J-domain protein chaperone circuits in proteostasis and disease
The J-domain proteins (JDP) form the largest protein family among cellular chaperones. In
cooperation with the Hsp70 chaperone system, these co-chaperones orchestrate a plethora …
cooperation with the Hsp70 chaperone system, these co-chaperones orchestrate a plethora …
Specification of Hsp70 function by type I and type II Hsp40
Cellular homeostasis and stress survival requires maintenance of the proteome and
suppression of proteotoxicity. Molecular chaperones promote cell survival through repair of …
suppression of proteotoxicity. Molecular chaperones promote cell survival through repair of …
Multi-scale structures of the mammalian radial spoke and divergence of axonemal complexes in ependymal cilia
X Meng, C Xu, J Li, B Qiu, J Luo, Q Hong… - Nature …, 2024 - nature.com
Radial spokes (RS) transmit mechanochemical signals between the central pair (CP) and
axonemal dynein arms to coordinate ciliary motility. Atomic-resolution structures of …
axonemal dynein arms to coordinate ciliary motility. Atomic-resolution structures of …
Sis1 potentiates the stress response to protein aggregation and elevated temperature
Cells adapt to conditions that compromise protein conformational stability by activating
various stress response pathways, but the mechanisms used in sensing misfolded proteins …
various stress response pathways, but the mechanisms used in sensing misfolded proteins …
Class-specific interactions between Sis1 J-domain protein and Hsp70 chaperone potentiate disaggregation of misfolded proteins
H Wyszkowski, A Janta… - Proceedings of the …, 2021 - National Acad Sciences
Protein homeostasis is constantly being challenged with protein misfolding that leads to
aggregation. Hsp70 is one of the versatile chaperones that interact with misfolded proteins …
aggregation. Hsp70 is one of the versatile chaperones that interact with misfolded proteins …
In vivo properties of the disaggregase function of J‐proteins and Hsc70 in Caenorhabditis elegans stress and aging
J Kirstein, K Arnsburg, A Scior, A Szlachcic… - Aging cell, 2017 - Wiley Online Library
Protein aggregation is enhanced upon exposure to various stress conditions and aging,
which suggests that the quality control machinery regulating protein homeostasis could …
which suggests that the quality control machinery regulating protein homeostasis could …
Hsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines
M Reidy, R Sharma, S Shastry, BL Roberts… - PLoS …, 2014 - journals.plos.org
Hsp100 family chaperones of microorganisms and plants cooperate with the
Hsp70/Hsp40/NEF system to resolubilize and reactivate stress-denatured proteins. In yeast …
Hsp70/Hsp40/NEF system to resolubilize and reactivate stress-denatured proteins. In yeast …
Ab initio protein structure prediction: the necessary presence of external force field as it is delivered by Hsp40 chaperone
I Roterman, K Stapor, L Konieczny - BMC bioinformatics, 2023 - Springer
Background The aqueous environment directs the protein folding process towards the
generation of micelle-type structures, which results in the exposure of hydrophilic residues …
generation of micelle-type structures, which results in the exposure of hydrophilic residues …
Characterizing the altered cellular proteome induced by the stress-independent activation of heat shock factor 1
The heat shock response is an evolutionarily conserved, stress-responsive signaling
pathway that adapts cellular proteostasis in response to pathologic insult. In metazoans, the …
pathway that adapts cellular proteostasis in response to pathologic insult. In metazoans, the …
Identification of subfunctionalized aggregate-remodeling J-domain proteins in Arabidopsis thaliana
J-domain proteins (JDPs) are critical components of the cellular protein quality control
machinery, playing crucial roles in preventing the formation and, solubilization of cytotoxic …
machinery, playing crucial roles in preventing the formation and, solubilization of cytotoxic …