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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
Target confirmed: The literature surveyed matches the UniProt-provided identity (P10591) for S. cerevisiae SSA1, also referenced by its systematic ORF YAL005C, encoding Ssa1, a cytosolic/nuclear Hsp70-family molecular chaperone. SSA1 is explicitly identified as “heat shock protein SSA1 (YAL005C)” and placed in the cytosolic Hsp70 subfamily in quantitative proteomics/network analyses (Apr 2015, https://doi.org/10.1002/pmic.201400527) (jarnuczak2015quantitativeproteomicsand pages 1-2). This matches expected Hsp70 domain architecture and cochaperone dependence (shan2023roleofhsp70 pages 1-2).
SSA1 encodes Ssa1, an ATP-dependent Hsp70 “foldase”/chaperone hub that binds non-native protein segments (typically exposed hydrophobic stretches) and promotes:
- folding of nascent chains,
- refolding of stress-denatured proteins,
- disaggregation in cooperation with other chaperones,
- and protein-quality-control (PQC) triage toward degradation pathways (farley2023effectsofhsp70 pages 2-4, shan2023roleofhsp70 pages 1-2, lotz2019notquitethe pages 1-3).
Mechanistically, expert consensus and reviews describe Hsp70s as having an N-terminal nucleotide-binding domain (NBD) and substrate-binding domain (SBD); ATP binding/hydrolysis in the NBD drives conformational switching in the SBD that controls client affinity, while J-domain proteins (Hsp40s) accelerate ATP hydrolysis and nucleotide exchange factors (NEFs) accelerate ADP release to reset the cycle (shan2023roleofhsp70 pages 1-2, lotz2019notquitethe pages 1-3, masser2019cytoplasmicproteinmisfolding pages 1-2).
Ssa1’s “decision point” behavior—fold vs hold vs degrade—emerges from cochaperone control:
- J-domain proteins (e.g., Sis1, Ydj1) stimulate ATP hydrolysis and target delivery (shan2023roleofhsp70 pages 1-2, rupali2018hsp4070110chaperonesadapt pages 1-2).
- NEFs (e.g., Fes1; Hsp110-class Sse1) catalyze ADP→ATP exchange and client release (masser2019cytoplasmicproteinmisfolding pages 1-2, nicklow2020activityofthe pages 7-8).
A particularly important structural feature for eukaryotic cytosolic Hsp70s is the C-terminal EEVD motif, which mediates interactions with cochaperones (including TPR-domain proteins) and also participates in Hsp70–JDP communication (shan2023roleofhsp70 pages 1-2, matos2024nmrstudieson pages 1-2).
Ssa1 is primarily cytosolic but also functions in the nucleus (e.g., nuclear accumulation is measurable in some genetic contexts), consistent with broad roles in cytosolic/nuclear proteostasis and quality control (farley2023effectsofhsp70 pages 2-4, farley2023effectsofhsp70 pages 24-26, rupali2018hsp4070110chaperonesadapt pages 1-2). Recombinant tagged Ssa proteins remain mainly cytosolic in microscopy-based assessments (matveenko2025optimizationofconditions pages 7-9).
A major 2024 mechanistic advance is the mapping of an Ssa1/Sis1 binding site on the Sup35 prion domain outside the amyloid core and demonstration that exposure of this site controls disaggregation efficiency and prion propagation (PNAS, Dec 2024, https://doi.org/10.1073/pnas.2318162121) (shen2024exposedhsp70bindingsite pages 1-2).
Key mechanistic findings:
- Ssa1 binding maps to Sup35NM residues 143–164, a segment consistent with Hsp70-binding chemistry; ATP-dependent binding is enhanced by Sis1 (shen2024exposedhsp70bindingsite pages 2-3).
- Deletion of 143–164 abolishes productive disaggregation by the Ssa1/Sis1/Hsp104 system and disrupts [PSI+] propagation in vivo (shen2024exposedhsp70bindingsite pages 4-6).
- Quantitative in vitro conditions reported include disaggregation assays using 5 µM Sup35NM with 2 µM Ssa1, 2 µM Sis1, 1 µM Hsp104 (shen2024exposedhsp70bindingsite pages 6-7) and multiple experiments with replication (e.g., ThT readouts with n=3) (shen2024exposedhsp70bindingsite pages 9-10).
This work positions SSA1 as a determinant of amyloid strain phenotypes through site-specific engagement that initiates the downstream disaggregation cascade (shen2024exposedhsp70bindingsite pages 9-10, shen2024exposedhsp70bindingsite pages 7-9).
A 2024 NMR study mapped how the Ssa1 C-terminal EEVD motif binds Sis1 at multiple sites, refining the physical basis of Hsp70–JDP coordination (Molecules, Dec 2024, https://doi.org/10.3390/molecules30010011) (matos2024nmrstudieson pages 1-2).
Quantitative/biophysical details include:
- PRE/CSP-based site mapping with defined thresholds (PRE < 0.88/0.7; CSP > 0.018) and contacts spanning GF region and CTDI (matos2024nmrstudieson pages 10-12).
- EEVD binding altered Sis1 dynamics; e.g., apparent correlation time τappc decreased from 9.8 ± 1.0 ns to 9.2 ± 1.0 ns (p < 0.05) for the J-domain, consistent with EEVD-modulated conformational behavior (matos2024nmrstudieson pages 10-12).
A 2023 study showed Ssa1 and Ssa2 act as chaperone regulators of the Ste5 MAPK scaffold, affecting Ste5 abundance, integrity, and localization and thereby controlling mating signaling output (PLOS ONE, Oct 2023, https://doi.org/10.1371/journal.pone.0289339) (farley2023effectsofhsp70 pages 1-2).
Quantitative highlights:
- Ste5 co-IP gel densitometry yielded Ste5:Hsp70 ratios of 1.45 (−α factor) vs 0.67 (+α factor), consistent with dynamic association changes upon pheromone stimulation (farley2023effectsofhsp70 pages 14-15).
- A functional readout showed Fus3-HA kinase activity in an ssa1Δ ssa2Δ background was ~16.7% of wild type, despite higher Fus3-HA abundance in the mutant (farley2023effectsofhsp70 pages 31-33).
- Shmoo formation after Ssa1 depletion for 6 h fell to 3.2 ± 0.25% (≈10-fold reduction) with p = 0.023095 (farley2023effectsofhsp70 pages 34-36).
- Quantitative proteomics cited within the study places Ssa1 at ~45,137 to 314,830 molecules/cell, highlighting its high abundance relative to pathway components like Ste5 (∼814 molecules/cell) (farley2023effectsofhsp70 pages 45-46).
These data support SSA1 as a proteostasis gatekeeper for signaling complexes (Ste5) in a canonical yeast MAPK pathway (farley2023effectsofhsp70 pages 31-33, farley2023effectsofhsp70 pages 34-36).
A 2023 study cautioned that Ssa1-GFP fusion can impair Ssa1 function and trigger large insoluble deposits (HADS) under mild stress conditions (Int. J. Mol. Sci., Aug 2023, https://doi.org/10.3390/ijms241612758) (grosfeld2023fusionofhsp70 pages 1-2).
Key observations:
- HADS form in high-density cultures and on non-fermentable carbon sources and are reduced by antioxidants, implicating oxidative damage contributions (grosfeld2023fusionofhsp70 pages 1-2, grosfeld2023fusionofhsp70 pages 2-6).
- Deposits colocalize with other chaperones and can be disassembled by Hsp104, consistent with chaperone-managed aggregate compartments (grosfeld2023fusionofhsp70 pages 1-2, grosfeld2023fusionofhsp70 pages 2-6).
- Replicate counting and significance reporting are described (150–600 cells/replicate; p<0.05, *p<0.01), although exact foci percentages are not included in the excerpt (grosfeld2023fusionofhsp70 pages 6-7).
Systems-level proteomics/network analyses place SSA1 among the central folding hubs:
- SSA1 abundance is ~8178 ppm (PaxDB-based estimate) and SSA1 has ~2489 client-protein links in curated interaction maps, consistent with high “hubness” (jarnuczak2015quantitativeproteomicsand pages 1-2).
- Chaperone network throughput analysis estimates that ~44% of all protein synthesis flux passes through the Hsp70 class (RAC–Hsp70–Hsp40 route) in budding yeast (Proteomics, Mar 2013, https://doi.org/10.1002/pmic.201200412) (brownridge2013quantitativeanalysisof pages 11-12, brownridge2013quantitativeanalysisof pages 12-15).
These provide quantitative justification for treating SSA1 as a primary functional node in proteome biogenesis (brownridge2013quantitativeanalysisof pages 11-12, jarnuczak2015quantitativeproteomicsand pages 1-2).
SSA1/Ssa1 contributes to the heat-shock response both as a chaperone capacity buffer and via PTM-mediated tuning:
- A mechanistic model shows Hsp70 binding restrains Hsf1, and misfolded proteins titrate Hsp70 away under heat shock, freeing Hsf1 activity; NEFs (Fes1, Sse1/2) affect this regulation, and fes1Δ is associated with constitutive Hsf1 activation (eLife, Sep 2019, https://doi.org/10.7554/elife.47791) (masser2019cytoplasmicproteinmisfolding pages 1-2).
- Quantitative MS shows that heat stress (37°C, 30 min) triggers rapid Ssa1 deacetylation at K86, K185, K354, K562, remodeling the Hsp70 interaction network while preserving essential function (Sci Rep, Nov 2019, https://doi.org/10.1038/s41598-019-52545-3) (xu2019rapiddeacetylationof pages 1-2).
SSA1/Ssa1 participates in PQC pathways that route cytosolic misfolded clients into nuclear QC machineries:
- In San1/Ubr1 QC pathways, Ssa1/Ssa2 are required both outside and inside the nucleus, while Ydj1 and Sse1 contribute to trafficking/import and Sis1 is required inside the nucleus for processing substrates (J Cell Biol, Jun 2018, https://doi.org/10.1083/jcb.201706091) (rupali2018hsp4070110chaperonesadapt pages 1-2).
Quantitative enzymology shows how NEFs regulate Hsp70 cycling relevant to SSA1 function:
- In Ssa1 peptide-release assays, Fes1 increased peptide off-rate from 0.083 ± 0.002 s−1 to 0.66 ± 0.017 s−1 (~8-fold); oxidant-treated Fes1 reduced this to 0.136 ± 0.023 s−1, and reductase treatment partially restored activity (J Biol Chem, Jan 2020, https://doi.org/10.1074/jbc.ra119.010125) (nicklow2020activityofthe pages 7-8).
This links redox stress to altered Ssa1 client cycling via NEF modulation (nicklow2020activityofthe pages 7-8).
A 2023 industrially oriented synthetic biology study reports that SSA1 deletion enhanced ethyl acetate production in engineered yeast (Biotechnology for Biofuels and Bioproducts, Apr 2023, https://doi.org/10.1186/s13068-023-02322-2) (cui2023genomewideanalysisreveals pages 10-11).
- The excerpt does not provide the exact % increase for SSA1 deletion alone (it refers to Fig. 6a), but it explicitly states the directionality (“enhanced ethyl acetate production”).
- It also reports that adding HSF1 overexpression on top of an SSA1-deleted background did not significantly increase ethyl acetate further (cui2023genomewideanalysisreveals pages 10-11).
This is a direct example of SSA1 manipulation being operationalized for metabolite titer engineering (cui2023genomewideanalysisreveals pages 10-11).
A 2024 review of engineering strategies for heterologous protein production in S. cerevisiae lists SSA1 among genes implicated in secretion-associated phenotypes from RNAi/microfluidic screening studies (Microbial Cell Factories, Jan 2024, https://doi.org/10.1186/s12934-024-02299-z) (zhao2024engineeringstrategiesfor pages 11-12). Although this does not quantify SSA1’s effect size, it supports SSA1 as a recurrent target when secretion and intracellular folding capacity limit recombinant production (zhao2024engineeringstrategiesfor pages 11-12).
SSA1/Ssa1 is central to yeast prion systems that are widely used as tractable models for amyloid dynamics and chaperone-based disaggregation principles relevant to proteopathies:
- 2024 PNAS provides a concrete blueprint for site-specific chaperone engagement to tune disaggregation, including engineered systems that degrade otherwise resistant fibrils (shen2024exposedhsp70bindingsite pages 1-2, shen2024exposedhsp70bindingsite pages 7-9).
Method papers optimize the recombinant production and purification of Ssa1 to support in vitro assays and structural studies (Ecological Genetics, Jun 2025, https://doi.org/10.17816/ecogen676918) (matveenko2025optimizationofconditions pages 7-9, matveenko2025optimizationofconditions pages 1-3). While not an industrial product per se, this is a real-world enabling technology for mechanistic and screening work on SSA1 (matveenko2025optimizationofconditions pages 7-9).
Key expert viewpoints from high-citation reviews and leading journals converge on SSA1 as:
- a central proteostasis hub whose ATPase-driven cycle and cochaperone regulation establish broad influence across folding, degradation, and signaling (shan2023roleofhsp70 pages 1-2, lotz2019notquitethe pages 1-3);
- a component of a feedback system controlling Hsf1 (heat shock response) via chaperone titration (masser2019cytoplasmicproteinmisfolding pages 1-2, lotz2019notquitethe pages 4-6);
- and a factor whose isoform-level differences (Ssa1 vs Ssa2 vs inducible Ssa3/4) can produce distinct outcomes in prion biology and client triage, emphasizing that “redundant” paralogs can still be functionally specialized (lotz2019notquitethe pages 1-3, lotz2019notquitethe pages 4-6).
SSA1 (P10591; YAL005C) encodes Ssa1, a highly abundant cytosolic/nuclear Hsp70 that uses an ATP-driven NBD/SBD cycle to bind non-native polypeptides and coordinate folding, disaggregation, trafficking, and degradation. Its specificity and pathway integration are tuned by cochaperones (Sis1/Ydj1) and NEFs (Fes1/Sse1), and recent work reveals residue-level interaction mechanisms (EEVD–Sis1 binding) and site-specific amyloid engagement governing prion disaggregation. SSA1’s function is sufficiently central that perturbations alter signaling scaffold stability (Ste5/MAPK) and can impact engineered metabolite yield (ethyl acetate), making SSA1 both a fundamental proteostasis gene and a practical engineering lever (jarnuczak2015quantitativeproteomicsand pages 1-2, matos2024nmrstudieson pages 10-12, shen2024exposedhsp70bindingsite pages 4-6, farley2023effectsofhsp70 pages 31-33, cui2023genomewideanalysisreveals pages 10-11).
The following table provides a compact, evidence-linked annotation with dates/URLs and quantitative values:
| Category | Summary |
|---|---|
| Identity/Domains | SSA1 is the Saccharomyces cerevisiae YAL005C gene encoding Ssa1, a major cytosolic/nuclear Hsp70-family chaperone; this matches UniProt P10591 context and the literature describing SSA1 as an abundant cytosolic Hsp70 hub. Canonical Hsp70 architecture applies: N-terminal ATPase/nucleotide-binding domain, substrate-binding domain with peptide-binding and lid subdomains, plus a C-terminal EEVD motif for cochaperone interactions (shan2023roleofhsp70 pages 1-2, jarnuczak2015quantitativeproteomicsand pages 1-2, farley2023effectsofhsp70 pages 2-4). |
| Biochemical mechanism | Ssa1 is an ATP-dependent molecular chaperone that binds exposed hydrophobic segments in non-native polypeptides; J-domain proteins/Hsp40s stimulate ATP hydrolysis to trap clients, while NEFs accelerate ADP release and client cycling. This supports roles in folding, refolding, disaggregation, and targeting of proteins to downstream biogenesis or quality-control pathways (shan2023roleofhsp70 pages 1-2, matveenko2025optimizationofconditions pages 1-3). |
| Major pathways/processes | Core functions include proteostasis, nascent-chain folding, protein translocation to mitochondria/ER, protein quality control/degradation, and cooperation with Hsp90 for client maturation. Recent work also places Ssa1 in the mating MAPK pathway via Ste5 control and in prion/amyloid fragmentation and propagation with Sis1/Hsp104 (farley2023effectsofhsp70 pages 52-53, gaur2020theyeasthsp70 pages 1-1, shen2024exposedhsp70bindingsite pages 1-2, farley2023effectsofhsp70 pages 4-5, shen2024exposedhsp70bindingsite pages 6-7). |
| Localization | Ssa1 is predominantly cytosolic, but can show nuclear accumulation and acts on clients in both compartments. Fluorescently tagged recombinant Ssa proteins remained mainly cytosolic, while native-pathway studies support roles in cytoplasm, nucleus, and at protein deposits under proteotoxic stress (matveenko2025optimizationofconditions pages 7-9, farley2023effectsofhsp70 pages 2-4, farley2023effectsofhsp70 pages 26-28, farley2023effectsofhsp70 pages 24-26). |
| Key co-chaperones/partners | Major partners include Ydj1 and Sis1 (Hsp40/JDPs), Fes1/HspBP1-like NEFs, Hsp104, and Hsp90 pathway factors such as Sti1 via the EEVD-TPR interaction logic. Mechanistically, 2024 studies refined how the Ssa1 EEVD motif binds Sis1 and how Ssa1/Sis1 recognize exposed amyloid sites to initiate remodeling (shan2023roleofhsp70 pages 1-2, matos2024nmrstudieson pages 1-2, shen2024exposedhsp70bindingsite pages 9-10, matos2024nmrstudieson pages 10-12). |
| Representative recent studies 2023-2024 | Farley et al., 2023-10-04, PLOS ONE: Ssa1/Ssa2 support Ste5 abundance, localization, MAPK activation, and shmoo formation in mating signaling; URL: https://doi.org/10.1371/journal.pone.0289339 (farley2023effectsofhsp70 pages 1-2, farley2023effectsofhsp70 pages 31-33, farley2023effectsofhsp70 pages 34-36). Grosfeld et al., 2023-08, Int J Mol Sci: C-terminal Ssa1-GFP impairs function and promotes large HADS deposits under mild stress/respiration; URL: https://doi.org/10.3390/ijms241612758 (grosfeld2023fusionofhsp70 pages 1-2, grosfeld2023fusionofhsp70 pages 6-7). |
| Representative recent studies 2023-2024 | Shen et al., 2024-12, PNAS: mapped an Ssa1/Sis1-binding site in Sup35NM residues 143-164; site exposure determines prion disaggregation and propagation; URL: https://doi.org/10.1073/pnas.2318162121 (shen2024exposedhsp70bindingsite pages 1-2, shen2024exposedhsp70bindingsite pages 9-10, shen2024exposedhsp70bindingsite pages 2-3). Matos et al., 2024-12, Molecules: NMR showed Ssa1-EEVD engages multiple Sis1 sites and modulates Sis1 dynamics/conformation; URL: https://doi.org/10.3390/molecules30010011 (matos2024nmrstudieson pages 1-2, matos2024nmrstudieson pages 10-12). |
| Quantitative data/statistics | Network/proteome studies place SSA1 at ~8178 ppm abundance and ~2489 client links in curated interaction maps; Ssa proteins are among the most abundant chaperone hubs, and the Hsp70 class mediates ~44% of total protein synthesis flux in yeast (jarnuczak2015quantitativeproteomicsand pages 1-2, brownridge2013quantitativeanalysisof pages 11-12, brownridge2013quantitativeanalysisof pages 12-15). In signaling, Ste5:Hsp70 co-IP ratios were 1.45 (-α factor) vs 0.67 (+α factor), and ssa1Δ ssa2Δ reduced Fus3-HA kinase output to ~16.7% of wild type; after 6 h Ssa1 depletion, only 3.2 ± 0.25% of cells formed shmoos (p = 0.023095) (farley2023effectsofhsp70 pages 14-15, farley2023effectsofhsp70 pages 31-33, farley2023effectsofhsp70 pages 34-36). |
Table: This table summarizes verified identity, mechanism, localization, pathways, partners, recent 2023-2024 studies, and quantitative findings for yeast SSA1/Ssa1. It is useful as a compact evidence-linked functional annotation reference for UniProt P10591 / YAL005C.
References
(jarnuczak2015quantitativeproteomicsand pages 1-2): Andrew F. Jarnuczak, Claire E. Eyers, Jean‐Marc Schwartz, Christopher M. Grant, and Simon J. Hubbard. Quantitative proteomics and network analysis of ssa1 and ssb1 deletion mutants reveals robustness of chaperone hsp70 network in saccharomyces cerevisiae. Proteomics, 15:3126-3139, Apr 2015. URL: https://doi.org/10.1002/pmic.201400527, doi:10.1002/pmic.201400527. This article has 17 citations and is from a peer-reviewed journal.
(shan2023roleofhsp70 pages 1-2): Shu-ou Shan. Role of hsp70 in post-translational protein targeting: tail-anchored membrane proteins and beyond. International Journal of Molecular Sciences, 24:1170, Jan 2023. URL: https://doi.org/10.3390/ijms24021170, doi:10.3390/ijms24021170. This article has 11 citations.
(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.
(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 51 citations and is from a peer-reviewed journal.
(masser2019cytoplasmicproteinmisfolding pages 1-2): Anna E Masser, Wenjing Kang, Joydeep Roy, Jayasankar Mohanakrishnan Kaimal, Jany Quintana-Cordero, Marc R Friedländer, and Claes Andréasson. Cytoplasmic protein misfolding titrates hsp70 to activate nuclear hsf1. eLife, Sep 2019. URL: https://doi.org/10.7554/elife.47791, doi:10.7554/elife.47791. This article has 127 citations and is from a domain leading peer-reviewed journal.
(rupali2018hsp4070110chaperonesadapt pages 1-2): Rupali Prasad, Chengchao Xu, and Davis T. W. Ng. Hsp40/70/110 chaperones adapt nuclear protein quality control to serve cytosolic clients. The Journal of Cell Biology, 217:2019-2032, Jun 2018. URL: https://doi.org/10.1083/jcb.201706091, doi:10.1083/jcb.201706091. This article has 54 citations.
(nicklow2020activityofthe pages 7-8): Erin E. Nicklow and Carolyn S. Sevier. Activity of the yeast cytoplasmic hsp70 nucleotide-exchange factor fes1 is regulated by reversible methionine oxidation. Journal of Biological Chemistry, 295:552-569, Jan 2020. URL: https://doi.org/10.1074/jbc.ra119.010125, doi:10.1074/jbc.ra119.010125. This article has 24 citations and is from a domain leading peer-reviewed journal.
(matos2024nmrstudieson pages 1-2): Carolina O. Matos, Glaucia M. S. Pinheiro, Icaro P. Caruso, Gisele C. Amorim, Fabio C. L. Almeida, and Carlos H. I. Ramos. Nmr studies on the structure of yeast sis1 and the dynamics of its interaction with ssa1-eevd. Molecules, 30:11, Dec 2024. URL: https://doi.org/10.3390/molecules30010011, doi:10.3390/molecules30010011. This article has 3 citations.
(farley2023effectsofhsp70 pages 24-26): 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.
(matveenko2025optimizationofconditions pages 7-9): A. Matveenko, A. A. Tsvetkov, Tatiana M Rogoza, Yury A. Barbitoff, and G. Zhouravleva. Optimization of conditions for the productionof hsp70 chaperones in saccharomyces cerevisiae cells. Ecological genetics, Jun 2025. URL: https://doi.org/10.17816/ecogen676918, doi:10.17816/ecogen676918. This article has 0 citations.
(shen2024exposedhsp70bindingsite pages 1-2): Chih-hao Howard Shen, Yusuke Komi, Yoshiko Nakagawa, Yuji O. Kamatari, Takashi Nomura, Hiromi Kimura, Toshinobu Shida, John Burke, Shingo Tamai, Yasuhiro Ishida, and Motomasa Tanaka. Exposed hsp70-binding site impacts yeast sup35 prion disaggregation and propagation. Proceedings of the National Academy of Sciences of the United States of America, Dec 2024. URL: https://doi.org/10.1073/pnas.2318162121, doi:10.1073/pnas.2318162121. This article has 12 citations and is from a highest quality peer-reviewed journal.
(shen2024exposedhsp70bindingsite pages 2-3): Chih-hao Howard Shen, Yusuke Komi, Yoshiko Nakagawa, Yuji O. Kamatari, Takashi Nomura, Hiromi Kimura, Toshinobu Shida, John Burke, Shingo Tamai, Yasuhiro Ishida, and Motomasa Tanaka. Exposed hsp70-binding site impacts yeast sup35 prion disaggregation and propagation. Proceedings of the National Academy of Sciences of the United States of America, Dec 2024. URL: https://doi.org/10.1073/pnas.2318162121, doi:10.1073/pnas.2318162121. This article has 12 citations and is from a highest quality peer-reviewed journal.
(shen2024exposedhsp70bindingsite pages 4-6): Chih-hao Howard Shen, Yusuke Komi, Yoshiko Nakagawa, Yuji O. Kamatari, Takashi Nomura, Hiromi Kimura, Toshinobu Shida, John Burke, Shingo Tamai, Yasuhiro Ishida, and Motomasa Tanaka. Exposed hsp70-binding site impacts yeast sup35 prion disaggregation and propagation. Proceedings of the National Academy of Sciences of the United States of America, Dec 2024. URL: https://doi.org/10.1073/pnas.2318162121, doi:10.1073/pnas.2318162121. This article has 12 citations and is from a highest quality peer-reviewed journal.
(shen2024exposedhsp70bindingsite pages 6-7): Chih-hao Howard Shen, Yusuke Komi, Yoshiko Nakagawa, Yuji O. Kamatari, Takashi Nomura, Hiromi Kimura, Toshinobu Shida, John Burke, Shingo Tamai, Yasuhiro Ishida, and Motomasa Tanaka. Exposed hsp70-binding site impacts yeast sup35 prion disaggregation and propagation. Proceedings of the National Academy of Sciences of the United States of America, Dec 2024. URL: https://doi.org/10.1073/pnas.2318162121, doi:10.1073/pnas.2318162121. This article has 12 citations and is from a highest quality peer-reviewed journal.
(shen2024exposedhsp70bindingsite pages 9-10): Chih-hao Howard Shen, Yusuke Komi, Yoshiko Nakagawa, Yuji O. Kamatari, Takashi Nomura, Hiromi Kimura, Toshinobu Shida, John Burke, Shingo Tamai, Yasuhiro Ishida, and Motomasa Tanaka. Exposed hsp70-binding site impacts yeast sup35 prion disaggregation and propagation. Proceedings of the National Academy of Sciences of the United States of America, Dec 2024. URL: https://doi.org/10.1073/pnas.2318162121, doi:10.1073/pnas.2318162121. This article has 12 citations and is from a highest quality peer-reviewed journal.
(shen2024exposedhsp70bindingsite pages 7-9): Chih-hao Howard Shen, Yusuke Komi, Yoshiko Nakagawa, Yuji O. Kamatari, Takashi Nomura, Hiromi Kimura, Toshinobu Shida, John Burke, Shingo Tamai, Yasuhiro Ishida, and Motomasa Tanaka. Exposed hsp70-binding site impacts yeast sup35 prion disaggregation and propagation. Proceedings of the National Academy of Sciences of the United States of America, Dec 2024. URL: https://doi.org/10.1073/pnas.2318162121, doi:10.1073/pnas.2318162121. This article has 12 citations and is from a highest quality peer-reviewed journal.
(matos2024nmrstudieson pages 10-12): Carolina O. Matos, Glaucia M. S. Pinheiro, Icaro P. Caruso, Gisele C. Amorim, Fabio C. L. Almeida, and Carlos H. I. Ramos. Nmr studies on the structure of yeast sis1 and the dynamics of its interaction with ssa1-eevd. Molecules, 30:11, Dec 2024. URL: https://doi.org/10.3390/molecules30010011, doi:10.3390/molecules30010011. This article has 3 citations.
(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.
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