ReviewApoptosis : an international journal on programmed cell death2021
Heat shock proteins-driven stress granule dynamics: yet another avenue for cell survival.
Review in Apoptosis : an international journal on programmed cell death, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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.
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Who cites it
32 citing papers in PubMed, 42 citations in OpenAlex.
- Delaying Stress Granule Disassembly by PARG Inhibition Attenuates Renal Tubular Cell Pyroptosis in Acute Kidney Injury.International journal of molecular sciences · 2026Article
- Stress granule phase separation in stress-responsive cytosolic extract-in-oil droplets.Nature communications · 2026Article
- Heat shock proteins in male infertility: recent advances and clinical implications.Frontiers in cell and developmental biology · 2026Review
- Heat shock proteins in farmed aquatic animals: advancing animal health and welfare management through building resilience.Frontiers in immunology · 2026Review
- G3BP1 methylation by PRMT5 facilitates its recruitment of TBK1 for IRF3 activation during host response to foreign ribonucleic acids.Frontiers in immunology · 2026Article
- Spatial proteomics reveals recombinant human laminin-111 restores adhesion signaling to laminin-α2-deficient muscle.JCI insight · 2025Article
- Role of heat shock proteins in renal function and adaptation to heat stress: Implications for global warming.World journal of nephrology · 2025Review
- Low expression of HSP27 and HSP70 predicts poor prognosis in laryngeal squamous cell carcinoma.Journal of cancer research and clinical oncology · 2025Article
- The impact of stress in domestic animals: roles of heat shock proteins and acute-phase proteins.Veterinary research communications · 2025Review
- The phenomenon of anhydrobiosis-structural and functional changes in yeast cells.Applied microbiology and biotechnology · 2025Review
- Biogenesis of stress granules and their role in the regulation of stress-induced male reproduction disorders.Cell communication and signaling : CCS · 2025Review
- Stress Granule Induction in Rat Retinas Damaged by Constant LED Light.Investigative ophthalmology & visual science · 2025Article
- Reshuffling Overcrowded Milieu: Stress-Induced Reorganization of the Eukaryotic Membrane-Less Organelles.Sub-cellular biochemistry · 2025Review
- Calcium signaling from damaged lysosomes induces cytoprotective stress granules.The EMBO journal · 2024Article
- Intrinsically disordered regions and RNA binding domains contribute to protein enrichment in biomolecular condensates in Xenopus oocytes.Scientific reports · 2024Article
- Biological resilience in health and disease.Disease models & mechanisms · 2024Review
- Article
- Pifithrin-µ Induces Stress Granule Formation, Regulates Cell Survival, and Rewires Cellular Signaling.Cells · 2024Article
- Impact of Polyethylene Terephthalate Microplastics onBiology · 2024Article
- A mechanism that transduces lysosomal damage signals to stress granule formation for cell survival.bioRxiv : the preprint server for biology · 2024Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Heat shock proteins (HSPs) are evolutionary conserved 'stress-response' proteins that facilitate cell survival against various adverse conditions. HSP-mediated cytoprotection was hitherto reported to occur principally in two ways. Firstly, HSPs interact directly or indirectly with apoptosis signaling components and suppress apoptosis. Secondly, through chaperon activity, HSPs suppress proteotoxicity and maintain protein-homeostasis. Recent studies highlight the interaction of HSPs with cytoplasmic stress granules (SGs). SGs are conserved cytoplasmic mRNPs granules that aid in cell survival under stressful conditions. We primarily aim to describe the distinct cell survival strategy mediated by HSPs as the crucial regulators of SGs assembly and disassembly. Based on the growing evidence, HSPs and associated co-chaperones act as important determinants of SG assembly, composition and dissolution. Under cellular stress, as a 'stress-coping mechanism', the formation of SGs reprograms protein translation machinery and modulates signaling pathways indispensable for cell survival. Besides their role in suppressing apoptosis, HSPs also regulate protein-homeostasis by their chaperone activity as well as by their tight regulation of SG dynamics. The intricate molecular signaling in and around the nexus of HSPs-SGs and its importance in diseases has to be unearthed. These studies have significant implications in the management of chronic diseases such as cancer and neurodegenerative diseases where SGs possess pathological functions.
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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.