ArticleJournal of virology1996
Prion protein PrPc interacts with molecular chaperones of the Hsp60 family.
Article in Journal of virology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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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
42 citing papers in PubMed, 157 citations in OpenAlex.
- Trial
- Molecular Dynamics Simulations Reveal Novel Interacting Regions of Human Prion Protein to Brucella abortus Hsp60 Protein.Molecular biotechnology · 2024Article
- APP deficiency and HTRA2 modulates PrPBBA advances · 2022Article
- Structural and Computational Study of the GroEL-Prion Protein Complex.Biomedicines · 2021Article
- Functional genomics screen identifies proteostasis targets that modulate prion protein (PrP) stability.Cell stress & chaperones · 2021Article
- The Role of Cellular Prion Protein in Promoting Stemness and Differentiation in Cancer.Cancers · 2021Review
- Cross-Linking Cellular Prion Protein Induces Neuronal Type 2-Like Hypersensitivity.Frontiers in immunology · 2021Article
- Understanding and exploiting interactions between cellular proteostasis pathways and infectious prion proteins for therapeutic benefit.Open biology · 2020Article
- Cellular Prion Protein (PrPc): Putative Interacting Partners and Consequences of the Interaction.International journal of molecular sciences · 2020Review
- LRP/LR specific antibody IgG1-iS18 impedes neurodegeneration in Alzheimer's disease mice.Oncotarget · 2018Article
- Prion protein is required for tumor necrosis factor α (TNFα)-triggered nuclear factor κB (NF-κB) signaling and cytokine production.The Journal of biological chemistry · 2017Article
- Soluble polymorphic bank vole prion proteins induced by co-expression of quiescin sulfhydryl oxidase in E. coli and their aggregation behaviors.Microbial cell factories · 2017Article
- Membrane-enriched proteome changes and prion protein expression during neural differentiation and in neuroblastoma cells.BMC genomics · 2017Article
- Article
- Prion protein (PrP) gene-knockout cell lines: insight into functions of the PrP.Frontiers in cell and developmental biology · 2014Review
- Cellular transcripts regulated during infections with Highly Pathogenic H5N1 Avian Influenza virus in 3 host systems.Virology journal · 2011Article
- Heat shock proteins: cellular and molecular mechanisms in the central nervous system.Progress in neurobiology · 2010Review
- Review
- Interactions of prion protein with intracellular proteins: so many partners and no consequences?Cellular and molecular neurobiology · 2010Review
- The fatal attraction between pro-prion and filamin A: prion as a marker in human cancers.Biomarkers in medicine · 2010Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prions mediate the pathogenesis of certain neurodegenerative diseases, including bovine spongiform encephalopathy in cattle and Creutzfeldt-Jakob disease in humans. The prion particle consists mainly, if not entirely, of PrPSc, a posttranslationally modified isoform of the cellular host-encoded prion protein (PrPc). It has been suggested that additional cellular factors might be involved in the physiological function of PrPc and in the propagation of PrPSc. Here we employ a Saccharomyces cerevisiae two-hybrid screen to search for proteins which interact specifically with the Syrian golden hamster prion protein. Screening of a HeLa cDNA library identified heat shock protein 60 (Hsp60), a cellular chaperone as a major interactor for PrPc. The specificity of the interaction was confirmed in vitro for the recombinant proteins PrPc23-231 and rPrP27-30 fused to glutathione S-transferase with recombinant human Hsp60 as well as the bacterial GroEL. The interaction site for recombinant Hsp60 and GroEL proteins was mapped between amino acids 180 and 210 of the prion protein by screening with a set of recombinant PrPc fragments. The binding of Hsp60 and GroEL occurs within a region which contains parts of the putative alpha-helical domains H3 and H4 of the prion protein.
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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.