ReviewEMBO reports2004
The J-protein family: modulating protein assembly, disassembly and translocation.
Review in EMBO reports, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 248 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
248 citing papers in PubMed, 1 synthesis or guideline pooled it.
- HSP expression depends on its molecular construction and different organs of the chicken: a meta-analysis.Scientific reports · 2022Pooled it
- Wiring of cellular proteostasis by J-domain proteins.Cell stress & chaperones · 2026Review
- Differential roles of Scj1 and Djp1, two DnaJ homologs, in virulence, cell wall integrity, and multi-stress tolerance of Beauveria bassiana.Antonie van Leeuwenhoek · 2026Article
- Unveiling DNAJB12 and DNAJB14 as crucial chaperones in hepatitis B and D virus particle morphogenesis.iScience · 2026Article
- The mitochondrial proteome of diplonemids: from conventional pathways to eccentric RNA editing and transcript processing.BMC genomics · 2025Article
- Transcriptomic Analysis of Copper Resistance inAntibiotics (Basel, Switzerland) · 2025Article
- Genome-wide analysis of the DnaJ gene family and their expression profiles under salt stress in potato.BMC genomics · 2025Article
- Mechanisms of multidrug resistance caused by an Ipi1 mutation in the fungal pathogen Candida glabrata.Nature communications · 2025Article
- Article
- Co-chaperones fine-tune the function of heat shock protein 70 (Hsp70), whether to fold, hold, or degrade substrates in ensuring cellular protein homeostasis.Journal of biosciences · 2025Review
- Deciphering the proteome ofComputational and structural biotechnology journal · 2025Article
- The potential functions ofFrontiers in plant science · 2025Article
- Genome-wide identification and expression profiling ofFrontiers in plant science · 2025Article
- The J Domain Proteins ofInternational journal of molecular sciences · 2024Review
- Genome-Wide Identification of the DnaJ Gene Family in Citrus and Functional Characterization ofInternational journal of molecular sciences · 2024Article
- Integrative analysis of bulk and single-cell transcriptomic data reveals novel insights into lipid metabolism and prognostic factors in hepatocellular carcinoma.Discover oncology · 2024Article
- Article
- Two novel DnaJ chaperone proteins CG5001 and P58IPK regulate the pathogenicity of Huntington's disease related aggregates.Scientific reports · 2024Article
- Genome-Wide Identification and Analysis of MaizePlants (Basel, Switzerland) · 2024Article
- Pam16 and Pam18 were repurposed during Trypanosoma brucei evolution to regulate the replication of mitochondrial DNA.PLoS biology · 2024Article
188 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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DnaJ is a molecular chaperone and the prototypical member of the J-protein family. J proteins are defined by the presence of a J domain that can regulate the activity of 70-kDa heat-shock proteins. Sequence analysis on the genome of Saccharomyces cerevisiae has revealed 22 proteins that establish four distinguishing structural features of the J domain: predicted helicity in segments I-IV, precisely placed interhelical contact residues, a lysine-rich surface on helix II and placement of the diagnostic sequence HPD between the predicted helices II and III. We suggest that this definition of the J-protein family could be used for other genome-wide studies. In addition, three J-like proteins were identified in yeast that contain regions closely resembling a J domain, but in which the HPD motif is non-conservatively replaced. We suggest that J-like proteins might function to regulate the activity of bona fide J proteins during protein translocation, assembly and disassembly.
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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.