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

Pathogenic VCP mutations induce mitochondrial uncoupling and reduced ATP levels.

Neuron - 10 Apr 2013

Bartolome Fernando, Wu Hsiu-Chuan, Burchell Victoria S, Preza Elisavet, Wray Selina, Mahoney Colin J, Fox Nick C, Calvo Andrea, Canosa Antonio, Moglia Cristina, Mandrioli Jessica, Chiò Adriano, Orrell Richard W, Houlden Henry, Hardy John, Abramov Andrey Y, Plun-Favreau Helene

Abstract excerpt

Valosin-containing protein (VCP) is a highly expressed member of the type II AAA+ ATPase family. VCP mutations are the cause of inclusion body myopathy, Paget's disease of the bone, and frontotemporal dementia (IBMPFD) and they account for 1%-2% of familial amyotrophic lateral sclerosis (ALS). Using fibroblasts from patients carrying three independent pathogenic mutations in the VCP gene, we show that VCP...

Read the complete abstract on PubMed

Topics

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

Share to Frontotemporal Dementia
Share to Lipid Peroxidation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Membrane Potential, Mitochondrial

Share to Muscular Dystrophies, Limb-Girdle

Share to Myositis, Inclusion Body

Share to Osteitis Deformans

Share to Valosin Containing Protein

Source

Open in PubMed Open full text

Identifiers

PMID: 23498975
DOI: 10.1016/j.neuron.2013.02.028
PMCID: PMC3843114

Genes

VCP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Pathogenic VCP mutations induce mitochondrial uncoupling and reduced ATP levels.PMID 23498975Read ↗

Mutations in valosin-containing protein (VCP) decrease ADP/ATP translocation across the mitochondrial membrane and impair energy metabolism in human neurons.Semantic proximity Read ↗

A pathogenic mutation in the ALS/FTD gene VCP induces mitochondrial hypermetabolism by modulating the permeability transition pore.Semantic proximity Read ↗

Valosin-containing protein gene mutations: cellular phenotypes relevant to neurodegeneration.Semantic proximity Read ↗

Autosomal Dominant Inclusion Body Myopathy, Paget Disease of Bone, and Frontotemporal DementiaSemantic proximity Read ↗

Valosin-containing protein (VCP) is required for autophagy and is disrupted in VCP disease.Semantic proximity Read ↗

The Role of VCP Mutations in the Spectrum of Amyotrophic Lateral Sclerosis—Frontotemporal DementiaSemantic proximity Read ↗

Valosin containing protein associated inclusion body myopathy: abnormal vacuolization, autophagy and cell fusion in myoblasts.Semantic proximity Read ↗

VCP activator reverses nuclear proteostasis defects and enhances TDP-43 aggregate clearance in multisystem proteinopathy modelsSemantic proximity Read ↗

Exome sequencing reveals VCP mutations as a cause of familial ALS.Semantic proximity Read ↗

Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein.Semantic proximity Read ↗

Valosin-containing protein disease: inclusion body myopathy with Paget's disease of the bone and fronto-temporal dementia.Semantic proximity Read ↗

The multiple faces of valosin-containing protein-associated diseases: inclusion body myopathy with Paget's disease of bone, frontotemporal dementia, and amyotrophic lateral sclerosis.Semantic proximity Read ↗

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