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Structural and functional similarities of bovine alpha-crystallin and mouse small heat-shock protein. A family of chaperones.
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Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea.
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Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.
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Protease activity of CND41, a chloroplast nucleoid DNA-binding protein, isolated from cultured tobacco cells.
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The molecular evolution of the small heat-shock proteins in plants.
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The immunoglobulin heavy-chain matrix-associating regions are bound by Bright: a B cell-specific trans-activator that describes a new DNA-binding protein family.
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Multimerization of Hsp42p, a novel heat shock protein of Saccharomyces cerevisiae, is dependent on a conserved carboxyl-terminal sequence.
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Synthesis of small heat-shock proteins is part of the developmental program of late seed maturation.
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Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin.
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Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.
EMBO J. 1997 Jan 15;16(2):221-9
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A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state.
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