Results 1 to 10 of about 132,845 (313)

Role of Heat Shock Proteins (HSP70 and HSP90) in Viral Infection [PDF]

open access: yesInternational 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   +3 more sources

Heat Shock Proteins and Ferroptosis

open access: yesFrontiers 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   +2 more sources

Differential roles of HSP70 and HSP90 in Senecavirus A infection: IRES-dependent translational regulation and viral replication mechanisms [PDF]

open access: yesVirulence
As 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
doaj   +2 more sources

SARS-CoV-2 Helicase (NSP13) Interacts with Mammalian Polyamine and HSP Partners in Promoting Viral Replication [PDF]

open access: yesCurrent Issues in Molecular Biology
We 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
doaj   +2 more sources

Heat shock protein 90: biological functions, diseases, and therapeutic targets

open access: yesMedComm
Heat shock protein 90 (Hsp90) is a predominant member among Heat shock proteins (HSPs), playing a central role in cellular protection and maintenance by aiding in the folding, stabilization, and modification of diverse protein substrates. It collaborates
Huiyun Wei   +7 more
doaj   +2 more sources

Heat shock proteins HSP27, HSP60, HSP70, and HSP90 [PDF]

open access: yesCancer, 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   +6 more
openaire   +3 more sources

Heat Shock Protein 90 (HSP90) and Her2 in Adenocarcinomas of the Esophagus [PDF]

open access: goldCancers, 2014
Her2 overexpression and amplification can be found in a significant subset of esophageal adenocarcinomas. The activity of Her2 has been shown to be modulated by molecular chaperones such as HSP90. We analyzed expression/amplification data for HSP90 and Her2 on 127 primary resected esophageal adenocarcinomas in order to evaluate a possible relationship ...
Julia Slotta‐Huspenina   +4 more
openalex   +5 more sources

The 90-kDa Heat Shock Protein Hsp90 Protects Tubulin against Thermal Denaturation [PDF]

open access: hybridJournal of Biological Chemistry, 2010
Hsp90 and tubulin are among the most abundant proteins in the cytosol of eukaryotic cells. Although Hsp90 plays key roles in maintaining its client proteins in their active state, tubulin is essential for fundamental processes such as cell morphogenesis and division. Several studies have suggested a possible connection between Hsp90 and the microtubule
Félix Weis   +4 more
openalex   +3 more sources

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