observations and a case study of tripeptidyl-peptidase 1.Semantic proximity Read ↗

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

Protein thermal stability does not correlate with cellular half-life: Global observations and a case study of tripeptidyl-peptidase 1Semantic proximity Read ↗

Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.Semantic proximity Read ↗

A critical tryptophan and Ca2+ in activation and catalysis of TPPI, the enzyme deficient in classic late-infantile neuronal ceroid lipofuscinosis.Semantic proximity Read ↗

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

Chemical chaperones and permissive temperatures alter localization of Gaucher disease associated glucocerebrosidase variants.Semantic proximity Read ↗

Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo.Semantic proximity Read ↗

Lysosomal high molecular weight multienzyme complex.Semantic proximity Read ↗

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