Super Spy variants implicate flexibility in chaperone action
eLife, 2014 Experimental study of the role of disorder in protein function is challenging. It has been proposed that proteins utilize disordered regions in the adaptive recognition of their various binding partners.
Shu Quan +8 more
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Differential Interactions of Molecular Chaperones and Yeast Prions
Journal of Fungi, 2022 Baker’s yeast Saccharomyces cerevisiae is an important model organism that is applied to study various aspects of eukaryotic cell biology. Prions in yeast are self-perpetuating heritable protein aggregates that can be leveraged to study the interaction ...
Yury A. Barbitoff +2 more
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Protein trafficking in the mitochondrial intermembrane space: mechanisms and links to human disease [PDF]
, 2017 Mitochondria fulfill a diverse range of functions in cells including oxygen metabolism, homeostasis of inorganic ions and execution of apoptosis. Biogenesis of mitochondria relies on protein import pathways that are ensured by dedicated multiprotein ...
MacPherson, Lisa +1 more
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Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumption
eLife, 2014 70-kDa Heat shock proteins are ATP-driven molecular chaperones that perform a myriad of essential cellular tasks. Although structural and biochemical studies have shed some light on their functional mechanism, the fundamental issue of the role of energy ...
Paolo De Los Rios, Alessandro Barducci
doaj +1 more source
A Chaperone-Like Role for EBI3 in Collaboration With Calnexin Under Inflammatory Conditions
Frontiers in Immunology, 2021 The interleukin-6 (IL-6)/IL-12 family of cytokines plays critical roles in the induction and regulation of innate and adaptive immune responses. Among the various cytokines, only this family has the unique characteristic of being composed of two distinct
Aruma Watanabe +12 more
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Small heat-shock proteins: important players in regulating cellular proteostasis [PDF]
, 2015 Small heat-shock proteins (sHsps) are a diverse family of intra-cellular molecular chaperone proteins that play a critical role in mitigating and preventing protein aggregation under stress conditions such as elevated temperature, oxidation and infection.
Carver, John A. +3 more
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Evolution of an intricate J-protein network driving protein disaggregation in eukaryotes
eLife, 2017 Hsp70 participates in a broad spectrum of protein folding processes extending from nascent chain folding to protein disaggregation. This versatility in function is achieved through a diverse family of J-protein cochaperones that select substrates for ...
Nadinath B Nillegoda +8 more
doaj +1 more source
Frontiers in Plant Science, 2021 Ascorbate peroxidase (APX) is an important reactive oxygen species (ROS)-scavenging enzyme, which catalyzes the removal of hydrogen peroxide (H2O2) to prevent oxidative damage.
Shubhpreet Kaur +17 more
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Chaperone-assisted translocation of flexible polymers in three dimensions
, 2016 Polymer translocation through a nanometer-scale pore assisted by chaperones binding to the polymer is a process encountered in vivo for proteins. Studying the relevant models by computer simulations is computationally demanding.
Linna, R. P., Suhonen, P. M.
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Myelin pathology: Involvement of molecular chaperones and the promise of chaperonotherapy [PDF]
, 2019 The process of axon myelination involves various proteins including molecular chaperones. Myelin alteration is a common feature in neurological diseases due to structural and functional abnormalities of one or more myelin proteins.
Cappello F. +4 more
core +1 more source