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

Quantification and characterization of the 5' exonuclease activity of the lysosomal nuclease PLD3 by a novel cell-based assay.

The Journal of biological chemistry - 1 Jan 2000

Cappel Cedric, Gonzalez Adriana Carolina, Damme Markus

Abstract excerpt

Phospholipase D3 (PLD3) and phospholipase D4 (PLD4), the most recently described lysosomal nucleases, are associated with Alzheimer's disease, spinocerebellar ataxia, and systemic lupus erythematosus. They exhibit 5' exonuclease activity on single-stranded DNA, hydrolyzing it at the acidic pH associated with the lysosome. However, their full cellular function is inadequately understood. To examine these enzymes,...

Read the complete abstract on PubMed

Topics

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

Share to Biological Assay
Share to Exonucleases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HeLa Cells

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Phospholipase D

Share to Proteolysis

Source

Open in PubMed Open full text

Identifiers

PMID: 33288674
DOI: 10.1074/jbc.RA120.015867
PMCID: PMC7857491

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Quantification and characterization of the 5' exonuclease activity of the lysosomal nuclease PLD3 by a novel cell-based assay.PMID 33288674Read ↗

Structural and mechanistic insights into disease-associated endolysosomal exonucleases PLD3 and PLD4.Semantic proximity Read ↗

Crystal structure of Alzheimer's disease phospholipase D3 provides a molecular basis for understanding its normal and pathological functions.Semantic proximity Read ↗

AMPylation regulates PLD3 processingSemantic proximity Read ↗

Phospholipase D3 regulates lysosomal morphology, biogenesis, and function in neuronsSemantic proximity Read ↗

Cleavage of DNA and RNA by PLD3 and PLD4 limits autoinflammatory triggering by multiple sensors.Semantic proximity Read ↗

Drosophila CG3303 is an essential endoribonuclease linked to TDP-43-mediated neurodegeneration.Semantic proximity Read ↗

High-throughput siRNA screening reveals functional interactions and redundancies of human processive exoribonucleasesSemantic proximity Read ↗

PLD3 is a neuronal lysosomal phospholipase D associated with β-amyloid plaques and cognitive function in Alzheimer's disease.Semantic proximity Read ↗

PLD3 is a neuronal lysosomal phospholipase D associated with β-amyloid plaques and cognitive function in Alzheimer’s diseaseSemantic proximity Read ↗

Plasma DNA Profile Associated with DNASE1L3 Gene Mutations: Clinical Observations, Relationships to Nuclease Substrate Preference, and In Vivo Correction.Semantic proximity Read ↗

Oligoribonuclease is a common downstream target of lithium-induced pAp accumulation in Escherichia coli and human cells.Semantic proximity Read ↗

Breaking Bad: Exploring & Complementing the Effects of the DNASE1L3 p.Arg206Cys Variant on Cell-Free DNA from an Isogenic Cell Line ModelSemantic proximity Read ↗

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