Heat shock proteins research

This study identifies two distinct hydrophobic binding sites on Hsc70 for CMA substrates using computational methods and experimental data.

The paper shows that the mitochondrial targeting signal (MTS) regulates chaperone dynamics on mitochondrial precursors to buffer degradation and maintain import competence during stress.

This study investigates the 3D structure and function of the human R2SP complex using biochemical and structural methods, revealing similarities to the canonical R2TP complex and differences in ATPase activity and adaptor binding.

The paper compares transcriptomic responses to heat shock in three human cell lines, identifying conserved and cell-specific pathways.

The paper investigates Lambda N as a substrate for studying Escherichia coli Lon's regulatory function in RNA transcription using biochemical and structural methods.

This paper quantifies how E. coli ClpB unfolds and translocates protein substrates, showing ATP-dependent changes in step-size and processivity.

This study identifies the p23-FKBP51 chaperone complex as an Hsp90-independent regulator of tau aggregation, showing it forms a trimeric complex that inhibits tau fibril formation.

This study identifies the temperature-dependent phase separation mechanism of HSF1, revealing its molecular basis and species-specific regulation through simulations and experiments.

The paper shows that reducing Cofilin dosage in Drosophila embryos enhances stress adaptation and thermotolerance by priming stress response pathways.

The paper identifies HSP70 local translation in astrocyte endfeet after cerebral ischemia using RiboTag RNA sequencing and finds it correlates with proteostasis and ubiquitination changes.

This study uses single-particle tracking to show that Trigger factor binds to translating ribosomes in E. coli with two distinct modes and competes with SRP for RNC binding.

The paper determines the structure of human mortalin-GrpEL1 complexes using cryoEM and identifies mechanisms of nucleotide and substrate release in the Hsp70 system.

The paper shows that neuronal stress response involves localized synthesis of HSPA8 mRNA in dendrites to maintain proteostasis and prevent neurodegeneration.

This study investigates p47's role in retrotranslocation by enhancing talin's mechanical stability and generating pulling forces to facilitate ER-to-cytosol protein export.

This study identifies EID1 as an E3 ubiquitin ligase that regulates acquired thermotolerance by modulating HSBP translocation during heat stress.

This study investigates the roles of periplasmic chaperones in Gram-negative bacteria, showing some act as foldases and others as holdases during protein translocation.

This study identifies acetylation sites on yeast Ydj1 that affect its interactions with chaperones and client proteins, impacting proteostasis and translational fidelity.

This study examines HSP70 expression in a freeze-tolerant cricket under heat and freezing stress, finding that HSP70 is upregulated by heat but not freezing.

This study identifies ClpS as a key regulator of primary N-end rule proteolysis in Mycolicibacterium smegmatis, showing it binds canonical N-degrons and enhances substrate specificity for ClpC1P1P2 protease.

The paper identifies cytosolic mutant proteins degraded by the proteasome and shows DNAJA2 stabilizes some mutants while being dispensable for wild-type proteins.

This paper identifies design principles for modifying Hsp104 to enhance its therapeutic potential by tuning its collaboration with Hsp70 and Hsp40.

This study shows HOP/STIP1 is essential for KSHV lytic replication in primary effusion cell lines.

The paper examines how RNA Polymerase III transcription changes in mouse embryonic stem cells during heat shock, showing initial downregulation followed by upregulation, with HSF1 involvement in the latter.

The paper investigates the structural dynamics of αB-crystallin by mutating the NT-IXI motif, revealing how this affects fibrillar assembly and chaperone function using cryo-EM.

The paper tests a pharmacological chaperone's ability to rescue expression of destabilizing variants in the V2R gene, finding it effective for most variants.

This study shows HSP90 buffers BRCA1 mutations, reducing their clinical severity and contributing to PARP inhibitor resistance in cancer cells.

This study shows calmodulin acts as a chaperone during co-translational folding of the Kv7.2 channel's calcium responsive domain by stabilizing metastable hairpins.

This study shows that ssDNA binding and charge changes at DNA binding sites regulate Lon protease activity through allosteric effects and oligomerization.

This study identifies three deleterious SNPs in HSPB5 that disrupt the αB-crystallin domain's structure and function, contributing to proteotoxicity-related diseases.