Functional interplay between heat shock protein 90 (HSP90) and heat shock factors (HSFs) [PDF]
Maintenance of protein homeostasis, also known as proteostasis, is essential for cellular survival under both basal and stress conditions. Proteostasis relies on a coordinated action between molecular chaperones, such as heat shock proteins (HSPs), and ...
Abir Chakraborty +2 more
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Role of Heat Shock Proteins (HSP70 and HSP90) in Viral Infection [PDF]
Heat shock proteins (HSPs) are a large group of chaperones found in most eukaryotes and bacteria. They are responsible for the correct protein folding, protection of the cell against stressors, presenting immune and inflammatory cytokines; furthermore, they are important factors in regulating cell differentiation, survival and death.
Anna Lubkowska +2 more
exaly +3 more sources
The evolution of heat shock protein 90 C-terminal inhibitors: From novobiocin to potential clinical candidates [PDF]
Heat shock protein 90 (Hsp90) is a highly conserved molecular chaperone that regulates the maturation of various client proteins. Most therapeutic studies have focused on N-terminal Hsp90 inhibitors, but these are limited by dose-escalating toxicities ...
Xiaosheng Jiang, Brian S.J. Blagg
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Coordinated regulation of the metaboproteome by Hsp90 chaperones controls metabolic plasticity [PDF]
Summary: Heat shock protein 90 (Hsp90) chaperones participate in the stabilization and activation of hundreds of proteins, thereby acting as signaling hubs.
R. Felipe Perez +7 more
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The membrane-associated transient receptor potential vanilloid channel is the central heat shock receptor controlling the cellular heat shock response in epithelial cells. [PDF]
The heat shock response (HSR) is a highly conserved molecular response to various types of stresses, including heat shock, during which heat-shock proteins (Hsps) are produced to prevent and repair damages in labile proteins and membranes.
Zohar Bromberg +3 more
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Structure-Activity Relationships of Benzothiazole-Based Hsp90 C-Terminal-Domain Inhibitors
Heat shock protein 90 (Hsp90) is a chaperone responsible for the maturation of many cancer-related proteins, and is therefore an important target for the design of new anticancer agents.
Jaka Dernovšek +6 more
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The Onset of Molecule‐Spanning Dynamics in Heat Shock Protein Hsp90
AbstractProtein dynamics have been investigated on a wide range of time scales. Nano‐ and picosecond dynamics have been assigned to local fluctuations, while slower dynamics have been attributed to larger conformational changes. However, it is largely unknown how fast (local) fluctuations can lead to slow global (allosteric) changes.
Sohmen, Benedikt +11 more
openaire +7 more sources
The 90-kDa heat shock protein (HSP90) of eukaryotes is a highly abundant and essential chaperone required for the maturation of regulatory and signal proteins.
Eugenia Bifeld +5 more
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Circulating heat shock protein 90 (Hsp90) and autoantibodies to Hsp90 are increased in patients with atopic dermatitis [PDF]
Atopic dermatitis (AD) is one of the most common chronic inflammatory dermatoses characterized by persistent itching and recurrent eczematous lesions. While the primary events and key drivers of AD are topics of ongoing debate, cutaneous inflammation due to inappropriate IgE (auto)antibody-related immune reactions is frequently considered.
Krzysztof Sitko +4 more
openaire +2 more sources
Heat Shock Proteins and Ferroptosis
Ferroptosis is a new form of regulatory cell death named by Dixon in 2012, which is characterized by the accumulation of lipid peroxides and iron ions. Molecular chaperones are a class of evolutionarily conserved proteins in the cytoplasm. They recognize
Ying Liu +28 more
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