2015
DOI: 10.1007/978-3-319-16077-1
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The Big Book on Small Heat Shock Proteins

Abstract: Heat Shock Proteins: key mediators of Health and Disease. Heat shock proteins (HSP) are essential molecules conserved through cellular evolution required for cells to survive the stresses encountered in the environment and in the tissues of the developing and aging organism. These proteins play the essential roles in stress of preventing the initiation of programmed cell death and repairing damage to the proteome permitting resumption of normal metabolism. Loss of the HSP is lethal either in the short-term in … Show more

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Cited by 22 publications
(12 citation statements)
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References 782 publications
(1,257 reference statements)
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“…Small heat-shock proteins (sHsps) 5 are a class of ATP-independent chaperones, expressed across all kingdoms of life, that are proposed to act as a cell's "first-responders" under stress conditions (1)(2)(3)(4)(5)(6). Mutations or misexpression of specific human sHsps are associated with myopathies, neuropathies, and cancers (1,(7)(8)(9).…”
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confidence: 99%
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“…Small heat-shock proteins (sHsps) 5 are a class of ATP-independent chaperones, expressed across all kingdoms of life, that are proposed to act as a cell's "first-responders" under stress conditions (1)(2)(3)(4)(5)(6). Mutations or misexpression of specific human sHsps are associated with myopathies, neuropathies, and cancers (1,(7)(8)(9).…”
mentioning
confidence: 99%
“…sHsps are characterized by a 90 -amino acid, ␤-sheet-rich ␣-crystallin domain (ACD, or Hsp20 domain, PF00011), flanked by sequences of variable length and composition (N-terminal (NT) sequence; C-terminal (CT) sequence) (11,12). The majority form large oligomers containing 12 to Ͼ40 units, with a dimeric substructure (1,3,5), although there are a few dimeric sHsps, some of which are active chaperones (5,(13)(14)(15). Although vertebrate sHsps assemble principally as polydisperse oligomers, some bacterial, yeast, and plant sHsps are monodisperse.…”
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confidence: 99%
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“…Our results provide a mechanistic basis for the impact of the P182L mutation on HSP27, and highlight the general importance of the IxI/V motif and its role in protein-protein interaction networks. Introduction HSP27 (HSPB1) is a systemically expressed human small heat-shock protein (sHSP) that performs diverse functions under basal and stressful cellular conditions (1)(2)(3). With significant roles in the maintenance of protein homeostasis, regulation of the redox environment, prevention of apoptosis, and stabilization of the cytoskeletal network, the biological activity of HSP27 is critical to overall cellular health (4)(5)(6)(7)(8).…”
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confidence: 99%