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Geldanamycin as a potential anti-cancer agent: its molecular target and biochemical activity

author

Edward G Mimnaugh

Len Neckers

Theodor W Schulte

published in: Investigational New Drugs

date of publication: 1999-01-01

Cites articles 112

Date

Title

Authors

1999-01-01

The benzoquinone ansamycin geldanamycin stimulates proteolytic degradation of focal adhesion kinase

Len Neckers, Jane B Trepel, Theodor W Schulte
1999-02-01

Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones

Chrisostomos Prodromou
1999-01-28

Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin

Chrisostomos Prodromou
1999-03-01

Benzoquinoid ansamycins (herbimycin A and geldanamycin) interfere with the maturation of growth factor receptor tyrosine kinases
1998-08

The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review,The 90-kDa Molecular Chaperone Family
1998-05

Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol
1998-06

Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin

Len Neckers, Theodor W Schulte
1998-01-01

The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin

Len Neckers, Theodor W Schulte
1998-08-01

ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo

Chrisostomos Prodromou
1998-08-01

Recent Advances in the Study of hsp90 Structure and Mechanism of Action
1998-12-01

Molecular chaperones: biology and prospects for pharmacological intervention
1998-02-01

Hop modulates Hsp70/Hsp90 interactions in protein folding

Eric D. Ross
1997-07-01

ATP-binding properties of human Hsp90.
1997-04-01

The heat shock protein 83 (Hsp83) is required for Raf-mediated signalling in Drosophila
1997-03-01

Nucleotides and two functional states of hsp90
1997-07-15

Cdc37 is a molecular chaperone with specific functions in signal transduction
1997-03-27

An atypical topoisomerase II from Archaea with implications for meiotic recombination
1997-04-18

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

Franz-Ulrich Hartl
1997-02

Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor
1997-01-01

Depletion of p185erbB2, Raf-1 and mutant p53 proteins by geldanamycin derivatives correlates with antiproliferative activity

Mikhail Blagosklonny, Len Neckers
1997-06-01

Geldanamycin-stimulated destabilization of mutated p53 is mediated by the proteasome in vivo

Mikhail Blagosklonny, Len Neckers, Theodor W Schulte
1997-02-01

The hsp90-binding antibiotic geldanamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Raf kinase
1997-07-01

Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

Chrisostomos Prodromou, John E. Ladbury
1997-04-24

Interaction between Cdc37 and Cdk4 in human cells
1997-09-19

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

Len Neckers, Edward G Mimnaugh, Theodor W Schulte
1997-05-01

Selective interaction of hsp90 with an estrogen receptor ligand-binding domain containing a point mutation

John H. White
1997-02-01

Interaction of endoplasmic reticulum chaperone GRP94 with peptide substrates is adenine nucleotide-independent

Pamela A. Wearsch
1997-01

In vivo analysis of the Hsp90 cochaperone Sti1 (p60)
1997-06

A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone

Chrisostomos Prodromou
1997-04

The complexity of Raf-1 regulation
1997-10-01

Geldanamycin-induced destabilization of Raf-1 involves the proteasome

Len Neckers, Theodor W Schulte
1996-06-15

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

Article - wd:Q33888219

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