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Volumn 5, Issue 4, 2013, Pages 307-314

Synthesis of 19-substituted geldanamycins with altered conformations and their binding to heat shock protein Hsp90

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC ANTIBIOTIC; BENZOQUINONE DERIVATIVE; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; MACROCYCLIC LACTAM;

EID: 84875435418     PISSN: 17554330     EISSN: 17554349     Source Type: Journal    
DOI: 10.1038/nchem.1596     Document Type: Article
Times cited : (70)

References (57)
  • 1
    • 33746377987 scopus 로고    scopus 로고
    • Inhibitors of the Hsp90 molecular chaperone: Attacking the master regulator in cancer
    • McDonald, E., Workman, P. & Jones, K. Inhibitors of the Hsp90 molecular chaperone: attacking the master regulator in cancer. Curr. Top. Med. Chem. 6, 1091-1107 (2006).
    • (2006) Curr. Top. Med. Chem. , vol.6 , pp. 1091-1107
    • McDonald, E.1    Workman, P.2    Jones, K.3
  • 2
    • 77952544010 scopus 로고    scopus 로고
    • ATPase inhibitors of heat-shock protein 90, second season
    • Janin, Y. L. ATPase inhibitors of heat-shock protein 90, second season. Drug Discov. Today 15, 342-353 (2010).
    • (2010) Drug Discov. Today , vol.15 , pp. 342-353
    • Janin, Y.L.1
  • 3
    • 77952551024 scopus 로고    scopus 로고
    • Discovery and development of Hsp90 inhibitors: A promising pathway for cancer therapy
    • Porter, J. R., Fritz, C. C. & Depew, K. M. Discovery and development of Hsp90 inhibitors: a promising pathway for cancer therapy. Curr. Opin. Chem. Biol. 14, 412-420 (2010).
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 412-420
    • Porter, J.R.1    Fritz, C.C.2    Depew, K.M.3
  • 4
    • 77955444211 scopus 로고    scopus 로고
    • Application of chemoproteomics to drug discovery: Identification of a clinical candidate targeting Hsp90
    • Fadden, P. et al. Application of chemoproteomics to drug discovery: identification of a clinical candidate targeting Hsp90. Chem. Biol. 17, 686-694 (2010).
    • (2010) Chem. Biol. , vol.17 , pp. 686-694
    • Fadden, P.1
  • 5
    • 77958516062 scopus 로고    scopus 로고
    • ATPases as drug targets: Insights from heat shock proteins 70 and 90
    • Massey, A. J. ATPases as drug targets: insights from heat shock proteins 70 and 90. J. Med. Chem. 53, 7280-7286 (2010).
    • (2010) J. Med. Chem. , vol.53 , pp. 7280-7286
    • Massey, A.J.1
  • 7
    • 74849111762 scopus 로고    scopus 로고
    • Heat shock protein 90: Inhibitors in clinical trials
    • Biamonte, M. A. et al. Heat shock protein 90: inhibitors in clinical trials. J. Med. Chem. 53, 3-17 (2010).
    • (2010) J. Med. Chem. , vol.53 , pp. 3-17
    • Biamonte, M.A.1
  • 8
    • 32844475529 scopus 로고    scopus 로고
    • Targeting Hsp90 to halt neurodegeneration
    • Gallo, K. A. Targeting Hsp90 to halt neurodegeneration. Chem. Biol. 13, 115-116 (2006).
    • (2006) Chem. Biol. , vol.13 , pp. 115-116
    • Gallo, K.A.1
  • 9
    • 33746724745 scopus 로고    scopus 로고
    • Modulation of Hsp90 function in neurodegenerative disorders: A molecular-targeted therapy against disease-causing protein
    • Waza, M. et al. Modulation of Hsp90 function in neurodegenerative disorders: a molecular-targeted therapy against disease-causing protein. J. Mol. Med. 84, 635-646 (2006).
    • (2006) J. Mol. Med. , vol.84 , pp. 635-646
    • Waza, M.1
  • 10
    • 33846483687 scopus 로고    scopus 로고
    • Are heat shock proteins therapeutic target for Parkinson's disease?
    • Luo, G-R., Chen, S. & Le, W-D. Are heat shock proteins therapeutic target for Parkinson's disease? Int. J. Biol. Sci. 3, 20-26 (2007).
    • (2007) Int. J. Biol. Sci. , vol.3 , pp. 20-26
    • Luo, G.-R.1    Chen, S.2    Le, W.-D.3
  • 11
    • 73649130290 scopus 로고    scopus 로고
    • Heat shock proteins in neurodegenerative diseases: Pathogenic roles and therapeutic implications
    • Adachi, H. et al. Heat shock proteins in neurodegenerative diseases: pathogenic roles and therapeutic implications. Int. J. Hyperther. 25, 647-654 (2009).
    • (2009) Int. J. Hyperther. , vol.25 , pp. 647-654
    • Adachi, H.1
  • 12
    • 77949877628 scopus 로고    scopus 로고
    • Heat shock proteins: Therapeutic drug targets for chronic neurodegeneration?
    • Sajjad, M. U., Samson, B. & Wyttenbach, A. Heat shock proteins: therapeutic drug targets for chronic neurodegeneration? Curr. Pharm. Biotechnol. 11, 198-215 (2010).
    • (2010) Curr. Pharm. Biotechnol. , vol.11 , pp. 198-215
    • Sajjad, M.U.1    Samson, B.2    Wyttenbach, A.3
  • 13
    • 78649239916 scopus 로고    scopus 로고
    • Molecular chaperones as rational drug targets for Parkinson's disease therapeutics
    • Kalia, S. K., Kalia, L. V. & McLean, P. J. Molecular chaperones as rational drug targets for Parkinson's disease therapeutics. CNS Neurol. Disord.: Drug Targets 9, 741-753 (2010).
    • (2010) CNS Neurol. Disord.: Drug Targets , vol.9 , pp. 741-753
    • Kalia, S.K.1    Kalia, L.V.2    McLean, P.J.3
  • 14
    • 79955830308 scopus 로고    scopus 로고
    • Protective role of heat shock proteins in Parkinson's disease
    • Aridon, P. et al. Protective role of heat shock proteins in Parkinson's disease. Neurodegen. Dis. 8, 155-168 (2011).
    • (2011) Neurodegen. Dis. , vol.8 , pp. 155-168
    • Aridon, P.1
  • 15
    • 0029056501 scopus 로고
    • Preclinical pharmacological evaluation of geldanamycin as an antitumor agent
    • Supko, J. G., Hickman, R. L., Grever, M. R. & Malspeis, L. Preclinical pharmacological evaluation of geldanamycin as an antitumor agent. Cancer Chemother. Pharmacol. 36, 305-315 (1995).
    • (1995) Cancer Chemother. Pharmacol. , vol.36 , pp. 305-315
    • Supko, J.G.1    Hickman, R.L.2    Grever, M.R.3    Malspeis, L.4
  • 16
    • 33645471864 scopus 로고    scopus 로고
    • Reaction of geldanamycin and C17-substituted analogues with glutathione: Product identifications and pharmacological implications
    • Cysyk, R. L. et al. Reaction of geldanamycin and C17-substituted analogues with glutathione: product identifications and pharmacological implications. Chem. Res. Toxicol. 19, 376-381 (2006).
    • (2006) Chem. Res. Toxicol. , vol.19 , pp. 376-381
    • Cysyk, R.L.1
  • 17
    • 33845956606 scopus 로고    scopus 로고
    • Biotransformation of geldanamycin and 17-allylamino-17- demethoxygeldanamycin by human liver microsomes: Reductive versus oxidative metabolism and implications
    • Lang, W. et al. Biotransformation of geldanamycin and 17-allylamino-17-demethoxygeldanamycin by human liver microsomes: reductive versus oxidative metabolism and implications. Drug Metab. Dispos. 35, 21-29 (2007).
    • (2007) Drug Metab. Dispos. , vol.35 , pp. 21-29
    • Lang, W.1
  • 18
    • 52949096836 scopus 로고    scopus 로고
    • Enzymatic reduction and glutathione conjugation of benzoquinone ansamycin heat shock protein 90 inhibitors: Relevance for toxicity and mechanism of action
    • Guo, W., Reigan, P., Siegel, D. & Ross, D. Enzymatic reduction and glutathione conjugation of benzoquinone ansamycin heat shock protein 90 inhibitors: relevance for toxicity and mechanism of action. Drug Metab. Dispos. 36, 2050-2057 (2008).
    • (2008) Drug Metab. Dispos. , vol.36 , pp. 2050-2057
    • Guo, W.1    Reigan, P.2    Siegel, D.3    Ross, D.4
  • 19
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins, C. E. et al. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 89, 239-250 (1997).
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1
  • 20
    • 0032959590 scopus 로고    scopus 로고
    • Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
    • Roe, S. M. et al. Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J. Med. Chem. 42, 260-266 (1999).
    • (1999) J. Med. Chem. , vol.42 , pp. 260-266
    • Roe, S.M.1
  • 21
    • 0141683523 scopus 로고    scopus 로고
    • NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADR AMP-PNP, geldanamycin, and radicicol
    • Dehner, A. et al. NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADR AMP-PNP, geldanamycin, and radicicol. ChemBioChem 4, 870-877 (2003).
    • (2003) ChemBioChem , vol.4 , pp. 870-877
    • Dehner, A.1
  • 22
    • 79960985354 scopus 로고    scopus 로고
    • HSP90 inhibition is effective in breast cancer: A phase 2 trial of tanespimycin (17AAG) plus trastuzumab in patients with HER2-positive metastatic breast cancer progressing on trastuzumab
    • Modi, S. et al. HSP90 inhibition is effective in breast cancer: a phase 2 trial of tanespimycin (17AAG) plus trastuzumab in patients with HER2-positive metastatic breast cancer progressing on trastuzumab. Clin. Cancer Res. 17, 5132-5139 (2011).
    • (2011) Clin. Cancer Res. , vol.17 , pp. 5132-5139
    • Modi, S.1
  • 23
    • 28844451001 scopus 로고    scopus 로고
    • Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice
    • Shen, H-Y. et al. Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice. J. Biol. Chem. 280, 39962-39969 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 39962-39969
    • Shen, H.-Y.1
  • 24
    • 27144503120 scopus 로고    scopus 로고
    • 17-AAG, an Hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration
    • Waza, M. et al. 17-AAG, an Hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration. Nature Med. 11, 1088-1095 (2005).
    • (2005) Nature Med. , vol.11 , pp. 1088-1095
    • Waza, M.1
  • 25
    • 34447540087 scopus 로고    scopus 로고
    • Alleviating neurodegeneration by an anticancer agent-an Hsp90 inhibitor (17-AAG)
    • Waza, M. et al. Alleviating neurodegeneration by an anticancer agent-an Hsp90 inhibitor (17-AAG). Ann. NY Acad. Sci. 1086, 21-34 (2006).
    • (2006) Ann. NY Acad. Sci. , vol.1086 , pp. 21-34
    • Waza, M.1
  • 26
    • 34247373120 scopus 로고    scopus 로고
    • Geldanamycin derivatives and neuroprotective effect on cultured P19-derived neurons
    • Tadtong, S. et al. Geldanamycin derivatives and neuroprotective effect on cultured P19-derived neurons. Bioorg. Med. Chem. Lett. 17, 2939-2943 (2007).
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , pp. 2939-2943
    • Tadtong, S.1
  • 28
    • 0001402694 scopus 로고
    • [3, 3]-sigmatropic rearrangements in an ansamycin-stereospecific conversion of an (S)-allylic alcohol to an (S)-allylic amine derivative
    • Schnur, R. C. & Corman, M. L. Tandem [3, 3]-sigmatropic rearrangements in an ansamycin-stereospecific conversion of an (S)-allylic alcohol to an (S)-allylic amine derivative. J. Org. Chem. 59, 2581-2584 (1994).
    • (1994) J. Org. Chem. , vol.59 , pp. 2581-2584
    • Schnur, R.C.1    Tandem, L.C.M.2
  • 29
    • 0344511727 scopus 로고    scopus 로고
    • Crystal structure and molecular modeling of 17-DMAG in complex with human Hsp90
    • Jez, J. M. et al. Crystal structure and molecular modeling of 17-DMAG in complex with human Hsp90. Chem. Biol. 10, 361-368 (2003).
    • (2003) Chem. Biol. , vol.10 , pp. 361-368
    • Jez, J.M.1
  • 30
    • 3242893125 scopus 로고    scopus 로고
    • Quantum chemical calculations and mutational analysis suggest heat shock protein 90 catalyzes trans-cis isomerization of geldanamycin
    • Lee, Y-S., Marcu, M. G. & Neckers, L. Quantum chemical calculations and mutational analysis suggest heat shock protein 90 catalyzes trans-cis isomerization of geldanamycin. Chem. Biol. 11, 991-998 (2004).
    • (2004) Chem. Biol. , vol.11 , pp. 991-998
    • Lee, Y.-S.1    Marcu, M.G.2    Neckers, L.3
  • 31
    • 33947427870 scopus 로고    scopus 로고
    • Relationship among ligand conformations in solution, in the solid state, and at the Hsp90 binding site: Geldanamycin and radicicol
    • Thepchatri, P. et al. Relationship among ligand conformations in solution, in the solid state, and at the Hsp90 binding site: geldanamycin and radicicol. J. Am. Chem. Soc. 129, 3127-3134 (2007).
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 3127-3134
    • Thepchatri, P.1
  • 32
    • 34547933867 scopus 로고    scopus 로고
    • Mechanistic studies on Hsp90 inhibition by ansamycin derivatives
    • Onuoha, S. C. et al. Mechanistic studies on Hsp90 inhibition by ansamycin derivatives. J. Mol. Biol. 372, 287-297 (2007).
    • (2007) J. Mol. Biol. , vol.372 , pp. 287-297
    • Onuoha, S.C.1
  • 33
    • 79955042825 scopus 로고    scopus 로고
    • A mechanistic and structural analysis of the inhibition of the 90-kDa heat shock protein by the benzoquinone and hydroquinone ansamycins
    • Reigan, P., Siegel, D., Guo, W. & Ross, D. A mechanistic and structural analysis of the inhibition of the 90-kDa heat shock protein by the benzoquinone and hydroquinone ansamycins. Mol. Pharmacol. 79, 823-832 (2011).
    • (2011) Mol. Pharmacol. , vol.79 , pp. 823-832
    • Reigan, P.1    Siegel, D.2    Guo, W.3    Ross, D.4
  • 34
    • 28144440479 scopus 로고    scopus 로고
    • Heat shock protein 90 inhibitors. A text book example of medicinal chemistry
    • Janin, Y. L. Heat shock protein 90 inhibitors. A text book example of medicinal chemistry. J. Med. Chem. 48, 7503-7512 (2005).
    • (2005) J. Med. Chem. , vol.48 , pp. 7503-7512
    • Janin, Y.L.1
  • 35
    • 57049086938 scopus 로고    scopus 로고
    • Design and synthesis of ansamycin antibiotics
    • Wrona, I. E., Agouridas, V. & Panek, J. S. Design and synthesis of ansamycin antibiotics. C. R. Chimie 11, 1483-1522 (2008).
    • (2008) C. R. Chimie , vol.11 , pp. 1483-1522
    • Wrona, I.E.1    Agouridas, V.2    Panek, J.S.3
  • 37
    • 0029122080 scopus 로고
    • Inhibition of the oncogene product P185(Erbb-2) in vitro and in vivo by geldanamycin and dihydrogeldanamycin derivatives
    • Schnur, R. C. et al. Inhibition of the oncogene product P185(Erbb-2) in vitro and in vivo by geldanamycin and dihydrogeldanamycin derivatives. J. Med. Chem. 38, 3806-3812 (1995).
    • (1995) J. Med. Chem. , vol.38 , pp. 3806-3812
    • Schnur, R.C.1
  • 38
    • 0017407702 scopus 로고
    • Synthesis of hydrazones and oximes of geldanaldehyde as potential polymerase inhibitors
    • Rinehart, K. L. et al. Synthesis of hydrazones and oximes of geldanaldehyde as potential polymerase inhibitors. Bioorg. Chem. 6, 341-351 (1977).
    • (1977) Bioorg. Chem. , vol.6 , pp. 341-351
    • Rinehart, K.L.1
  • 41
    • 0000131734 scopus 로고
    • Large rate accelerations in the Stille reaction with tri-2-furylphosphine and triphenylarsine as palladium ligands-mechanistic and synthetic implications
    • Farina, V. & Krishnan, B. Large rate accelerations in the Stille reaction with tri-2-furylphosphine and triphenylarsine as palladium ligands-mechanistic and synthetic implications. J. Am. Chem. Soc. 113, 9585-9595 (1991).
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 9585-9595
    • Farina, V.1    Krishnan, B.2
  • 42
    • 33845282857 scopus 로고
    • Nickel-catalyzed or palladium-catalyzed cross coupling. 31. Palladium-catalyzed or nickel-catalyzed reactions of alkenylmetals with unsaturated organic halides as a selective route to arylated alkenes and conjugated dienes-scope, limitations, and mechanism
    • Negishi, E-I. et al. Nickel-catalyzed or palladium-catalyzed cross coupling. 31. Palladium-catalyzed or nickel-catalyzed reactions of alkenylmetals with unsaturated organic halides as a selective route to arylated alkenes and conjugated dienes-scope, limitations, and mechanism. J. Am. Chem. Soc. 109, 2393-2401 (1987).
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 2393-2401
    • Negishi, E.-I.1
  • 43
    • 33751554191 scopus 로고
    • 3-Stannylcyclobutenediones as nucleophilic cyclobutenedione equivalents-synthesis of substituted cyclobutenediones and cyclobutenedione monoacetals and the beneficial effect of catalytic copper iodide on the Stille reaction
    • Liebeskind, L. S. & Fengl, R. W. 3-Stannylcyclobutenediones as nucleophilic cyclobutenedione equivalents-synthesis of substituted cyclobutenediones and cyclobutenedione monoacetals and the beneficial effect of catalytic copper iodide on the Stille reaction. J. Org. Chem. 55, 5359-5364 (1990).
    • (1990) J. Org. Chem. , vol.55 , pp. 5359-5364
    • Liebeskind, L.S.1    Fengl, R.W.2
  • 44
    • 77955829634 scopus 로고    scopus 로고
    • Potassium carbonate-silica: A highly effective stationary phase for the chromatographic removal of organotin impurities
    • Harrowven, D. C. et al. Potassium carbonate-silica: a highly effective stationary phase for the chromatographic removal of organotin impurities. Chem. Commun. 46, 6335-6337 (2010).
    • (2010) Chem. Commun. , vol.46 , pp. 6335-6337
    • Harrowven, D.C.1
  • 45
    • 27544446054 scopus 로고    scopus 로고
    • Formation of 17-allylamino-demethoxygeldanamycin (17-AAG) hydroquinone by NAD(P)H:quinone oxidoreductase 1 (NQO1): Role of 17-AAG hydroquinone in heat shock protein 90 inhibition
    • Guo, W. et al. Formation of 17-allylamino-demethoxygeldanamycin (17-AAG) hydroquinone by NAD(P)H:quinone oxidoreductase 1 (NQO1): role of 17-AAG hydroquinone in heat shock protein 90 inhibition. Cancer Res. 65, 10006-10015 (2005).
    • (2005) Cancer Res. , vol.65 , pp. 10006-10015
    • Guo, W.1
  • 46
    • 33748923662 scopus 로고    scopus 로고
    • The bioreduction of a series of benzoquinone ansamycins by NAD(P)H: Quinone oxidoreductase 1 to more potent heat shock protein 90 inhibitors, the hydroquinone ansamycins
    • Guo, W. et al. The bioreduction of a series of benzoquinone ansamycins by NAD(P)H: quinone oxidoreductase 1 to more potent heat shock protein 90 inhibitors, the hydroquinone ansamycins. Mol. Pharmacol. 70, 1194-1203 (2006).
    • (2006) Mol. Pharmacol. , vol.70 , pp. 1194-1203
    • Guo, W.1
  • 47
    • 79951993000 scopus 로고    scopus 로고
    • Role for NAD(P)H:quinone oxidoreductase 1 and manganese-dependent superoxide dismutase in 17-(allylamino)-17-demethoxygeldanamycin-induced heat shock protein 90 inhibition in pancreatic cancer cells
    • Siegel, D. et al. Role for NAD(P)H:quinone oxidoreductase 1 and manganese-dependent superoxide dismutase in 17-(allylamino)-17- demethoxygeldanamycin-induced heat shock protein 90 inhibition in pancreatic cancer cells. J. Pharmacol. Exp. Ther. 336, 874-880 (2011).
    • (2011) J. Pharmacol. Exp. Ther. , vol.336 , pp. 874-880
    • Siegel, D.1
  • 48
    • 0032408087 scopus 로고    scopus 로고
    • Protective effects of the anti-Parkinsonian drugs talipexole and pramipexole against 1-methyl-4-phenylpyridinium-induced apoptotic death in human neuroblastoma SH-SY5Y cells
    • Kitamura, Y. et al. Protective effects of the anti-Parkinsonian drugs talipexole and pramipexole against 1-methyl-4-phenylpyridinium-induced apoptotic death in human neuroblastoma SH-SY5Y cells. Mol. Pharmacol. 54, 1046-1054 (1998).
    • (1998) Mol. Pharmacol. , vol.54 , pp. 1046-1054
    • Kitamura, Y.1
  • 49
    • 20444416315 scopus 로고    scopus 로고
    • Alpha-Synuclein phosphorylation enhances eosinophilic cytoplasmic inclusion formation in SH-SY5Y cells
    • Smith, W. W. et al. alpha-Synuclein phosphorylation enhances eosinophilic cytoplasmic inclusion formation in SH-SY5Y cells. J. Neurosci. 25, 5544-5552 (2005).
    • (2005) J. Neurosci. , vol.25 , pp. 5544-5552
    • Smith, W.W.1
  • 50
    • 84863499045 scopus 로고    scopus 로고
    • Transduced Tat-DJ-1 protein protects against oxidative stress-induced SH-SY5Y cell death and Parkinson disease in a mouse model
    • Jeong, H. J. et al. Transduced Tat-DJ-1 protein protects against oxidative stress-induced SH-SY5Y cell death and Parkinson disease in a mouse model. Mol. Cell 33, 471-478 (2012).
    • (2012) Mol. Cell , vol.33 , pp. 471-478
    • Jeong, H.J.1


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