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Volumn 3, Issue 5, 2003, Pages 371-376

Development of purine-scaffold small molecule inhibitors of Hsp90

Author keywords

[No Author keywords available]

Indexed keywords

17 ALLYLAMINO 17 DEMETHOXYGELDANAMYCIN; ANTINEOPLASTIC AGENT; GELDANAMYCIN; HEAT SHOCK PROTEIN 90 INHIBITOR; PROTEIN INHIBITOR; PURINE DERIVATIVE; RADICICOL; UNCLASSIFIED DRUG;

EID: 0141485327     PISSN: 15680096     EISSN: None     Source Type: Journal    
DOI: 10.2174/1568009033481778     Document Type: Review
Times cited : (104)

References (38)
  • 1
    • 0032924953 scopus 로고    scopus 로고
    • Hsp90 & Co. - A holding for folding
    • Buchner, J. Hsp90 & Co. - A Holding for Folding. Trends Biochem. Sci. 1999, 4, 136-144.
    • (1999) Trends Biochem. Sci. , vol.4 , pp. 136-144
    • Buchner, J.1
  • 2
    • 0031848850 scopus 로고    scopus 로고
    • Recent advances in the study of Hsp90 structure and mechanism of action
    • Toft, O. D. Recent Advances in the Study of Hsp90 Structure and Mechanism of Action. Trends Endocrinol. Med. 1998, 9, 238-243.
    • (1998) Trends Endocrinol. Med. , vol.9 , pp. 238-243
    • Toft, O.D.1
  • 3
    • 0031693703 scopus 로고    scopus 로고
    • The Hsp90 complex - A super-chaperone machine as a novel drug target
    • Scheibel, T.; Buchner, J. The Hsp90 Complex - A Super-Chaperone Machine as a Novel Drug Target. Biochem. Pharmacol. 1998, 56, 675-682.
    • (1998) Biochem. Pharmacol. , vol.56 , pp. 675-682
    • Scheibel, T.1    Buchner, J.2
  • 4
    • 0036219609 scopus 로고    scopus 로고
    • Hsp90 inhibitors as novel cancer chemotherapeutic agents
    • Neckers, L. Hsp90 Inhibitors as Novel Cancer Chemotherapeutic Agents. Trends Mol. Med. 2002, 8, S55-S61.
    • (2002) Trends Mol. Med. , vol.8
    • Neckers, L.1
  • 5
    • 0035989680 scopus 로고    scopus 로고
    • HSP90 as a new therapeutic target for cancer therapy: The story unfolds
    • Workman, P.; Maloney, A. HSP90 as a New Therapeutic Target for Cancer Therapy: the Story Unfolds. Expert Opin. Biol. Ther. 2002, 2, 3-24.
    • (2002) Expert Opin. Biol. Ther. , vol.2 , pp. 3-24
    • Workman, P.1    Maloney, A.2
  • 6
    • 0024453582 scopus 로고
    • Nucleotide sequence of a full-length cDNA for 90 kDa heat-shock protein from human peripheral blood lymphocytes
    • Yamazaki, M.; Akaogi, K.; Miwa, T.; Imai, T.; Soeda, E.; Yokoyama, K. Nucleotide Sequence of a Full-Length cDNA for 90 kDa Heat-Shock Protein from Human Peripheral Blood Lymphocytes. Nucleic Acids Res. 1989, 17, 7108.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 7108
    • Yamazaki, M.1    Akaogi, K.2    Miwa, T.3    Imai, T.4    Soeda, E.5    Yokoyama, K.6
  • 7
    • 0023224123 scopus 로고
    • Nucleotide sequence of a cDNA for a member of the human 90-KDa heat-shock protein family
    • Rebbe, N. F.; Ware, J. Bertina, R. M.; Modrich, P.; Stafford, D. W. Nucleotide Sequence of a cDNA for a Member of the Human 90-KDa Heat-Shock Protein Family. Gene. 1987, 53, 235-245.
    • (1987) Gene , vol.53 , pp. 235-245
    • Rebbe, N.F.1    Ware, J.2    Bertina, R.M.3    Modrich, P.4    Stafford, D.W.5
  • 8
    • 0033210210 scopus 로고    scopus 로고
    • GRP94, an ER chaperone with protein and peptide binding properties
    • Argon, Y.; Simen, B. B. GRP94, an ER Chaperone with Protein and Peptide Binding Properties. Semin. Cell Dev. Biol. 1999, 5, 495-505.
    • (1999) Semin. Cell Dev. Biol. , vol.5 , pp. 495-505
    • Argon, Y.1    Simen, B.B.2
  • 9
    • 0034603178 scopus 로고    scopus 로고
    • The Hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties
    • Felts, S. J.; Owen, B. A.; Nguyen, P.; Trepel, J.; Donner, D. B.; Toft, D. O. The Hsp90-Related Protein TRAP1 is a Mitochondrial Protein with Distinct Functional Properties. J. Biol. Chem. 2000, 275, 3305-3312.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3305-3312
    • Felts, S.J.1    Owen, B.A.2    Nguyen, P.3    Trepel, J.4    Donner, D.B.5    Toft, D.O.6
  • 10
    • 0030901877 scopus 로고    scopus 로고
    • A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone
    • Prodromou, C.; Roe, S. M.; Piper, P. W.; Pearl, L. H. A Molecular Clamp in the Crystal Structure of the N-Terminal Domain of the Yeast Hsp90 Chaperone. Nat. Struct. Biol. 1997, 6, 477-482.
    • (1997) Nat. Struct. Biol. , vol.6 , pp. 477-482
    • Prodromou, C.1    Roe, S.M.2    Piper, P.W.3    Pearl, L.H.4
  • 11
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou, C.; Roe, S. M.; O'Brien, R.; Ladbury, J. E.; Piper, P. W.; Pearl, L. H. Identification and Structural Characterization of the ATP/ADP-Binding Site in the Hsp90 Molecular Chaperone. Cell 1997, 90, 65-75.
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 13
    • 0032541344 scopus 로고    scopus 로고
    • ATP binding hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
    • Panaretou, B.; Prodromou, C.; Roe, S. M.; O'Brien, R.; Ladbury, J. E.; Piper, P. W.; Pearl, L. H. ATP Binding and Hydrolysis Are Essential to the Function of the Hsp90 Molecular Chaperone in Vivo. EMBO J. 1998, 17, 4829-4836.
    • (1998) EMBO J. , vol.17 , pp. 4829-4836
    • Panaretou, B.1    Prodromou, C.2    Roe, S.M.3    O'Brien, R.4    Ladbury, J.E.5    Piper, P.W.6    Pearl, L.H.7
  • 14
    • 0030987132 scopus 로고    scopus 로고
    • An atypical topoisomerase 11 from archaea with implications for meiotic recombination
    • Bergerat, A.; De Massy, B.; Gadelle, D.; Varoutas, P. C.; Nicolas, A.; Forterre, P. an Atypical Topoisomerase 11 from Archaea with Implications for Meiotic Recombination. Nature 1997, 386, 414-417.
    • (1997) Nature , vol.386 , pp. 414-417
    • Bergerat, A.1    De Massy, B.2    Gadelle, D.3    Varoutas, P.C.4    Nicolas, A.5    Forterre, P.6
  • 15
    • 0030915681 scopus 로고    scopus 로고
    • Positionally cloned human disease genes: Patterns of evolutionary conservation and functional motifs
    • Mushegian, A. R.; Bassett, D. E. Jr.; Boguski, M. S.; Bork, P.; Koonin, E. V. Positionally Cloned Human Disease Genes: Patterns of Evolutionary Conservation and Functional Motifs. Proc. Natl. Acad. Sci. USA 1997, 94, 5831-5836.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5831-5836
    • Mushegian, A.R.1    Bassett D.E., Jr.2    Boguski, M.S.3    Bork, P.4    Koonin, E.V.5
  • 16
    • 0033985080 scopus 로고    scopus 로고
    • GHKL, an emergent Atpase/kinase superfamily
    • Dutta, R.; Inouye, M. GHKL, an Emergent Atpase/Kinase Superfamily. Trends Biochem. Sci. 2000, 25, 24-28.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 24-28
    • Dutta, R.1    Inouye, M.2
  • 17
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins, C. E.; Russo, A. A.; Schneider, C.; Rosen, N.; Hartl, F. U., Pavletich, N. P. Crystal Structure of an Hsp90-Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor Agent. Cell 1997, 89, 239-250.
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 18
    • 0031844350 scopus 로고    scopus 로고
    • Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin
    • Schulte, T. W.; Akinaga, S.; Soga, S.; Sullivan, W.; Stensgard, B.; Toft, D.; Neckers, L. M. Antibiotic Radicicol Binds to the N-Terminal Domain of Hsp90 and Shares Important Biologic Activities with Geldanamycin. Cell Stress Chap. 1998, 2, 100-108.
    • (1998) Cell Stress Chap. , vol.2 , pp. 100-108
    • Schulte, T.W.1    Akinaga, S.2    Soga, S.3    Sullivan, W.4    Stensgard, B.5    Toft, D.6    Neckers, L.M.7
  • 19
    • 0032959590 scopus 로고    scopus 로고
    • Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
    • Roe, S. M.; Prodromou, C.; O'Brien, R.; Ladbury, J. E.; Piper, P. W.; Pearl, L. H. Structural Basis for Inhibition of the Hsp90 Molecular Chaperone by the Antitumor Antibiotics Radicicol and Geldanamycin. J. Med. Chem. 1999, 42, 260-266.
    • (1999) J. Med. Chem. , vol.42 , pp. 260-266
    • Roe, S.M.1    Prodromou, C.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 20
    • 0024467122 scopus 로고
    • Irreversible inhibition of V-Src tyrosine kinase activity by herbimycin a and its abrogation by sulfhydryl compounds
    • Uehara, Y.; Fukazawa, H.; Murakami, Y.; Mizuno, S. Irreversible Inhibition of V-Src Tyrosine Kinase Activity by Herbimycin a and Its Abrogation by Sulfhydryl Compounds. Biochem. Biophys. Res. Commun. 1989, 163, 803-809.
    • (1989) Biochem. Biophys. Res. Commun. , vol.163 , pp. 803-809
    • Uehara, Y.1    Fukazawa, H.2    Murakami, Y.3    Mizuno, S.4
  • 21
  • 22
    • 0031875042 scopus 로고    scopus 로고
    • The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to Hsp90 and shares important biologic activities with geldanamycin
    • Schulte, T. W.; Neckers, L. M. The Benzoquinone Ansamycin 17-Allylamino-17-Demethoxygeldanamycin Binds to Hsp90 and Shares Important Biologic Activities with Geldanamycin. Cancer Chemother. Pharmacol. 1998, 42, 273-279.
    • (1998) Cancer Chemother. Pharmacol. , vol.42 , pp. 273-279
    • Schulte, T.W.1    Neckers, L.M.2
  • 23
    • 0033579175 scopus 로고    scopus 로고
    • DT-diaphorase expression and tumor cell sensitivity to 17-allyamino-17-demethoxygeldanamycin, an inhibitor of heat shock protein 90
    • Kelland, L. R.; Sharp, S. Y.; Rogers, P. M.; Myers, T. G.; Workman, P. DT-Diaphorase Expression and Tumor Cell Sensitivity to 17-Allyamino-17-Demethoxygeldanamycin, an Inhibitor of Heat Shock Protein 90. J. Natl. Cancer Inst. 1999, 91, 1940-1949.
    • (1999) J. Natl. Cancer Inst. , vol.91 , pp. 1940-1949
    • Kelland, L.R.1    Sharp, S.Y.2    Rogers, P.M.3    Myers, T.G.4    Workman, P.5
  • 24
    • 0034665760 scopus 로고    scopus 로고
    • Novel oxime derivatives of radicicol induce erythroid differentiation associated with preferential G(1) phase accumulation against chronic myelogenous leukemia cells through destabilization of Bcr-Abl with Hsp90 complex
    • Shiotsu, Y.; Neckers, L. M.; Wortman, I.; An, W. G.; Schulte, T. W.; Soga, S.; Murakata, C.; Tamaoki, T.; Akinaga, S. Novel Oxime Derivatives of Radicicol Induce Erythroid Differentiation Associated with Preferential G(1) Phase Accumulation against Chronic Myelogenous Leukemia Cells Through Destabilization of Bcr-Abl with Hsp90 Complex. Blood 2000, 96, 2284-2291.
    • (2000) Blood , vol.96 , pp. 2284-2291
    • Shiotsu, Y.1    Neckers, L.M.2    Wortman, I.3    An, W.G.4    Schulte, T.W.5    Soga, S.6    Murakata, C.7    Tamaoki, T.8    Akinaga, S.9
  • 25
    • 0033564430 scopus 로고    scopus 로고
    • Novel oxime derivatives of radicicol induce erythroid differentiation associated with preferential G(1) phase accumulation against chronic myelogenous leukemia cells through destabilization of Bcr-Abl with Hsp90 complex
    • Soga, S.; Neckers, L. M.; Schulte, T. W.; Shiotsu, Y.; Akasaka, K.; Narumi, H.; Agatsuma, T.; Ikuina, Y.; Murakata, C.; Tamaoki, T.; Akinaga, S. Novel Oxime Derivatives of Radicicol Induce Erythroid Differentiation Associated with Preferential G(1) Phase Accumulation against Chronic Myelogenous Leukemia Cells through Destabilization of Bcr-Abl with Hsp90 Complex. Cancer Res. 1999, 59, 2931-2938.
    • (1999) Cancer Res. , vol.59 , pp. 2931-2938
    • Soga, S.1    Neckers, L.M.2    Schulte, T.W.3    Shiotsu, Y.4    Akasaka, K.5    Narumi, H.6    Agatsuma, T.7    Ikuina, Y.8    Murakata, C.9    Tamaoki, T.10    Akinaga, S.11
  • 26
    • 0035676830 scopus 로고    scopus 로고
    • A radicicol derivative KF58333, inhibits expression of hypoxia-inducible factor-1alpha and vascular endothelial growth factor, angiogenesis and growth of human breast cancer xenografts
    • Kurebayashi, J.; Otsuki, T.; Kurosumi, M.; Soga, S.; Akinaga, S.; Sonoo, H. A Radicicol Derivative, KF58333, Inhibits Expression of Hypoxia-Inducible Factor-1alpha and Vascular Endothelial Growth Factor, Angiogenesis and Growth of Human Breast Cancer Xenografts. Jpn. J. Cancer Res. 2001, 92, 1342-1351.
    • (2001) Jpn. J. Cancer Res. , vol.92 , pp. 1342-1351
    • Kurebayashi, J.1    Otsuki, T.2    Kurosumi, M.3    Soga, S.4    Akinaga, S.5    Sonoo, H.6
  • 31
    • 0035071607 scopus 로고    scopus 로고
    • A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells
    • Chiosis, G.; Timaul, M. N.; Lucas, B.; Munster, M. N.; Zheng, F. F.; Sepp-Lorenzino, L.; Rosen, N. A Small Molecule Designed to Bind to the Adenine Nucleotide Pocket of Hsp90 Causes Her2 Degradation and the Growth Arrest and Differentiation of Breast Cancer Cells. Chem. Biol. 2001, 8, 289-299.
    • (2001) Chem. Biol. , vol.8 , pp. 289-299
    • Chiosis, G.1    Timaul, M.N.2    Lucas, B.3    Munster, M.N.4    Zheng, F.F.5    Sepp-Lorenzino, L.6    Rosen, N.7
  • 33
    • 0031024171 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and developmental settings
    • Lipinski, C. A.; Lombardo, F.; Dominy, B. W., Feeney, P. J. Experimental and Computational Approaches to Estimate Solubility and Permeability in Drug Discovery and Developmental Settings. Adv. Drug Deliv. Rev. 1997, 23, 3-25,
    • (1997) Adv. Drug Deliv. Rev. , vol.23 , pp. 3-25
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 34
    • 0035514005 scopus 로고    scopus 로고
    • Facile synthesis of 9-alkyl-8-benzyl-9H-purin-6-ylamine derivatives
    • Lucas, B.; Rosen, N.; Chiosis, G. Facile Synthesis of 9-Alkyl-8-Benzyl-9H-Purin-6-Ylamine Derivatives. J. Comb. Chem. 2001, 3, 518-520.
    • (2001) J. Comb. Chem. , vol.3 , pp. 518-520
    • Lucas, B.1    Rosen, N.2    Chiosis, G.3
  • 36
    • 0036836964 scopus 로고    scopus 로고
    • Development of a purine-based novel class of Hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase
    • Chiosis, G.; Huezo, H; Lucas, B; Rosen, N. Development of a Purine-Based Novel Class of Hsp90 Binders That Inhibit the Proliferation of Cancer Cells and Induce the Degradation of Her2 Tyrosine Kinase. Bioorg. Med. Chem. 2002, 10, 3555-3564.
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 3555-3564
    • Chiosis, G.1    Huezo, H.2    Lucas, B.3    Rosen, N.4
  • 37
    • 0141454205 scopus 로고    scopus 로고
    • Development of 9-alkyl-8-benzyl-9H-purin-6-ylamines as inhibitors of the Hsp90 family
    • Chiosis, G.; Shtil, A.; Lucas, B.; Huezo, H.; Rosen, N. Development of 9-Alkyl-8-Benzyl-9H-Purin-6-Ylamines as Inhibitors of the Hsp90 Family. Clinic. Cancer Res. 2001, 7, 474 Suppl. S.
    • (2001) Clinic. Cancer Res. , vol.7 , Issue.SUPPL. S , pp. 474
    • Chiosis, G.1    Shtil, A.2    Lucas, B.3    Huezo, H.4    Rosen, N.5
  • 38
    • 0042855994 scopus 로고    scopus 로고
    • 17AAG - Low target binding affinity and potent cell activity: Finding an explanation. [Apparent and real potency of ansamycins: Which one is to trust?]
    • Chiosis, G.; Huezo, H.; Rosen, N.; Mimnaugh, E.; Whitesell, L.; Neckers, L. 17AAG - Low Target Binding Affinity and Potent Cell Activity: Finding an Explanation. [Apparent and Real Potency of Ansamycins: Which One Is to Trust?]. Mol. Cancer Ther. 2003, 2, 123-219.
    • (2003) Mol. Cancer Ther. , vol.2 , pp. 123-219
    • Chiosis, G.1    Huezo, H.2    Rosen, N.3    Mimnaugh, E.4    Whitesell, L.5    Neckers, L.6


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