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  • Author: Stromer T
  • References

Author: Stromer T


References 10 references


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  • Haslbeck M, et al. (2020) Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae. EMBO J 39(12):e105112 PMID:32548883
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  • Slotta U, et al. (2007) Spider silk and amyloid fibrils: a structural comparison. Macromol Biosci 7(2):183-8 PMID:17295405
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  • Ranson N, et al. (2006) Insights into the architecture of the Ure2p yeast protein assemblies from helical twisted fibrils. Protein Sci 15(11):2481-7 PMID:17001037
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  • White HE, et al. (2006) Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26. Structure 14(7):1197-204 PMID:16843901
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  • Haslbeck M, et al. (2005) Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104. J Biol Chem 280(25):23861-8 PMID:15843375
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  • Haslbeck M, et al. (2004) A domain in the N-terminal part of Hsp26 is essential for chaperone function and oligomerization. J Mol Biol 343(2):445-55 PMID:15451672
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  • Haslbeck M, et al. (2004) Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae. EMBO J 23(3):638-49 PMID:14749732
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  • Stromer T, et al. (2004) Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation: the N-terminal domail is important for oligomer assembly and the binding of unfolding proteins. J Biol Chem 279(12):11222-8 PMID:14722093
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  • Stromer T, et al. (2003) Analysis of the interaction of small heat shock proteins with unfolding proteins. J Biol Chem 278(20):18015-21 PMID:12637495
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  • Haslbeck M, et al. (1999) Hsp26: a temperature-regulated chaperone. EMBO J 18(23):6744-51 PMID:10581247
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