Heat shock proteins research

This study identifies Hero proteins as heat-resistant proteins that stabilize other proteins and prevent aggregation, extending lifespan in Drosophila.

The paper shows that Hsp90 chaperones and the F-box protein MEC-15 have opposing roles in neuronal differentiation, with Hsp90 inhibiting neurite growth and synaptic development in C. elegans.

This study shows HSF-1 protects C. elegans from oxidative stress through two distinct mechanisms depending on temperature conditions.

This study investigates the functional interaction between the J-protein Tbj2 and cytosolic Hsp70/Hsp70.4 in Trypanosoma brucei, showing their cooperative role in protein refolding.

This paper shows that HSV-1's ICP22 protein functions as a viral J-like co-chaperone that interacts with Hsc70 to manage protein aggregation during lytic infection.

This paper presents the first high-resolution cryo-EM structure of ClpXP from Listeria monocytogenes, revealing the binding interface and activation mechanism of the complex.

This study shows that misfolded proteins in the heart can disrupt brain function and worsen stroke damage through prion-like mechanisms.

The paper identifies hsp-16.2 chaperone biomarkers as indicators of proteome dosage states in C. elegans, revealing cell-to-cell variation linked to gene expression differences.

The paper presents structural analysis of the Plasmodium falciparum Hsp40-Hsp70 chaperone pair to elucidate their binding mechanism and inform drug design.

This study shows that heat shock in C. elegans affects the expression of various non-coding RNAs, some of which are directly regulated by HSF-1.

The paper shows that ribosome assembly stress triggers a pathway that balances Hsf1 and Ifh1 activity to prevent proteotoxic stress in yeast.

The paper determines the cryo-EM structure of Y. pestis Lon protease during substrate processing, revealing a distinct hand-over-hand translocation mechanism unique to the HCLR clade.

The paper shows that over-expression of Hsp83 in the absence of hsrω lncRNAs causes synthetic lethality and phenocopies l(2)gl mutants in Drosophila.

This study identifies chaperone systems as limiting factors for cell-cycle entry, showing their role in regulating nuclear accumulation of the G1 Cdk-cyclin complex and linking cell-cycle progression to growth and stress conditions.

The paper investigates the interaction between PFA0660w, PfHsp70-x, and PfEMP1 in Plasmodium falciparum, showing their role in PfEMP1 transport via cholesterol-rich J-dots.

The paper identifies three natural compound allosteric modulators of Hsp90 and assesses their effect on the protein's conformational dynamics.

The paper investigates cellular responses to proteostasis impairments in yeast, finding that transcriptional responses often fail to restore proteostasis and that over-expression of alternative machineries can partially compensate for gene deletions.

This study uses transgenic zebrafish to compare molecular effects of cataract-linked αA-crystallin mutants, revealing differences in their impact on lens proteostasis.

The paper investigates the role of bacterial Hsp90 (HtpG) in collaboration with Hsp70 (DnaK) and shows that HtpG mediates degradation of aggregation-prone substrates via HslUV proteolysis.

The paper shows that dimeric subunits of sHsps are functional units for substrate capture, and that dimer stability affects chaperone efficiency.

The paper quantifies Hsf1 binding and transcription in yeast under basal and heat shock conditions, revealing a continuum of Hsf1 occupancy and activity across the genome.

This study shows that heat shock stress activates transposon expression by disrupting piRNA biogenesis through Hsp70's interaction with the Hsc70-Hsp90 complex in Drosophila.

This study shows that HSP90 reduces the penetrance of newly introduced mutations in plants, leading to fewer embryonic lethality and phenotypic abnormalities compared to HSP90-reduced plants.

This study identifies that loss of rsks-1/S6-Kinase rescues developmental arrest in C. elegans hsf-1 mutants, revealing an unexplained regulatory link between heat-shock transcription factors and the TOR pathway during development.

This study investigates the holdase function of Escherichia coli DnaK chaperone using single-molecule assays, showing it stabilizes unfolded proteins and switches between holding and releasing states upon ATP binding.

The paper investigates transcriptional and translational changes in Streptomyces coelicolor under heat stress, revealing significant translational control and novel stress response mechanisms.

The paper shows that Hsf1 phosphorylation creates cell-to-cell variation in Hsp90 levels, which enhances phenotypic plasticity in budding yeast.

This study uses computational methods to analyze how ATP and ADP affect the conformational dynamics of human Hsp90, identifying key residues involved in allosteric modulation.

The paper systematically analyzes chaperome deregulation across 22 solid cancers using gene expression data and develops a tool to visualize proteostasis alterations.

The paper shows ATP hydrolysis in TRAP1 is sequential and asymmetric, with conformational flipping during the cycle to remodel client proteins.