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Volumn 9, Issue 15, 2009, Pages 1369-1385

Structural and computational biology of the molecular chaperone Hsp90: From understanding molecular mechanisms to computer-based inhibitor design

Author keywords

Allosteric regulation; Computer aided drug design; In silico screening; Inhibitor identification; Molecular docking; Protein dynamics; Signal communication

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 90;

EID: 74249085580     PISSN: 15680266     EISSN: None     Source Type: Journal    
DOI: 10.2174/156802609789895700     Document Type: Review
Times cited : (23)

References (197)
  • 1
    • 0034892432 scopus 로고    scopus 로고
    • Hsp90: Chaperoning signal transduction
    • Richter, K.; Buchner, J. Hsp90: chaperoning signal transduction. J. Cell Physiol. 2001, 188, 281-290.
    • (2001) J. Cell Physiol , vol.188 , pp. 281-290
    • Richter, K.1    Buchner, J.2
  • 2
    • 0035939668 scopus 로고    scopus 로고
    • Hsp90: A specialized but essential protein-folding tool
    • Young, J. C.; Moarefi, I.; Hartl, F. U. Hsp90: a specialized but essential protein-folding tool. J. Cell Biol. 2001, 154, 267-273.
    • (2001) J. Cell Biol , vol.154 , pp. 267-273
    • Young, J.C.1    Moarefi, I.2    Hartl, F.U.3
  • 3
    • 0036810352 scopus 로고    scopus 로고
    • Heat-shock protein 90, a chaperone for folding and regulation
    • Picard, D. Heat-shock protein 90, a chaperone for folding and regulation. Cell Mol. Life Sci. 2002, 59, 1640-1648.
    • (2002) Cell Mol. Life Sci , vol.59 , pp. 1640-1648
    • Picard, D.1
  • 4
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt, W. B.; Toft, D. O. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med. (Maywood) 2003, 228, 111-133.
    • (2003) Exp. Biol. Med. (Maywood) , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 6
    • 25844519550 scopus 로고    scopus 로고
    • Hsp90 and the chaperoning of cancer
    • Whitesell, L.; Lindquist, S. L. Hsp90 and the chaperoning of cancer. Nat. Rev. Cancer 2005, 5, 761-772.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 7
    • 35148876623 scopus 로고    scopus 로고
    • The Hsp90 capacitor, developmental remodeling, and evolution: The robustness of gene networks and the curious evolvability of metamorphosis
    • Rutherford, S.; Hirate, Y.; Swalla, B. J. The Hsp90 capacitor, developmental remodeling, and evolution: the robustness of gene networks and the curious evolvability of metamorphosis. Crit. Rev. Biochem. Mol. Biol. 2007, 42, 355-372.
    • (2007) Crit. Rev. Biochem. Mol. Biol , vol.42 , pp. 355-372
    • Rutherford, S.1    Hirate, Y.2    Swalla, B.J.3
  • 8
    • 34248187981 scopus 로고    scopus 로고
    • Heat shock protein 90: The cancer chaperone
    • Neckers, L. Heat shock protein 90: the cancer chaperone. J. Biosci. 2007, 32, 517-530.
    • (2007) J. Biosci , vol.32 , pp. 517-530
    • Neckers, L.1
  • 9
    • 41149111451 scopus 로고    scopus 로고
    • The Hsp90 molecular chaperone: An open and shut case for treatment
    • Pearl, L. H.; Prodromou, C.; Workman, P. The Hsp90 molecular chaperone: an open and shut case for treatment. Biochem. J. 2008, 410, 439-453.
    • (2008) Biochem. J , vol.410 , pp. 439-453
    • Pearl, L.H.1    Prodromou, C.2    Workman, P.3
  • 10
    • 34848926209 scopus 로고    scopus 로고
    • Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches
    • Mcclellan, A. J.; Xia, Y.; Deutschbauer, A. M.; Davis, R. W.; Gerstein, M.; Frydman, J. Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches. Cell 2007, 131, 121-135.
    • (2007) Cell , vol.131 , pp. 121-135
    • Mcclellan, A.J.1    Xia, Y.2    Deutschbauer, A.M.3    Davis, R.W.4    Gerstein, M.5    Frydman, J.6
  • 12
    • 0043288724 scopus 로고    scopus 로고
    • Heat shock protein 90 as a molecular target for cancer therapeutics
    • Isaacs, J. S.; Xu, W.; Neckers, L. Heat shock protein 90 as a molecular target for cancer therapeutics. Cancer Cell 2003, 3, 213-217.
    • (2003) Cancer Cell , vol.3 , pp. 213-217
    • Isaacs, J.S.1    Xu, W.2    Neckers, L.3
  • 13
    • 4143095430 scopus 로고    scopus 로고
    • Altered Hsp90 function in cancer: A unique therapeutic opportunity
    • Bagatell, R.; Whitesell, L. Altered Hsp90 function in cancer: a unique therapeutic opportunity. Mol. Cancer Ther. 2004, 3, 1021-1030.
    • (2004) Mol. Cancer Ther , vol.3 , pp. 1021-1030
    • Bagatell, R.1    Whitesell, L.2
  • 14
    • 34250162144 scopus 로고    scopus 로고
    • Targeting the molecular chaperone heat shock protein 90 provides a multifaceted effect on diverse cell signaling pathways of cancer cells
    • Xu, W.; Neckers, L. Targeting the molecular chaperone heat shock protein 90 provides a multifaceted effect on diverse cell signaling pathways of cancer cells. Clin. Cancer Res. 2007, 13, 1625-1629.
    • (2007) Clin. Cancer Res , vol.13 , pp. 1625-1629
    • Xu, W.1    Neckers, L.2
  • 15
  • 16
    • 0141596941 scopus 로고    scopus 로고
    • Overview: Translating Hsp90 biology into Hsp90 drugs
    • Workman, P. Overview: translating Hsp90 biology into Hsp90 drugs. Curr. Cancer Drug Targets 2003, 3, 297-300.
    • (2003) Curr. Cancer Drug Targets , vol.3 , pp. 297-300
    • Workman, P.1
  • 17
    • 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. 2006, 6, 1091-1107.
    • (2006) Curr. Top. Med. Chem , vol.6 , pp. 1091-1107
    • Mcdonald, E.1    Workman, P.2    Jones, K.3
  • 18
    • 36848998942 scopus 로고    scopus 로고
    • Putting the heat on cancer
    • Workman, P.; de Billy, E. Putting the heat on cancer. Nat. Med. 2007, 13, 1415-1417.
    • (2007) Nat. Med , vol.13 , pp. 1415-1417
    • Workman, P.1    de Billy, E.2
  • 19
    • 33746191768 scopus 로고    scopus 로고
    • Inhibitors of the HSP90 molecular chaperone: Current status
    • Sharp, S.; Workman, P. Inhibitors of the HSP90 molecular chaperone: current status. Adv. Cancer Res. 2006, 95, 323-348.
    • (2006) Adv. Cancer Res , vol.95 , pp. 323-348
    • Sharp, S.1    Workman, P.2
  • 20
    • 34447507818 scopus 로고    scopus 로고
    • Inhibitors of the heat shock response: Biology and pharmacology
    • Powers, M. V.; Workman, P. Inhibitors of the heat shock response: biology and pharmacology. FEBS Lett. 2007, 581, 3758-3769.
    • (2007) FEBS Lett , vol.581 , pp. 3758-3769
    • Powers, M.V.1    Workman, P.2
  • 21
    • 35348890981 scopus 로고    scopus 로고
    • Drugging the cancer chaperone HSP90: Combinatorial therapeutic exploitation of oncogene addiction and tumor stress
    • Workman, P.; Burrows, F.; Neckers, L.; Rosen, N. Drugging the cancer chaperone HSP90: combinatorial therapeutic exploitation of oncogene addiction and tumor stress. Ann. N. Y. Acad. Sci. 2007, 1113, 202-216.
    • (2007) Ann. N. Y. Acad. Sci , vol.1113 , pp. 202-216
    • Workman, P.1    Burrows, F.2    Neckers, L.3    Rosen, N.4
  • 22
    • 0033741503 scopus 로고    scopus 로고
    • Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90
    • Chadli, A.; Bouhouche, I.; Sullivan, W.; Stensgard, B.; Mcmahon, N.; Catelli, M. G.; Toft, D. O. Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90. Proc. Natl. Acad. Sci. USA 2000, 97, 12524-12529.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12524-12529
    • Chadli, A.1    Bouhouche, I.2    Sullivan, W.3    Stensgard, B.4    Mcmahon, N.5    Catelli, M.G.6    Toft, D.O.7
  • 24
    • 0037352446 scopus 로고    scopus 로고
    • Structural and functional analysis of the middle segment of hsp90: Implications for ATP hydrolysis and client protein and cochaperone interactions
    • Meyer, P.; Prodromou, C.; Hu, B.; Vaughan, C.; Roe, M. S.; Panaretou, B.; Piper, P. W.; Pearl, L. H. Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions. Mol. Cell 2003, 11, 647-658.
    • (2003) Mol. Cell , vol.11 , pp. 647-658
    • Meyer, P.1    Prodromou, C.2    Hu, B.3    Vaughan, C.4    Roe, M.S.5    Panaretou, B.6    Piper, P.W.7    Pearl, L.H.8
  • 25
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • Pearl, L. H.; Prodromou, C. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 2006, 75, 271-294.
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 26
    • 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, 4, 477-482.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 477-482
    • Prodromou, C.1    Roe, S.M.2    Piper, P.W.3    Pearl, L.H.4
  • 27
    • 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
  • 28
    • 17044403753 scopus 로고    scopus 로고
    • Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding
    • Huai, Q.; Wang, H.; Liu, Y.; Kim, H. Y.; Toft, D.; Ke, H. Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding. Structure 2005, 13, 579-590.
    • (2005) Structure , vol.13 , pp. 579-590
    • Huai, Q.1    Wang, H.2    Liu, Y.3    Kim, H.Y.4    Toft, D.5    Ke, H.6
  • 29
    • 33750983940 scopus 로고    scopus 로고
    • The middle domain of Hsp90 acts as a discriminator between different types of client proteins
    • Hawle, P.; Siepmann, M.; Harst, A.; Siderius, M.; Reusch, P. H.; Obermann, W. M. J. The middle domain of Hsp90 acts as a discriminator between different types of client proteins. Mol. Cell Biol . 2006, 26, 8385-8395.
    • (2006) Mol. Cell Biol , vol.26 , pp. 8385-8395
    • Hawle, P.1    Siepmann, M.2    Harst, A.3    Siderius, M.4    Reusch, P.H.5    Obermann, W.M.J.6
  • 30
  • 31
    • 24044518180 scopus 로고    scopus 로고
    • Structure of unliganded GRP94, the endoplasmic reticulum Hsp90. Basis for nucleotide-induced conformational change
    • Dollins, E. D.; Immormino, R. M.; Gewirth, D. T. Structure of unliganded GRP94, the endoplasmic reticulum Hsp90. Basis for nucleotide-induced conformational change J. Biol. Chem. 2005, 280, 30438-30447.
    • (2005) J. Biol. Chem , vol.280 , pp. 30438-30447
    • Dollins, E.D.1    Immormino, R.M.2    Gewirth, D.T.3
  • 32
    • 2942533020 scopus 로고    scopus 로고
    • The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site
    • Harris, S. F.; Shiau, A. K.; Agard, D. A. The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site. Structure 2004, 12, 1087-1097.
    • (2004) Structure , vol.12 , pp. 1087-1097
    • Harris, S.F.1    Shiau, A.K.2    Agard, D.A.3
  • 34
    • 33750008686 scopus 로고    scopus 로고
    • Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements
    • Shiau, A. K.; Harris, S. F.; Southworth, D. R.; Agard, D. A. Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell 2006, 127, 329-340.
    • (2006) Cell , vol.127 , pp. 329-340
    • Shiau, A.K.1    Harris, S.F.2    Southworth, D.R.3    Agard, D.A.4
  • 35
    • 34948893963 scopus 로고    scopus 로고
    • Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones
    • Dollins, E. D.; Warren, J. J.; Immormino, R. M.; Gewirth, D. T. Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones. Mol. Cell 2007, 28, 41-56.
    • (2007) Mol. Cell , vol.28 , pp. 41-56
    • Dollins, E.D.1    Warren, J.J.2    Immormino, R.M.3    Gewirth, D.T.4
  • 39
    • 51049093018 scopus 로고    scopus 로고
    • Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90
    • Cunningham, C. N.; Krukenberg, K. A.; Agard, D. A. Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90. J. Biol. Chem. 2008, 283, 21170-21178.
    • (2008) J. Biol. Chem , vol.283 , pp. 21170-21178
    • Cunningham, C.N.1    Krukenberg, K.A.2    Agard, D.A.3
  • 40
    • 42949147146 scopus 로고    scopus 로고
    • Multiple conformations of E. coli Hsp90 in solution: Insights into the conformational dynamics of Hsp90
    • Krukenberg, K. A.; Forster, F.; Rice, L. M.; Sali, A.; Agard, D. A. Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90. Structure 2008, 16, 755-765.
    • (2008) Structure , vol.16 , pp. 755-765
    • Krukenberg, K.A.1    Forster, F.2    Rice, L.M.3    Sali, A.4    Agard, D.A.5
  • 42
    • 69249083558 scopus 로고    scopus 로고
    • Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide
    • Krukenberg, K. A.; Böttcher, U.M., Southworth, D. R.; Agard, D. A. Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide. Protein Sci. 2009, 18(9), 1815-1827.
    • (2009) Protein Sci , vol.18 , Issue.9 , pp. 1815-1827
    • Krukenberg, K.A.1    Böttcher, U.M.2    Southworth, D.R.3    Agard, D.A.4
  • 43
    • 57649215437 scopus 로고    scopus 로고
    • A common conformationally coupled ATPase mechanism for yeast and human cytoplasmic Hsp90s
    • Vaughan, C. K.; Piper, P. W.; Pearl, L. H.; Prodromou, C. A common conformationally coupled ATPase mechanism for yeast and human cytoplasmic Hsp90s. FEBS J. 2009, 276, 199-209.
    • (2009) FEBS J , vol.276 , pp. 199-209
    • Vaughan, C.K.1    Piper, P.W.2    Pearl, L.H.3    Prodromou, C.4
  • 44
    • 56849131626 scopus 로고    scopus 로고
    • Species-dependent ensembles of conserved conformational States define the Hsp90 chaperone ATPase cycle
    • Southworth, D. R.; Agard, D. A. Species-dependent ensembles of conserved conformational States define the Hsp90 chaperone ATPase cycle Mol. Cell 2008, 32, 631-640.
    • (2008) Mol. Cell , vol.32 , pp. 631-640
    • Southworth, D.R.1    Agard, D.A.2
  • 46
    • 37249011744 scopus 로고    scopus 로고
    • The ATPase cycle of the endoplasmic chaperone Grp94
    • Frey, S.; Leskovar, A.; Reinstein, J.; Buchner, J. The ATPase cycle of the endoplasmic chaperone Grp94. J. Biol. Chem. 2007, 282, 35612-35620.
    • (2007) J. Biol. Chem , vol.282 , pp. 35612-35620
    • Frey, S.1    Leskovar, A.2    Reinstein, J.3    Buchner, J.4
  • 47
    • 67349184994 scopus 로고    scopus 로고
    • pH-dependent conformational changes in bacterial Hsp90 reveal a Grp94-like conformation at pH 6 that is highly active in suppression of citrate synthase aggregation
    • Krukenberg, K. A.; Southworth, D. R.; Street, T. O.; Agard, D. A. pH-dependent conformational changes in bacterial Hsp90 reveal a Grp94-like conformation at pH 6 that is highly active in suppression of citrate synthase aggregation. J. Mol. Biol. 2009, 390, 278-291.
    • (2009) J. Mol. Biol , vol.390 , pp. 278-291
    • Krukenberg, K.A.1    Southworth, D.R.2    Street, T.O.3    Agard, D.A.4
  • 48
    • 33750983940 scopus 로고    scopus 로고
    • The middle domain of Hsp90 acts as a discriminator between different types of client proteins
    • Hawle, P.; Siepmann, M.; Harst, A.; Siderius, M.; Reusch, P. H.; Obermann, W. M. J. The middle domain of Hsp90 acts as a discriminator between different types of client proteins. Mol. Cell Biol. 2006, 26, 8385-8395.
    • (2006) Mol. Cell Biol , vol.26 , pp. 8385-8395
    • Hawle, P.1    Siepmann, M.2    Harst, A.3    Siderius, M.4    Reusch, P.H.5    Obermann, W.M.J.6
  • 51
    • 10644265069 scopus 로고    scopus 로고
    • Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle
    • Siligardi, G.; Hu, B.; Panaretou, B.; Piper, P. W.; Pearl, L. H.; Prodromou, C. Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle. J. Biol. Chem. 2004, 279, 51989-51998.
    • (2004) J. Biol. Chem , vol.279 , pp. 51989-51998
    • Siligardi, G.1    Hu, B.2    Panaretou, B.3    Piper, P.W.4    Pearl, L.H.5    Prodromou, C.6
  • 52
    • 4444291743 scopus 로고    scopus 로고
    • The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle
    • Richter, K.; Walter, S.; Buchner, J. The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle. J. Mol. Biol. 2004, 342, 1403-1413.
    • (2004) J. Mol. Biol , vol.342 , pp. 1403-1413
    • Richter, K.1    Walter, S.2    Buchner, J.3
  • 54
    • 44349097402 scopus 로고    scopus 로고
    • Structural studies on the co-chaperone Hop and its complexes with Hsp90
    • Onuoha, S. C.; Coulstock, E. T.; Grossmann, J. G.; Jackson, S. E. Structural studies on the co-chaperone Hop and its complexes with Hsp90. J. Mol. Biol. 2008, 379, 732-744.
    • (2008) J. Mol. Biol , vol.379 , pp. 732-744
    • Onuoha, S.C.1    Coulstock, E.T.2    Grossmann, J.G.3    Jackson, S.E.4
  • 55
    • 34249041590 scopus 로고    scopus 로고
    • Definition of the minimal fragments of Sti1 required for dimerization, interaction with Hsp70 and Hsp90 and in vivo functions
    • Flom, G.; Behal, R. H.; Rosen, L.; Cole, D. G.; Johnson, J. L. Definition of the minimal fragments of Sti1 required for dimerization, interaction with Hsp70 and Hsp90 and in vivo functions. Biochem J. 2007, 404, 159-167.
    • (2007) Biochem J , vol.404 , pp. 159-167
    • Flom, G.1    Behal, R.H.2    Rosen, L.3    Cole, D.G.4    Johnson, J.L.5
  • 58
    • 33846181647 scopus 로고    scopus 로고
    • Nucleotide-dependent interaction of Saccharomyces cerevisiae Hsp90 with the cochaperone proteins Sti1, Cpr6, and Sba1
    • Johnson, J. L.; Halas, A.; Flom, G. Nucleotide-dependent interaction of Saccharomyces cerevisiae Hsp90 with the cochaperone proteins Sti1, Cpr6, and Sba1. Mol. Cell Biol. 2007, 27, 768-76.
    • (2007) Mol. Cell Biol , vol.27 , pp. 768-776
    • Johnson, J.L.1    Halas, A.2    Flom, G.3
  • 59
    • 12344291243 scopus 로고    scopus 로고
    • Pearl, L. H. Hsp90 and Cdc37 - a chaperone cancer conspiracy. Curr. Opin. Genet. Dev. 2005, 15, 55-61.
    • Pearl, L. H. Hsp90 and Cdc37 - a chaperone cancer conspiracy. Curr. Opin. Genet. Dev. 2005, 15, 55-61.
  • 60
    • 33846651282 scopus 로고    scopus 로고
    • Molecular chaperones and protein kinase quality control
    • Caplan, A. J.; Mandal, A. K.; Theodoraki, M. A. Molecular chaperones and protein kinase quality control. Trends Cell Biol. 2007, 17, 87-92.
    • (2007) Trends Cell Biol , vol.17 , pp. 87-92
    • Caplan, A.J.1    Mandal, A.K.2    Theodoraki, M.A.3
  • 61
    • 38449090443 scopus 로고    scopus 로고
    • Cdc37 regulation of the kinome: When to hold 'em and when to fold 'em
    • Karnitz, L. M.; Felts, S. J. Cdc37 regulation of the kinome: when to hold 'em and when to fold 'em. Sci. STKE 2007, 385.
    • (2007) Sci. STKE , vol.385
    • Karnitz, L.M.1    Felts, S.J.2
  • 62
    • 33746628448 scopus 로고    scopus 로고
    • Hsp90 inhibition transiently activates Src kinase and promotes Src-dependent Akt and Erk activation
    • Koga, F.; Xu, W.; Karpova, T. S.; Mcnally, J. G.; Baron, R.; Neckers, L. Hsp90 inhibition transiently activates Src kinase and promotes Src-dependent Akt and Erk activation. Proc. Natl. Acad. Sci. USA 2006, 103, 11318-22.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11318-11322
    • Koga, F.1    Xu, W.2    Karpova, T.S.3    Mcnally, J.G.4    Baron, R.5    Neckers, L.6
  • 63
    • 33845804718 scopus 로고    scopus 로고
    • Loss of Hsp90 association up-regulates Src-dependent ErbB2 activity
    • Xu, W.; Yuan, X.; Beebe, K.; Xiang, Z.; Neckers, L. Loss of Hsp90 association up-regulates Src-dependent ErbB2 activity. Mol. Cell Biol. 2007, 27, 220-228.
    • (2007) Mol. Cell Biol , vol.27 , pp. 220-228
    • Xu, W.1    Yuan, X.2    Beebe, K.3    Xiang, Z.4    Neckers, L.5
  • 64
    • 36148967696 scopus 로고    scopus 로고
    • Signal responsiveness of IkappaB kinases is determined by Cdc37-assisted transient interaction with Hsp90
    • Hinz, M.; Broemer, M.; Arslan, S. C.; Otto, A.; Mueller, E. C.; Dettmer, R.; Scheidereit, C. Signal responsiveness of IkappaB kinases is determined by Cdc37-assisted transient interaction with Hsp90. J. Biol. Chem .2007, 282, 32311-32319.
    • (2007) J. Biol. Chem , vol.282 , pp. 32311-32319
    • Hinz, M.1    Broemer, M.2    Arslan, S.C.3    Otto, A.4    Mueller, E.C.5    Dettmer, R.6    Scheidereit, C.7
  • 65
    • 48249099342 scopus 로고    scopus 로고
    • Critical regulation of TGFbeta signaling by Hsp90
    • Wrighton, K. H.; Lin, X.; Feng, X. H. Critical regulation of TGFbeta signaling by Hsp90. Proc. Natl. Acad. Sci. USA 2008, 105, 9244-9249.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 9244-9249
    • Wrighton, K.H.1    Lin, X.2    Feng, X.H.3
  • 68
    • 0026669310 scopus 로고
    • The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity
    • Miyata, Y.; Yahara, I. The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity. J. Biol. Chem. 1992, 267, 7042-7047.
    • (1992) J. Biol. Chem , vol.267 , pp. 7042-7047
    • Miyata, Y.1    Yahara, I.2
  • 69
    • 0029063877 scopus 로고
    • Interaction between casein kinase II and the 90-kDa stress protein, HSP90
    • Miyata, Y.; Yahara, I. Interaction between casein kinase II and the 90-kDa stress protein, HSP90. Biochemistry 1995, 34, 8123-8129.
    • (1995) Biochemistry , vol.34 , pp. 8123-8129
    • Miyata, Y.1    Yahara, I.2
  • 70
    • 0037155901 scopus 로고    scopus 로고
    • Involvement of Hsp90 in signaling and stability of 3-phosphoinositide-dependent kinase-1
    • Fujita, N.; Sato, S.; Ishida, A.; Tsuruo, T. Involvement of Hsp90 in signaling and stability of 3-phosphoinositide-dependent kinase-1. J. Biol. Chem. 2002, 277, 10346-10353.
    • (2002) J. Biol. Chem , vol.277 , pp. 10346-10353
    • Fujita, N.1    Sato, S.2    Ishida, A.3    Tsuruo, T.4
  • 71
    • 0034718540 scopus 로고    scopus 로고
    • Modulation of Akt kinase activity by binding to Hsp90
    • Sato, S.; Fujita, N.; Tsuruo, T. Modulation of Akt kinase activity by binding to Hsp90. Proc. Natl. Acad. Sci. USA 2000, 97, 10832-10837.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10832-10837
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 73
    • 15544372341 scopus 로고    scopus 로고
    • Surface charge and hydrophobicity determine ErbB2 binding to the Hsp90 chaperone complex
    • Xu, W.; Yuan, X.; Xiang, Z.; Mimnaugh, E.; Marcu, M.; Neckers, L. Surface charge and hydrophobicity determine ErbB2 binding to the Hsp90 chaperone complex. Nat. Struct. Mol. Biol. 2005, 12, 120-126.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 120-126
    • Xu, W.1    Yuan, X.2    Xiang, Z.3    Mimnaugh, E.4    Marcu, M.5    Neckers, L.6
  • 74
    • 4544254444 scopus 로고    scopus 로고
    • Definition of protein kinase sequence motifs that trigger high affinity binding of Hsp90 and Cdc37
    • Prince, T.; Matts, R. L. Definition of protein kinase sequence motifs that trigger high affinity binding of Hsp90 and Cdc37. J. Biol. Chem. 2004, 279, 39975-39981.
    • (2004) J. Biol. Chem , vol.279 , pp. 39975-39981
    • Prince, T.1    Matts, R.L.2
  • 75
    • 1842477464 scopus 로고    scopus 로고
    • Identification of a conserved sequence motif that promotes Cdc37 and cyclin D1 binding to Cdk4
    • Zhao, Q.; Boschelli, F.; Caplan, A. J.; Arndt, K. T. Identification of a conserved sequence motif that promotes Cdc37 and cyclin D1 binding to Cdk4. J. Biol. Chem. 2004, 279, 12560-12564.
    • (2004) J. Biol. Chem , vol.279 , pp. 12560-12564
    • Zhao, Q.1    Boschelli, F.2    Caplan, A.J.3    Arndt, K.T.4
  • 78
    • 63549083573 scopus 로고    scopus 로고
    • Sreeramulu, S.; Jonker, H. R. A.; Langer, T.; Richter, C.; Roy,; Schwalbe, H. The human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopy. J. Biol. Chem. 2009, 284, 3885-3896.
    • Sreeramulu, S.; Jonker, H. R. A.; Langer, T.; Richter, C.; Roy,; Schwalbe, H. The human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopy. J. Biol. Chem. 2009, 284, 3885-3896.
  • 79
    • 64149128633 scopus 로고    scopus 로고
    • The chaperones Hsp90 and Cdc37 mediate the maturation and stabilization of protein kinase C through a conserved PXXP motif in the C-terminal tail
    • Gould, C. M.; Kannan, N.; Taylor, S. S.; Newton, A. C. The chaperones Hsp90 and Cdc37 mediate the maturation and stabilization of protein kinase C through a conserved PXXP motif in the C-terminal tail. J. Biol. Chem. 2009, 284, 4921-4935.
    • (2009) J. Biol. Chem , vol.284 , pp. 4921-4935
    • Gould, C.M.1    Kannan, N.2    Taylor, S.S.3    Newton, A.C.4
  • 80
    • 53149118242 scopus 로고    scopus 로고
    • The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts
    • Pratt, W. B.; Morishima, Y.; Osawa, Y. The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts. J. Biol. Chem. 2008, 283, 22885-22889.
    • (2008) J. Biol. Chem , vol.283 , pp. 22885-22889
    • Pratt, W.B.1    Morishima, Y.2    Osawa, Y.3
  • 81
    • 54349122449 scopus 로고    scopus 로고
    • Structural and functional coupling of Hsp90- and Sgt1-centred multi-protein complexes
    • Zhang, M.; Boter, M.; Li, K.; Kadota, Y.; Panaretou, B.; Prodromou, C.; Shirasu, K.; Pearl, L. H. Structural and functional coupling of Hsp90- and Sgt1-centred multi-protein complexes. EMBO J. 2008, 27, 2789-2798.
    • (2008) EMBO J , vol.27 , pp. 2789-2798
    • Zhang, M.1    Boter, M.2    Li, K.3    Kadota, Y.4    Panaretou, B.5    Prodromou, C.6    Shirasu, K.7    Pearl, L.H.8
  • 82
    • 45849120595 scopus 로고    scopus 로고
    • Understanding ligand-based modulation of the Hsp90 molecular chaperone dynamics at atomic resolution
    • Colombo, G.; Morra, G.; Meli, M.; Verkhivker, G. Understanding ligand-based modulation of the Hsp90 molecular chaperone dynamics at atomic resolution. Proc. Natl. Acad. Sci. USA 2008, 105, 7976-7981.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7976-7981
    • Colombo, G.1    Morra, G.2    Meli, M.3    Verkhivker, G.4
  • 83
    • 63549104682 scopus 로고    scopus 로고
    • Morra, G.; Verkhivker, G.; Colombo, G. Modeling signal propagation mechanisms and ligand-based conformational dynamics of the Hsp90 molecular chaperone full-length dimer. PLoS Comput. Biol . 2009, 5, e1000323.
    • Morra, G.; Verkhivker, G.; Colombo, G. Modeling signal propagation mechanisms and ligand-based conformational dynamics of the Hsp90 molecular chaperone full-length dimer. PLoS Comput. Biol . 2009, 5, e1000323.
  • 84
    • 65349192770 scopus 로고    scopus 로고
    • Ho, B. K.; Agard, D. A. Probing the flexibility of large conformational changes in protein structures through local perturbations. PLoS Comput. Biol. 2009, 5, e1000343.
    • Ho, B. K.; Agard, D. A. Probing the flexibility of large conformational changes in protein structures through local perturbations. PLoS Comput. Biol. 2009, 5, e1000343.
  • 85
    • 0033970020 scopus 로고    scopus 로고
    • Folding and binding cascades: Dynamic landscapes and population shifts
    • Kumar, S.; Ma, B.; Tsai, C. J.; Sinha, N.; Nussinov, R. Folding and binding cascades: dynamic landscapes and population shifts. Protein Sci. 2000, 9, 10-19.
    • (2000) Protein Sci , vol.9 , pp. 10-19
    • Kumar, S.1    Ma, B.2    Tsai, C.J.3    Sinha, N.4    Nussinov, R.5
  • 86
    • 0345743709 scopus 로고    scopus 로고
    • Protein folding topology determines binding mechanism
    • Levy, Y.; Wolynes, P. G.; Onuchic, J. N. Protein folding topology determines binding mechanism. Proc. Natl.Acad. Sci. USA 2004, 101, 511-516.
    • (2004) Proc. Natl.Acad. Sci. USA , vol.101 , pp. 511-516
    • Levy, Y.1    Wolynes, P.G.2    Onuchic, J.N.3
  • 88
    • 0037627721 scopus 로고    scopus 로고
    • Simulating disorder - order transitions in molecular recognition of unstructured proteins : Where folding meets binding
    • Verkhivker, G. M.; Bouzida, D.; Gehlhaar, D. K.; Rejto, P. A.; Freer , S.T.; Rose, P. W. Simulating disorder - order transitions in molecular recognition of unstructured proteins : where folding meets binding. Proc. Natl. Acad. Sci. USA 2003, 100, 5148-5153.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5148-5153
    • Verkhivker, G.M.1    Bouzida, D.2    Gehlhaar, D.K.3    Rejto, P.A.4    Freer, S.T.5    Rose, P.W.6
  • 89
    • 0038266221 scopus 로고    scopus 로고
    • Energy landscape theory, funnels, specificity, and optimal criterion of biomolecular binding
    • Wang, J.; Verkhivker, G. M. Energy landscape theory, funnels, specificity, and optimal criterion of biomolecular binding. Phys. Rev. Lett. 2003, 90, 188101.
    • (2003) Phys. Rev. Lett , vol.90 , pp. 188101
    • Wang, J.1    Verkhivker, G.M.2
  • 90
  • 91
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder, H.; Sligar, S. G.; Wolynes, P. G. The energy landscapes and motions of proteins Science 1991, 254, 1598-1603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 92
    • 0041806720 scopus 로고    scopus 로고
    • Myoglobin: The hydrogen atom of biology and a paradigm of complexity
    • Frauenfelder, H.; Mcmahon, B. H.; Fenimore, P. W. Myoglobin: the hydrogen atom of biology and a paradigm of complexity. Proc. Natl. Acad. Sci. USA 2003, 100, 8615-8617.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8615-8617
    • Frauenfelder, H.1    Mcmahon, B.H.2    Fenimore, P.W.3
  • 93
    • 36849048228 scopus 로고    scopus 로고
    • Katherine,; Thai, V.; Lei, M.; Ott, M.; Watz, M. W.; Fenn, T.; Pozharski, E.; Wilson, M. A.; Petsko, G. A.; Karplus, M.; Hubner, C. G.; Kern, D. Intrinsic motions along an enzymatic reaction trajectory. Nature 2007, 450, 838-844.
    • Katherine,; Thai, V.; Lei, M.; Ott, M.; Watz, M. W.; Fenn, T.; Pozharski, E.; Wilson, M. A.; Petsko, G. A.; Karplus, M.; Hubner, C. G.; Kern, D. Intrinsic motions along an enzymatic reaction trajectory. Nature 2007, 450, 838-844.
  • 94
    • 36849039429 scopus 로고    scopus 로고
    • A hierarchy of timescales in protein dynamics is linked to enzyme catalysis
    • Katherine,; Lei, M.; Thai, V.; Kerns, J. S.; Karplus, M.; Kern, D. A hierarchy of timescales in protein dynamics is linked to enzyme catalysis. Nature 2007, 450, 913-916.
    • (2007) Nature , vol.450 , pp. 913-916
    • Katherine1    Lei, M.2    Thai, V.3    Kerns, J.S.4    Karplus, M.5    Kern, D.6
  • 97
    • 35548976322 scopus 로고    scopus 로고
    • Open-to-closed transition inapo maltose-binding protein observed by paramagnetic NMR
    • Tang, C.; Schwieters, C. D.; Clore, M. G. Open-to-closed transition inapo maltose-binding protein observed by paramagnetic NMR. Nature 2007, 449, 1078-1082.
    • (2007) Nature , vol.449 , pp. 1078-1082
    • Tang, C.1    Schwieters, C.D.2    Clore, M.G.3
  • 98
    • 0037470496 scopus 로고    scopus 로고
    • Antibody multispecificity mediated by conformational diversity
    • James, L. C.; Roversi, P.; Tawfik, D. S. Antibody multispecificity mediated by conformational diversity. Science 2003, 299, 1362-1367.
    • (2003) Science , vol.299 , pp. 1362-1367
    • James, L.C.1    Roversi, P.2    Tawfik, D.S.3
  • 99
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan, D.; Weinberg, R. A. The hallmarks of cancer. Cell 2000, 100, 57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 100
    • 0141819961 scopus 로고    scopus 로고
    • Genes and proteins governing the cellular sensitivity to HSP90 inhibitors: A mechanistic perspective
    • Maloney, A.; Clarke, P. A.; Workman, P. Genes and proteins governing the cellular sensitivity to HSP90 inhibitors: a mechanistic perspective. Curr. Cancer Drug Targets 2003, 3, 331-341.
    • (2003) Curr. Cancer Drug Targets , vol.3 , pp. 331-341
    • Maloney, A.1    Clarke, P.A.2    Workman, P.3
  • 101
    • 0037025173 scopus 로고    scopus 로고
    • Addiction to oncogenes-the Achilles heal of cancer
    • Weinstein, B. I. Addiction to oncogenes-the Achilles heal of cancer. Science 2002, 297, 63-64.
    • (2002) Science , vol.297 , pp. 63-64
    • Weinstein, B.I.1
  • 102
    • 37249003928 scopus 로고    scopus 로고
    • Oncogene addiction: Setting the stage for molecularly targeted cancer therapy
    • Sharma, S. V.; Settleman, J. Oncogene addiction: setting the stage for molecularly targeted cancer therapy. Genes Dev. 2007, 21, 3214-3231.
    • (2007) Genes Dev , vol.21 , pp. 3214-3231
    • Sharma, S.V.1    Settleman, J.2
  • 103
    • 33244484848 scopus 로고    scopus 로고
    • Targeting chaperones in transformed systems-a focus on Hsp90 and cancer
    • Chiosis, G. Targeting chaperones in transformed systems-a focus on Hsp90 and cancer. Expert Opin. Ther. Targets 2006, 10, 37-50.
    • (2006) Expert Opin. Ther. Targets , vol.10 , pp. 37-50
    • Chiosis, G.1
  • 104
    • 58849160500 scopus 로고    scopus 로고
    • Heat shock protein 90 as a drug target: Some like it hot
    • Banerji, U. Heat shock protein 90 as a drug target: some like it hot. Clin. Cancer Res. 2009, 15, 9-14.
    • (2009) Clin. Cancer Res , vol.15 , pp. 9-14
    • Banerji, U.1
  • 105
    • 33745174538 scopus 로고    scopus 로고
    • Heat shock protein-90 inhibitors: A chronicle from geldanamycin to today's agents
    • Chiosis, G.; Lopes, E. C.; Solit, D. Heat shock protein-90 inhibitors: a chronicle from geldanamycin to today's agents. Curr. Opin. Investig. Drugs 2006, 7, 534-541.
    • (2006) Curr. Opin. Investig. Drugs , vol.7 , pp. 534-541
    • Chiosis, G.1    Lopes, E.C.2    Solit, D.3
  • 106
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • Kamal, A.; Thao, L.; Sensintaffar, J.; Zhang, L.; Boehm, M. F.; Fritz, L.C.; Burrows, F. J. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 2003, 425, 407-410.
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1    Thao, L.2    Sensintaffar, J.3    Zhang, L.4    Boehm, M.F.5    Fritz, L.C.6    Burrows, F.J.7
  • 107
    • 2642521990 scopus 로고    scopus 로고
    • Therapeutic and diagnostic implications of Hsp90 activation
    • Kamal, A.; Boehm, M. F.; Burrows, F. J. Therapeutic and diagnostic implications of Hsp90 activation. Trends Mol. Med. 2004, 10, 283-290.
    • (2004) Trends Mol. Med , vol.10 , pp. 283-290
    • Kamal, A.1    Boehm, M.F.2    Burrows, F.J.3
  • 108
    • 0141708701 scopus 로고    scopus 로고
    • Natural product origins of Hsp90 inhibitors
    • Uehara, Y. Natural product origins of Hsp90 inhibitors. Curr. Cancer Drug Targets 2003, 3, 325-330.
    • (2003) Curr. Cancer Drug Targets , vol.3 , pp. 325-330
    • Uehara, Y.1
  • 109
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • Whitesell, L.; Mimnaugh, E. G.; De Costa, B.; Myers, C. E.; Neckers, L. M. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc. Natl. Acad. Sci. USA 1994, 91, 8324-8.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 110
    • 0028828273 scopus 로고
    • Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent
    • Smith, D. F.; Whitesell, L.; Nair, S. C.; Chen, S.; Prapapanich, V.; Rimerman, R.A.; Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent. Mol. Cell Biol. 1995, 15, 6804-6812.
    • (1995) Mol. Cell Biol , vol.15 , pp. 6804-6812
    • Smith, D.F.1    Whitesell, L.2    Nair, S.C.3    Chen, S.4    Prapapanich, V.5    Rimerman, R.A.6
  • 111
    • 0032554763 scopus 로고    scopus 로고
    • Sharma, S. V.; Agatsuma, T.; Nakano, H. argeting of the protein chaperone, Hsp90, by the transformation suppressing agent, radicicol. Oncogene 1998, 16, 2639-2645.
    • Sharma, S. V.; Agatsuma, T.; Nakano, H. argeting of the protein chaperone, Hsp90, by the transformation suppressing agent, radicicol. Oncogene 1998, 16, 2639-2645.
  • 113
    • 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. 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    Piper, P.W.7    Pearl, L.H.8
  • 114
    • 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
  • 115
    • 0042855994 scopus 로고    scopus 로고
    • 17AAG: Low target binding affinity and potent cell activity-finding an explanation
    • Chiosis, G.; Huezo, H.; Rosen, N.; Mimnaugh, E.; Whitesell, L.; Neckers, L. 17AAG: low target binding affinity and potent cell activity-finding an explanation. Mol. Cancer Ther. 2003, 2, 123-129.
    • (2003) Mol. Cancer Ther , vol.2 , pp. 123-129
    • Chiosis, G.1    Huezo, H.2    Rosen, N.3    Mimnaugh, E.4    Whitesell, L.5    Neckers, L.6
  • 116
    • 0043269344 scopus 로고    scopus 로고
    • Auditing the pharmacological accounts for Hsp90 molecular chaperone inhibitors: Unfolding the relationship between pharmacokinetics and pharmacodynamics
    • Workman, P. Auditing the pharmacological accounts for Hsp90 molecular chaperone inhibitors: unfolding the relationship between pharmacokinetics and pharmacodynamics. Mol. Cancer Ther. 2003, 2, 131-138.
    • (2003) Mol. Cancer Ther , vol.2 , pp. 131-138
    • Workman, P.1
  • 117
    • 0035872442 scopus 로고    scopus 로고
    • Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17- demethoxygeldanamycin results in cytostasis and apoptosis
    • Hostein, I.; Robertson, D.; Distefano, F.; Workman, P.; Clarke, P. A. Inhibition of signal transduction by the Hsp90 inhibitor 17-allylamino-17- demethoxygeldanamycin results in cytostasis and apoptosis. Cancer Res. 2001, 61, 4003-4009.
    • (2001) Cancer Res , vol.61 , pp. 4003-4009
    • Hostein, I.1    Robertson, D.2    Distefano, F.3    Workman, P.4    Clarke, P.A.5
  • 120
    • 21244466289 scopus 로고    scopus 로고
    • Comparison of 17 dimethylaminoethylamino-17-demethoxygeldanamycin (17DMAG) and 17-allylamino-17-demethoxygeldanamycin (17AAG) in vitro: Effects on Hsp90 and client proteins in melanoma models
    • Smith, V.; Sausville, E. A.; Camalier, R. F.; Fiebig, H. H.; Burger, A. M. Comparison of 17 dimethylaminoethylamino-17-demethoxygeldanamycin (17DMAG) and 17-allylamino-17-demethoxygeldanamycin (17AAG) in vitro: effects on Hsp90 and client proteins in melanoma models. Cancer Chemother. Pharmacol. 2005, 56, 126-137.
    • (2005) Cancer Chemother. Pharmacol , vol.56 , pp. 126-137
    • Smith, V.1    Sausville, E.A.2    Camalier, R.F.3    Fiebig, H.H.4    Burger, A.M.5
  • 122
    • 33751258297 scopus 로고    scopus 로고
    • Sydor, J. R.; Normant, E.; Pien, C. S.; Porter, J. R.; Ge, J.; Grenier, L.; Pak, R. H.; Ali, J. A.; Dembski, M. S.; Hudak, J.; Patterson, J.; Penders, C.; Pink, M.; Read, M. A.; Sang, J.; Woodward, C.; Zhang, Y.; Grayzel, D. S.; Wright, J.; Barrett, J. A.; Palombella, V. J.; Adams, J.; Tong, J. K. Development of 17-allylamino-17 demethoxy-geldanamycin hydroquinone hydrochloride (IPI-504), an anti-cancer agent directed against Hsp90. Proc. Natl. Acad. Sci. USA 2006, 103, 17408-17413.
    • Sydor, J. R.; Normant, E.; Pien, C. S.; Porter, J. R.; Ge, J.; Grenier, L.; Pak, R. H.; Ali, J. A.; Dembski, M. S.; Hudak, J.; Patterson, J.; Penders, C.; Pink, M.; Read, M. A.; Sang, J.; Woodward, C.; Zhang, Y.; Grayzel, D. S.; Wright, J.; Barrett, J. A.; Palombella, V. J.; Adams, J.; Tong, J. K. Development of 17-allylamino-17 demethoxy-geldanamycin hydroquinone hydrochloride (IPI-504), an anti-cancer agent directed against Hsp90. Proc. Natl. Acad. Sci. USA 2006, 103, 17408-17413.
  • 123
    • 0344511727 scopus 로고    scopus 로고
    • Crystal structure and molecular modeling of 17-DMAG in complex with human Hsp90
    • Jez, J. M.; Chen, J. C. H.; Rastelli, G.; Stroud, R. M.; Santi, D. V. Crystal structure and molecular modeling of 17-DMAG in complex with human Hsp90. Chem. Biol.2003, 10, 361-368.
    • (2003) Chem. Biol , vol.10 , pp. 361-368
    • Jez, J.M.1    Chen, J.C.H.2    Rastelli, G.3    Stroud, R.M.4    Santi, D.V.5
  • 125
  • 126
    • 64749110949 scopus 로고    scopus 로고
    • Structure-based design of molecular cancer therapeutics
    • van Montfort, R. L. M.; Workman, P. Structure-based design of molecular cancer therapeutics. Trends Biotechnol. 2009, 27, 315-228.
    • (2009) Trends Biotechnol , vol.27 , pp. 315-228
    • van Montfort, R.L.M.1    Workman, P.2
  • 127
    • 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, P. N.; Zheng, F.F.; Lorenzino, S.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, P.N.4    Zheng, F.F.5    Lorenzino, S.L.6    Rosen, N.7
  • 132
    • 34248166042 scopus 로고    scopus 로고
    • Sharp, S. Y.; Prodromou, C.; Boxall, K.; Powers, M. V.; Holmes, J. L.; Box, G.; Matthews, T. P.; Ming, K.; Kalusa, A.; James, K.; Hayes, A.; Hardcastle, A.; Dymock, B., Brough, P. A., Barril, X., Cansfield, J. E., Wright, L., Surgenor, A., Foloppe, N.; Hubbard, R. E.; Aherne, W.; Pearl, L.; Jones, K.; Mcdonald, E.; Raynaud, F.; Eccles, S.; Drysdale, M.; Workman, P. Inhibition of the heat shock protein 90 molecular chaperone in vitro and in vivo by novel, synthetic, potent resorcinylic pyrazole/isoxazole amide analogues. Mol. Cancer Ther. 2007, 6, 1198-1211.
    • Sharp, S. Y.; Prodromou, C.; Boxall, K.; Powers, M. V.; Holmes, J. L.; Box, G.; Matthews, T. P.; Ming, K.; Kalusa, A.; James, K.; Hayes, A.; Hardcastle, A.; Dymock, B., Brough, P. A., Barril, X., Cansfield, J. E., Wright, L., Surgenor, A., Foloppe, N.; Hubbard, R. E.; Aherne, W.; Pearl, L.; Jones, K.; Mcdonald, E.; Raynaud, F.; Eccles, S.; Drysdale, M.; Workman, P. Inhibition of the heat shock protein 90 molecular chaperone in vitro and in vivo by novel, synthetic, potent resorcinylic pyrazole/isoxazole amide analogues. Mol. Cancer Ther. 2007, 6, 1198-1211.
  • 133
    • 38349157746 scopus 로고    scopus 로고
    • Brough, P. A.; Aherne, W.; Barril, X.; Borgognoni, J.; Boxall, K.; Cansfield, J. E.; Kwai Collins, I.; Davies, N. G. M.; Drysdale, M. J.; Dymock, B.; Eccles, S. A.; Finch, H.; Fink, A.; Hayes, A.; Howes, R.; Hubbard, R. E.; James, K.; Jordan, A. M.; Lockie, A.; Martins, V.; Massey, A.; Matthews, T. P.; Mcdonald, E.; Northfield, C. J.; Pearl, L. H.; Prodromou, C.; Ray, S.; Raynaud, F. I.; Roughley, S. D.; Sharp, S. Y.; Surgenor, A.; Walmsley, L. D.; Webb, P.; Wood, M.; Workman, P.; Wright, L. 4,5-diarylisoxazole Hsp90 chaperone inhibitors: potential therapeutic agents for the treatment of cancer. J. Med. Chem. 2008, 51, 196-218.
    • Brough, P. A.; Aherne, W.; Barril, X.; Borgognoni, J.; Boxall, K.; Cansfield, J. E.; Kwai Collins, I.; Davies, N. G. M.; Drysdale, M. J.; Dymock, B.; Eccles, S. A.; Finch, H.; Fink, A.; Hayes, A.; Howes, R.; Hubbard, R. E.; James, K.; Jordan, A. M.; Lockie, A.; Martins, V.; Massey, A.; Matthews, T. P.; Mcdonald, E.; Northfield, C. J.; Pearl, L. H.; Prodromou, C.; Ray, S.; Raynaud, F. I.; Roughley, S. D.; Sharp, S. Y.; Surgenor, A.; Walmsley, L. D.; Webb, P.; Wood, M.; Workman, P.; Wright, L. 4,5-diarylisoxazole Hsp90 chaperone inhibitors: potential therapeutic agents for the treatment of cancer. J. Med. Chem. 2008, 51, 196-218.
  • 134
    • 42349084306 scopus 로고    scopus 로고
    • Eccles, S. A.; Massey, A.; Raynaud, F. I.; Sharp, S. Y.; Box, G.; Valenti, M.; Patterson, L.; de Haven Brandon, Gowan, S.; Boxall, F.; Aherne, W.; Rowlands, M.; Hayes, A.; Martins, V.; Urban, F.; Boxall, K.; Prodromou, C.; Pearl, L.; James, K.; Matthews, T. P.; Cheung, K. M.; Kalusa, A.; Jones, K.; Mcdonald, E.; Barril, X.; Brough, P. A.; Cansfield, J. E.; Dymock, B.; Drysdale, M. J.; Finch, H.; Howes, R.; Hubbard, R. E.; Surgenor, A.; Webb, P.; Wood, M.; Wright, L.; Workman, P. NVP-AUY922: a novel heat shock protein 90 inhibitor active against xenograft tumor growth, angiogenesis, and metastasis. Cancer Res. 2008, 68, 2850-2860.
    • Eccles, S. A.; Massey, A.; Raynaud, F. I.; Sharp, S. Y.; Box, G.; Valenti, M.; Patterson, L.; de Haven Brandon, Gowan, S.; Boxall, F.; Aherne, W.; Rowlands, M.; Hayes, A.; Martins, V.; Urban, F.; Boxall, K.; Prodromou, C.; Pearl, L.; James, K.; Matthews, T. P.; Cheung, K. M.; Kalusa, A.; Jones, K.; Mcdonald, E.; Barril, X.; Brough, P. A.; Cansfield, J. E.; Dymock, B.; Drysdale, M. J.; Finch, H.; Howes, R.; Hubbard, R. E.; Surgenor, A.; Webb, P.; Wood, M.; Wright, L.; Workman, P. NVP-AUY922: a novel heat shock protein 90 inhibitor active against xenograft tumor growth, angiogenesis, and metastasis. Cancer Res. 2008, 68, 2850-2860.
  • 137
    • 35148840116 scopus 로고    scopus 로고
    • A novel class of Hsp90 inhibitors isolated by structure-based virtual screening
    • Park, H.; Kim, Y. J.; Hahn, J. S. A novel class of Hsp90 inhibitors isolated by structure-based virtual screening. Bioorg. Med. Chem. Lett. 2007, 17, 6345-6349.
    • (2007) Bioorg. Med. Chem. Lett , vol.17 , pp. 6345-6349
    • Park, H.1    Kim, Y.J.2    Hahn, J.S.3
  • 141
    • 33746914732 scopus 로고    scopus 로고
    • Structural and quantum chemical studies of 8-aryl-sulfanyl adenine class Hsp90 inhibitors
    • Immormino, R. M.; Kang, Y.; Chiosis, G.; Gewirth, D. T. Structural and quantum chemical studies of 8-aryl-sulfanyl adenine class Hsp90 inhibitors. J. Med. Chem. 2006, 49, 4953-6490.
    • (2006) J. Med. Chem , vol.49 , pp. 4953-6490
    • Immormino, R.M.1    Kang, Y.2    Chiosis, G.3    Gewirth, D.T.4
  • 143
    • 55749083540 scopus 로고    scopus 로고
    • Kung, P. P.; Funk, L.; Meng, J.; Collins, M.; Zhou, J. Z.; Johnson, C. M.; Ekker, A.; Wang, J.; Mehta, P.; Yin, M. J.; Rodgers, C.; Jay, Bayman, E.; Smeal, T.; Maegley, K. A.; Gehring, M. R. Dihydroxylphenyl amides as inhibitors of the Hsp90 molecular chaperone. Bioorg. Med. Chem. Lett. 2008, 18, 6273-6278.
    • Kung, P. P.; Funk, L.; Meng, J.; Collins, M.; Zhou, J. Z.; Johnson, C. M.; Ekker, A.; Wang, J.; Mehta, P.; Yin, M. J.; Rodgers, C.; Jay, Bayman, E.; Smeal, T.; Maegley, K. A.; Gehring, M. R. Dihydroxylphenyl amides as inhibitors of the Hsp90 molecular chaperone. Bioorg. Med. Chem. Lett. 2008, 18, 6273-6278.
  • 147
    • 67349154388 scopus 로고    scopus 로고
    • Different poses for ligand and chaperone in inhibitor-bound Hsp90 and GRP94: Implications for paralog-specific drug design
    • Immormino, R. M.; 4th Metzger, L. E.; Reardon, P. N.; Dollins, D. E.; Blagg, B. S. J.; Gewirth, D. T. Different poses for ligand and chaperone in inhibitor-bound Hsp90 and GRP94: implications for paralog-specific drug design. J. Mol. Biol. 2009, 388, 1033-1042.
    • (2009) J. Mol. Biol , vol.388 , pp. 1033-1042
    • Immormino 4th, R.M.1    Metzger, L.E.2    Reardon, P.N.3    Dollins, D.E.4    Blagg, B.S.J.5    Gewirth, D.T.6
  • 149
    • 4344632851 scopus 로고    scopus 로고
    • Virtual screening in structure-based drug discovery Mini Rev
    • Barril, X.; Hubbard, R. E.; Morley, S. D. Virtual screening in structure-based drug discovery Mini Rev. Med. Chem. 2004, 4, 779-791.
    • (2004) Med. Chem , vol.4 , pp. 779-791
    • Barril, X.1    Hubbard, R.E.2    Morley, S.D.3
  • 150
    • 33847381100 scopus 로고    scopus 로고
    • A decade of fragment-based drug design: Strategic advances and lessons learned
    • Hajduk, P. J.; Greer, J. A decade of fragment-based drug design: strategic advances and lessons learned. Nat. Rev. Drug Discov. 2007, 6, 211-219.
    • (2007) Nat. Rev. Drug Discov , vol.6 , pp. 211-219
    • Hajduk, P.J.1    Greer, J.2
  • 151
    • 36248956723 scopus 로고    scopus 로고
    • The SeeDs approach: Integrating fragments into drug discovery
    • Hubbard, R. E.; Davis, B.; Chen, I.; Drysdale, M. J. The SeeDs approach: integrating fragments into drug discovery Curr. Top. Med. Chem. 2007, 7, 1568-1581.
    • (2007) Curr. Top. Med. Chem , vol.7 , pp. 1568-1581
    • Hubbard, R.E.1    Davis, B.2    Chen, I.3    Drysdale, M.J.4
  • 153
    • 68549115383 scopus 로고    scopus 로고
    • Brough, P.A.; Barril, X.; Borgognoni, J.; Chene, P.; Davies, N.G.; Davis, B.; Drysdale, M.J.; Dymock, B.; Eccles, S.A.; Garcia-Echeverria, C.; Fromont, C.; Hayes, A.; Hubbard, R.E.; Jordan, A.M.; Jensen, M.R.; Massey, A.; Merrett, A.; Padfield, A.; Parsons, R.; Radimerski, T.; Raynaud, F.I.; Robertson, A.; Roughley, S.D.; Schoepfer, J.; Simmonite, H.; Sharp, S.Y.; Surgenor, A.; Valenti, M.; Walls, S.; Webb, P.; Wood, M.; Workman, P.; Wright, L. Combining hit identification strategies: fragment-based and in silico approaches to orally active 2-aminothieno[2,3-d]pyrimidine Inhibitors of the Hsp90 Molecular Chaperone. J. Med. Chem. 2009, 52(15), 4794-4809.
    • Brough, P.A.; Barril, X.; Borgognoni, J.; Chene, P.; Davies, N.G.; Davis, B.; Drysdale, M.J.; Dymock, B.; Eccles, S.A.; Garcia-Echeverria, C.; Fromont, C.; Hayes, A.; Hubbard, R.E.; Jordan, A.M.; Jensen, M.R.; Massey, A.; Merrett, A.; Padfield, A.; Parsons, R.; Radimerski, T.; Raynaud, F.I.; Robertson, A.; Roughley, S.D.; Schoepfer, J.; Simmonite, H.; Sharp, S.Y.; Surgenor, A.; Valenti, M.; Walls, S.; Webb, P.; Wood, M.; Workman, P.; Wright, L. Combining hit identification strategies: fragment-based and in silico approaches to orally active 2-aminothieno[2,3-d]pyrimidine Inhibitors of the Hsp90 Molecular Chaperone. J. Med. Chem. 2009, 52(15), 4794-4809.
  • 154
    • 65249117573 scopus 로고    scopus 로고
    • Integration of ligand and structure-based virtual screening for the identification of the first dual targeting agent for heat shock protein 90 (Hsp90) and tubulin
    • Knox, A. J. S.; Price, T.; Pawlak, M.; Golfis, G.; Flood, C. T.; Fayne, D.; Williams, D. C.; Meegan, M. J.; Lloyd, D. G. Integration of ligand and structure-based virtual screening for the identification of the first dual targeting agent for heat shock protein 90 (Hsp90) and tubulin. J. Med. Chem. 2009, 52, 2177-2180.
    • (2009) J. Med. Chem , vol.52 , pp. 2177-2180
    • Knox, A.J.S.1    Price, T.2    Pawlak, M.3    Golfis, G.4    Flood, C.T.5    Fayne, D.6    Williams, D.C.7    Meegan, M.J.8    Lloyd, D.G.9
  • 155
    • 67651108949 scopus 로고    scopus 로고
    • Identification of new Hsp90 inhibitors by structure-based virtual screening
    • Hong, T. J.; Park, H.; Kim, Y. J.; Jeong, J. H.; Hahn, J. S. Identification of new Hsp90 inhibitors by structure-based virtual screening. Bioorg. Med. Chem. Lett. 2009, 19, 4839-4842.
    • (2009) Bioorg. Med. Chem. Lett , vol.19 , pp. 4839-4842
    • Hong, T.J.1    Park, H.2    Kim, Y.J.3    Jeong, J.H.4    Hahn, J.S.5
  • 157
    • 67650741952 scopus 로고    scopus 로고
    • Huang, K. H.; Veal, J. M.; Fadden, R. P.; Rice, J. W.; Eaves, J.; Strachan, J. P.; Barabasz, A. F.; Foley, B. E.; Barta, T. E.; Ma, W.; Silinski, M. A.; Hu, M.; Partridge, J. M.; Scott, A.; Dubois, L. G.; Freed, T.; Steed, P. M.; Ommen, A. J.; Smith, E. D.; Hughes, P. F.; Woodward, A. R.; Hanson, G. J.; Mccall, W. S.; Markworth, C. J.; Hinkley, L.; Jenks, M.; Geng, L.; Lewis, M.; Otto, J.; Pronk, B.; Verleysen, K.; Hall, S. E. Discovery of novel 2-aminobenzamide inhibitors of heat shock protein 90 as potent, selective and orally active antitumor agents. J. Med. Chem. 2009, 52, 4288-4305.
    • Huang, K. H.; Veal, J. M.; Fadden, R. P.; Rice, J. W.; Eaves, J.; Strachan, J. P.; Barabasz, A. F.; Foley, B. E.; Barta, T. E.; Ma, W.; Silinski, M. A.; Hu, M.; Partridge, J. M.; Scott, A.; Dubois, L. G.; Freed, T.; Steed, P. M.; Ommen, A. J.; Smith, E. D.; Hughes, P. F.; Woodward, A. R.; Hanson, G. J.; Mccall, W. S.; Markworth, C. J.; Hinkley, L.; Jenks, M.; Geng, L.; Lewis, M.; Otto, J.; Pronk, B.; Verleysen, K.; Hall, S. E. Discovery of novel 2-aminobenzamide inhibitors of heat shock protein 90 as potent, selective and orally active antitumor agents. J. Med. Chem. 2009, 52, 4288-4305.
  • 158
    • 67349273712 scopus 로고    scopus 로고
    • The HSP90 binding mode of a radicicol-like E-oxime determined by docking, binding free energy estimations, and NMR 15N chemical shifts
    • Spichty, M.; Taly, A.; Hagn, F.; Kessler, H.; Barluenga, S.; Winssinger, N.; Karplus, M. The HSP90 binding mode of a radicicol-like E-oxime determined by docking, binding free energy estimations, and NMR 15N chemical shifts. Biophys. Chem. 2009, 143, 111-23.
    • (2009) Biophys. Chem , vol.143 , pp. 111-123
    • Spichty, M.1    Taly, A.2    Hagn, F.3    Kessler, H.4    Barluenga, S.5    Winssinger, N.6    Karplus, M.7
  • 159
    • 58849127710 scopus 로고    scopus 로고
    • Inside the Hsp90 inhibitors binding mode through induced fit docking
    • Lauria, A.; Ippolito, M.; Almerico, A. M. Inside the Hsp90 inhibitors binding mode through induced fit docking. J. Mol. Graph. Model. 2009, 27, 712-722.
    • (2009) J. Mol. Graph. Model , vol.27 , pp. 712-722
    • Lauria, A.1    Ippolito, M.2    Almerico, A.M.3
  • 160
    • 70349194386 scopus 로고    scopus 로고
    • Principal component analysis on molecular descriptors as an alternative point of view in the search of new Hsp90 inhibitors
    • July 23, Epub ahead of print
    • Lauria, A.; Ippolito, M.; Almerico, A.M. Principal component analysis on molecular descriptors as an alternative point of view in the search of new Hsp90 inhibitors. Comput. Biol. Chem. 2009, July 23, [Epub ahead of print]
    • (2009) Comput. Biol. Chem
    • Lauria, A.1    Ippolito, M.2    Almerico, A.M.3
  • 161
    • 33846108633 scopus 로고    scopus 로고
    • Liu, T.; Lin, Y.; Wen, X.; Jorissen, R. N.; Gilson, M. K. BindingDB: a web-accessible database of experimentally determined protein-ligand binding affinities. Nucleic Acids Res. 2007, 35, D198-D201.
    • Liu, T.; Lin, Y.; Wen, X.; Jorissen, R. N.; Gilson, M. K. BindingDB: a web-accessible database of experimentally determined protein-ligand binding affinities. Nucleic Acids Res. 2007, 35, D198-D201.
  • 162
    • 37649024109 scopus 로고    scopus 로고
    • Development and application of Hsp90 inhibitors
    • Solit, D. B.; Chiosis. G. Development and application of Hsp90 inhibitors. Drug Discov. Today 2008, 13, 38-43.
    • (2008) Drug Discov. Today , vol.13 , pp. 38-43
    • Solit, D.B.1    Chiosis, G.2
  • 163
    • 51449093764 scopus 로고    scopus 로고
    • Targeting Hsp90: Small molecule inhibitors and their clinical development
    • Taldone, T.; Gozman, A.; Maharaj, R.; Chiosis, G.Targeting Hsp90: small molecule inhibitors and their clinical development Curr. Opin. Pharmacol. 2008, 8, 370-374.
    • (2008) Curr. Opin. Pharmacol , vol.8 , pp. 370-374
    • Taldone, T.1    Gozman, A.2    Maharaj, R.3    Chiosis, G.4
  • 164
    • 69749112702 scopus 로고    scopus 로고
    • Structure-based and in silico design of Hsp90 inhibitors
    • Sgobba M, Rastelli G. Structure-based and in silico design of Hsp90 inhibitors. ChemMedChem 2009, 4(9), 1399-1409.
    • (2009) ChemMedChem , vol.4 , Issue.9 , pp. 1399-1409
    • Sgobba, M.1    Rastelli, G.2
  • 166
    • 0036088471 scopus 로고    scopus 로고
    • Nat Rev IAP proteins: Blocking the road to death's door
    • Salvesen, G. S.; Duckett, C. S. Nat Rev IAP proteins: blocking the road to death's door. Mol. Cell Biol. 2002, 3, 401-410.
    • (2002) Mol. Cell Biol , vol.3 , pp. 401-410
    • Salvesen, G.S.1    Duckett, C.S.2
  • 167
    • 0037267333 scopus 로고    scopus 로고
    • Validating survivin as a cancer therapeutic target
    • Altieri, D. C. Validating survivin as a cancer therapeutic target. Nat. Rev. Cancer 2003, 3, 46-54.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 46-54
    • Altieri, D.C.1
  • 168
    • 0344974238 scopus 로고    scopus 로고
    • Targeting survivin expression induces cell proliferation defect and subsequent cell death involving mitochondrial pathway in myeloid leukemic cells
    • Carter, B. Z.; Wang, R. Y.; Schober, W. D.; Milella, M.; Chism, D.; Andreeff, M.; Targeting survivin expression induces cell proliferation defect and subsequent cell death involving mitochondrial pathway in myeloid leukemic cells. Cell Cycle 2003, 2, 488-493.
    • (2003) Cell Cycle , vol.2 , pp. 488-493
    • Carter, B.Z.1    Wang, R.Y.2    Schober, W.D.3    Milella, M.4    Chism, D.5    Andreeff, M.6
  • 170
    • 0042702002 scopus 로고    scopus 로고
    • Survivin and aven: Two distinct antiapoptotic signals in acute leukemias
    • Paydas, S.; Tanriverdi, K.; Yavuz, S.; Disel, U.; Sahin, B.; Burgut, R. Survivin and aven: two distinct antiapoptotic signals in acute leukemias. Ann. Oncol. 2003, 14, 1045-1050.
    • (2003) Ann. Oncol , vol.14 , pp. 1045-1050
    • Paydas, S.1    Tanriverdi, K.2    Yavuz, S.3    Disel, U.4    Sahin, B.5    Burgut, R.6
  • 175
    • 33845915755 scopus 로고    scopus 로고
    • Small-molecule targeting of heat shock protein 90 chaperone function: Rational identification of a new anticancer lead
    • Meli, M.; Pennati, M.; Curto, M.; Daidone, M. G.; Plescia, J.; Toba, S.; Altieri, D. C.; Zaffaroni, N.; Colombo, G. Small-molecule targeting of heat shock protein 90 chaperone function: rational identification of a new anticancer lead. J. Med. Chem. 2006, 49, 7721-7730.
    • (2006) J. Med. Chem , vol.49 , pp. 7721-7730
    • Meli, M.1    Pennati, M.2    Curto, M.3    Daidone, M.G.4    Plescia, J.5    Toba, S.6    Altieri, D.C.7    Zaffaroni, N.8    Colombo, G.9
  • 177
    • 38349153572 scopus 로고    scopus 로고
    • A novel Hsp90 inhibitor to disrupt Hsp90/Cdc37 complex against pancreatic cancer cells
    • Zhang, T.; Hamza, A.; Cao, X.; Wang, B.; Yu, S.; Zhan, C. G.; Sun, D. A novel Hsp90 inhibitor to disrupt Hsp90/Cdc37 complex against pancreatic cancer cells. Mol. Cancer Ther. 2008, 7, 162-170.
    • (2008) Mol. Cancer Ther , vol.7 , pp. 162-170
    • Zhang, T.1    Hamza, A.2    Cao, X.3    Wang, B.4    Yu, S.5    Zhan, C.G.6    Sun, D.7
  • 178
    • 54549105458 scopus 로고    scopus 로고
    • Gedunin, a novel hsp90 inhibitor: Semisynthesis of derivatives and preliminary structure-activity relationships
    • Brandt, G. E. L.; Schmidt, M. D.; Prisinzano, T. E.; Blagg, B. S. J. Gedunin, a novel hsp90 inhibitor: semisynthesis of derivatives and preliminary structure-activity relationships. J. Med. Chem. 2008, 51, 6495-6502.
    • (2008) J. Med. Chem , vol.51 , pp. 6495-6502
    • Brandt, G.E.L.1    Schmidt, M.D.2    Prisinzano, T.E.3    Blagg, B.S.J.4
  • 179
    • 0034594644 scopus 로고    scopus 로고
    • Novobiocin and related coumarins and depletion of heat shock protein 90-dependent signaling proteins
    • Marcu, M. G.; Schulte, T. W.; Neckers, L. Novobiocin and related coumarins and depletion of heat shock protein 90-dependent signaling proteins. J. Natl. Cancer Inst. 2000, 92, 242-248.
    • (2000) J. Natl. Cancer Inst , vol.92 , pp. 242-248
    • Marcu, M.G.1    Schulte, T.W.2    Neckers, L.3
  • 180
    • 0034711270 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone
    • Marcu, M. G.; Chadli, A.; Bouhouche, I.; Catelli, M.; Neckers, L. M. The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone. J. Biol. Chem. 2000, 275, 37181-37186.
    • (2000) J. Biol. Chem , vol.275 , pp. 37181-37186
    • Marcu, M.G.1    Chadli, A.2    Bouhouche, I.3    Catelli, M.4    Neckers, L.M.5
  • 182
    • 0036510547 scopus 로고    scopus 로고
    • A Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocket
    • Soti, C.; Racz, A.; Csermely, P. A Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocket J. Biol. Chem. 2002, 277, 7066-7075.
    • (2002) J. Biol. Chem , vol.277 , pp. 7066-7075
    • Soti, C.1    Racz, A.2    Csermely, P.3
  • 183
    • 0038730655 scopus 로고    scopus 로고
    • Comparative analysis of the ATP-binding sites of Hsp90 by nucleotide affinity cleavage: A distinct nucleotide specificity of the C-terminal ATPbinding site
    • Soti, C.; Vermes, A.; Haystead, T. A. J.; Csermely, P. Comparative analysis of the ATP-binding sites of Hsp90 by nucleotide affinity cleavage: a distinct nucleotide specificity of the C-terminal ATPbinding site. Eur. J. Biochem. 2003, 270, 2421-2428.
    • (2003) Eur. J. Biochem , vol.270 , pp. 2421-2428
    • Soti, C.1    Vermes, A.2    Haystead, T.A.J.3    Csermely, P.4
  • 185
    • 33646371009 scopus 로고    scopus 로고
    • Modulation of chaperone function and cochaperone interaction by novobiocin in the C-terminal domain of Hsp90: Evidence that coumarin antibiotics disrupt Hsp90 dimerization
    • Allan, R. K.; Mok, D.; Ward, B. K.; Ratajczak, T. Modulation of chaperone function and cochaperone interaction by novobiocin in the C-terminal domain of Hsp90: evidence that coumarin antibiotics disrupt Hsp90 dimerization. J. Biol. Chem. 2006, 281, 7161-7171.
    • (2006) J. Biol. Chem , vol.281 , pp. 7161-7171
    • Allan, R.K.1    Mok, D.2    Ward, B.K.3    Ratajczak, T.4
  • 186
    • 33845306864 scopus 로고    scopus 로고
    • Novobiocin: Redesigning a DNA gyrase inhibitor for selective inhibition of Hsp90
    • Burlison, J. A.; Neckers, L.; Smith, A. B.; Maxwell, A.; Blagg, B. S. J. Novobiocin: redesigning a DNA gyrase inhibitor for selective inhibition of Hsp90. J. Am. Chem. Soc. 2006, 128, 15529-15536.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 15529-15536
    • Burlison, J.A.1    Neckers, L.2    Smith, A.B.3    Maxwell, A.4    Blagg, B.S.J.5
  • 187
    • 34248569319 scopus 로고    scopus 로고
    • A library of noviosylated coumarin analogues
    • Huang, Y. T.; Blagg, B. S. J. A library of noviosylated coumarin analogues. J. Org. Chem. 2007, 72, 3609-3613.
    • (2007) J. Org. Chem , vol.72 , pp. 3609-3613
    • Huang, Y.T.1    Blagg, B.S.J.2
  • 188
    • 37849037720 scopus 로고    scopus 로고
    • New novobiocin analogues as antiproliferative agents in breast cancer cells and potential inhibitors of heat shock protein 90
    • Le Bras, G.; Radanyi, C.; Peyrat, J. F.; Brion, J. D.; Alami, M.; Marsaud, V.; Stella, B.; Renoir, J. M. New novobiocin analogues as antiproliferative agents in breast cancer cells and potential inhibitors of heat shock protein 90. J. Med. Chem. 2007, 50, 6189-6200.
    • (2007) J. Med. Chem , vol.50 , pp. 6189-6200
    • Le Bras, G.1    Radanyi, C.2    Peyrat, J.F.3    Brion, J.D.4    Alami, M.5    Marsaud, V.6    Stella, B.7    Renoir, J.M.8
  • 189
    • 56449125983 scopus 로고    scopus 로고
    • The design, synthesis, and evaluation of coumarin ring derivatives of the novobiocin scaffold that exhibit antiproliferative activity
    • Donnelly, A. C.; Mays, J. R.; Burlison, J. A.; Nelson, J. T.; Vielhauer, G.; Holzbeierlein, J.; Blagg, B. S. J. The design, synthesis, and evaluation of coumarin ring derivatives of the novobiocin scaffold that exhibit antiproliferative activity. J. Org. Chem. 2008, 73, 8901-8920.
    • (2008) J. Org. Chem , vol.73 , pp. 8901-8920
    • Donnelly, A.C.1    Mays, J.R.2    Burlison, J.A.3    Nelson, J.T.4    Vielhauer, G.5    Holzbeierlein, J.6    Blagg, B.S.J.7
  • 190
    • 41849084518 scopus 로고    scopus 로고
    • Development of novobiocin analogues that manifest anti-proliferative activity against several cancer cell lines
    • Burlison, J. A.; Avila, C.; Vielhauer, G.; Lubbers, D. J.; Holzbeierlein, J.; Blagg, B. S. J. Development of novobiocin analogues that manifest anti-proliferative activity against several cancer cell lines. J. Org. Chem. 2008, 73, 2130-2137.
    • (2008) J. Org. Chem , vol.73 , pp. 2130-2137
    • Burlison, J.A.1    Avila, C.2    Vielhauer, G.3    Lubbers, D.J.4    Holzbeierlein, J.5    Blagg, B.S.J.6
  • 191
    • 61649098007 scopus 로고    scopus 로고
    • Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket
    • Donnelly, A.; Blagg, B. S. J. Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket. Curr. Med. Chem. 2008, 15, 2702-2717.
    • (2008) Curr. Med. Chem , vol.15 , pp. 2702-2717
    • Donnelly, A.1    Blagg, B.S.J.2
  • 192
    • 0345735766 scopus 로고    scopus 로고
    • Pharmacological and genetic analysis of 90-kDa heat shock isoprotein-aryl hydrocarbon receptor complexes
    • Cox, M. B.; Miller CA 3rd. Pharmacological and genetic analysis of 90-kDa heat shock isoprotein-aryl hydrocarbon receptor complexes. Mol. Pharmacol. 2003, 64, 1549-1556.
    • (2003) Mol. Pharmacol , vol.64 , pp. 1549-1556
    • Cox, M.B.1    Miller 3rd, C.A.2
  • 193
    • 42049094683 scopus 로고    scopus 로고
    • Structural models and binding site prediction of the C-terminal domain of human Hsp90: A new target for anticancer drugs
    • Sgobba, M.; Degliesposti, G.; Ferrari, A. M.; Rastelli, G. Structural models and binding site prediction of the C-terminal domain of human Hsp90: a new target for anticancer drugs. Chem. Biol. Drug Des. 2008, 71, 420-433.
    • (2008) Chem. Biol. Drug Des , vol.71 , pp. 420-433
    • Sgobba, M.1    Degliesposti, G.2    Ferrari, A.M.3    Rastelli, G.4
  • 194
    • 67650511415 scopus 로고    scopus 로고
    • Cancer cells harboring MET gene amplification activate alternative signaling pathways to escape MET inhibition but remain sensitive to Hsp90 inhibitors
    • Wang, S.; Pashtan, I.; Tsutsumi, S.; Xu, W.; Neckers, L. Cancer cells harboring MET gene amplification activate alternative signaling pathways to escape MET inhibition but remain sensitive to Hsp90 inhibitors. Cell Cycle 2009, 8, 2050-2056.
    • (2009) Cell Cycle , vol.8 , pp. 2050-2056
    • Wang, S.1    Pashtan, I.2    Tsutsumi, S.3    Xu, W.4    Neckers, L.5
  • 195
    • 70350705983 scopus 로고    scopus 로고
    • HSP90 inhibitors: Multi-targeted antitumor effects and novel combinatorial therapeutic approaches in cancer therapy
    • Hwang, M.; Moretti, L.; Lu, B. HSP90 inhibitors: multi-targeted antitumor effects and novel combinatorial therapeutic approaches in cancer therapy. Curr. Med. Chem. 2009, 16, 3081-3092.
    • (2009) Curr. Med. Chem , vol.16 , pp. 3081-3092
    • Hwang, M.1    Moretti, L.2    Lu, B.3


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