Page last updated: 2024-08-17

adenosine diphosphate and geldanamycin

adenosine diphosphate has been researched along with geldanamycin in 12 studies

Research

Studies (12)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's4 (33.33)18.2507
2000's4 (33.33)29.6817
2010's4 (33.33)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Chiosis, G; Evans, CE; Gewirth, D; Ochiana, S; Patel, HJ; Patel, M; Patel, PD; Rodina, A; Shah, SK; Taldone, T; Uddin, M1
Ladbury, JE; O'Brien, R; Pearl, LH; Piper, PW; Prodromou, C; Roe, SM2
Clark, J; Fadden, P; Grenert, JP; Haystead, TA; Krutzsch, H; Mimnaugh, E; Neckers, LM; Ochel, HJ; Sausville, E; Schulte, TW; Sullivan, WP; Toft, DO1
Hartl, FU; Obermann, WM; Pavletich, NP; Russo, AA; Sondermann, H1
Babior, BM; Catz, SD; Johnson, JL1
Carreras, CW; Santi, DV; Schirmer, A; Zhong, Z1
Bharti, A; Borkan, SC; Calderwood, S; Guo, X; Kuramochi, Y; Peng, X; Sawyer, DB1
Burlingame, AL; Chiosis, G; Chu, F; Maynard, JC; Nicchitta, CV1
Gano, JJ; Simon, JA1
Berger, JM; Corbett, KD1
Millson, SH; Piper, PW1

Reviews

1 review(s) available for adenosine diphosphate and geldanamycin

ArticleYear
Spotlight on the microbes that produce heat shock protein 90-targeting antibiotics.
    Open biology, 2012, Dec-12, Volume: 2, Issue:12

    Topics: Adenosine Diphosphate; Adenosine Triphosphatases; Adenosine Triphosphate; Anti-Bacterial Agents; Bacteria; Benzoquinones; Binding Sites; Clinical Trials as Topic; Drug Resistance; Fungi; HSP90 Heat-Shock Proteins; Humans; Lactams, Macrocyclic; Macrolides; Models, Molecular; Protein Binding

2012

Other Studies

11 other study(ies) available for adenosine diphosphate and geldanamycin

ArticleYear
Experimental and structural testing module to analyze paralogue-specificity and affinity in the Hsp90 inhibitors series.
    Journal of medicinal chemistry, 2013, Sep-12, Volume: 56, Issue:17

    Topics: Amino Acid Sequence; Cell Line, Tumor; Fluorescence Polarization; HSP90 Heat-Shock Proteins; Humans; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Probes; Molecular Sequence Data; Molecular Structure; Sequence Homology, Amino Acid; Spectrometry, Mass, Electrospray Ionization

2013
Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone.
    Cell, 1997, Jul-11, Volume: 90, Issue:1

    Topics: Adenosine Diphosphate; Amino Acid Sequence; Antibiotics, Antineoplastic; Benzoquinones; Binding Sites; Calorimetry; Conserved Sequence; Crystallography, X-Ray; DNA Gyrase; DNA Topoisomerases, Type II; HSP90 Heat-Shock Proteins; Lactams, Macrocyclic; Models, Molecular; Models, Structural; Molecular Sequence Data; Protein Folding; Protein Structure, Secondary; Quinones; Saccharomyces cerevisiae; Sequence Alignment

1997
The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation.
    The Journal of biological chemistry, 1997, Sep-19, Volume: 272, Issue:38

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Amino Acid Sequence; Benzoquinones; HSP90 Heat-Shock Proteins; Humans; Lactams, Macrocyclic; Molecular Sequence Data; Mutagenesis; Protein Binding; Protein Conformation; Quinones; Sequence Deletion

1997
In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis.
    The Journal of cell biology, 1998, Nov-16, Volume: 143, Issue:4

    Topics: Adenosine Diphosphate; Adenosine Triphosphatases; Adenosine Triphosphate; Benzoquinones; Cell Division; Chaperonins; Crystallography; DNA Topoisomerases, Type II; Enzyme Inhibitors; Fungal Proteins; Gene Expression Regulation, Fungal; Heat-Shock Proteins; HSP90 Heat-Shock Proteins; Humans; Hydrolysis; Lactams, Macrocyclic; Magnesium; Mutagenesis; Protein Structure, Tertiary; Quinones; Saccharomyces cerevisiae Proteins; Yeasts

1998
Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin.
    Journal of medicinal chemistry, 1999, Jan-28, Volume: 42, Issue:2

    Topics: Adenosine Diphosphate; Adenosine Triphosphatases; Antibiotics, Antineoplastic; Benzoquinones; Calorimetry; Crystallography, X-Ray; HSP90 Heat-Shock Proteins; Lactams, Macrocyclic; Lactones; Macrolides; Models, Molecular; Molecular Mimicry; Quinones; Structure-Activity Relationship

1999
Characterization of the nucleotide-binding capacity and the ATPase activity of the PIP3-binding protein JFC1.
    Proceedings of the National Academy of Sciences of the United States of America, 2001, Sep-25, Volume: 98, Issue:20

    Topics: Adenosine Diphosphate; Adenosine Triphosphatases; Adenosine Triphosphate; Affinity Labels; Amino Acid Sequence; Animals; Azides; Benzoquinones; Binding Sites; Cross-Linking Reagents; Deoxyadenine Nucleotides; Glutathione Transferase; Guanosine Triphosphate; Kinetics; Lactams, Macrocyclic; Magnesium; Membrane Proteins; Molecular Sequence Data; Phosphatidylinositol Phosphates; Quinones; Recombinant Fusion Proteins; Sequence Deletion; Substrate Specificity

2001
Filter binding assay for the geldanamycin-heat shock protein 90 interaction.
    Analytical biochemistry, 2003, Jun-01, Volume: 317, Issue:1

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Benzoquinones; Binding Sites; Binding, Competitive; Biotinylation; Filtration; HSP90 Heat-Shock Proteins; Humans; Kinetics; Lactams, Macrocyclic; Protein Binding; Quinones; Radioligand Assay; Recombinant Fusion Proteins; Sensitivity and Specificity; Streptomyces; Tritium

2003
Heat shock protein 90 stabilization of ErbB2 expression is disrupted by ATP depletion in myocytes.
    The Journal of biological chemistry, 2005, Apr-01, Volume: 280, Issue:13

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Animals; Benzoquinones; Cell Proliferation; Cells, Cultured; Dose-Response Relationship, Drug; Glycolysis; HSP90 Heat-Shock Proteins; Immunoprecipitation; Lactams, Macrocyclic; Ligands; Male; Muscle Cells; Myocytes, Cardiac; Oxygen Consumption; Phosphorylation; Protein Binding; Quinones; Rats; Rats, Sprague-Dawley; Receptor, ErbB-2; Receptors, Adrenergic, beta; Time Factors

2005
Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94.
    Protein science : a publication of the Protein Society, 2006, Volume: 15, Issue:6

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Animals; Benzoquinones; Chromatography, Liquid; Cross-Linking Reagents; Dimerization; Endoplasmic Reticulum; HSP70 Heat-Shock Proteins; HSP90 Heat-Shock Proteins; Lactams, Macrocyclic; Mass Spectrometry; Membrane Proteins; Models, Molecular; Molecular Chaperones; Protein Conformation; Protein Structure, Quaternary; Protein Structure, Tertiary; Quinones; Succinimides; Swine

2006
A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein.
    Molecular & cellular proteomics : MCP, 2010, Volume: 9, Issue:2

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Benzoquinones; Carrier Proteins; Cell Line; HSP90 Heat-Shock Proteins; Humans; Lactams, Macrocyclic; Ligands; Mass Spectrometry; Mutation; Phosphate-Binding Proteins; Protein Binding; Protein Structure, Tertiary; Proteomics

2010
Structure of the ATP-binding domain of Plasmodium falciparum Hsp90.
    Proteins, 2010, Volume: 78, Issue:13

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Animals; Antibiotics, Antineoplastic; Benzoquinones; Binding Sites; HSP90 Heat-Shock Proteins; Hydrogen Bonding; Lactams, Macrocyclic; Models, Molecular; Plasmodium falciparum; Protein Structure, Secondary; Protein Structure, Tertiary; Protozoan Proteins

2010