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Giese, K.C., E. Basha, B.Y. Catague, and E. Vierling. 2005. Evidence for an essential function of the N terminus of a small heat shock protein in vivo, independent of in vitro chaperone activity. Proceedings of the National Academy of Sciences U.S.A. 102: 18896-18901.
Larkindale, J., J.D. Hall, M.R. Knight, and E. Vierling. 2005. Heat stress phenotypes of Arabidopsis mutants implicate multiple signaling pathways in the acquisition of thermotolerance. Plant Physiology 138: 882-897.
Lee, U., C. Wie, M. Escobar, B. Williams, S.W. Hong, and E. Vierling. 2005. Genetic analysis reveals domain interactions of Arabidopsis Hsp100/ClpB and cooperation with the small heat shock protein chaperone system. The Plant Cell 17: 559-571.
Giese, K.C., and E. Vierling. 2004. Mutants in a small heat shock protein that affect the oligomeric state. Analysis and allele-specific suppression. Journal of Biological Chemistry 279: 32674-32683.
Basha, E., G.J. Lee, B. Demeler, and E. Vierling. 2004. Chaperone activity of cytosolic small heat shock proteins from wheat. European Journal of Biochemistry 271: 1426-1436.
Basha, E., G.J. Lee, L.A. Breci, A.C. Hausrath, N.R. Buan, K.C. Giese, and E. Vierling. 2004. 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. Journal of Biological Chemistry 279: 7566-7575.
Friedrich, K.L., K.C. Giese, N.R. Buan, and E. Vierling. 2004. Interactions between small heat shock protein subunits and substrate in small heat shock protein-substrate complexes. Journal of Biological Chemistry 279: 1080-1089.
Liu, Z., S.W. Hong, M. Escobar, E. Vierling, D.L. Mitchell, D.W. Mount, and J.D. Hall. 2003. Arabidopsis UVH6, a homolog of human XPD and yeast RAD3 DNA repair genes, functions in DNA repair and is essential for plant growth. Plant Physiology 132: 1405-1414.
Hong, S.W., U. Lee, and E. Vierling. 2003. Arabidopsis hot mutants define multiple functions required for acclimation to high temperatures. Plant Physiology 132: 757-767.
Giese, K.C., E. Vierling. 2002. Changes in oligomerization are essential for the chaperone activity of a small heat shock protein in vivo and in vitro. Journal of Biological Chemistry 277: 46310-46318.
Van Montfort, R., C. Slingsby, and E. Vierling. 2001. Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones. Advances in Protein Chemistry 59: 105-56.
Van Montfort, R., E. Basha, K.L. Friedrich, C. Slingsby, and E. Vierling. 2001. Crystal structure and assembly of a eukaryotic small heat shock protein. Nature Structural Biology 8: 1025-1030
Hong, S.-W., and E.Vierling. 2001. Hsp101 is necessary for heat tolerance but dispensable for development and germination in the absence of stress. Plant Journal 27: 25-35.
chaperones in higher plants (including Arabidopsis) and the model single-celled organisms, the cyanobacterium Synechocystis. Molecular chaperones are proteins that bind to other proteins that are in unstable structural states. They thereby facilitate many cellular processes, including folding of substrates, transport of proteins across membranes, modulation of protein activity, and prevention of irreversible protein aggregation. We are interested in the roles of chaperones in the survival of plants and other organisms during stress (particularly high temperature) and also during normal development. Research approaches include 
chaperones. We propose that sHSPs bind to denatured proteins and maintain them in a form competent for reactivation/refolding by other cellular components. The structural basis of this activity is being tested by site-directed mutation, and genetic 
