ReviewCurrent genetics2019
Not quite the SSAme: unique roles for the yeast cytosolic Hsp70s.
Review in Current genetics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
26 citing papers in PubMed.
- Mechanosensor-mediated Hsp70 phosphorylation orchestrates the landscape of the heat shock response.Nature communications · 2025Article
- Hsp70 chaperones, Ssa1 and Ssa2, limit poly(A) binding protein aggregation.Molecular biology of the cell · 2025Article
- Chaperone overexpression boosts heterologous small molecule production in Saccharomyces cerevisiae.Microbial cell factories · 2025Article
- Selective Translation Under Heat Shock: Integrating HSP70 mRNA Regulation with Cellular Stress Responses in Yeast and Mammals.Molecular biology of the cell · 2025Review
- Acetylation of the yeast Hsp40 chaperone protein Ydj1 fine-tunes proteostasis and translational fidelity.PLoS genetics · 2024Article
- Engineering cell-free systems by chemoproteomic-assisted phenotypic screening.RSC chemical biology · 2024Article
- Article
- The Physiological and Biochemical Response of Ribbed Mussels to Rising Temperatures: Benefits of Salt Marsh Cordgrass.Integrative organismal biology (Oxford, England) · 2024Article
- Article
- Chaperone requirements for de novo folding ofMolecular biology of the cell · 2022Article
- Feeling the heat: how chaperones deal with biomolecular condensates.Trends in biochemical sciences · 2022Article
- The APE2 Exonuclease Is a Client of the Hsp70-Hsp90 Axis in Yeast and Mammalian Cells.Biomolecules · 2022Article
- Structural and Functional Insights into GID/CTLH E3 Ligase Complexes.International journal of molecular sciences · 2022Review
- The C-terminal domain of Hsp70 is responsible for paralog-specific regulation of ribonucleotide reductase.PLoS genetics · 2022Article
- Genome-Wide Analyses of Heat Shock Protein Superfamily Provide New Insights on Adaptation to Sulfide-Rich Environments inInternational journal of molecular sciences · 2022Article
- Differential Interactions of Molecular Chaperones and Yeast Prions.Journal of fungi (Basel, Switzerland) · 2022Review
- Chaperone Networks in Fungal Pathogens of Humans.Journal of fungi (Basel, Switzerland) · 2021Review
- Post-translational modifications of Hsp70 family proteins: Expanding the chaperone code.The Journal of biological chemistry · 2020Review
- The Yeast Hsp70 Cochaperone Ydj1 Regulates Functional Distinction of Ssa Hsp70s in the Hsp90 Chaperoning Pathway.Genetics · 2020Article
- Functional diversity between HSP70 paralogs caused by variable interactions with specific co-chaperones.The Journal of biological chemistry · 2020Article
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
Abstract
The Heat Shock Protein 70s (Hsp70s) are an essential family of proteins involved in folding of new proteins and triaging of damaged proteins for proteasomal-mediated degradation. They are highly conserved in all organisms, with each organism possessing multiple highly similar Hsp70 variants (isoforms). These isoforms have been previously thought to be identical in function differing only in their spatio-temporal expression pattern. The model organism Saccharomyces cerevisiae (baker's yeast) expresses four Hsp70 isoforms Ssa1, 2, 3 and 4. Here, we review recent findings that suggest that despite their similarity, Ssa isoforms may have unique cellular 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.