(Q28280296)

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William H Piel

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Liming Gui

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Antónia Monteiro

The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review

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language of work or name

English

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publication date

December 2005

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published in

Genomics

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volume

86

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issue

6

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page(s)

627-37

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cites work

1 reference

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Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones

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Hsp90 as a capacitor for morphological evolution

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Hsp90 isoforms: functions, expression and clinical importance

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The Hsp90 family of proteins in Arabidopsis thaliana

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Evolutionary origins of Hsp90 chaperones and a deep paralogy in their bacterial ancestors

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Nucleotide sequence of a cDNA for a member of the human 90-kDa heat-shock protein family

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Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related genes encode formerly identified tumour-specific transplantation antigens

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HSP 90 alpha and HSP 90 beta genes are present in the zebrafish and are differentially regulated in developing embryos.

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The role of Hsp90N, a new member of the Hsp90 family, in signal transduction and neoplastic transformation

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Phylogenetic relationships of organellar Hsp90 homologs reveal fundamental differences to organellar Hsp70 and Hsp60 evolution

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Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor

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A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock

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Mapping of the gene family for human heat-shock protein 90α to chromosomes 1, 4, 11, and 14

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Assignment of an Intron-Containing Human Heat-Shock Protein Gene (hsp90β, HSPCB) to Chromosome 6 near TCTE1 (6p21) and Two Intronless Pseudogenes to Chromosomes 4 and 15 by Polymerase Chain Reaction Amplification from a Panel of Hybrid Cell Lines

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Mapping of the genes for human endoplasmic reticular heat shock protein gp96/grp94

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In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis

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Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent

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Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions

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Hsp90 chaperone activity requires the full-length protein and interaction among its multiple domains

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The heat-shock response

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Invited review: Effects of heat and cold stress on mammalian gene expression

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RNA splicing is interrupted by heat shock and is rescued by heat shock protein synthesis.

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Integrative annotation of 21,037 human genes validated by full-length cDNA clones

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Initial sequencing and analysis of the human genome

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Biochemical, cell biological and immunological issues surrounding the endoplasmic reticulum chaperone GRP94/gp96.

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Immunotherapy of tumors with autologous tumor-derived heat shock protein preparations

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Glucose-regulated protein (GRP94 and GRP78) genes share common regulatory domains and are coordinately regulated by common trans-acting factors

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Differential interactions of p23 and the TPR-containing proteins Hop, Cyp40, FKBP52 and FKBP51 with Hsp90 mutants

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Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90

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Unique behavior of a dictyostelium homologue of TRAP-1, coupling with differentiation of D. discoideum cells

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Evolution by gene duplication: an update

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Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

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The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools

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Finding the genes in genomic DNA.

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Evaluation of gene structure prediction programs.

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Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites

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Improved prediction of signal peptides: SignalP 3.0

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Recent improvements to the PROSITE database

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InterProScan--an integration platform for the signature-recognition methods in InterPro

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The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation

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