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

Enhanced J-protein interaction and compromised protein stability of mtHsp70 variants lead to mitochondrial dysfunction in Parkinson's disease.

Human molecular genetics - 1 Aug 2012

Goswami Arvind Vittal, Samaddar Madhuja, Sinha Devanjan, Purushotham Jaya, D'Silva Patrick

Abstract excerpt

Parkinson's disease (PD) is the second most prevalent progressive neurological disorder commonly associated with impaired mitochondrial function in dopaminergic neurons. Although familial PD is multifactorial in nature, a recent genetic screen involving PD patients identified two mitochondrial Hsp70 variants (P509S and R126W) that are suggested in PD pathogenesis. However, molecular mechanisms underlying how...

Read the complete abstract on PubMed

Topics

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

Share to DNA, Mitochondrial
Share to Dopaminergic Neurons

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HSP70 Heat-Shock Proteins

Share to Mitochondria

Share to Molecular Chaperones

Share to Parkinson Disease

Share to Protein Stability

Share to Transfection

Source

Open in PubMed Open full text

Identifiers

PMID: 22544056
DOI: 10.1093/hmg/dds162
PMCID: PMC3392108

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Enhanced J-protein interaction and compromised protein stability of mtHsp70 variants lead to mitochondrial dysfunction in Parkinson's disease.PMID 22544056Read ↗

Versatile members of the DNAJ family show Hsp70 dependent anti-aggregation activity on RING1 mutant parkin C289G.Semantic proximity Read ↗

Disease-associated mutations within the yeast DNAJB6 homolog Sis1 slow conformer-specific substrate processing and can be corrected by the modulation of nucleotide exchange factors.Semantic proximity Read ↗

Effect of endogenous Hsp104 chaperone in yeast models of sporadic and familial Parkinson's disease.Semantic proximity Read ↗

Client processing is altered by novel myopathy-causing mutations in the HSP40 J domain.Semantic proximity Read ↗

Dissecting the role of the mitochondrial chaperone mortalin in Parkinson's disease: functional impact of disease-related variants on mitochondrial homeostasis.Semantic proximity Read ↗

Client processing is altered by novel myopathy-causing mutations in the HSP40 J domainSemantic proximity Read ↗

The PINK1 p.I368N mutation affects protein stability and ubiquitin kinase activity.Semantic proximity Read ↗

Mutations in the Yeast Hsp70, Ssa1, at P417 Alter ATP Cycling, Interdomain Coupling, and Specific Chaperone Functions.Semantic proximity Read ↗

A yeast model of the ALS protein Matrin3 uncovers Hsp90 and its co-chaperone Sti1 as modifiers of misfolding and toxicitySemantic proximity Read ↗

Myopathy mutations in DNAJB6 slow conformer specific substrate processing that is corrected by NEF modulationSemantic proximity Read ↗

Scouring the human Hsp70 network uncovers diverse chaperone safeguards buffering TDP-43 toxicitySemantic proximity Read ↗

Mitochondrial hsp60 chaperonopathy causes an autosomal-recessive neurodegenerative disorder linked to brain hypomyelination and leukodystrophy.Semantic proximity Read ↗

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