Functional interplay between heat shock protein 90 (HSP90) and heat shock factors (HSFs) [PDF]
Cell Stress & ChaperonesMaintenance 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]
International Journal of Molecular Sciences, 2021 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
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The evolution of heat shock protein 90 C-terminal inhibitors: From novobiocin to potential clinical candidates [PDF]
Cell Stress & ChaperonesHeat 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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Heat shock proteins HSP27, HSP60, HSP70, and HSP90 [PDF]
Cancer, 2003 AbstractBACKGROUNDHeat shock proteins (HSPs) are synthesized by cells in response to various stress conditions, including carcinogenesis. The expression of HSPs in neoplasia has been implicated in the regulation of apoptosis, and HSPs also can act by increasing immunity. In the current study, the authors attempted to clarify the significance of HSPs in
Thierry Lebret +2 more
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SARS-CoV-2 Helicase (NSP13) Interacts with Mammalian Polyamine and HSP Partners in Promoting Viral Replication [PDF]
Current Issues in Molecular BiologyWe present a computational study that precedes the potential interactions between SARS-CoV-2 helicase (NSP13) and selected host proteins implicated in chaperone-assisted folding and polyamine metabolism.
Zingisa Sitobo +7 more
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CD91 Is a Common Receptor for Heat Shock Proteins gp96, hsp90, hsp70, and Calreticulin [PDF]
Immunity, 2001 Complexes of the heat shock protein gp96 and antigenic peptides are taken up by antigen-presenting cells and presented by MHC class I molecules. In order to explain the unusual efficiency of this process, the uptake of gp96 had been postulated to occur through a receptor, identified recently as CD91.
Robert J Binder, Pramod K Srivastava
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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]
PLoS ONE, 2013 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
Pharmaceutics, 2021 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
Advanced Science, 2023 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
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mSystems, 2018 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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