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Current Opinion in Oncology, 2003
Heat shock protein 90 (Hsp90) is a molecular chaperone required for the stability and function of a number of conditionally activated and/or expressed signaling proteins, as well as multiple mutated, chimeric, or overexpressed signaling proteins, which promote cancer cell growth or survival or both.
Len, Neckers, S Percy, Ivy
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Heat shock protein 90 (Hsp90) is a molecular chaperone required for the stability and function of a number of conditionally activated and/or expressed signaling proteins, as well as multiple mutated, chimeric, or overexpressed signaling proteins, which promote cancer cell growth or survival or both.
Len, Neckers, S Percy, Ivy
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The stress (heat shock) proteins
International Journal of Biochemistry, 1991When prokaryotic and eukaryotic cells are exposed to a variety of physiological stresses such as a nonlethal temperature (4&43”C) and heavy metals, the synthesis of most proteins is suppressed, but a small number of proteins are rapidly synthesized. This reaction is referred to as the “stress response” or “heat shock response” and the induced proteins ...
H, Itoh, Y, Tashima
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Heat Shock Proteins in Glioblastomas
Neurosurgery Clinics of North America, 2010Glioblastoma multiforme is the most common primary central nervous system tumor. The prognosis for these malignant brain tumors is poor, with a median survival of 14 months and a 5-year survival rate below 2%. Development of novel treatments is essential to improving survival and quality of life for these patients.
Isaac, Yang +2 more
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1990
The finding that tumor cells are more thermosensitive than their normal counterparts (1–4) prompted research on the effect of heat on normal and neoplastic cells. In 1970, the phenomenon of thermotolerance was described for the first time (5). Cells of L12l0 leukemia after being exposed to sublethal hyperthermia (52% of BDF1 mice survivors after ...
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The finding that tumor cells are more thermosensitive than their normal counterparts (1–4) prompted research on the effect of heat on normal and neoplastic cells. In 1970, the phenomenon of thermotolerance was described for the first time (5). Cells of L12l0 leukemia after being exposed to sublethal hyperthermia (52% of BDF1 mice survivors after ...
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Heat shock proteins in immunopathology
Current Biology, 1991In recent years, studies have suggested that autoimmunity and/or immunopathology may sometimes result from the immune response to heat shock proteins of autologous cells and microorganisms. Focusing on the T-cell mediated responses, we review the latest literature on this issue with regard to three hypothetical concepts of immunopathology in which heat
P C, Res, J E, Thole, R R, de Vries
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Heat shock proteins and psoriasis
European Journal of Dermatology, 2019Psoriasis is a chronic disfiguring skin condition which may be induced or exacerbated by stress. Heat shock proteins (HSPs), as molecular chaperones, play a central role in protein folding and cellular protein homeostasis. The many different functions of HSPs in the cell depend on the specific HSP involved.
Wen-Ming, Wang, Hong-Zhong, Jin
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Heat Shock Proteins and Diabetes
Canadian Journal of Diabetes, 2016Diabetes is a chronic disease, and its prevalence continues to rise and can increase the risk for the progression of microvascular (such as nephropathy, retinopathy and neuropathy) and also macrovascular complications. Diabetes is a condition in which the oxidative stress and inflammation rise.
Marzie, Zilaee, Saeed, Shirali
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Heat Shock Proteins and Cancer
Trends in Pharmacological Sciences, 2017Heat shock proteins (HSPs) constitute a large family of proteins involved in protein folding and maturation whose expression is induced by heat shock or other stressors. The major groups are classified based on their molecular weights and include HSP27, HSP40, HSP60, HSP70, HSP90, and large HSPs.
Jianming, Wu +5 more
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Heat Shock Proteins And Neuroprotection
Recent Patents on DNA & Gene Sequences, 2007Heat shock proteins (HSPs) (also known as stress proteins) protect the cells from damages caused due to different stresses like heat, injury, chemical induced toxicity, etc. Some HSPs can act as molecular chaperones to help in correct folding of proteins or directing misfolded proteins for degradation.
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Heat Shock Proteins and Alcohol
2005In response to many metabolic disturbances and injuries, the cells mount a stress response with the induction of a variety of proteins, most notably the 70 kDa family of heat shock proteins. Included in this family are hsp70 (the inducible form), hsc70 (heat shock cognate, the constitutive form) and grp78 (the constitutively expressed glucoseregulated ...
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