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The heat shock response: life on the verge of death.
This Review summarizes the concepts of the protective Hsp network, and the most conserved Hsps are molecular chaperones that prevent the formation of nonspecific protein aggregates and assist proteins in the acquisition of their native structures. Expand
Some like it hot: the structure and function of small heat-shock proteins
Small heat-shock proteins are a widespread and diverse class of molecular chaperones that maintain protein homeostasis by binding proteins in non-native conformations, thereby preventing substrate aggregation. Expand
Hsp26: a temperature‐regulated chaperone
The temperature‐dependent dissociation of the large storage form of Hsp26 into a smaller, active species and the subsequent re‐association to a defined large chaperone–substrate complex represents a novel mechanism for the functional activation of a molecular chaperones. Expand
A first line of stress defense: small heat shock proteins and their function in protein homeostasis.
Small heat shock proteins (sHsps) are virtually ubiquitous molecular chaperones that can prevent the irreversible aggregation of denaturing proteins and have evolved independently in metazoans, plants and fungi. Expand
Sti1 Is a Novel Activator of the Ssa Proteins*
Analysis of the underlying activation mechanism revealed that ATP hydrolysis is rate-limiting in the Ssa1 ATPase cycle and that this step is accelerated by Sti1, a potent novel effector for the Hsp70 ATPase. Expand
Multiple molecular architectures of the eye lens chaperone αB-crystallin elucidated by a triple hybrid approach
This work presents a pseudoatomic model of a 24-meric αB-crystallin assembly obtained by a triple hybrid approach combining data from cryoelectron microscopy, NMR spectroscopy, and structural modeling, and explains how “heterogeneity” is achieved by a small set of defined structural variations. Expand
Factors masking HMGB1 in human serum and plasma
Sensitive ELISAs for the detection of high mobility group box 1 protein in cell culture medium and cell lysates are described, but these assays failed to reliably quantitate HMGB1 in serum and plasma when compared with immunoblot analysis. Expand
sHsps and their role in the chaperone network
  • M. Haslbeck
  • Biology, Medicine
  • Cellular and Molecular Life Sciences CMLS
  • 1 October 2002
In some cases, the release of substrate proteins from the sHsp complex is achieved in cooperation with Hsp70 in an ATP-dependent reaction, suggesting that the role of sHsps in the network of chaperones is to create a reservoir of nonnative refoldable protein. Expand
Elucidation of the Final Reactions of DIMBOA-Glucoside Biosynthesis in Maize: Characterization of Bx6 and Bx71[W][OA]
The localization studies indicate a cytoplasmic localization of the dioxygenase in Bx6 and Bx7, which are highest expressed in seedling tissue and have no close relatives among the members of their respective gene families. Expand
Independent evolution of the core domain and its flanking sequences in small heat shock proteins
Analysis of 8714 sHsps revealed a broad variation of primary sequences within the superfamily as well as phyla‐dependent differences, and Reconstruction of the evolutionary tree for the sHsp superfamily shows that the flanking regions fall into several subgroups, indicating that they were remodeled several times in parallel but independent of the evolution of the α‐crystallin domain. Expand