A domain in the N-terminal part of Hsp26 is essential for chaperone function and oligomerization. Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation - The N-terminal domain is important for oligomer assembly and the binding of unfolding proteins. Stromer, T., Fischer, E., Richter, K., Haslbeck, M. Formation of cytoplasmic heat shock granules in tomato cell cultures and leaves. Chaperone activity of cytosolic small heat shock proteins from wheat. Analysis of the interaction of small heat shock proteins with unfolding proteins. Stromer, T., Ehrnsperger, M., Gaestel, M. The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. Purification and characterization of the 16-kDa heat-shock-responsive protein from the thermophilic cyanobacterium Synechococcus vulcanus, which is an alpha-crystallin-related, small heat shock protein. Chaperone activity and homo- and hetero-oligomer formation of bacterial small heat shock proteins. Small heat shock proteins are molecular chaperones. Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin. Hsp26 is not required for growth at high temperatures, nor for thermotolerance, spore development, or germination. The IXI/V motif in the C-terminal extension of alpha-crystallins: alternative interactions and oligomeric assemblies. Small heat shock proteins: dynamic players in the folding game. Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae. The small heat shock proteins of the nematode Caenorhabditis elegans: structure, regulation and biology. Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones. The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure. Crystal structure and assembly of a eukaryotic small heat shock protein. Van Montfort, R.L., Basha, E., Friedrich, K.L., Slingsby, C. Hsp26: a temperature-regulated chaperone. Dodecameric structure of the small heat shock protein ACR1 from mycobacterium tuberculosis. Crystal structure of a small heat-shock protein. ![]() Protection of neuronal and cardiac cells by HSP27. Small heat-shock proteins and their potential role in human disease. Regulation of aging and age-related disease by DAF-16 and heat-shock factor. The molecular chaperone alphaB-crystallin enhances amyloid beta neurotoxicity. Targeted disruption of the mouse alpha A-crystallin gene induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein alpha B-crystallin. Alpha-crystallin can function as a molecular chaperone. Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli. Small heat shock proteins from extremophiles: a review. Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network. Evolution, structure and function of the small heat shock proteins in plants. Evolution and diversity of prokaryotic small heat shock proteins.
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