Heat shock proteins research

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

The paper presents a cryo-EM structure of a ClpXP-substrate complex, revealing an intermediate state in protein unfolding by the AAA+ proteolytic machine.

This study investigates how Grp94-selective ligands bind to Grp94 and Hsp90 by analyzing structural changes and identifies helix 1 as a key determinant of selectivity.

This study shows ADP-bound mtHSP70 binds preferentially to GRPEL1 over GRPEL2, with structural insights into their functional differences.

This study uses single-molecule nanopore experiments to demonstrate Hsp70 chaperones exert forces equivalent to 46 pN to extract trapped polypeptides, supporting the Entropic Pulling mechanism.

This study identifies S-HsfA2 in Arabidopsis as a factor that prevents hyperactivation of the heat stress response, balancing heat resistance and growth.

The paper disrupts each gene in the yeast heat shock response to identify feedback loops regulating Hsp70 expression and localization, revealing spatiotemporal control mechanisms.

This study visualizes the Cdc48 AAA+ ATPase unfolding pathway using structural snapshots, revealing a hand-over-hand mechanism and the sequential ATP hydrolysis and substrate interaction between D1 and D2 subunits.

This study shows that inhibiting host Hsp70 reduces SARS-CoV-2 infection more effectively than Remdesivir by blocking viral entry and autophagy.

This study investigates how HSP60 deficiency disrupts mitochondrial proteostasis and dysregulates cholesterol synthesis, leading to developmental abnormalities and hypomyelination.

This study shows that HOP stabilizes HSFA1a in Arabidopsis, which is required for the heat stress response during thermomorphogenesis.

This study identifies the thermodynamic mechanisms underlying trigger factor binding to ribosomes and nascent chains during co-translational protein synthesis.

This study uses a single turnover stopped-flow fluorescence method to show ClpB catalyzes processive protein unfolding at ~0.9 aa/s with a step-size of ~60 amino acids.

This study shows that loss of zebrafish Ba-crystallin (cryaba) increases age-related cataract, while loss of A-crystallin (cryaa) does not, highlighting an ontogenetic shift in crystallin function during lens development.

The paper determines cryo-EM structures of a mtHsp60 mutant to show how apical domains coordinate client engagement and chaperonin assembly during the ATP-dependent cycle.

This study investigates the functional mechanisms of Hsp60 in Sulfolobus acidocaldarius, revealing its role in protein folding and membrane protection under stress.

The paper investigates how chaperones coordinate during cotranslational protein folding in bacteria, showing they create a protected space for maturation without destabilizing intermediates.

This study shows that knocking out six Hsp70 genes in Drosophila reduces locomotor speed and disrupts adaptation to exercise training, with changes in leg muscle gene expression.

This paper identifies VA1, a small molecule that activates VCP/p97, and reveals its allosteric mechanism through cryo-EM structures and mutagenesis studies.

The paper shows mitochondrial thermogenesis generates heat that triggers a nuclear heat-shock response in mammalian cells.

The paper develops a fluorescence-based sensor to measure protein kinase stability in live cells and shows its utility in studying oncogenic mutations and HSP90 chaperone effects.

This study shows that CUL-6 ubiquitin ligase promotes thermotolerance by degrading HSP-90 in intestinal lysosomes, independent of HSF-1.

This study shows that 3xGFP overproduction causes cytotoxicity through degradation overload, not aggregate formation, as it traps Hsp70 and disrupts the ubiquitin-proteasome system.

This study identifies that the amino acid at residue 103 of HSF1 regulates trimer formation temperature through intermolecular interactions with aromatic residues.

This study identifies the role of Ranbp2's cyclophilin domain in regulating crystallin proteostasis and neuroprotection in the chorioretina through proteomic analysis of genetically modified mice.

This study reveals the tertiary structure and conformational dynamics of DNAJB6b at atomistic resolution, showing it cycles between three states and has an autoinhibitory mechanism linked to disease mutations.

The paper shows that DnaK duplication and regional evolution in bacteria increase proteomic complexity by expanding substrate specificity and function.

The paper investigates how J-domain proteins in yeast regulate Hsp70 chaperones through intramolecular interactions, showing auto-regulatory effects that reduce ATPase cycles.

This study identifies a unique chaperoning mechanism in class-A JDPs that recognizes and stabilizes mutant p53, promoting cancer progression by preventing its degradation.