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Hsp26: a temperature‐regulated chaperone
TLDR
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
Analysis of the Interaction of Small Heat Shock Proteins with Unfolding Proteins*
TLDR
The formation of large uniform sHsp-substrate complexes seems to be a general feature of sHsps, and this unique chaperone mechanism is conserved from yeast to mammals. Expand
Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae
TLDR
Hsp42 is defined as an important player for protein homeostasis at physiological and under stress conditions and indicates a general protective function of sHsps for proteome stability in S. cerevisiae. Expand
Disassembling Protein Aggregates in the Yeast Cytosol
TLDR
It is shown that recovery of proteins from aggregates in the cell requires the chaperones to work together with defined but overlapping functions, and the results are consistent with a model of several interrelated defense lines against protein aggregation. Expand
Structure and morphology of the Alzheimer's amyloid fibril
TLDR
In combination with other techniques, including X‐ray fiber diffraction and solid state NMR, electron microscopy has revealed that the internal structure of the amyloid fibril is a ladder of β‐sheet structure arranged in a cross‐β conformation. Expand
A pancreas-specific glycosylated protein disulphide-isomerase binds to misfolded proteins and peptides with an interaction inhibited by oestrogens.
Using a cross-linking approach, we have demonstrated that radiolabeled model peptides or misfolded proteins specifically interact in vitro with two different luminal proteins in a crude extract fromExpand
Analysis of the Regulation of the Molecular Chaperone Hsp26 by Temperature-induced Dissociation
TLDR
The findings suggest that the quaternary structure of Hsp26 is determined by two elements, (i) weak, regulatory interactions required to form the shell of 24 subunits and (ii) a strong and stable dimerization of the C-terminal domain. Expand
A domain in the N-terminal part of Hsp26 is essential for chaperone function and oligomerization.
TLDR
The results suggest that the N-terminal segment of Hsp26 is involved in both, oligomerization and chaperone function and that the second part of the N.terminal region (amino acid residues 31-95) is essential for both functions. Expand
Spider silk and amyloid fibrils: a structural comparison.
TLDR
Recombinantly produced spider silk also self-assembles into nanofibrils, and these have been compared to amyloid-like fibrils to highlight structural similarities. Expand
Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26.
TLDR
Cryo-electron microscopy of yeast Hsp26 reveals two distinct forms, each comprising 24 subunits arranged in a porous shell with tetrahedral symmetry, providing the flexibility required for formation of supercomplexes with non-native proteins. Expand
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