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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
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HSC82 (YMR186W; UniProt P15108) is correctly identified as the constitutively expressed cytosolic Hsp90-family molecular chaperone of Saccharomyces cerevisiae S288c. It is not Hsc70/HSPA8 and should not be conflated with similarly named proteins in other organisms. Its close yeast paralog, HSP82, is the stress-inducible Hsp90 isoform. The supplied InterPro assignments—HATPase domain/superfamily, Hsp90-family signature, and HSP90 C-terminal region—match the experimentally established Hsp90 architecture and mechanism. Direct comparative work identifies Hsc82 as the constitutive isoform and Hsp82 as stress inducible; they share 97% sequence identity but are functionally non-identical (girstmair2019thehsp90isoforms pages 1-2, rios2024insightsintohsp90 pages 1-2).
Hsc82’s primary function is ATP-regulated folding, stabilization, activation, and conformational remodeling of a broad but selective set of client proteins. It is therefore not best annotated as an enzyme acting on one metabolic substrate. Although Hsc82 possesses ATPase activity, ATP is the regulatory fuel/ligand of its chaperone cycle, while the functional substrates are client proteins—especially conformationally unstable regulatory proteins and proteins containing accessible intrinsically disordered regions (IDRs) (kolhe2023thehsp90molecular pages 3-5, kolhe2023thehsp90molecular pages 6-8).
| Topic | Finding | Directness for HSC82/P15108 | Key quantitative values | Source (date; DOI URL) | Context citation |
|---|---|---|---|---|---|
| Identity / expression | HSC82 = YMR186W = UniProt P15108 in S. cerevisiae S288c, encoding the constitutively expressed cytosolic Hsp90 isoform; paralog HSP82 is stress inducible. The two proteins are 97% identical and differ by 16 amino acids. Under non-stress conditions, Hsc82 is ~10-fold more abundant than Hsp82; at 37°C Hsp82 rises to levels similar to Hsc82. Single-gene loss is tolerated with mild heat-related defects; loss of both yeast cytosolic Hsp90 genes is lethal. | Direct for Hsc82 identity/expression and redundancy in yeast | 97% identity; 16 aa differences; ~10-fold higher basal abundance; Hsc82 reduction to 1–5% of WT allows growth at optimal but not elevated temperature | Girstmair et al., 2019; https://doi.org/10.1038/s41467-019-11518-w ; Rios et al., 2024; https://doi.org/10.3389/fmolb.2024.1325590 | (girstmair2019thehsp90isoforms pages 1-2, rios2024insightsintohsp90 pages 1-2) |
| Domains | Hsc82 has the canonical Hsp90 architecture: N-terminal nucleotide-binding domain, middle domain, and C-terminal dimerization domain; a flexible loop in the middle domain regulates ATP hydrolysis. Sequence differences between Hsc82 and Hsp82 are concentrated mainly in the N-domain. | Direct for yeast Hsc82 domain organization; direct comparative evidence for Hsc82 vs Hsp82 | N-domain aa 1–216; middle domain aa 269–525; C-domain aa 529–705; isoform substitutions enriched in NTD (8 residues) and CTD (5 residues) | Hohrman et al., 2021; https://doi.org/10.1093/genetics/iyab009 ; Girstmair et al., 2019; https://doi.org/10.1038/s41467-019-11518-w | (hohrman2021disruptingprogressionof pages 3-4, girstmair2019thehsp90isoforms pages 1-2) |
| Biochemical mechanism | Hsc82 is an ATP-dependent molecular chaperone, not an enzyme with a fixed chemical substrate. It binds and remodels client proteins through a nucleotide-coupled conformational cycle. Hsc82 is more processive and occupies closed states more than Hsp82. Recent in vivo work shows ATP binding and nucleotide exchange are sufficient for essential Hsp90 function, whereas ATP hydrolysis is dispensable but regulatory. A nucleotide-binding-defective mutant is lethal, whereas hydrolysis-defective E33A can support viability with conditional defects. | Mixed: direct comparative for Hsc82/Hsp82 biophysics; direct in vivo yeast Hsp90 evidence largely tested with Hsp82 alleles and therefore family/paralog inference to Hsc82 core mechanism | Hsc82 thermal stability 57.1°C vs Hsp82 60.4°C; Hsp82-E33A viability support at ~1.8% of WT efficiency; cellular ATP:ADP ratio model ~4:1 | Girstmair et al., 2019; https://doi.org/10.1038/s41467-019-11518-w ; Reidy et al., 2023; https://doi.org/10.1038/s41467-023-38230-0 ; Rios et al., 2024; https://doi.org/10.3389/fmolb.2024.1325590 | (girstmair2019thehsp90isoforms pages 1-2, reidy2023nucleotideexchangeis pages 8-10, reidy2023nucleotideexchangeis pages 1-2, reidy2023nucleotideexchangeis pages 2-3, rios2024insightsintohsp90 pages 1-2) |
| Localization | Yeast Hsc82/Hsp90 is the cytosolic Hsp90 system and also functions in the nucleus through maturation/stabilization of signaling and regulatory clients. No evidence in the retrieved set supports secretion or residence in an organelle lumen for Hsc82. | Direct at the isoform-system level from yeast reviews; not a single dedicated localization study in the retrieved set | Not quantified in retrieved evidence | Rios et al., 2024; https://doi.org/10.3389/fmolb.2024.1325590 | (rios2024insightsintohsp90 pages 1-2) |
| Clients / pathways | Hsc82/Hsp90 acts on a broad client spectrum rather than a single substrate class. Retrieved yeast evidence supports roles in kinase maturation/signaling (with Cdc37 preference for kinase domains), Hsp70/Sti1-mediated client loading, Sba1/Cpr6-associated closed-state maturation, DNA-related clients such as Ssl2 and Utp21, and pathway-selective effects including cAMP/PKA signaling. Hsp90 client recognition is enriched for intrinsically disordered regions (IDRs) rather than a strict sequence motif. | Mixed: some direct Hsc82 mutant/client evidence; some generic yeast Hsp90 or crosslinked interactome inference | Hsp90 affects ~10–15% of yeast/human proteins; yeast interactome study identified 1,114 interactors, 629 dependent on crosslinking sites, and recovery of 11/14 known Hsp90 cochaperones | Hohrman et al., 2021; https://doi.org/10.1093/genetics/iyab009 ; Kolhe et al., 2023; https://doi.org/10.1016/j.molcel.2023.05.021 ; Rios et al., 2024; https://doi.org/10.3389/fmolb.2024.1325590 | (hohrman2021disruptingprogressionof pages 1-1, kolhe2023thehsp90molecular pages 3-5, kolhe2023thehsp90molecular pages 6-8, rios2024insightsintohsp90 pages 8-9, rios2024insightsintohsp90 pages 3-5) |
| Recent 2023–2024 findings | 2023: Hsp90 client recognition in yeast is strongly linked to IDRs, with different Hsp90 domains contacting distinct client subsets and networks. 2023: ATP hydrolysis is not strictly required for essential in vivo Hsp90 function; nucleotide exchange can be sufficient. 2024 expert synthesis: yeast studies establish Hsc82/Hsp82 as a tractable model for dissecting cochaperone control, conformational cycling, and client-selective maturation relevant across eukaryotes. | Mixed: direct yeast-system evidence; some conclusions apply to the Hsp90 machinery broadly rather than exclusively to Hsc82 | IDRs average ~33% of eukaryotic protein length vs ~10% in bacteria and 2% in archaea; 1,114 mapped yeast interactions; ATP-hydrolysis-defective support of viability retained | Kolhe et al., 2023; https://doi.org/10.1016/j.molcel.2023.05.021 ; Reidy et al., 2023; https://doi.org/10.1038/s41467-023-38230-0 ; Rios et al., 2024; https://doi.org/10.3389/fmolb.2024.1325590 | (kolhe2023thehsp90molecular pages 3-5, kolhe2023thehsp90molecular pages 6-8, reidy2023nucleotideexchangeis pages 8-10, reidy2023nucleotideexchangeis pages 1-2, rios2024insightsintohsp90 pages 1-2) |
Table: This table summarizes the most relevant evidence for the identity, function, domains, localization, client biology, and recent advances for the yeast HSC82 protein (UniProt P15108). It also flags where evidence is directly Hsc82-specific versus inferred from the broader yeast Hsp90 machinery or the inducible paralog Hsp82.
The literature consistently supports the requested identity: budding yeast has two cytosolic Hsp90 genes, HSC82 and HSP82. At 25–30°C, Hsc82 is one of the most abundant soluble proteins, whereas Hsp82 is present at low levels and rises strongly at 37°C. Under nonstress conditions Hsc82 is approximately tenfold more abundant than Hsp82 (girstmair2019thehsp90isoforms pages 1-2, rios2024insightsintohsp90 pages 1-2).
The paralogs are 97% identical and differ at only 16 amino-acid positions, but these substitutions produce measurable specialization. Hsc82 is more processive and samples closed conformations more extensively; Hsp82 is more thermally stable and refolds more efficiently after stress. Reported melting temperatures were approximately 57.1°C for Hsc82 and 60.4°C for Hsp82. Most functionally consequential sequence differences occur in the N-terminal domain, with eight substitutions there and five in the C-terminal region (girstmair2019thehsp90isoforms pages 1-2).
The proteins are substantially redundant for essential growth: deletion of either gene alone is tolerated, although elevated-temperature growth can be impaired, whereas removal of both cytosolic Hsp90 genes is lethal. Reducing Hsc82 to only 1–5% of normal abundance still permits growth at an optimal temperature but not at elevated temperature, indicating that normal Hsc82 abundance provides reserve chaperone capacity when client proteins are destabilized (hohrman2021disruptingprogressionof pages 3-4, rios2024insightsintohsp90 pages 1-2).
Hsc82 has the canonical three-part Hsp90 architecture:
These experimentally defined regions align with the supplied HATPase_C_sf, HATPase_dom, HSP90_C, Hsp90-family, and Hsp90 signature annotations. Hsc82 functions as a dynamic homodimer—or potentially as an isoform-mixed cytosolic Hsp90 dimer—rather than as a monomeric metabolic enzyme.
In the simplified cycle, nucleotide-free Hsc82 occupies an open state suited to client loading. ATP binding promotes N-terminal association and conversion toward a closed dimer, allowing conformational remodeling or maturation of the bound client. Subsequent nucleotide-state transitions reopen the dimer and release client and cochaperones. Direct Hsc82 mutagenesis shows that variants S481Y, T521I, and A583T have reduced ability to assemble the AMP-PNP-stabilized closed complex with Sba1 and Cpr6, linking closed-state formation to productive client maturation (hohrman2021disruptingprogressionof pages 4-4).
An important 2023 revision to the classical mechanism is that ATP binding and nucleotide exchange appear more fundamental than ATP hydrolysis itself. In a yeast complementation system lacking endogenous HSC82 and HSP82, the Hsp82-E33A variant—which binds ATP but cannot hydrolyze it—supported viability, albeit at only about 1.8% of wild-type efficiency and with conditional defects. In contrast, nucleotide-binding-defective D79N was lethal. Second-site suppressors restored near-normal function to hydrolysis-deficient proteins without restoring ATPase activity (reidy2023nucleotideexchangeis pages 1-2, reidy2023nucleotideexchangeis pages 2-3).
Further experiments indicated that a hydrolysis-defective E33A,K98A double variant, also compromised in productive ADP-state access, barely supported growth. The authors concluded that passage between ATP- and ADP-associated conformations through nucleotide exchange can sustain essential Hsp90 function, while hydrolysis normally controls cycle timing and responsiveness to clients and cochaperones. Cellular ATP:ADP was modeled at roughly 4:1 (reidy2023nucleotideexchangeis pages 8-10). Because these decisive experiments used Hsp82 alleles, this conclusion is strongest for the conserved yeast Hsp90 mechanism and is a well-supported paralog-level inference for Hsc82, rather than a direct P15108 catalytic-mutant result.
Hsc82 does not recognize one fixed metabolite or one simple peptide motif. It handles a diverse client population that includes kinases, transcriptional regulators, multiprotein-complex subunits, and proteins involved in DNA and RNA metabolism. Nevertheless, this is not wholly nonspecific anti-aggregation activity: cochaperones, client conformation, and different surfaces across all three Hsp90 domains confer selectivity (kolhe2023thehsp90molecular pages 3-5, rios2024insightsintohsp90 pages 3-5).
A 2023 yeast interactome study provided a mechanistic basis for this breadth. Hsp90 preferentially contacted intrinsically disordered regions, largely independently of their precise sequence or charge. Crosslinking mapped 1,114 yeast interactors and 181 direct contact sites; 629 interactions depended on the engineered crosslinking positions. The recovered network included 11 of the 14 recognized Hsp90 cochaperones and extensive connections with Hsp70, Hsp40, CCT, and Hsp104 systems (kolhe2023thehsp90molecular pages 3-5, kolhe2023thehsp90molecular pages 6-8).
Thus, a useful substrate-specificity annotation is: partially folded or conformationally dynamic cytosolic/nuclear client proteins, frequently engaged through exposed IDRs and selected further by cochaperones. Different Hsp90 regions contact different client/network subsets, explaining why point mutations can impair some clients while sparing others (kolhe2023thehsp90molecular pages 3-5, hohrman2021disruptingprogressionof pages 1-1).
Hsc82 is the central ATP-regulated scaffold of a multicomponent folding pathway rather than an isolated chaperone.
Yeast has at least 12 experimentally studied Hsp90 cochaperones, emphasizing that Hsc82 function is distributed across a regulated chaperone network rather than determined solely by its intrinsic ATPase rate (hohrman2021disruptingprogressionof pages 1-2, hohrman2021disruptingprogressionof pages 1-1).
Protein kinases are a major Hsp90 client class, commonly selected through Cdc37. Consequently, Hsc82 occupies a permissive upstream position in several signaling systems: it does not necessarily transmit the signal directly, but maintains signaling proteins in active or activation-competent conformations. Mutational evidence demonstrates that individual Hsc82 surfaces can selectively disrupt cAMP/PKA-associated signaling, supporting pathway-selective chaperoning rather than a uniform collapse of proteostasis (rios2024insightsintohsp90 pages 8-9, rios2024insightsintohsp90 pages 3-5).
Direct yeast studies used Ssl2, a DNA helicase and TFIIH component; Utp21, a ribosome-biogenesis factor; and heterologous v-Src as mechanistically distinct clients. Mutations affecting early Hsp70–Sti1 engagement or ATP-dependent closed-complex formation impaired all three, whereas mutations at other stages had narrower client effects. Synthetic lethality between utp21-S602F and several Hsc82 variants—including R46G, G309S, K394E, S481Y, T521I, and A583T—provides genetic evidence that precise Hsc82-cycle defects can become limiting for individual essential clients (hohrman2021disruptingprogressionof pages 1-1, hohrman2021disruptingprogressionof pages 4-4).
These findings place Hsc82 in the maintenance of nuclear transcription/DNA-processing machinery and nucleolar ribosome-biogenesis machinery, but the mechanistic role remains client folding or stabilization—not DNA catalysis, transcription, or ribosome assembly chemistry performed directly by Hsc82.
Hsc82 is the predominant housekeeping Hsp90 under normal growth conditions. Its abundance stabilizes proteins close to conformational failure and buffers environmental or mutational perturbation. Hsp82 supplies the more thermally resilient paralog during acute heat stress. The largely overlapping but non-identical interactomes of the two isoforms indicate division of labor rather than complete specialization (girstmair2019thehsp90isoforms pages 1-2, rios2024insightsintohsp90 pages 1-2).
Hsp90 perturbation affects approximately 10–15% of yeast or human proteins in commonly cited functional estimates. This breadth should be interpreted as network reach, not evidence that every affected protein is a direct Hsc82 client (hohrman2021disruptingprogressionof pages 1-1).
Hsc82 is principally a soluble cytosolic chaperone. It also supports nuclear and nucleolar functions by acting on clients such as transcription/DNA-processing and ribosome-biogenesis proteins. The available evidence therefore supports the annotation cytosol and nucleus/nucleolus through dynamic client-associated distribution, rather than localization to a membrane, extracellular compartment, ER lumen, or mitochondrial matrix (rios2024insightsintohsp90 pages 1-2, hohrman2021disruptingprogressionof pages 1-1).
The retrieved literature did not include a dedicated quantitative microscopy study establishing a fixed cytosol-to-nucleus distribution for P15108. Nuclear biological roles should therefore not be interpreted as evidence that Hsc82 is exclusively or constitutively nuclear. Its localization is best understood as that of a mobile, abundant cytosolic chaperone able to act on clients in multiple soluble cellular compartments.
IDR-centered client recognition—June 2023. Kolhe, Babu, and Freeman showed that Hsp90 broadly recognizes client IDRs using surfaces distributed across all three domains. Their mapping of 1,114 yeast interactions and 181 contact sites replaces the expectation of a single consensus client motif with a conformational-accessibility model. The study noted that IDRs constitute about 33% of eukaryotic proteins on average, versus approximately 10% in bacteria and 2% in archaea, providing an evolutionary rationale for the expanded eukaryotic Hsp90 client network. DOI: https://doi.org/10.1016/j.molcel.2023.05.021 (published June 2023) (kolhe2023thehsp90molecular pages 3-5, kolhe2023thehsp90molecular pages 6-8).
Nucleotide exchange rather than obligatory hydrolysis—April 2023. Reidy, Garzillo, and Masison demonstrated that hydrolysis-defective Hsp90 can sustain yeast viability and specialized functions if nucleotide-dependent conformational exchange remains possible. This reframes ATP hydrolysis as an important regulatory checkpoint, not necessarily the indispensable power stroke of the chaperone. DOI: https://doi.org/10.1038/s41467-023-38230-0 (published April 2023) (reidy2023nucleotideexchangeis pages 8-10, reidy2023nucleotideexchangeis pages 1-2, reidy2023nucleotideexchangeis pages 2-3).
Authoritative yeast-focused synthesis—February 2024. Rios, Hunsberger, and Johnson concluded that S. cerevisiae remains a particularly powerful in vivo system for linking Hsp90 conformational states, cochaperone interactions, client-specific phenotypes, and proteome-wide consequences. Their synthesis emphasizes that Hsc82 and Hsp82 differ in ATPase behavior, conformational dynamics, stability, and some client/cochaperone interactions despite near identity. DOI: https://doi.org/10.3389/fmolb.2024.1325590 (published February 2024) (rios2024insightsintohsp90 pages 1-2, rios2024insightsintohsp90 pages 8-9, rios2024insightsintohsp90 pages 3-5).
The most mature application of HSC82 is as an experimental platform. Yeast strains lacking chromosomal HSC82 and HSP82 can be maintained by plasmid-borne Hsp90 alleles, enabling stringent tests of mutant or heterologous Hsp90 proteins. This system has shown that human and pathogen Hsp90 orthologs can support yeast viability and allows conserved nucleotide-cycle mechanisms to be evaluated in living cells (reidy2023nucleotideexchangeis pages 1-2, reidy2023nucleotideexchangeis pages 2-3).
Hsc82 mutant panels also allow researchers to perturb specific cycle transitions rather than globally inhibiting Hsp90. Because early-loading, closed-state, and late-release defects produce different client phenotypes, this approach supports efforts to discover client- or cochaperone-selective Hsp90 interventions, potentially avoiding the toxicity expected from total Hsp90 blockade (rios2024insightsintohsp90 pages 3-5, hohrman2021disruptingprogressionof pages 1-1).
More broadly, yeast Hsc82 informs antifungal and human Hsp90 drug discovery because core Hsp90 architecture and cochaperone logic are conserved. However, a compound active against mammalian or pathogenic-fungal Hsp90 is not automatically an application of P15108 itself. The direct real-world role of P15108 remains as a model-system protein and as a determinant of yeast robustness, stress tolerance, and proteome function.
Recommended concise annotation:
Hsc82 is the abundant, constitutively expressed cytosolic Hsp90 isoform of S. cerevisiae. It forms an ATP-regulated dimeric molecular-chaperone machine that, together with Hsp70 and multiple cochaperones, loads, stabilizes, remodels, and activates conformationally dynamic client proteins in the cytosol and nucleus. Client selection is broad but nonrandom, involving exposed intrinsically disordered regions and cochaperone-mediated recruitment, particularly of protein kinases. Hsc82 supports proteostasis, signaling, transcription/DNA-processing, and ribosome-biogenesis pathways through maturation of their component proteins.
Confidence is high for identity, Hsp90-family membership, constitutive expression, cytosolic role, domain organization, ATP-regulated chaperoning, and partial redundancy with Hsp82. Confidence is moderate for assigning any individual pathway as uniquely Hsc82-dependent, because many yeast experiments use Hsp82, engineered Hsc82 alleles, or strains in which one paralog supplies all Hsp90 activity. The evidence supports substantial client overlap with isoform-specific tuning, not a single exclusive Hsc82 pathway (girstmair2019thehsp90isoforms pages 1-2, rios2024insightsintohsp90 pages 1-2).
References
(girstmair2019thehsp90isoforms pages 1-2): Hannah Girstmair, Franziska Tippel, Abraham Lopez, Katarzyna Tych, Frank Stein, Per Haberkant, Philipp Werner Norbert Schmid, Dominic Helm, Matthias Rief, Michael Sattler, and Johannes Buchner. The hsp90 isoforms from s. cerevisiae differ in structure, function and client range. Nature Communications, Aug 2019. URL: https://doi.org/10.1038/s41467-019-11518-w, doi:10.1038/s41467-019-11518-w. This article has 93 citations and is from a highest quality peer-reviewed journal.
(rios2024insightsintohsp90 pages 1-2): Erick I. Rios, Isabel L. Hunsberger, and Jill L. Johnson. Insights into hsp90 mechanism and in vivo functions learned from studies in the yeast, saccharomyces cerevisiae. Frontiers in Molecular Biosciences, Feb 2024. URL: https://doi.org/10.3389/fmolb.2024.1325590, doi:10.3389/fmolb.2024.1325590. This article has 8 citations.
(kolhe2023thehsp90molecular pages 3-5): Janhavi A. Kolhe, Neethu L. Babu, and Brian C. Freeman. The hsp90 molecular chaperone governs client proteins by targeting intrinsically disordered regions. Molecular cell, 83:2035-2044.e7, Jun 2023. URL: https://doi.org/10.1016/j.molcel.2023.05.021, doi:10.1016/j.molcel.2023.05.021. This article has 64 citations and is from a highest quality peer-reviewed journal.
(kolhe2023thehsp90molecular pages 6-8): Janhavi A. Kolhe, Neethu L. Babu, and Brian C. Freeman. The hsp90 molecular chaperone governs client proteins by targeting intrinsically disordered regions. Molecular cell, 83:2035-2044.e7, Jun 2023. URL: https://doi.org/10.1016/j.molcel.2023.05.021, doi:10.1016/j.molcel.2023.05.021. This article has 64 citations and is from a highest quality peer-reviewed journal.
(hohrman2021disruptingprogressionof pages 3-4): Kaitlyn Hohrman, Davi Gonçalves, Kevin A Morano, and Jill L Johnson. Disrupting progression of the yeast hsp90 folding pathway at different transition points results in client-specific maturation defects. Genetics, Jan 2021. URL: https://doi.org/10.1093/genetics/iyab009, doi:10.1093/genetics/iyab009. This article has 15 citations and is from a domain leading peer-reviewed journal.
(reidy2023nucleotideexchangeis pages 8-10): Michael Reidy, Kevin Garzillo, and Daniel C. Masison. Nucleotide exchange is sufficient for hsp90 functions in vivo. Nature Communications, Apr 2023. URL: https://doi.org/10.1038/s41467-023-38230-0, doi:10.1038/s41467-023-38230-0. This article has 28 citations and is from a highest quality peer-reviewed journal.
(reidy2023nucleotideexchangeis pages 1-2): Michael Reidy, Kevin Garzillo, and Daniel C. Masison. Nucleotide exchange is sufficient for hsp90 functions in vivo. Nature Communications, Apr 2023. URL: https://doi.org/10.1038/s41467-023-38230-0, doi:10.1038/s41467-023-38230-0. This article has 28 citations and is from a highest quality peer-reviewed journal.
(reidy2023nucleotideexchangeis pages 2-3): Michael Reidy, Kevin Garzillo, and Daniel C. Masison. Nucleotide exchange is sufficient for hsp90 functions in vivo. Nature Communications, Apr 2023. URL: https://doi.org/10.1038/s41467-023-38230-0, doi:10.1038/s41467-023-38230-0. This article has 28 citations and is from a highest quality peer-reviewed journal.
(hohrman2021disruptingprogressionof pages 1-1): Kaitlyn Hohrman, Davi Gonçalves, Kevin A Morano, and Jill L Johnson. Disrupting progression of the yeast hsp90 folding pathway at different transition points results in client-specific maturation defects. Genetics, Jan 2021. URL: https://doi.org/10.1093/genetics/iyab009, doi:10.1093/genetics/iyab009. This article has 15 citations and is from a domain leading peer-reviewed journal.
(rios2024insightsintohsp90 pages 8-9): Erick I. Rios, Isabel L. Hunsberger, and Jill L. Johnson. Insights into hsp90 mechanism and in vivo functions learned from studies in the yeast, saccharomyces cerevisiae. Frontiers in Molecular Biosciences, Feb 2024. URL: https://doi.org/10.3389/fmolb.2024.1325590, doi:10.3389/fmolb.2024.1325590. This article has 8 citations.
(rios2024insightsintohsp90 pages 3-5): Erick I. Rios, Isabel L. Hunsberger, and Jill L. Johnson. Insights into hsp90 mechanism and in vivo functions learned from studies in the yeast, saccharomyces cerevisiae. Frontiers in Molecular Biosciences, Feb 2024. URL: https://doi.org/10.3389/fmolb.2024.1325590, doi:10.3389/fmolb.2024.1325590. This article has 8 citations.
(hohrman2021disruptingprogressionof pages 4-4): Kaitlyn Hohrman, Davi Gonçalves, Kevin A Morano, and Jill L Johnson. Disrupting progression of the yeast hsp90 folding pathway at different transition points results in client-specific maturation defects. Genetics, Jan 2021. URL: https://doi.org/10.1093/genetics/iyab009, doi:10.1093/genetics/iyab009. This article has 15 citations and is from a domain leading peer-reviewed journal.
(hohrman2021disruptingprogressionof pages 1-2): Kaitlyn Hohrman, Davi Gonçalves, Kevin A Morano, and Jill L Johnson. Disrupting progression of the yeast hsp90 folding pathway at different transition points results in client-specific maturation defects. Genetics, Jan 2021. URL: https://doi.org/10.1093/genetics/iyab009, doi:10.1093/genetics/iyab009. This article has 15 citations and is from a domain leading peer-reviewed journal.