The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The gene symbol SSA4 in this report refers specifically to the heat shock protein SSA4 (Ssa4) from Saccharomyces cerevisiae strain S288c, encoded by YER103W and corresponding to UniProt P22202. This identity match is explicitly stated in a focused review of yeast cytosolic Hsp70 isoforms, which lists Ssa4 (YER103W, UniProt P22202) as one of the four cytosolic Ssa Hsp70 paralogs. (lotz2019notquitethe pages 1-3)
SSA4 encodes Ssa4, a member of the cytosolic Hsp70 (70 kDa heat shock protein) family. In yeast, the Ssa subfamily comprises four paralogs (Ssa1–Ssa4) that support essential proteostasis functions, including:
- binding exposed hydrophobic segments in client proteins;
- assisting folding/refolding of nascent or stress-damaged proteins;
- cooperating with other chaperone systems to route clients toward refolding, sequestration, or degradation. (verghese2012biologyofthe pages 13-13, farley2023effectsofhsp70 pages 2-4)
Hsp70 proteins have a canonical domain architecture consisting of an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD) connected by a flexible linker. Sequence differences among Ssa paralogs are concentrated in the SBD “lid” and an NBD surface implicated in J-protein cochaperone interactions, supporting the idea that paralogs can differ in cochaperone/client preferences even when broadly redundant. (lotz2019notquitethe pages 1-3)
A major organizing principle for the Ssa paralogs is expression regulation:
- SSA1/SSA2 are largely constitutively expressed.
- SSA3/SSA4 are stress-inducible (e.g., induced during heat shock) and can also be induced in strains lacking SSA1/SSA2. (verghese2012biologyofthe pages 13-13, lotz2019notquitethe pages 1-3)
Although any single Ssa isoform can support viability, ssa1Δ ssa2Δ double mutants show severe growth defects and thermosensitivity, suggesting SSA3/SSA4 do not fully replace all Ssa1/Ssa2 functions under normal growth. (verghese2012biologyofthe pages 13-13)
SSA4 encodes an ATP-dependent molecular chaperone (Hsp70 family) rather than an enzyme with a discrete small-molecule substrate. Its “substrate specificity” is primarily proteins/peptides exposing hydrophobic segments, typical of unfolded or partially folded polypeptides. The Ssa family contributes to:
- folding/refolding,
- prevention of aggregation,
- triage of damaged proteins toward degradation,
- and cooperation with disaggregation machinery (notably Hsp104 in yeast). (verghese2012biologyofthe pages 13-13, lotz2019notquitethe pages 1-3, jawed2023balancedactivitiesof pages 1-2)
A central pathway involving SSA4 is the yeast heat shock response, governed by Hsf1, where Hsp70 provides negative feedback:
- Hsf1 activates transcription of Hsp70 genes including SSA3/SSA4.
- Hsp70 represses Hsf1, establishing a two-component negative feedback loop.
This architecture was experimentally tested by genetically decoupling Hsf1 regulation from cytosolic Hsp70 paralogs (SSA1/2/3/4), demonstrating that without heat-induced Hsp70 transcription, Hsf1 fails to deactivate efficiently after heat shock. (krakowiak2018hsf1andhsp70 pages 2-4, krakowiak2018hsf1andhsp70 pages 1-2)
SSA4 is also directly assayed as an Hsf1 target gene in mechanistic studies of Hsf1 regulation by Hsp70–Hsf1 physical contacts, where SSA4 transcript induction is tracked by RNA-seq/qRT-PCR under heat shock and altered when Hsp70–Hsf1 regulation is disrupted. (peffer2019regulationofthe pages 18-20)
Ssa-family Hsp70s cooperate with degradation pathways:
- The Ssa Hsp70 system interfaces with the ubiquitin–proteasome system (UPS) and helps balance refolding vs degradation demands; proteostasis defects can trigger UPS induction, and inappropriate UPS upregulation can worsen growth in some low-Hsp70-capacity contexts. (jawed2023balancedactivitiesof pages 1-2)
- In disease-protein models, stress-inducible Ssa isoforms including Ssa4 can reduce toxicity of aggregation-prone proteins by promoting clearance mechanisms, including autophagy (see §4). (gupta2018theyeaststress pages 1-2)
In the evidence retrieved here, Ssa4 is consistently classified as a cytosolic/cytoplasmic Hsp70 (Ssa family). (lotz2019notquitethe pages 1-3, verghese2012biologyofthe pages 13-13)
More granular stress-dependent relocalization is most clearly developed at the Hsp70-system level (rather than SSA4 specifically) in recent work suggesting spatiotemporal control of Hsp70 partitioning (nuclear vs cytosolic condensates) contributes to heat shock feedback. SSA paralogs (including SSA4) are included among feedback effector genes in that framework, but the excerpted evidence does not isolate Ssa4 localization dynamics from other paralogs. (garde2024feedbackcontrolof pages 1-4)
A major recent SSA4-specific advance is the discovery that SSA4 is regulated not only transcriptionally but also post-transcriptionally at the mRNA translation/decay level.
In Nucleic Acids Research (publication date: May 2023), Boopathy et al. show that:
- SSA4 coding sequence is enriched in low-frequency codons, promoting ribosome stalling during heat stress.
- Stalled ribosomes on SSA4 are recognized by RQC factors Asc1 and Hel2, and by ribosomal proteins identified as novel components (Rps28A, Rps19B).
- This RQC engagement downregulates Ssa4 protein synthesis during heat shock, preventing overproduction.
- Unexpectedly, RQC recognition does not trigger canonical No-Go Decay of SSA4 mRNA; instead, Asc1 promotes rapid SSA4 mRNA destabilization during recovery via an off-ribosome mechanism (independent of Asc1 ribosome binding and independent of SSA4 codon optimality). (boopathy2023theribosomequality pages 1-2)
Quantitative SSA4 data (Boopathy et al., 2023):
- WT SSA4 mRNA half-life ~30 min.
- Asc1 M1X mutant increases SSA4 mRNA half-life to 84 min.
- The M1X strain produces ~7-fold more Ssa4 protein than WT upon heat shock.
- Deleting ASC1 increased SSA4 mRNA half-life ~2.5× in a comparison described in the excerpt; RPS28A or EDC3 deletions prolonged half-life by ~1.5×. (boopathy2023theribosomequality pages 12-13)
These results update the prevailing “HSF1 transcription induces Hsp70” view by showing SSA4 output is also tuned by translational and mRNA-decay control during stress and recovery.
A 2024 systems analysis preprint (bioRxiv; publication date: Jan 2024) proposes that negative feedback in the HSR is organized around a core loop controlling Hsp70 expression, reinforced by an auxiliary loop controlling Hsp70 localization/condensate interactions.
Key quantitative statements from the excerpt include:
- the yeast Hsf1 regulon is a compact set of 42 target genes;
- induction magnitudes across these targets span <10% to >8-fold;
- Hsp70 repression of Hsf1 is restored on the order of ~15 minutes after heat shock (rebinding/repression kinetics described in the excerpt). (garde2024feedbackcontrolof pages 1-4)
While this excerpt is not SSA4-exclusive, it places SSA paralogs (including SSA4) in the modern feedback-control framing of the HSR.
Evidence supports both redundancy and specialization among Ssa paralogs:
- Physical interactome coverage under standard conditions suggests inducible Ssa3/Ssa4 have far smaller reported interactomes (e.g., Ssa4: 57 proteins) than constitutive Ssa1/Ssa2 (e.g., Ssa1: 717), though this may reflect lower abundance at 30°C and condition dependence. Only ~1.5% of interactions are shared across all Ssa isoforms in the cited global datasets. (lotz2019notquitethe pages 3-4)
- Protein stability differs markedly among paralogs: reported half-lives include Ssa4 >100 h, much longer than Ssa1–3 in the same dataset. (lotz2019notquitethe pages 1-3)
These data support a model where Ssa4 is an inducible but long-lived cytosolic Hsp70 that may be deployed as a durable proteostasis component following stress.
In a yeast model of proteotoxicity (publication date: Oct 2018), cells expressing stress-inducible Ssa3 or Ssa4 as the sole Ssa isoform showed reduced α-synuclein toxicity, and protection extended to other inclusion-forming proteins (e.g., polyQ). The mechanism supported in the excerpt is promotion of α-synuclein degradation through autophagy, not simply induction of a generalized stress response, highlighting isoform-dependent proteostasis control. (gupta2018theyeaststress pages 1-2)
Although SSA4 itself is a basic cell-biology gene, the literature supports several applied uses of SSA4/Ssa4 biology:
Synthetic biology / strain engineering for stress tolerance and production stability (conceptual and emerging): The ability of Hsf1–Hsp70 networks to manage unfolded-protein stress is being leveraged in biotechnology contexts; studies of Hsf1/Hsp networks in yeast production settings suggest chaperone networks can influence yields under high expression burden. While not SSA4-specific in the excerpt, SSA4 is explicitly an Hsf1-regulated Hsp70 effector in the HSR network. (krakowiak2018hsf1andhsp70 pages 2-4, garde2024feedbackcontrolof pages 1-4)
Proteostasis engineering in yeast as a platform for human disease protein aggregation: SSA4’s inducible isoform properties and its link to autophagic clearance in α-synuclein models make it relevant to yeast-based screening and mechanistic dissection of aggregation and clearance pathways. (gupta2018theyeaststress pages 1-2)
mRNA design/translation control under stress: The 2023 findings that SSA4 output is tuned via codon usage, ribosome stalling, and Asc1/Hel2 pathways provides a concrete framework for engineering stress-responsive expression systems where translation persists under heat shock but is shut off rapidly during recovery. (boopathy2023theribosomequality pages 1-2, boopathy2023theribosomequality pages 12-13)
The following table summarizes SSA4 findings, separating SSA4-specific evidence from Ssa-family/system-level statements and providing URLs/DOIs and publication dates.
| Aspect | Key finding | Evidence type (review/primary) | System/condition | Quantitative/statistics (if any) | Citation (context id) | Publication (authors, year, journal) | URL/DOI |
|---|---|---|---|---|---|---|---|
| Identity/domains | SSA4 is verified as Ssa4, a cytosolic Hsp70 of Saccharomyces cerevisiae, encoded by YER103W and corresponding to UniProt P22202; canonical Hsp70 architecture includes an NBD and SBD linked by a flexible linker, with inter-isoform variation enriched in the SBD lid and an NBD surface implicated in J-protein interactions. | Review | Budding yeast cytosolic Hsp70 family | Ssa1 shares ~85% identity with Ssa4 | (lotz2019notquitethe pages 1-3) | Lotz et al., 2019, Current Genetics | https://doi.org/10.1007/s00294-019-00978-8 |
| Identity/regulation | Ssa1–4 are the four cytosolic Ssa Hsp70s; SSA3/SSA4 are stress-inducible, whereas SSA1/SSA2 are constitutive. Any single Ssa can support viability, but ssa1Δ ssa2Δ cells are slow-growing and thermosensitive, indicating inducible paralogs do not fully replace constitutive ones. | Review | Yeast heat-shock/proteostasis network | No explicit SSA4 fold-change in excerpt | (verghese2012biologyofthe pages 13-13) | Verghese et al., 2012, Microbiology and Molecular Biology Reviews | https://doi.org/10.1128/MMBR.05018-11 |
| Regulation | SSA4 is an Hsf1-induced gene; Hsf1-mediated induction of SSA3/SSA4 is central to the Hsp70–Hsf1 negative-feedback loop. A strain with all four SSA genes decoupled from Hsf1 regulation failed to induce Hsp70 during heat shock despite elevated basal Hsp70. | Primary | Heat shock response; feedback-severed DFBL yeast strain | Qualitative result: no heat-induced Hsp70 induction in DFBL | (krakowiak2018hsf1andhsp70 pages 2-4) | Krakowiak et al., 2018, eLife | https://doi.org/10.7554/eLife.31668 |
| Regulation | SSA4 was assayed as an Hsf1 target by RNA-seq and qRT-PCR; disruption of bipartite Hsp70–Hsf1 contacts caused constitutive Hsf1 activation, slow growth, and dysregulated target-gene expression including SSA4. | Primary | 37°C heat shock; Hsf1 mutant backgrounds | RNA-seq at 37°C for 15 min; qRT-PCR statistics reported but numeric SSA4 values not given in excerpt | (peffer2019regulationofthe pages 18-20) | Peffer et al., 2019, Journal of Biological Chemistry | https://doi.org/10.1074/jbc.RA119.008822 |
| Regulation/localization | Recent systems analysis places cytosolic Hsp70 paralogs (SSA1, SSA3, SSA4) in the heat-shock feedback architecture, where Hsp70 rebinding represses Hsf1 after stress and auxiliary loops regulate Hsp70 partitioning between nucleus and cytosolic condensates. | Primary preprint | Yeast heat shock response dynamics | Hsf1 regulon: 42 genes; induction magnitudes range from <10% to >8-fold across targets (not SSA4-specific) | (garde2024feedbackcontrolof pages 1-4) | Garde et al., 2024, bioRxiv | https://doi.org/10.1101/2024.01.09.574867 |
| Quantitative data/regulation | SSA4 mRNA is uniquely enriched in low-frequency codons that promote ribosome stalling during heat shock; Asc1/Hel2 and RQC factors tune SSA4 translation and recovery-phase decay rather than triggering standard NGD. | Primary | Heat shock and recovery | WT SSA4 mRNA t1/2 ~30 min; Asc1 M1X t1/2 84 min; ASC1 deletion increased half-life ~2.5× in one comparison; M1X produced ~7-fold more Ssa4 protein after heat shock | (boopathy2023theribosomequality pages 12-13, boopathy2023theribosomequality pages 7-8, boopathy2023theribosomequality pages 1-2) | Boopathy et al., 2023, Nucleic Acids Research | https://doi.org/10.1093/nar/gkad338 |
| Localization | Ssa4 is a cytosolic Hsp70; inducible Ssa3/4 are low at 30°C, likely biasing interactome studies toward constitutive isoforms under non-stress conditions. | Review | Standard growth vs stress conditions | Reported physical interactors: Ssa4 57 vs Ssa1 717, Ssa2 375, Ssa3 69; only ~1.5% shared across isoforms | (lotz2019notquitethe pages 3-4) | Lotz et al., 2019, Current Genetics | https://doi.org/10.1007/s00294-019-00978-8 |
| Function/pathways | Cytosolic Ssa Hsp70s including Ssa4 function in protein folding/refolding, prevention of aggregation, disaggregation with Hsp104, and triage of damaged proteins for degradation. | Review | General proteostasis network | Ssa4 half-life reported as >100 h | (lotz2019notquitethe pages 1-3) | Lotz et al., 2019, Current Genetics | https://doi.org/10.1007/s00294-019-00978-8 |
| Function/pathways | The Ssa family broadly supports folding, translocation, and degradation; depletion/inactivation causes client-folding defects, while stress-inducible SSA3/SSA4 are induced by heat shock or SSA1/2 loss. | Review | General yeast proteostasis | Any single Ssa supports viability, but inducible paralogs incompletely complement Ssa1/2 loss | (verghese2012biologyofthe pages 13-13) | Verghese et al., 2012, Microbiology and Molecular Biology Reviews | https://doi.org/10.1128/MMBR.05018-11 |
| Function/pathways | Cells expressing stress-inducible Ssa3 or Ssa4 as the sole Ssa isoform show reduced α-synuclein toxicity and protection against other aggregation-prone proteins; mechanism implicated is promotion of autophagic degradation, not simply general stress induction. | Primary | Yeast models of α-synuclein/polyQ proteotoxicity | No exact fold-change in excerpt | (gupta2018theyeaststress pages 1-2) | Gupta et al., 2018, PLoS Genetics | https://doi.org/10.1371/journal.pgen.1007751 |
| Function/pathways | Ssa1–4 are essential cytosolic Hsp70s; Hsp70 capacity must be balanced with the ubiquitin–proteasome system (UPS) and sequestration pathways. Hsp70 cooperates with Hsp104 for disaggregation and with Hsp90 for client folding. | Primary review-style research | Proteostasis mutants with low Hsp70 capacity | Simultaneous deletion of SSA1–SSA4 is lethal; reducing 26S proteasome levels improved growth/refolding in low-Hsp70-capacity mutants | (jawed2023balancedactivitiesof pages 1-2) | Jawed et al., 2023, Frontiers in Molecular Biosciences | https://doi.org/10.3389/fmolb.2022.1106477 |
| Function/pathways | The Ssa family is described as managing irretrievably misfolded proteins—including aggregates and prions—through proteasomal or lysosomal/autophagic routes; however, Farley et al. chiefly establish Ssa1/Ssa2 roles and do not provide a distinct SSA4 mechanism in the excerpt. | Primary | Ste5 scaffold quality-control context; mating MAPK pathway | Qualitative family-level statement; no SSA4-specific statistic | (farley2023effectsofhsp70 pages 2-4, farley2023effectsofhsp70 pages 1-2) | Farley et al., 2023, PLOS ONE | https://doi.org/10.1371/journal.pone.0289339 |
| Comparative pathway evidence | During arsenite stress, aggregate clearance depends on Hsp104/Hsp70/Hsp40 systems; the excerpt directly supports Ssa1/2 rather than Ssa4, but it places Ssa1–Ssa4 within the cytoplasmic Hsp70 disaggregation framework. | Primary | Arsenite-induced proteotoxic stress | ssa1Δ ssa2Δ mutants accumulated more Sis1-GFP foci and cleared aggregates more slowly | (hua2022differentialcontributionsof pages 5-6) | Hua et al., 2022, Journal of Biological Chemistry | https://doi.org/10.1016/j.jbc.2022.102680 |
| Regulation/redox sensing | Heat-inducible Ssa3/4 are distinguished from constitutive Ssa1/2 by cysteine content; Ssa3/4 lack the Ssa1/Ssa2 C264 but contain C303, supporting biochemical divergence among paralogs in stress sensing/regulation. | Primary | Thiol-reactive compound response; Hsf1 regulation context | No SSA4-specific fold-change in excerpt | (wang2012theyeasthsp70 pages 6-7) | Wang et al., 2012, Molecular Biology of the Cell | https://doi.org/10.1091/mbc.E12-06-0447 |
Table: This table summarizes identity, regulation, localization, function, and quantitative findings for yeast SSA4/Ssa4 (YER103W; UniProt P22202) from key reviews and primary studies. It highlights where evidence is SSA4-specific versus family-level, and emphasizes recent 2023-2024 mechanistic work on SSA4 mRNA regulation.
SSA4 (YER103W; UniProt P22202) encodes Ssa4, a stress-inducible cytosolic Hsp70 chaperone that supports proteostasis by binding non-native polypeptides and cooperating with cochaperones and downstream quality-control systems to refold, sequester, or degrade damaged proteins. SSA4 is a direct part of the Hsf1 heat shock transcriptional program and contributes to the Hsf1–Hsp70 negative feedback loop controlling heat shock response dynamics. Beyond transcriptional induction, SSA4 output is now understood to be post-transcriptionally tuned: the SSA4 coding sequence promotes ribosome stalling and engages Asc1/Hel2-dependent ribosome quality control that limits Ssa4 overproduction during heat shock and drives rapid SSA4 mRNA clearance during recovery. (lotz2019notquitethe pages 1-3, verghese2012biologyofthe pages 13-13, krakowiak2018hsf1andhsp70 pages 2-4, boopathy2023theribosomequality pages 1-2, boopathy2023theribosomequality pages 12-13)
References
(lotz2019notquitethe pages 1-3): Sarah K. Lotz, Laura E. Knighton, Nitika, Gary W. Jones, and Andrew W. Truman. Not quite the ssame: unique roles for the yeast cytosolic hsp70s. Current Genetics, 65:1127-1134, Apr 2019. URL: https://doi.org/10.1007/s00294-019-00978-8, doi:10.1007/s00294-019-00978-8. This article has 52 citations and is from a peer-reviewed journal.
(verghese2012biologyofthe pages 13-13): Jacob Verghese, Jennifer Abrams, Yanyu Wang, and Kevin A. Morano. Biology of the heat shock response and protein chaperones: budding yeast (saccharomyces cerevisiae) as a model system. Microbiology and Molecular Biology Reviews, 76:115-158, Jun 2012. URL: https://doi.org/10.1128/mmbr.05018-11, doi:10.1128/mmbr.05018-11. This article has 768 citations and is from a domain leading peer-reviewed journal.
(farley2023effectsofhsp70 pages 2-4): Francis W. Farley, Ryan R. McCully, Paul B. Maslo, Lu Yu, Mark A. Sheff, Homayoun Sadeghi, and Elaine A. Elion. Effects of hsp70 chaperones ssa1 and ssa2 on ste5 scaffold and the mating mitogen-activated protein kinase (mapk) pathway in saccharomyces cerevisiae. PLOS ONE, 18:e0289339, Oct 2023. URL: https://doi.org/10.1371/journal.pone.0289339, doi:10.1371/journal.pone.0289339. This article has 2 citations and is from a peer-reviewed journal.
(jawed2023balancedactivitiesof pages 1-2): Areeb Jawed, Chi-Ting Ho, Tomas Grousl, Aseem Shrivastava, Thomas Ruppert, Bernd Bukau, and Axel Mogk. Balanced activities of hsp70 and the ubiquitin proteasome system underlie cellular protein homeostasis. Frontiers in Molecular Biosciences, Jan 2023. URL: https://doi.org/10.3389/fmolb.2022.1106477, doi:10.3389/fmolb.2022.1106477. This article has 14 citations.
(krakowiak2018hsf1andhsp70 pages 2-4): Joanna Krakowiak, Xu Zheng, Nikit Patel, Jayamani Anandhakumar, Kendra Valerius, David S. Gross, Ahmad S. Khalil, and David Pincus. Hsf1 and hsp70 constitute a two-component feedback loop that regulates the yeast heat shock response. eLife, Aug 2018. URL: https://doi.org/10.7554/elife.31668, doi:10.7554/elife.31668. This article has 189 citations and is from a domain leading peer-reviewed journal.
(krakowiak2018hsf1andhsp70 pages 1-2): Joanna Krakowiak, Xu Zheng, Nikit Patel, Jayamani Anandhakumar, Kendra Valerius, David S. Gross, Ahmad S. Khalil, and David Pincus. Hsf1 and hsp70 constitute a two-component feedback loop that regulates the yeast heat shock response. eLife, Aug 2018. URL: https://doi.org/10.7554/elife.31668, doi:10.7554/elife.31668. This article has 189 citations and is from a domain leading peer-reviewed journal.
(peffer2019regulationofthe pages 18-20): Sara Peffer, Davi Gonçalves, and Kevin A. Morano. Regulation of the hsf1-dependent transcriptome via conserved bipartite contacts with hsp70 promotes survival in yeast. Aug 2019. URL: https://doi.org/10.1074/jbc.ra119.008822, doi:10.1074/jbc.ra119.008822. This article has 77 citations and is from a domain leading peer-reviewed journal.
(gupta2018theyeaststress pages 1-2): Arpit Gupta, Anuradhika Puri, Prashant Singh, Surabhi Sonam, Richa Pandey, and Deepak Sharma. The yeast stress inducible ssa hsp70 reduces α-synuclein toxicity by promoting its degradation through autophagy. PLOS Genetics, 14:e1007751, Oct 2018. URL: https://doi.org/10.1371/journal.pgen.1007751, doi:10.1371/journal.pgen.1007751. This article has 27 citations and is from a domain leading peer-reviewed journal.
(garde2024feedbackcontrolof pages 1-4): Rania Garde, Annisa Dea, Madeline F. Herwig, and David Pincus. Feedback control of the heat shock response by spatiotemporal regulation of hsp70. bioRxiv, Jan 2024. URL: https://doi.org/10.1101/2024.01.09.574867, doi:10.1101/2024.01.09.574867. This article has 17 citations.
(boopathy2023theribosomequality pages 1-2): Lokha R Alagar Boopathy, Emma Beadle, Alan RuoChen Xiao, Aitana Garcia-Bueno Rico, Celia Alecki, Irene Garcia de-Andres, Kyla Edelmeier, Luca Lazzari, Mehdi Amiri, and Maria Vera. The ribosome quality control factor asc1 determines the fate of hsp70 mrna on and off the ribosome. Nucleic Acids Research, 51:6370-6388, May 2023. URL: https://doi.org/10.1093/nar/gkad338, doi:10.1093/nar/gkad338. This article has 13 citations and is from a highest quality peer-reviewed journal.
(boopathy2023theribosomequality pages 12-13): Lokha R Alagar Boopathy, Emma Beadle, Alan RuoChen Xiao, Aitana Garcia-Bueno Rico, Celia Alecki, Irene Garcia de-Andres, Kyla Edelmeier, Luca Lazzari, Mehdi Amiri, and Maria Vera. The ribosome quality control factor asc1 determines the fate of hsp70 mrna on and off the ribosome. Nucleic Acids Research, 51:6370-6388, May 2023. URL: https://doi.org/10.1093/nar/gkad338, doi:10.1093/nar/gkad338. This article has 13 citations and is from a highest quality peer-reviewed journal.
(lotz2019notquitethe pages 3-4): Sarah K. Lotz, Laura E. Knighton, Nitika, Gary W. Jones, and Andrew W. Truman. Not quite the ssame: unique roles for the yeast cytosolic hsp70s. Current Genetics, 65:1127-1134, Apr 2019. URL: https://doi.org/10.1007/s00294-019-00978-8, doi:10.1007/s00294-019-00978-8. This article has 52 citations and is from a peer-reviewed journal.
(boopathy2023theribosomequality pages 7-8): Lokha R Alagar Boopathy, Emma Beadle, Alan RuoChen Xiao, Aitana Garcia-Bueno Rico, Celia Alecki, Irene Garcia de-Andres, Kyla Edelmeier, Luca Lazzari, Mehdi Amiri, and Maria Vera. The ribosome quality control factor asc1 determines the fate of hsp70 mrna on and off the ribosome. Nucleic Acids Research, 51:6370-6388, May 2023. URL: https://doi.org/10.1093/nar/gkad338, doi:10.1093/nar/gkad338. This article has 13 citations and is from a highest quality peer-reviewed journal.
(farley2023effectsofhsp70 pages 1-2): Francis W. Farley, Ryan R. McCully, Paul B. Maslo, Lu Yu, Mark A. Sheff, Homayoun Sadeghi, and Elaine A. Elion. Effects of hsp70 chaperones ssa1 and ssa2 on ste5 scaffold and the mating mitogen-activated protein kinase (mapk) pathway in saccharomyces cerevisiae. PLOS ONE, 18:e0289339, Oct 2023. URL: https://doi.org/10.1371/journal.pone.0289339, doi:10.1371/journal.pone.0289339. This article has 2 citations and is from a peer-reviewed journal.
(hua2022differentialcontributionsof pages 5-6): Sansan Hua, Agnieszka Kłosowska, Joana I. Rodrigues, Gabriel Petelski, Lidia A. Esquembre, Emma Lorentzon, Lars F. Olsen, Krzysztof Liberek, and Markus J. Tamás. Differential contributions of the proteasome, autophagy, and chaperones to the clearance of arsenite-induced protein aggregates in yeast. Journal of Biological Chemistry, 298:102680, Dec 2022. URL: https://doi.org/10.1016/j.jbc.2022.102680, doi:10.1016/j.jbc.2022.102680. This article has 11 citations and is from a domain leading peer-reviewed journal.
(wang2012theyeasthsp70 pages 6-7): Yanyu Wang, Patrick A. Gibney, James D. West, and Kevin A. Morano. The yeast hsp70 ssa1 is a sensor for activation of the heat shock response by thiol-reactive compounds. Molecular Biology of the Cell, 23:3290-3298, Sep 2012. URL: https://doi.org/10.1091/mbc.e12-06-0447, doi:10.1091/mbc.e12-06-0447. This article has 88 citations and is from a domain leading peer-reviewed journal.