Titlebook: HSP70 in Human Diseases and Disorders; Alexzander A. A. Asea,Punit Kaur Book 2018 Springer International Publishing AG, part of Springer N

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Umesh Hodeghatta Rao,Umesha Nayakeat shock or other stressors. The major groups, which are classified based on their molecular weight, include HSP27, HSP40, HSP60, HSP70, HSP90, and large HSP (HSP110 and glucose-regulated protein 170). The human HSP70 family is consists of 13 members and five of them have a strong association with

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https://doi.org/10.1057/9780230113992ular one constitutively expressed member (Hsc70) and another one inducibly expressed under several stress conditions (Hsp70). To date, the intracellular functions of Hsp70 are well defined, and increasing evidences establish its roles in the extracellular environment, such as cytoprotection and immu

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pecially the capacity (i) to induce the presentation and cross-presentation of associated or client proteins and, (ii) to control myeloid cell activation. Several studies were focused on the identification of HSP70-binding elements that contribute to their immune properties. A general consensus was

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https://doi.org/10.1007/3-540-33156-5he surrounding aqueous cytoplasm or nucleoplasm through a process known as liquid-liquid phase separation. In healthy cells, ribonucleoprotein (RNP) granules are highly dynamic compartments. In contrast, in aging cells or due to environmental stresses or genetic mutations, RNP granules, in particula

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https://doi.org/10.1007/978-3-642-48423-0ressors including heat, oxidative and chemical stress. Expression of HSP helps in numerous reparative processes including the refolding of damaged proteins and removal of irreparably damaged proteins that would accumulate and initiate cellular death or apoptosis. A growing body of evidence in recent

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