The Hsp90 family of proteins in Arabidopsis thaliana

[1]  S. Hill,et al.  Cold-Induced Accumulation of hsp90 Transcripts in Brassica napus , 1995, Plant physiology.

[2]  D. Toft Recent Advances in the Study of hsp90 Structure and Mechanism of Action , 1998, Trends in Endocrinology & Metabolism.

[3]  K. Marrs,et al.  Characterization of two maize HSP90 heat shock protein genes: expression during heat shock, embryogenesis, and pollen development. , 1993, Developmental genetics.

[4]  P. Csermely,et al.  Associate Editor: D. Shugar The 90-kDa Molecular Chaperone Family: Structure, Function, and Clinical Applications. A Comprehensive Review , 1998 .

[5]  N Yabe,et al.  Analysis of tissue-specific expression of Arabidopsis thaliana HSP90-family gene HSP81. , 1994, Plant & cell physiology.

[6]  G. Britton,et al.  Isolation and analysis , 1995 .

[7]  The Arabidopsis Genome Initiative Analysis of the genome sequence of the flowering plant Arabidopsis thaliana , 2000, Nature.

[8]  J. Chory,et al.  Brassinosteroid signal transduction: still casting the actors. , 2000, Current opinion in plant biology.

[9]  K. Nakai,et al.  PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization. , 1999, Trends in biochemical sciences.

[10]  J. Chory,et al.  Weaving the complex web of signal transduction. , 2001, Plant physiology.

[11]  I. Kurek,et al.  High-molecular-weight FK506-binding proteins are components of heat-shock protein 90 heterocomplexes in wheat germ lysate. , 1998, Plant physiology.

[12]  D. Donner,et al.  The hsp90-related Protein TRAP1 Is a Mitochondrial Protein with Distinct Functional Properties* , 2000, The Journal of Biological Chemistry.

[13]  M S Waterman,et al.  Identification of common molecular subsequences. , 1981, Journal of molecular biology.

[14]  T. Colangelo,et al.  Heat-Induced Expression and Chemically Induced Expression of the Escherichia coli Stress Protein HtpG Are Affected by the Growth Environment , 1999, Applied and Environmental Microbiology.

[15]  S. Henikoff,et al.  Amino acid substitution matrices from protein blocks. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[16]  W. Pratt,et al.  Animal and plant cell lysates share a conserved chaperone system that assembles the glucocorticoid receptor into a functional heterocomplex with hsp90. , 1996, Biochemistry.

[17]  R. Reddy,et al.  The 90 kDa heat shock protein (hsp90) is expressed throughout Brassica napus seed development and germination , 1998 .

[18]  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.

[19]  Neal Rosen,et al.  Crystal Structure of an Hsp90–Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor Agent , 1997, Cell.

[20]  C. Lamb,et al.  Perception of brassinosteroids by the extracellular domain of the receptor kinase BRI1. , 2000, Science.

[21]  M. Delseny,et al.  Genomic analysis of the Hsp70 superfamily in Arabidopsis thaliana , 2001, Cell stress & chaperones.

[22]  S. Henikoff,et al.  Amino acid substitution matrices. , 2000, Advances in protein chemistry.

[23]  J. Wootton,et al.  Analysis of compositionally biased regions in sequence databases. , 1996, Methods in enzymology.

[24]  E. Baulieu,et al.  Selective deletions in the 90 kDa heat shock protein (hsp90) impede hetero-oligomeric complex formation with the glucocorticosteroid receptor (GR) or hormone binding by GR , 1994, The Journal of Steroid Biochemistry and Molecular Biology.

[25]  J. Miernyk The J-domain proteins of Arabidopsis thaliana: an unexpectedly large and diverse family of chaperones , 2001, Cell stress & chaperones.

[26]  L. Pearl,et al.  Structure and in vivo function of Hsp90. , 2000, Current opinion in structural biology.

[27]  S. Naito,et al.  Isolation and analysis of the expression of two genes for the 81-kilodalton heat-shock proteins from Arabidopsis. , 1992, Plant physiology.

[28]  J. J. Dougherty,et al.  Identification of the 90 kDa substrate of rat liver type II casein kinase with the heat shock protein which binds steroid receptors. , 1987, Biochimica et biophysica acta.

[29]  U. Dechert,et al.  A protein kinase isolated from porcine brain microvessels is similar to a class of heat-shock proteins. , 1994, European journal of biochemistry.

[30]  W. Pearson Effective protein sequence comparison. , 1996, Methods in enzymology.

[31]  G. Thompson,et al.  Orthologs in Arabidopsis thaliana of the Hsp70 interacting protein Hip , 2001, Cell stress & chaperones.

[32]  L. Comai,et al.  Developmental expression of tomato heat-shock cognate protein 80. , 1992, Plant physiology.

[33]  S. Brunak,et al.  Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. , 2000, Journal of molecular biology.

[34]  J. Buchner,et al.  Hsp90 & Co. - a holding for folding. , 1999, Trends in biochemical sciences.

[35]  D. Picard,et al.  Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[36]  R. T. Nagao,et al.  Sequence and Expression of a HSP83 from Arabidopsis thaliana. , 1990, Plant physiology.

[37]  P Vincens,et al.  Computational method to predict mitochondrially imported proteins and their targeting sequences. , 1996, European journal of biochemistry.

[38]  S. Clouse Brassinosteroid signal transduction: clarifying the pathway from ligand perception to gene expression. , 2002, Molecular cell.

[39]  S. Lindquist,et al.  Hsp90 as a capacitor for morphological evolution , 1998, Nature.

[40]  L. Pearl,et al.  ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo , 1998, The EMBO journal.

[41]  M. Sacco,et al.  Effects of 24‐epibrassinolide on freezing and thermotolerance of bromegrass (Bromus inermis) cell cultures , 1995 .

[42]  W. Pratt,et al.  Binding of immunophilins to the 90 kDa heat shock protein (hsp90) via a tetratricopeptide repeat domain is a conserved protein interaction in plants. , 1996, Biochemistry.

[43]  R. Felsheim,et al.  Structure and Expression of a Heat-Shock Protein 83 Gene of Pharbitis nil. , 1992, Plant physiology.

[44]  S. Lindquist,et al.  The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. , 1993, Annual review of genetics.

[45]  A. Galat Sequence diversification of the FK506-binding proteins in several different genomes. , 2000, European journal of biochemistry.