ReviewProtein science : a publication of the Protein Society2005
Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions.
Review in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 142 papers, 1 of them a synthesis that pooled it.
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
142 citing papers in PubMed, 1 synthesis or guideline pooled it, 300 citations in OpenAlex.
- Guidelines for the nomenclature of the human heat shock proteins.Cell stress & chaperones · 2009Guideline
- Genome-Wide Identification ofPlants (Basel, Switzerland) · 2025Article
- Essential role for PfHSP40 in asexual replication and thermotolerance of malaria parasites.PLoS pathogens · 2025Article
- Aging and diet alter the protein ubiquitylation landscape in the mouse brain.Nature communications · 2025Article
- SIGHT-A System for Solvent-Tight Incubation and Growth Monitoring in High Throughput.Engineering in life sciences · 2025Article
- Genomic insights into Thermomonas hydrothermalis: potential applications in industrial biotechnology.World journal of microbiology & biotechnology · 2025Article
- Genome-Wide Analysis of Heat Shock Protein Family and Identification of Their Functions in Rice Quality and Yield.International journal of molecular sciences · 2024Article
- Decoding transcriptomic signatures of cysteine string protein alpha-mediated synapse maintenance.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Exploring the gene expression network involved in the heat stress response of a thermotolerant tomato genotype.BMC genomics · 2024Article
- Tertiary structure and conformational dynamics of the anti-amyloidogenic chaperone DNAJB6b at atomistic resolution.Nature communications · 2024Article
- Recruitment of BAG2 to DNAJ-PKAc scaffolds promotes cell survival and resistance to drug-induced apoptosis in fibrolamellar carcinoma.Cell reports · 2024Article
- ACD15, ACD21, and SLN regulate the accumulation and mobility of MBD6 to silence genes and transposable elements.Science advances · 2023Article
- Data-driven large-scale genomic analysis reveals an intricate phylogenetic and functional landscape in J-domain proteins.Proceedings of the National Academy of Sciences of the United States of America · 2023Review
- Chloroplast metalloproteinase SlL2 reduces the thermotolerance of tomato by decreasing the content of SlCDJ1.Protoplasma · 2023Article
- Integrated Analysis of miRNAome and Transcriptome Identify Regulators of Elm Seed Aging.Plants (Basel, Switzerland) · 2023Article
- J-domain protein chaperone circuits in proteostasis and disease.Trends in cell biology · 2023Review
- TheFrontiers in molecular biosciences · 2023Review
- A tomato chloroplast-targeted DnaJ protein, SlDnaJ20 maintains the stability of photosystem I/II under chilling stress.Plant signaling & behavior · 2022Article
- Biased gene expression reveals the contribution of subgenome to altitude adaptation in allopolyploidEcology and evolution · 2022Article
- Environmental Signals Act as a Driving Force for Metabolic and Defense Responses in the Antarctic PlantPlants (Basel, Switzerland) · 2022Article
82 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
Heat shock protein 40s (Hsp40s) and heat shock protein 70s (Hsp70s) form chaperone partnerships that are key components of cellular chaperone networks involved in facilitating the correct folding of a broad range of client proteins. While the Hsp40 family of proteins is highly diverse with multiple forms occurring in any particular cell or compartment, all its members are characterized by a J domain that directs their interaction with a partner Hsp70. Specific Hsp40-Hsp70 chaperone partnerships have been identified that are dedicated to the correct folding of distinct subsets of client proteins. The elucidation of the mechanism by which these specific Hsp40-Hsp70 partnerships are formed will greatly enhance our understanding of the way in which chaperone pathways are integrated into finely regulated protein folding networks. From in silico analyses, domain swapping and rational protein engineering experiments, evidence has accumulated that indicates that J domains contain key specificity determinants. This review will critically discuss the current understanding of the structural features of J domains that determine the specificity of interaction between Hsp40 proteins and their partner Hsp70s. We also propose a model in which the J domain is able to integrate specificity and chaperone activity.
Indexed as
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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.