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Shock, Hemorrhagic: Acute hemorrhage or excessive fluid loss resulting in HYPOVOLEMIA.Shock, Septic: Sepsis associated with HYPOTENSION or hypoperfusion despite adequate fluid resuscitation. Perfusion abnormalities may include, but are not limited to LACTIC ACIDOSIS; OLIGURIA; or acute alteration in mental status.Shock: A pathological condition manifested by failure to perfuse or oxygenate vital organs.Heat-Shock Proteins: Proteins which are synthesized in eukaryotic organisms and bacteria in response to hyperthermia and other environmental stresses. They increase thermal tolerance and perform functions essential to cell survival under these conditions.Shock, Cardiogenic: Shock resulting from diminution of cardiac output in heart disease.Shock, Traumatic: Shock produced as a result of trauma.HSP70 Heat-Shock Proteins: A class of MOLECULAR CHAPERONES found in both prokaryotes and in several compartments of eukaryotic cells. These proteins can interact with polypeptides during a variety of assembly processes in such a way as to prevent the formation of nonfunctional structures.Heat-Shock Response: A constellation of responses that occur when an organism is exposed to excessive heat. Responses include synthesis of new proteins and regulation of others.High-Energy Shock Waves: High-amplitude compression waves, across which density, pressure, and particle velocity change drastically. The mechanical force from these shock waves can be used for mechanically disrupting tissues and deposits.Hot Temperature: Presence of warmth or heat or a temperature notably higher than an accustomed norm.HSP90 Heat-Shock Proteins: A class of MOLECULAR CHAPERONES whose members act in the mechanism of SIGNAL TRANSDUCTION by STEROID RECEPTORS.HSP27 Heat-Shock Proteins: A subfamily of small heat-shock proteins that function as molecular chaperones that aid in refolding of non-native proteins. They play a protective role that increases cellular survival during times of stress.Chaperonin 60: A group I chaperonin protein that forms the barrel-like structure of the chaperonin complex. It is an oligomeric protein with a distinctive structure of fourteen subunits, arranged in two rings of seven subunits each. The protein was originally studied in BACTERIA where it is commonly referred to as GroEL protein.HSP72 Heat-Shock Proteins: Stress-inducible members of the heat-shock proteins 70 family. HSP72 heat shock proteins function with other MOLECULAR CHAPERONES to mediate PROTEIN FOLDING and to stabilize pre-existent proteins against aggregation.Electroshock: Induction of a stress reaction in experimental subjects by means of an electrical shock; applies to either convulsive or non-convulsive states.Resuscitation: The restoration to life or consciousness of one apparently dead. (Dorland, 27th ed)