Results 41 to 50 of about 86,733 (300)
Heat Shock Protein 70 (Hsp70) as an Emerging Drug Target [PDF]
Journal of Medicinal Chemistry, 2010 Heat shock protein 70 (Hsp70) is a molecular chaperone that is expressed in response to stress. In this role, Hsp70 binds to its protein substrates and stabilize them against denaturation or aggregation until conditions improve.1 In addition to its functions during a stress response, Hsp70 has multiple responsibilities during normal growth; it assists ...
Christopher G, Evans +2 more
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Additional sex combs interacts with enhancer of zeste and trithorax and modulates levels of trimethylation on histone H3K4 and H3K27 during transcription of hsp70. [PDF]
, 2017 BACKGROUND: Maintenance of cell fate determination requires the Polycomb group for repression; the trithorax group for gene activation; and the enhancer of trithorax and Polycomb (ETP) group for both repression and activation.
Brock, Hugh W +4 more
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Heat Shock Proteins (HSP70) as Biomarkers in Ecotoxicological Studies
Ecotoxicology and Environmental Safety, 1997 Hsp70, so-called stress proteins, were studied in the centipede Lithobius mutabilis when exposed in laboratory tests to different concentrations of the insecticide dimethoate (DMT; 0, 0.012, 0.111 mg kg-1 dwt), the detergent linear alkilobenzene sulfonate (LAS; 0, 16, 80, 400, 2000, 10,000 mg kg-1 dwt), and copper (Cu; 0, 56, 167, 500, 1000, 1500 mg kg-
Pyza, Elżbieta +3 more
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Heat shock protein hsp70 overexpression confers resistance against nitric oxide [PDF]
FEBS Letters, 1996 Heat stress is known to render rat islet cells resistant against the toxic effects of nitric oxide, reactive oxygen intermediates and the islet cell toxin streptozotocin. We report here for the first time that protection against nitric oxide is mediated by the major heat shock protein, hsp70, even in the absence of heat stress. The human hsp70 gene was
Bellmann, Kerstin +4 more
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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 +6 more
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Dataset of Nematostella vectensis Hsp70 isoform interactomes upon heat shock
Data in Brief, 2019 Nematostella vectensis is an estuarine sea anemone that has emerged as a model species to characterize molecular responses to physiological stressors due to its exposure to diverse, extreme abiotic conditions.
Laura E. Knighton +4 more
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Hyperglycaemia and oxidative stress upregulate HSP60 & HSP70 expression in HeLa cells [PDF]
, 2013 Heat Shock Proteins 60 & 70 (HSP60 & HSP70) are intracellular protein that has been shown to be present at elevated levels in systemic circulation in Type 2 Diabetes mellitus (T2DM) patients.
Hall, Luke, Martinus, Ryan Dennis
core +2 more sources
Molecular Plant-Microbe Interactions, 2001 We analyzed, with respect to heat shock proteins (HSPs), systemically reacting tobacco leaves inoculated with Tobacco mosaic virus (TMV), wild-type vulgare, and temperature-sensitive coat protein (CP) mutants Ni 118 (P20L) and flavum (D19A), kept at 23 ...
Harald Jockusch +3 more
doaj +1 more source
The neuroprotective potential of heat shock protein 70 (HSP70)
Molecular Medicine Today, 1999 In response to many metabolic disturbances and injuries, including stroke, neurodegenerative disease, epilepsy and trauma, the cell mounts a stress response with induction of a variety of proteins, most notably the 70-kDa heat shock protein (HSP70). Whether stress proteins are neuroprotective has been hotly debated, as these proteins might be merely an
M A, Yenari +3 more
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Heat Shock Protein (Hsp) 40 Mutants Inhibit Hsp70 in Mammalian Cells [PDF]
Journal of Biological Chemistry, 1999 Heat shock protein (Hsp) 70 and Hsp40 expressed in mammalian cells had been previously shown to cooperate in accelerating the reactivation of heat-denatured firefly luciferase (Michels, A. A., Kanon, B., Konings, A. W. T., Ohtsuka, K., Bensaude, O., and Kampinga, H. H. (1997) J. Biol. Chem. 272, 33283-33289).
Michels, AA +3 more
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