Transient Interaction of Hsp90 with Early Unfolding Intermediates of Citrate Synthase
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J. Buchner | H. Lilie | U. Jakob | I. Meyer
[1] J. Buchner,et al. Hsp90 chaperones protein folding in vitro , 1992, Nature.
[2] R. Jove,et al. Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system. , 1993, The Journal of biological chemistry.
[3] N. C. Price,et al. The unfolding and attempted refolding of citrate synthase from pig heart. , 1990, Biochimica et biophysica acta.
[4] M. Gaestel,et al. Small heat shock proteins are molecular chaperones. , 1993, The Journal of biological chemistry.
[5] P. Srere,et al. Conformational stability of pig citrate synthase and some active-site mutants. , 1991, Biochemistry.
[6] W. Pratt. The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor. , 1993, The Journal of biological chemistry.
[7] F. Hartl,et al. Molecular chaperone functions of heat-shock proteins. , 1993, Annual review of biochemistry.
[8] S. Lindquist. Varying patterns of protein synthesis in Drosophila during heat shock: implications for regulation. , 1980, Developmental biology.
[9] R. Huber,et al. Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution. , 1984, Journal of molecular biology.
[10] D. Kohtz,et al. Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84) , 1992, Molecular and cellular biology.
[11] K. Suzuki,et al. The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo , 1994, Molecular and cellular biology.
[12] H. Pelham. Hsp70 accelerates the recovery of nucleolar morphology after heat shock. , 1984, The EMBO journal.
[13] R. Hurst,et al. ATP-dependent chaperoning activity of reticulocyte lysate. , 1994, The Journal of biological chemistry.
[14] R. Jaenicke,et al. Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation. , 1979, Biochemistry.
[15] Y. Argon,et al. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum , 1994, Nature.
[16] J. Buchner,et al. Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones. , 1994, Trends in biochemical sciences.
[17] P. Srere. Citrate-condensing enzyme-oxalacetate binary complex. Studies on its physical and chemical properties. , 1966, The Journal of biological chemistry.
[18] R. Jaenicke,et al. Folding and association of proteins. , 1982, Biophysics of structure and mechanism.
[19] S. Lindquist,et al. Heat-shock protein hsp90 governs the activity of pp60v-src kinase. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[20] E. Gabellieri,et al. Heterogeneity of protein conformation in solution from the lifetime of tryptophan phosphorescence. , 1994, Biophysical chemistry.
[21] M. Kashlev,et al. Protein aggregation and inclusion body formation in Escherichia coli rpoH mutant defective in heat shock protein induction , 1991, FEBS letters.
[22] Y. Miyata,et al. The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity. , 1992, The Journal of biological chemistry.
[23] J. Buchner,et al. Hsc70, immunoglobulin heavy chain binding protein, and Hsp90 differ in their ability to stimulate transport of precursor proteins into mammalian microsomes. , 1993, The Journal of biological chemistry.
[24] S. Lindquist,et al. The heat-shock proteins. , 1988, Annual review of genetics.
[25] M. Morange,et al. Protein denaturation during heat shock and related stress. Escherichia coli beta-galactosidase and Photinus pyralis luciferase inactivation in mouse cells. , 1989, The Journal of biological chemistry.
[26] P. Srere,et al. The Citrate Condensing Enzyme of Pigeon Breast Muscle and Moth Flight Muscle. , 1963 .
[27] D. Wetlaufer,et al. Ultraviolet spectra Of Proteins and Amino Acids , 1963 .
[28] D. Kohtz,et al. Structural and functional aspects of basic helix-loop-helix protein folding by heat-shock protein 90. , 1994, The Journal of biological chemistry.
[29] M. M. Bradford. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.
[30] E. Garaci,et al. Stress Proteins: Induction and Function , 1991 .
[31] G. Lorimer,et al. Chaperonin cpn60 from Escherichia coli protects the mitochondrial enzyme rhodanese against heat inactivation and supports folding at elevated temperatures. , 1992, The Journal of biological chemistry.
[32] M. Welsh,et al. Evidence that the 90-kilodalton heat shock protein is associated with tubulin-containing complexes in L cell cytosol and in intact PtK cells. , 1988, Molecular endocrinology.
[33] J Deisenhofer,et al. Crystal structure analysis and molecular model of a complex of citrate synthase with oxaloacetate and S-acetonyl-coenzyme A. , 1984, Journal of molecular biology.