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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 C. elegans gene hsp-110 (systematic name C30C11.4; UniProt accession Q05036) encodes Heat Shock Protein 110, a member of the HSP70 superfamily belonging to the HSP110/Grp170 subfamily. The C. elegans genome encodes three Hsp70-related putative nucleotide exchange factors (NEFs): two ER-localized Grp170 family members and a single cytosolic HSP110 member, which is C30C11.4/HSP-110 (rampelt2012metazoanhsp70machines pages 8-9, tittelmeier2020thehsp110hsp70disaggregation pages 2-4). This makes HSP-110 the sole cytosolic HSP110-type NEF in the nematode, underscoring its non-redundant importance in cytoplasmic protein quality control.
HSP-110 shares the core domain organization of canonical Hsp70 proteins but with distinguishing features. It contains an N-terminal nucleotide-binding domain (NBD), a β-sandwich peptide-binding domain (PBD-β), and an α-helical bundle domain (PBD-α), along with longer insertions and C-terminal extensions relative to canonical Hsp70 (bracher2015thenucleotideexchange pages 2-4). A particularly notable structural feature is a negatively charged ~100-residue acidic insertion loop located between strands 7 and 8 of the β-sandwich subdomain, which is unique to the HSP110 family (sousa2014structuralmechanismsof pages 3-4). Additionally, the interdomain linker between the NBD and the substrate-binding domain is charged rather than hydrophobic, further distinguishing HSP-110 from canonical Hsp70 proteins (yakubu2018rolesofthe pages 1-3).
The primary biochemical function of HSP-110 is to serve as a nucleotide exchange factor (NEF) for Hsp70/Hsc70 chaperones. HSP-110 catalyzes the release of ADP from Hsp70, allowing ATP to rebind and thereby triggering substrate release from the Hsp70 peptide-binding cleft (sousa2014structuralmechanismsof pages 3-4, rampelt2012metazoanhsp70machines pages 1-2). This NEF activity is the most potent among eukaryotic cytosolic Hsp70 NEFs, making HSP110 proteins the dominant regulators of the Hsp70 chaperone cycle in the cytosol (sousa2014structuralmechanismsof pages 3-4).
Structural studies of the yeast ortholog Sse1 (in complex with Ssa1/Hsp70) have revealed the molecular mechanism of HSP110-mediated nucleotide exchange. The NBDs of HSP110 and Hsp70 face each other asymmetrically, forming extensive contacts between opposite NBD lobes (andreasson2008insightsintothe pages 1-2). A critical second contact involves the protruding C-terminal β-helical subdomain of HSP110 interacting with the periphery of Hsp70 NBD lobe II. The α-helix bundle domain of HSP110 fixes the Hsp70 NBD in an open conformation through highly conserved contacts (bracher2015thenucleotideexchange pages 2-4). This causes lobe displacement or rotation in the Hsp70 NBD, reducing Hsp70's affinity for ADP and enabling nucleotide exchange (yakubu2018rolesofthe pages 3-4). Importantly, ATP binding to the HSP110 NBD is required for complex formation with Hsp70, but ATP hydrolysis by HSP110 is not essential for its NEF function—ATPase-deficient HSP110 mutants can still rescue lethality from HSP110 deletion (yakubu2018rolesofthe pages 1-3, bracher2015thenucleotideexchange pages 2-4).
Beyond its NEF function, HSP-110 also acts as a passive chaperone ("holdase") capable of recognizing and binding unfolded or partially folded polypeptides to prevent their aggregation, without requiring energy input (yakubu2018rolesofthe pages 3-4). HSP110 displays faster binding kinetics and a preference for aromatic residue-rich peptides, in contrast to Hsp70's preference for aliphatic sequences (sousa2014structuralmechanismsof pages 3-4). However, in the context of protein disaggregation, the holdase function of HSP110 appears dispensable—studies using yeast Hsp110 mutants with partially inactivated substrate-binding domains showed no detrimental effect on disaggregation activity (yakubu2018rolesofthe pages 4-6).
HSP-110's most critical physiological role is as an essential component of the metazoan Hsp70-based protein disaggregation machinery. Unlike bacteria, fungi, and plants, which employ dedicated AAA+ ATPase Hsp100/Hsp104 disaggregases, metazoan organisms (including C. elegans) lack cytosolic Hsp100 homologs and instead rely on a tripartite chaperone system comprising Hsp70 (HSC70), J-domain proteins (Hsp40s), and HSP110 to solubilize protein aggregates (rampelt2012metazoanhsp70machines pages 1-2).
The disaggregation cycle operates as follows:
Aggregate recognition and Hsp70 recruitment: J-domain proteins (JDPs) of class A and class B recognize and target aggregated protein substrates, recruiting Hsp70 to the aggregate surface (nillegoda2015metazoanhsp70basedprotein pages 2-4, kirstein2017invivoproperties pages 1-1).
Hsp70 activation: JDPs stimulate Hsp70 ATPase activity, locking Hsp70 in its ADP-bound, high-affinity substrate-binding state on the aggregate.
HSP110-mediated nucleotide exchange: HSP110 is recruited to Hsp70 at the aggregate surface and catalyzes ADP-to-ATP exchange, which triggers substrate release and resets Hsp70 for another binding cycle (sztangierska2024earlystepsof pages 1-2).
Aggregate remodeling: Repeated cycles of Hsp70 binding and release, powered by HSP110-mediated nucleotide exchange, generate mechanical forces that extract polypeptides from aggregates. This may operate through an entropic pulling mechanism, where the bulky HSP110–Hsp70 complex transiently increases the effective volume near the aggregate, amplifying the unfolding/pulling forces (rebeaud2025ishsp110boosting pages 1-4).
Substrate refolding or degradation: Released polypeptides are either refolded by the Hsp70 system or handed off to degradation pathways.
Recent work (2024) has demonstrated that HSP110 plays a major role at the initial stages of disaggregation, catalyzing the recruitment of thick Hsp70 assemblies onto aggregate surfaces, which converts large aggregates into smaller species more readily processed by chaperones (sztangierska2024earlystepsof pages 1-2). HSP110's stimulation of Hsp70 is substantially stronger when working with class B J-domain proteins compared to class A, and this interaction requires the Hsp70 EEVD motif. Notably, HSP110 can also disrupt JDP-Hsp70 interactions, which may improve disaggregation efficiency but can inhibit activity if HSP110 concentrations exceed optimal sub-stoichiometric levels (sztangierska2024earlystepsof pages 1-2). This finding highlights that balanced interplay between the co-chaperones and Hsp70 is critical for effective disaggregation.
HSP-110 is identified as the sole cytosolic HSP110-type nucleotide exchange factor in C. elegans (tittelmeier2020thehsp110hsp70disaggregation pages 2-4). Its primary site of function is the cytoplasm, where it supports the Hsp70-based disaggregation machinery. Studies in yeast have demonstrated that the orthologous Hsp110 proteins (Sse1/Sse2) function in both the cytosol and nucleus, and that tethering Hsp110 away from either compartment impairs disaggregation in that location (kaimal2017coordinatedhsp110and pages 15-18). By analogy, C. elegans HSP-110 likely operates in both the cytoplasm and nucleus, though direct nuclear localization data in the worm are limited. The ER-localized Grp170 family members serve as the HSP70 NEFs in the endoplasmic reticulum, functionally complementing HSP-110 in that compartment (rampelt2012metazoanhsp70machines pages 8-9).
Complete hsp-110 knockout is lethal in C. elegans, demonstrating its essential role in normal cellular function (tittelmeier2020thehsp110hsp70disaggregation pages 2-4). Systemic RNAi knockdown also affects growth, development, and fertility (tittelmeier2020thehsp110hsp70disaggregation pages 2-4).
The landmark study by Rampelt et al. (2012) provided direct in vivo evidence for HSP-110's role in protein disaggregation using transgenic C. elegans expressing luciferase-YFP in muscle cells as an aggregation sensor. After heat shock (1 hour at 35°C), luciferase-YFP formed aggregated foci. In control animals, these aggregates were completely resolved within 24 hours of recovery at 20°C. However, in animals where hsp-110 was knocked down by RNAi, the aggregated luciferase foci persisted and remained insoluble and immobile at both 12 and 24 hours post-heat shock (rampelt2012metazoanhsp70machines pages 9-10, rampelt2012metazoanhsp70machines pages 8-9). Critically, knockdown of the alternative NEF bag-1 did not impair aggregate solubilization, demonstrating the non-redundant, specialized role of HSP-110 in the disaggregation machinery (rampelt2012metazoanhsp70machines pages 10-11, rampelt2012metazoanhsp70machines pages 9-10).
Under normal growth conditions at 20°C, hsp-110 RNAi causes only a modest lifespan reduction of 1–2 days. However, following heat shock, hsp-110-depleted animals exhibit a dramatic lifespan reduction of approximately 4.5 days compared to controls (rampelt2012metazoanhsp70machines pages 9-10). This indicates that HSP-110 becomes especially critical under conditions of high protein aggregation load, consistent with its role in the disaggregation pathway (rampelt2012metazoanhsp70machines pages 9-10).
A pivotal study by Tittelmeier et al. (2020) revealed that the HSP-110/HSP70 disaggregation system is a "double-edged sword" in the context of amyloid disease models. While HSP-110 depletion impaired general proteostasis (preventing resolubilization of amorphous aggregates and compromising cellular folding capacity), it paradoxically reduced α-synuclein foci formation, cell-to-cell transmission, and toxicity in C. elegans disease models (tittelmeier2020thehsp110hsp70disaggregation pages 1-2, tittelmeier2020thehsp110hsp70disaggregation pages 4-5). Specifically:
These findings demonstrate that the HSP70 disaggregation activity, while essential for maintaining cellular proteostasis, is also involved in generating toxic, spreading-competent amyloid species through fibril fragmentation, which can seed further polymerization and prion-like propagation (tittelmeier2020thehsp110hsp70disaggregation pages 6-9, tittelmeier2020thehsp110hsp70disaggregation pages 2-4).
HSP-110 knockdown shows complex age-dependent phenotypes. In young animals, HSP-110 depletion provides some tolerance to α-synuclein and polyQ toxicity. However, during aging, HSP-110-depleted animals show accelerated decline in motility compared to controls, likely due to progressive proteostasis collapse (tittelmeier2020thehsp110hsp70disaggregation pages 6-9). Age-dependent protein aggregation (measured by FlucSM foci) forms more rapidly in HSP-110 knockdown backgrounds, and the protective effects observed in younger animals are lost with age (tittelmeier2020thehsp110hsp70disaggregation pages 6-9).
In vivo studies in C. elegans have revealed that HSP-110 functions within a broader cooperative J-protein network. Class A and class B J-proteins (JDPs) form a flexible interactive network that relocalizes to protein aggregates upon heat shock and preferentially recruits constitutive Hsc70 for disaggregation (kirstein2017invivoproperties pages 1-1). This cooperation between J-protein classes is required for organismal health, promoting thermotolerance, maintenance of fecundity, and extended viability after heat stress (kirstein2017invivoproperties pages 7-8). Disruption of these cooperative interactions exacerbates age-dependent aggregation of polyQ proteins (kirstein2017invivoproperties pages 7-8).
HSP-110 represents a distinct evolutionary branch of the Hsp70 superfamily that has acquired specialized NEF function. In metazoan lineages that lost cytosolic Hsp100/Hsp104 disaggregases, the Hsp70-JDP-Hsp110 system became the primary disaggregation machinery (rampelt2012metazoanhsp70machines pages 1-2). This evolutionary transition underscores the importance of HSP-110 as a critical adaptation enabling metazoan cells to maintain proteostasis without dedicated AAA+ disaggregases. The system achieves disaggregation through a fundamentally different mechanism—iterative Hsp70 cycling powered by HSP110 NEF activity—rather than the threading mechanism employed by Hsp104 ring hexamers (torrente2013themetazoanprotein pages 4-5).
The following table provides a comprehensive overview of the key functional attributes of C. elegans hsp-110:
| Feature | Detail | Key Reference |
|---|---|---|
| Gene identity | hsp-110 corresponds to C30C11.4 in Caenorhabditis elegans and encodes the organism’s single cytosolic HSP110-type nucleotide exchange factor (NEF) for HSP70; this matches the UniProt entry Q05036 and distinguishes it from two ER-localized Grp170 family members. | (rampelt2012metazoanhsp70machines pages 8-9, tittelmeier2020thehsp110hsp70disaggregation pages 2-4) |
| Protein family | HSP-110 belongs to the HSP70 superfamily / HSP110 subfamily. Like other HSP110 proteins, it contains an N-terminal nucleotide-binding domain, β-sandwich peptide-binding domain, and α-helical bundle, with characteristic insertions including an acidic loop that distinguishes HSP110 proteins from canonical HSP70s. | (yakubu2018rolesofthe pages 1-3, bracher2015thenucleotideexchange pages 2-4, sousa2014structuralmechanismsof pages 3-4, yakubu2018rolesofthe pages 11-12) |
| Primary molecular function | The best-supported primary function is to act as a nucleotide exchange factor for HSP70/HSC70, promoting ADP release and ATP rebinding on HSP70 and thereby enabling substrate release and repeated chaperone cycles during protein quality control. In metazoan disaggregation, this NEF activity is the key catalytic contribution of HSP110. | (sousa2014structuralmechanismsof pages 3-4, yakubu2018rolesofthe pages 1-3, yakubu2018rolesofthe pages 3-4, rampelt2012metazoanhsp70machines pages 1-2) |
| Biochemical role in disaggregation | HSP-110 is essential for the HSP70-HSP40-HSP110 disaggregase system that solubilizes and reactivates aggregated proteins after stress. Direct work in C. elegans showed that HSP-110 is required for clearing heat-induced luciferase aggregates in vivo. | (rampelt2012metazoanhsp70machines pages 10-11, rampelt2012metazoanhsp70machines pages 9-10, rampelt2012metazoanhsp70machines pages 8-9) |
| ATP dependence / mechanism | Structural and biochemical studies of the HSP110 family show that ATP binding to HSP110 is required for productive interaction with HSP70, whereas ATP hydrolysis by HSP110 is not essential for its NEF function. HSP110 opens the HSP70 NBD through extensive NBD-NBD contacts and associated conformational changes. | (yakubu2018rolesofthe pages 1-3, bracher2015thenucleotideexchange pages 2-4, andreasson2008insightsintothe pages 1-2) |
| Additional chaperone properties | Beyond NEF activity, HSP110 family proteins can function as holdase chaperones that bind unfolded proteins and help prevent aggregation, though in disaggregation assays the central requirement is still the HSP70-directed NEF activity. | (yakubu2018rolesofthe pages 3-4, sousa2014structuralmechanismsof pages 3-4, yakubu2018rolesofthe pages 4-6) |
| Subcellular localization | In C. elegans, HSP-110 is identified as the sole cytosolic HSP110-type NEF. Available direct evidence supports cytosolic function, especially in muscle-cell proteostasis assays; by analogy with other eukaryotic HSP110 systems, related proteins can support disaggregation in both cytosol and nucleus, but C. elegans-specific nuclear localization evidence is limited. | (tittelmeier2020thehsp110hsp70disaggregation pages 2-4, kaimal2017coordinatedhsp110and pages 15-18) |
| Key interacting partners | Core functional partners are HSP70/HSC70 and J-domain proteins (HSP40s). The disaggregation machinery depends on cooperation between HSP110 and HSP70, while class A and class B J-proteins target aggregates and help recruit/activate HSP70 for extraction and refolding cycles. | (kirstein2017invivoproperties pages 1-1, rampelt2012metazoanhsp70machines pages 9-10, rampelt2012metazoanhsp70machines pages 1-2, nillegoda2015metazoanhsp70basedprotein pages 2-4, sztangierska2024earlystepsof pages 1-2) |
| Pathway involvement | hsp-110 functions in the cytosolic proteostasis network, specifically the metazoan HSP70-based protein disaggregation pathway that responds to heat stress, age-associated aggregation, and misfolded proteins. It is part of stress-recovery and aggregate-clearance pathways rather than a classic signaling enzyme pathway. | (kirstein2017invivoproperties pages 1-1, rampelt2012metazoanhsp70machines pages 9-10, rampelt2012metazoanhsp70machines pages 1-2) |
| Relationship to heat stress | In worms subjected to heat shock, HSP-110 is required for efficient recovery from proteotoxic stress. Loss of HSP-110 leaves heat-induced aggregates persistent and insoluble, indicating failure of post-stress protein recovery. | (rampelt2012metazoanhsp70machines pages 1-2, rampelt2012metazoanhsp70machines pages 9-10, rampelt2012metazoanhsp70machines pages 8-9) |
| Loss-of-function phenotype: viability | Complete hsp-110 knockout is lethal, indicating an essential housekeeping role in proteostasis. More moderate systemic RNAi knockdown also affects growth, development, and fertility. | (tittelmeier2020thehsp110hsp70disaggregation pages 2-4) |
| Loss-of-function phenotype: aggregate clearance | RNAi depletion of hsp-110 causes a strong defect in resolubilization of heat-induced luciferase aggregates in vivo; aggregates persist at 12–24 h after heat shock instead of clearing during recovery. | (rampelt2012metazoanhsp70machines pages 9-10, rampelt2012metazoanhsp70machines pages 8-9) |
| Loss-of-function phenotype: lifespan after stress | Under normal conditions, hsp-110 knockdown causes only a modest lifespan decrease, but after heat shock it causes a dramatic shortening of lifespan (~4.5 days), indicating that HSP-110 becomes especially critical under high aggregation load. | (rampelt2012metazoanhsp70machines pages 9-10) |
| Loss-of-function phenotype: amyloid models | In contrast to its protective role in general proteostasis, HSP-110 depletion can reduce α-synuclein and polyQ foci formation, spreading, and toxicity in worm disease models, showing that the disaggregase can be a double-edged sword by generating toxic amyloid-competent species while still supporting overall protein homeostasis. | (tittelmeier2020thehsp110hsp70disaggregation pages 6-9, tittelmeier2020thehsp110hsp70disaggregation pages 4-5, tittelmeier2020thehsp110hsp70disaggregation pages 1-2) |
| Expert interpretation | Authoritative reviews and mechanistic papers converge on the view that HSP110 is the major metazoan HSP70 NEF and a central amplifier of disaggregation capacity, acting early in aggregate processing and enabling efficient HSP70 cycling on difficult aggregate substrates. | (yakubu2018rolesofthe pages 4-6, nillegoda2015metazoanhsp70basedprotein pages 2-4, sztangierska2024earlystepsof pages 1-2) |
Table: This table summarizes the core functional annotation of C. elegans hsp-110/C30C11.4, including identity, molecular role, localization, partners, phenotypes, and pathway context. It is useful as a concise evidence-backed overview for gene annotation and literature review.
In conclusion, C. elegans HSP-110 (C30C11.4) is a cytosolic nucleotide exchange factor for Hsp70 that is essential for metazoan protein disaggregation. Its primary biochemical activity is catalyzing ADP release from Hsp70, enabling the iterative chaperone cycling required to extract and resolubilize aggregated proteins. HSP-110 is the sole cytosolic member of the HSP110 family in C. elegans, and its complete loss is lethal. Under proteotoxic stress conditions, HSP-110 is indispensable for aggregate clearance and organismal survival, while its activity in processing amyloid substrates represents a double-edged sword—essential for general proteostasis but also capable of generating toxic, spreading-competent amyloid species.
References
(rampelt2012metazoanhsp70machines pages 8-9): Heike Rampelt, Janine Kirstein-Miles, Nadinath B Nillegoda, Kang Chi, Sebastian R Scholz, Richard I Morimoto, and Bernd Bukau. Metazoan hsp70 machines use hsp110 to power protein disaggregation. The EMBO Journal, 31:4221-4235, Nov 2012. URL: https://doi.org/10.1038/emboj.2012.264, doi:10.1038/emboj.2012.264. This article has 383 citations.
(tittelmeier2020thehsp110hsp70disaggregation pages 2-4): Jessica Tittelmeier, Carl Alexander Sandhof, Heidrun Maja Ries, Silke Druffel‐Augustin, Axel Mogk, Bernd Bukau, and Carmen Nussbaum‐Krammer. The hsp110/hsp70 disaggregation system generates spreading‐competent toxic α‐synuclein species. The EMBO Journal, May 2020. URL: https://doi.org/10.15252/embj.2019103954, doi:10.15252/embj.2019103954. This article has 119 citations.
(bracher2015thenucleotideexchange pages 2-4): Andreas Bracher and Jacob Verghese. The nucleotide exchange factors of hsp70 molecular chaperones. Frontiers in Molecular Biosciences, Apr 2015. URL: https://doi.org/10.3389/fmolb.2015.00010, doi:10.3389/fmolb.2015.00010. This article has 299 citations.
(sousa2014structuralmechanismsof pages 3-4): Rui Sousa. Structural mechanisms of chaperone mediated protein disaggregation. Frontiers in Molecular Biosciences, Sep 2014. URL: https://doi.org/10.3389/fmolb.2014.00012, doi:10.3389/fmolb.2014.00012. This article has 42 citations.
(yakubu2018rolesofthe pages 1-3): Unekwu M. Yakubu and Kevin A. Morano. Roles of the nucleotide exchange factor and chaperone hsp110 in cellular proteostasis and diseases of protein misfolding. Biological Chemistry, 399:1215-1221, Sep 2018. URL: https://doi.org/10.1515/hsz-2018-0209, doi:10.1515/hsz-2018-0209. This article has 41 citations and is from a peer-reviewed journal.
(rampelt2012metazoanhsp70machines pages 1-2): Heike Rampelt, Janine Kirstein-Miles, Nadinath B Nillegoda, Kang Chi, Sebastian R Scholz, Richard I Morimoto, and Bernd Bukau. Metazoan hsp70 machines use hsp110 to power protein disaggregation. The EMBO Journal, 31:4221-4235, Nov 2012. URL: https://doi.org/10.1038/emboj.2012.264, doi:10.1038/emboj.2012.264. This article has 383 citations.
(andreasson2008insightsintothe pages 1-2): Claes Andréasson, Jocelyne Fiaux, Heike Rampelt, Silke Druffel-Augustin, and Bernd Bukau. Insights into the structural dynamics of the hsp110–hsp70 interaction reveal the mechanism for nucleotide exchange activity. Proceedings of the National Academy of Sciences, 105:16519-16524, Oct 2008. URL: https://doi.org/10.1073/pnas.0804187105, doi:10.1073/pnas.0804187105. This article has 107 citations and is from a highest quality peer-reviewed journal.
(yakubu2018rolesofthe pages 3-4): Unekwu M. Yakubu and Kevin A. Morano. Roles of the nucleotide exchange factor and chaperone hsp110 in cellular proteostasis and diseases of protein misfolding. Biological Chemistry, 399:1215-1221, Sep 2018. URL: https://doi.org/10.1515/hsz-2018-0209, doi:10.1515/hsz-2018-0209. This article has 41 citations and is from a peer-reviewed journal.
(yakubu2018rolesofthe pages 4-6): Unekwu M. Yakubu and Kevin A. Morano. Roles of the nucleotide exchange factor and chaperone hsp110 in cellular proteostasis and diseases of protein misfolding. Biological Chemistry, 399:1215-1221, Sep 2018. URL: https://doi.org/10.1515/hsz-2018-0209, doi:10.1515/hsz-2018-0209. This article has 41 citations and is from a peer-reviewed journal.
(nillegoda2015metazoanhsp70basedprotein pages 2-4): Nadinath B. Nillegoda and Bernd Bukau. Metazoan hsp70-based protein disaggregases: emergence and mechanisms. Frontiers in Molecular Biosciences, Oct 2015. URL: https://doi.org/10.3389/fmolb.2015.00057, doi:10.3389/fmolb.2015.00057. This article has 149 citations.
(kirstein2017invivoproperties pages 1-1): Janine Kirstein, Kristin Arnsburg, Annika Scior, Anna Szlachcic, D. Lys Guilbride, Richard I. Morimoto, Bernd Bukau, and Nadinath B. Nillegoda. In vivo properties of the disaggregase function of j‐proteins and hsc70 in caenorhabditis elegans stress and aging. Aging Cell, 16:1414-1424, Oct 2017. URL: https://doi.org/10.1111/acel.12686, doi:10.1111/acel.12686. This article has 87 citations and is from a domain leading peer-reviewed journal.
(sztangierska2024earlystepsof pages 1-2): Wiktoria Sztangierska, Hubert Wyszkowski, Maria Pokornowska, Klaudia Kochanowicz, Michał Rychłowski, Krzysztof Liberek, and Agnieszka Kłosowska. Early steps of protein disaggregation by hsp70 chaperone and class b j-domain proteins are shaped by hsp110. Sep 2024. URL: https://doi.org/10.7554/elife.94795.2, doi:10.7554/elife.94795.2. This article has 24 citations.
(rebeaud2025ishsp110boosting pages 1-4): Mathieu E. Rebeaud, Bruno Fauvet, Paolo De Los Rios, and Pierre Goloubinoff. Is hsp110 boosting the basal disaggregation activity hsp70 by enhanced entropic pulling strokes? bioRxiv, Apr 2025. URL: https://doi.org/10.1101/2025.04.01.646638, doi:10.1101/2025.04.01.646638. This article has 0 citations.
(kaimal2017coordinatedhsp110and pages 15-18): Jayasankar Mohanakrishnan Kaimal, Ganapathi Kandasamy, Fabian Gasser, and Claes Andréasson. Coordinated hsp110 and hsp104 activities power protein disaggregation in saccharomyces cerevisiae. Molecular and Cellular Biology, Jun 2017. URL: https://doi.org/10.1128/mcb.00027-17, doi:10.1128/mcb.00027-17. This article has 95 citations and is from a domain leading peer-reviewed journal.
(rampelt2012metazoanhsp70machines pages 9-10): Heike Rampelt, Janine Kirstein-Miles, Nadinath B Nillegoda, Kang Chi, Sebastian R Scholz, Richard I Morimoto, and Bernd Bukau. Metazoan hsp70 machines use hsp110 to power protein disaggregation. The EMBO Journal, 31:4221-4235, Nov 2012. URL: https://doi.org/10.1038/emboj.2012.264, doi:10.1038/emboj.2012.264. This article has 383 citations.
(rampelt2012metazoanhsp70machines pages 10-11): Heike Rampelt, Janine Kirstein-Miles, Nadinath B Nillegoda, Kang Chi, Sebastian R Scholz, Richard I Morimoto, and Bernd Bukau. Metazoan hsp70 machines use hsp110 to power protein disaggregation. The EMBO Journal, 31:4221-4235, Nov 2012. URL: https://doi.org/10.1038/emboj.2012.264, doi:10.1038/emboj.2012.264. This article has 383 citations.
(tittelmeier2020thehsp110hsp70disaggregation pages 1-2): Jessica Tittelmeier, Carl Alexander Sandhof, Heidrun Maja Ries, Silke Druffel‐Augustin, Axel Mogk, Bernd Bukau, and Carmen Nussbaum‐Krammer. The hsp110/hsp70 disaggregation system generates spreading‐competent toxic α‐synuclein species. The EMBO Journal, May 2020. URL: https://doi.org/10.15252/embj.2019103954, doi:10.15252/embj.2019103954. This article has 119 citations.
(tittelmeier2020thehsp110hsp70disaggregation pages 4-5): Jessica Tittelmeier, Carl Alexander Sandhof, Heidrun Maja Ries, Silke Druffel‐Augustin, Axel Mogk, Bernd Bukau, and Carmen Nussbaum‐Krammer. The hsp110/hsp70 disaggregation system generates spreading‐competent toxic α‐synuclein species. The EMBO Journal, May 2020. URL: https://doi.org/10.15252/embj.2019103954, doi:10.15252/embj.2019103954. This article has 119 citations.
(tittelmeier2020thehsp110hsp70disaggregation pages 6-9): Jessica Tittelmeier, Carl Alexander Sandhof, Heidrun Maja Ries, Silke Druffel‐Augustin, Axel Mogk, Bernd Bukau, and Carmen Nussbaum‐Krammer. The hsp110/hsp70 disaggregation system generates spreading‐competent toxic α‐synuclein species. The EMBO Journal, May 2020. URL: https://doi.org/10.15252/embj.2019103954, doi:10.15252/embj.2019103954. This article has 119 citations.
(kirstein2017invivoproperties pages 7-8): Janine Kirstein, Kristin Arnsburg, Annika Scior, Anna Szlachcic, D. Lys Guilbride, Richard I. Morimoto, Bernd Bukau, and Nadinath B. Nillegoda. In vivo properties of the disaggregase function of j‐proteins and hsc70 in caenorhabditis elegans stress and aging. Aging Cell, 16:1414-1424, Oct 2017. URL: https://doi.org/10.1111/acel.12686, doi:10.1111/acel.12686. This article has 87 citations and is from a domain leading peer-reviewed journal.
(torrente2013themetazoanprotein pages 4-5): Mariana P Torrente and James Shorter. The metazoan protein disaggregase and amyloid depolymerase system. Prion, 7:457-463, Nov 2013. URL: https://doi.org/10.4161/pri.27531, doi:10.4161/pri.27531. This article has 92 citations and is from a peer-reviewed journal.
(yakubu2018rolesofthe pages 11-12): Unekwu M. Yakubu and Kevin A. Morano. Roles of the nucleotide exchange factor and chaperone hsp110 in cellular proteostasis and diseases of protein misfolding. Biological Chemistry, 399:1215-1221, Sep 2018. URL: https://doi.org/10.1515/hsz-2018-0209, doi:10.1515/hsz-2018-0209. This article has 41 citations and is from a peer-reviewed journal.