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

Lysosomal dysfunction, autophagic defects, and CLN5 accumulation underlie the pathogenesis of KCTD7-mutated neuronal ceroid lipofuscinoses.

Autophagy - 1 Jun 2023

Wang Yalan, Wang Hongyan, Wang Chenji

Abstract excerpt

Lysosomes are essential catabolic organelles responsible for the degradation of biomacromolecules into low-molecular-weight materials for subsequent reuse. Neuronal ceroid lipofuscinoses (NCLs) are a group of fatal neurodegenerative lysosomal storage disorders characterized by the intracellular accumulation of lipoprotein aggregates (called ceroid lipofuscin) in neurons and other tissues. Mutations in KCTD7,...

Read the complete abstract on PubMed

Topics

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

Share to Autophagy
Share to Lysosomal Membrane Proteins
Share to Lysosomes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Membrane Proteins

Share to Mutation

Share to Neuronal Ceroid-Lipofuscinoses

Share to Potassium Channels

Share to Tripeptidyl-Peptidase 1

Source

Open in PubMed Open full text

Identifiers

PMID: 36368077
DOI: 10.1080/15548627.2022.2140882
PMCID: PMC10262767

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Lysosomal dysfunction, autophagic defects, and CLN5 accumulation underlie the pathogenesis of KCTD7-mutated neuronal ceroid lipofuscinoses.PMID 36368077Read ↗

KCTD7 mutations impair the trafficking of lysosomal enzymes through CLN5 accumulation to cause neuronal ceroid lipofuscinoses.Semantic proximity Read ↗

Emerging new roles of the lysosome and neuronal ceroid lipofuscinosesSemantic proximity Read ↗

The intracellular location and function of proteins of neuronal ceroid lipofuscinoses.Semantic proximity Read ↗

A homozygous mutation in KCTD7 links neuronal ceroid lipofuscinosis to the ubiquitin-proteasome system.Semantic proximity Read ↗

Homozygous TBC1 domain-containing kinase (TBCK) mutation causes a novel lysosomal storage disease – a new type of neuronal ceroid lipofuscinosis (CLN15)?Semantic proximity Read ↗

Functional biology of the neuronal ceroid lipofuscinoses (NCL) proteins.Semantic proximity Read ↗

Autophagy in the Neuronal Ceroid Lipofuscinoses (Batten Disease)Semantic proximity Read ↗

KCTD7 deficiency defines a distinct neurodegenerative disorder with a conserved autophagy‐lysosome defectSemantic proximity Read ↗

A lysosomal enigma CLN5 and its significance in understanding neuronal ceroid lipofuscinosis.Semantic proximity Read ↗

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

Recent Insight into the Genetic Basis, Clinical Features, and Diagnostic Methods for Neuronal Ceroid Lipofuscinosis.Semantic proximity Read ↗

Molecular basis of the neuronal ceroid lipofuscinoses: mutations in CLN1, CLN2, CLN3, and CLN5.Semantic proximity Read ↗

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