ReviewFrontiers in cellular neuroscience2014
J protein mutations and resulting proteostasis collapse.
Review in Frontiers in cellular neuroscience, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 35 citations in OpenAlex.
- Abnormal redox balance at membrane contact sites causes axonopathy inResearch square · 2024Article
- The HSP40 family chaperone isoform DNAJB6b prevents neuronal cells from tau aggregation.BMC biology · 2023Article
- Modulating Stress Proteins in Response to Therapeutic Interventions for Parkinson's Disease.International journal of molecular sciences · 2023Review
- Article
- A novel gene therapy for methamphetamine- induced cognitive disorder with a hyper-acidified fusion variant of DnaJB1.Molecular therapy. Nucleic acids · 2023Article
- DnaJC7 in Amyotrophic Lateral Sclerosis.International journal of molecular sciences · 2022Review
- Cysteine string protein alpha accumulates with early pre-synaptic dysfunction in Alzheimer's disease.Brain communications · 2022Article
- PolyQ-expanded proteins impair cellular proteostasis of ataxin-3 through sequestering the co-chaperone HSJ1 into aggregates.Scientific reports · 2021Article
- Deciphering Network Crosstalk: The Current Status and Potential of miRNA Regulatory Networks on the HSP40 Molecular Chaperone Network.Frontiers in genetics · 2021Review
- DNAJC6 Mutations Disrupt Dopamine Homeostasis in Juvenile Parkinsonism-Dystonia.Movement disorders : official journal of the Movement Disorder Society · 2020Article
- Article
- DNAJC proteins and pathways to parkinsonism.The FEBS journal · 2019Review
- Hsp70 molecular chaperones: multifunctional allosteric holding and unfolding machines.The Biochemical journal · 2019Review
- DNAJ Proteins in neurodegeneration: essential and protective factors.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Genetic variation in N- and C-terminal regions of bovineJournal of genomics · 2018Article
- Overexpression of Rice Auxilin-Like Protein, XB21, Induces Necrotic Lesions, up-Regulates Endocytosis-Related Genes, and Confers Enhanced Resistance to Xanthomonas oryzae pv. oryzae.Rice (New York, N.Y.) · 2017Article
- Evolution of an intricate J-protein network driving protein disaggregation in eukaryotes.eLife · 2017Article
- Neurons Export Extracellular Vesicles Enriched in Cysteine String Protein and Misfolded Protein Cargo.Scientific reports · 2017Article
- Interaction of the polyglutamine protein ataxin-3 with Rad23 regulates toxicity in Drosophila models of Spinocerebellar Ataxia Type 3.Human molecular genetics · 2017Article
- The Role of Co-chaperones in Synaptic Proteostasis and Neurodegenerative Disease.Frontiers in neuroscience · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Despite a century of intensive investigation the effective treatment of protein aggregation diseases remains elusive. Ordinarily, molecular chaperones ensure that proteins maintain their functional conformation. The appearance of misfolded proteins that aggregate implies the collapse of the cellular chaperone quality control network. That said, the cellular chaperone network is extensive and functional information regarding the detailed action of specific chaperones is not yet available. J proteins (DnaJ/Hsp40) are a family of chaperone cofactors that harness Hsc70 (heat shock cognate protein of 70 kDa) for diverse conformational cellular tasks and, as such, represent novel clinically relevant targets for diseases resulting from the disruption of proteostasis. Here we review incisive reports identifying mutations in individual J protein chaperones and the proteostasis collapse that ensues.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.