(Q27739168)

1

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author name string

S M Roe

2

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P W Piper

3

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L H Pearl

Nature structural biology

4

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publication date

June 1997

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published in

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volume

4

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page(s)

477-82

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issue

6

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cites work

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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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Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell

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The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo

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Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent

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Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70

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Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase

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Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84)

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Common non-hormone binding component in non-transformed chick oviduct receptors of four steroid hormones

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A cellular protein that associates with the transforming protein of Rous sarcoma virus is also a heat-shock protein

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Purification of a novel calcium-independent phospholipase A2 from rabbit kidney

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Chaperone function of Hsp90-associated proteins

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Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23

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Expression and crystallization of the yeast Hsp82 chaperone, and preliminary x‐ray diffraction studies of the amino‐terminal domain

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3D domain swapping: a mechanism for oligomer assembly

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Direct stoichiometric evidence that the untransformed Mr 300,000, 9S, glucocorticoid receptor is a core unit derived from a larger heteromeric complex

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Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways

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The 56-59-kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70- and 90-kilodalton heat shock proteins

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Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4

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Interaction of the Rous sarcoma virus protein pp60src with the cellular proteins pp50 and pp90.

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Interaction between casein kinase II and the 90-kDa stress protein, HSP90

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Cyclophilin 40 (CyP-40), mapping of its hsp90 binding domain and evidence that FKBP52 competes with CyP-40 for hsp90 binding

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A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains

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The ability of the immunophilin FKBP59-HBI to interact with the 90-kDa heat shock protein is encoded by its tetratricopeptide repeat domain

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A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis

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Snap helix with knob and hole: essential repeats in S. pombe nuclear protein nuc2+

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Structural analysis of substrate binding by the molecular chaperone DnaK

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Identifiers

DOI

10.1038/NSB0697-477

1 reference

Consolidated OpenCitations Corpus – April 2017

4772628

4772628

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference