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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Hsp90 orchestrates transcriptional regulation by Hsf1 and cell wall remodelling by MAPK signalling during thermal adaptation in a pathogenic yeast. [PDF]
PLoS Pathogens, 2012 Thermal adaptation is essential in all organisms. In yeasts, the heat shock response is commanded by the heat shock transcription factor Hsf1. Here we have integrated unbiased genetic screens with directed molecular dissection to demonstrate that ...
Michelle D Leach +5 more
doaj +4 more sources
Differential roles of HSP70 and HSP90 in Senecavirus A infection: IRES-dependent translational regulation and viral replication mechanisms [PDF]
VirulenceAs opportunistic intracellular pathogens, viruses rely on numerous sequential interactions between host and viral factors for their replication. Given the significance of molecular chaperones (heat shock protein 70 and heat shock protein 90) in mediating
Chen Li +5 more
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Changes in HSP gene and protein expression in natural scrapie with brain damage [PDF]
Veterinary Research, 2011 Heat shock proteins (Hsp) perform cytoprotective functions such as apoptosis regulation and inflammatory response control. These proteins can also be secreted to the extracellular medium, acting as inflammatory mediators, and their chaperone activity ...
Serrano Carmen +11 more
doaj +3 more sources
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
doaj +1 more source
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
doaj +1 more source
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 +3 more
openaire +2 more sources
Unleashing the full potential of Hsp90 inhibitors as cancer therapeutics through simultaneous inactivation of Hsp90, Grp94, and TRAP1 [PDF]
, 2020 Cancer therapeutics: Extending a drug's reach A new drug that blocks heat shock proteins (HSPs), helper proteins that are co-opted by cancer cells to promote tumor growth, shows promise for cancer treatment.
Chae, Young Chan +10 more
core +1 more source
Heat Shock Proteins and Ferroptosis
Frontiers in Cell and Developmental Biology, 2022 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
doaj +1 more source
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
doaj +3 more sources