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

Biosynthetic processing of cathepsins and lysosomal degradation are abolished in asparaginyl endopeptidase-deficient mice.

The Journal of biological chemistry - 29 Aug 2003

Shirahama-Noda Kanae, Yamamoto Akitsugu, Sugihara Kazushi, Hashimoto Noriyoshi, Asano Masahide, Nishimura Mikio, Hara-Nishimura Ikuko

Abstract excerpt

Asparaginyl endopeptidase (AEP)/legumain, an asparagine-specific cysteine proteinase in animals, is an ortholog of plant vacuolar processing enzyme (VPE), which processes the exposed asparagine residues of various vacuolar proteins. In search for its physiological role in mammals, here we generated and characterized AEP-deficient mice. Although their body weights were significantly reduced, they were normally...

Read the complete abstract on PubMed

Topics

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

Share to Asparagine
Share to Cathepsins

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

Share to Cysteine Endopeptidases

Share to Endopeptidases

Share to Endosomes

Share to Gene Library

Share to Lysosomes

Share to Tissue Distribution

Source

Identifiers

PMID: 12775715
DOI: 10.1074/jbc.M302742200

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

Biosynthetic processing of cathepsins and lysosomal degradation are abolished in asparaginyl endopeptidase-deficient mice.PMID 12775715Read ↗

Characterization of rat cathepsin E and mutants with changed active-site residues and lacking propeptides and N-glycosylation, expressed in human embryonic kidney 293T cells.Semantic proximity Read ↗

Blockade of Cysteine Cathepsin Caused Lysosome Dysfunction and Aggravated Adenine-induced Nephropathy by Inducing Tubular Cell SenescenceSemantic proximity Read ↗

Expression, Intracellular Localization, and Maturation of Cysteine Cathepsins in Renal Embryonic and Cancer Cell LinesSemantic proximity Read ↗

The Proteasome Modulates Endocytosis in a Glomerular Cell Type Specific Modality to Secure Kidney FiltrationSemantic proximity Read ↗

Lysosomal high molecular weight multienzyme complex.Semantic proximity Read ↗

Emerging roles for diverse intramembrane proteases in plant biology.Semantic proximity Read ↗

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

Types and families of endopeptidases.Semantic proximity Read ↗

Legumain (asparaginyl endopeptidase) modulates extracellular matrix dynamics in pulmonary fibrosisSemantic proximity Read ↗

Two Membrane-Anchored Aspartic Proteases Contribute to Pollen and Ovule Development.Semantic proximity Read ↗

A deeply conserved protease, acylamino acid-releasing enzyme (AARE), acts in ageing in Physcomitrella and ArabidopsisSemantic proximity Read ↗

Lysosomal cathepsins in embryonic programmed cell deathSemantic proximity Read ↗

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