ReviewCellular and molecular life sciences : CMLS2005
Hsp70 chaperones: cellular functions and molecular mechanism.
Review in Cellular and molecular life sciences : CMLS, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1,303 papers.
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Who cites it
1,303 citing papers in PubMed, 2,830 citations in OpenAlex.
- Differential roles of HSP70 and HSP90 in Senecavirus A infection: IRES-dependent translational regulation and viral replication mechanisms.Virulence · 2026Article
- Functional and genomic characterization of halotolerant Bacillus paramycoides MSR1 for MICCP-based durability enhancement of cementitious materials under saline conditions.World journal of microbiology & biotechnology · 2026Article
- Repeated Moderate and Severe Heat Exposure Has Divergent Effects on Skeletal Muscle Mitochondrial, Proteostatic and Neuromuscular Outcomes in Mice.Acta physiologica (Oxford, England) · 2026Article
- Proteostasis and ageing dissidence.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- HOM2 and TPK1 are associated with Kluyveromyces marxianus growth under high-temperature and reduced-aeration conditions.World journal of microbiology & biotechnology · 2026Article
- Endogenous Expression of HSP70 and Thioredoxin-1 During Methamphetamine-Induced Degeneration.Biomedicines · 2026Article
- Review
- Exploratory Cross-Cohort Transcriptomic Comparison of Coronary Artery Disease and Non-Obstructive Azoospermia.International journal of molecular sciences · 2026Article
- Integrative In Silico and Experimental Analysis Reveals MT1A and HSP70 as Components of a Dual Biomarker Axis for Heavy Metal Exposure.Biological trace element research · 2026Article
- Evolution and Active Learning Identify Terminal and Distal Determinants for Improved TAL in P-Coumaric Acid Production.Biotechnology and bioengineering · 2026Article
- Synergies and trade-offs in the heat shock response mechanism.PLoS computational biology · 2026Article
- A missing link in the METTL3 chain: Chaperone regulation of METTL3 as a BAG:HSP70 client protein.Neural regeneration research · 2026Article
- A Dosimetric Reappraisal of the Photobiomodulation Literature Assessing Animal Safety and Phototoxicity Evidence for Photobiomodulation in Oncology: Phantom Dangers.Biomedicines · 2026Review
- Fermented Navy Bean-Derived Agents Restore Antibiotic Susceptibility inJournal of microbiology and biotechnology · 2026Article
- Novel Insights into the Human Hsc70 Structure by Cross-Linking Mass Spectrometry and Molecular Modeling.Journal of proteome research · 2026Article
- Development of domain-specific probes ofAntimicrobial agents and chemotherapy · 2026Article
- Immunohistochemical Evaluation of TLR-4, HSP-70 and Caspase-3 Expressions in Lesional Areas of Ecthyma Disease.Veterinary dermatology · 2026Article
- Seasonal impact on the thermal tolerance window of a keystone coastal grazer, the common periwinkle Littorina littorea.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2026Article
- Proteasome inhibitors rescue hypomyelination in iPSC based model of HIKESHI-associated leukodystrophy.Journal of translational medicine · 2026Article
- Nitration in cancer signaling.Redox biology · 2026Review
1,243 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hsp70 proteins are central components of the cellular network of molecular chaperones and folding catalysts. They assist a large variety of protein folding processes in the cell by transient association of their substrate binding domain with short hydrophobic peptide segments within their substrate proteins. The substrate binding and release cycle is driven by the switching of Hsp70 between the low-affinity ATP bound state and the high-affinity ADP bound state. Thus, ATP binding and hydrolysis are essential in vitro and in vivo for the chaperone activity of Hsp70 proteins. This ATPase cycle is controlled by co-chaperones of the family of J-domain proteins, which target Hsp70s to their substrates, and by nucleotide exchange factors, which determine the lifetime of the Hsp70-substrate complex. Additional co-chaperones fine-tune this chaperone cycle. For specific tasks the Hsp70 cycle is coupled to the action of other chaperones, such as Hsp90 and Hsp100.
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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.