메뉴 건너뛰기




Volumn 23, Issue 1, 2016, Pages 158-172

Chemical Tools to Investigate Mechanisms Associated with HSP90 and HSP70 in Disease

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; GLUCOSE REGULATED PROTEIN 94; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; MOLECULAR PROBE;

EID: 84965057093     PISSN: 24519456     EISSN: 24519448     Source Type: Journal    
DOI: 10.1016/j.chembiol.2015.12.006     Document Type: Review
Times cited : (64)

References (115)
  • 4
    • 84873647676 scopus 로고    scopus 로고
    • Mitochondrial Hsp90s and tumor cell metabolism
    • D.C. Altieri Mitochondrial Hsp90s and tumor cell metabolism Autophagy 9 2013 244 245
    • (2013) Autophagy , vol.9 , pp. 244-245
    • Altieri, D.C.1
  • 7
    • 84884253288 scopus 로고    scopus 로고
    • Posttranslational modification and conformational state of heat shock protein 90 differentially affect binding of chemically diverse small molecule inhibitors
    • K. Beebe, M. Mollapour, B. Scroggins, C. Prodromou, W. Xu, M. Tokita, T. Taldone, L. Pullen, B.K. Zierer, M.J. Lee, and et al. Posttranslational modification and conformational state of heat shock protein 90 differentially affect binding of chemically diverse small molecule inhibitors Oncotarget 4 2013 1065 1074
    • (2013) Oncotarget , vol.4 , pp. 1065-1074
    • Beebe, K.1    Mollapour, M.2    Scroggins, B.3    Prodromou, C.4    Xu, W.5    Tokita, M.6    Taldone, T.7    Pullen, L.8    Zierer, B.K.9    Lee, M.J.10
  • 8
    • 80054805091 scopus 로고    scopus 로고
    • A unique role for heat shock protein 70 and its binding partner tissue transglutaminase in cancer cell migration
    • L.K. Boroughs, M.A. Antonyak, J.L. Johnson, and R.A. Cerione A unique role for heat shock protein 70 and its binding partner tissue transglutaminase in cancer cell migration J. Biol. Chem. 286 2011 37094 37107
    • (2011) J. Biol. Chem. , vol.286 , pp. 37094-37107
    • Boroughs, L.K.1    Antonyak, M.A.2    Johnson, J.L.3    Cerione, R.A.4
  • 10
    • 84924187480 scopus 로고    scopus 로고
    • GrpE, Hsp110/Grp170, Hspbp1/sil1 and bag domain proteins: Nucleotide exchange factors for Hsp70 molecular chaperones
    • A. Bracher, and J. Verghese GrpE, Hsp110/Grp170, Hspbp1/sil1 and bag domain proteins: nucleotide exchange factors for Hsp70 molecular chaperones Subcell. Biochem. 78 2015 1 33
    • (2015) Subcell. Biochem. , vol.78 , pp. 1-33
    • Bracher, A.1    Verghese, J.2
  • 13
    • 84861221245 scopus 로고    scopus 로고
    • Heat shock protein gp96 regulates toll-like receptor 9 proteolytic processing and conformational stability
    • J.C. Brooks, W. Sun, G. Chiosis, and C.A. Leifer Heat shock protein gp96 regulates toll-like receptor 9 proteolytic processing and conformational stability Biochem. Biophys. Res. Commun. 421 2012 780 784
    • (2012) Biochem. Biophys. Res. Commun. , vol.421 , pp. 780-784
    • Brooks, J.C.1    Sun, W.2    Chiosis, G.3    Leifer, C.A.4
  • 15
    • 84944622121 scopus 로고    scopus 로고
    • Chaperone-dependent neurodegeneration: A molecular perspective on therapeutic intervention
    • 007
    • A. Carman, S. Kishinevsky, J. Koren 3rd, W. Lou, and G. Chiosis Chaperone-dependent neurodegeneration: a molecular perspective on therapeutic intervention J. Alzheimers Dis. Parkinsonism 2013 Suppl 10 2013 10.4172/2161-0460.S10-007 007
    • (2013) J. Alzheimers Dis. Parkinsonism , vol.2013
    • Carman, A.1    Kishinevsky, S.2    Koren, J.3    Lou, W.4    Chiosis, G.5
  • 18
    • 0031795383 scopus 로고    scopus 로고
    • Selective antitumor activity of MKT-077, a delocalized lipophilic cation, on normal cells and cancer cells in vitro
    • Y. Chiba, T. Kubota, M. Watanabe, Y. Otani, T. Teramoto, Y. Matsumoto, K. Koya, and M. Kitajima Selective antitumor activity of MKT-077, a delocalized lipophilic cation, on normal cells and cancer cells in vitro J. Surg. Oncol. 69 1998 105 110
    • (1998) J. Surg. Oncol. , vol.69 , pp. 105-110
    • Chiba, Y.1    Kubota, T.2    Watanabe, M.3    Otani, Y.4    Teramoto, T.5    Matsumoto, Y.6    Koya, K.7    Kitajima, M.8
  • 19
    • 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
    • G. Chiosis, M.N. Timaul, B. Lucas, P.N. Munster, F.F. Zheng, L. Sepp-Lorenzino, and N. Rosen 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. 8 2001 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    Sepp-Lorenzino, L.6    Rosen, N.7
  • 20
    • 83755171532 scopus 로고    scopus 로고
    • A small molecule that binds to an ATPase domain of Hsc70 promotes membrane trafficking of mutant cystic fibrosis transmembrane conductance regulator
    • H.J. Cho, H.Y. Gee, K.H. Baek, S.K. Ko, J.M. Park, H. Lee, N.D. Kim, M.G. Lee, and I. Shin A small molecule that binds to an ATPase domain of Hsc70 promotes membrane trafficking of mutant cystic fibrosis transmembrane conductance regulator J. Am. Chem. Soc. 133 2011 20267 20276
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 20267-20276
    • Cho, H.J.1    Gee, H.Y.2    Baek, K.H.3    Ko, S.K.4    Park, J.M.5    Lee, H.6    Kim, N.D.7    Lee, M.G.8    Shin, I.9
  • 24
    • 34447528828 scopus 로고    scopus 로고
    • The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions
    • M. Daugaard, M. Rohde, and M. Jaattela The heat shock protein 70 family: highly homologous proteins with overlapping and distinct functions FEBS Lett. 581 2007 3702 3710
    • (2007) FEBS Lett. , vol.581 , pp. 3702-3710
    • Daugaard, M.1    Rohde, M.2    Jaattela, M.3
  • 25
    • 84858152540 scopus 로고    scopus 로고
    • Extracellular Hsp90 serves as a co-factor for NF-κB activation and cellular pathogenesis induced by an oncogenic herpesvirus
    • M.R. Defee, Z. Qin, L. Dai, B.P. Toole, J.S. Isaacs, and C.H. Parsons Extracellular Hsp90 serves as a co-factor for NF-κB activation and cellular pathogenesis induced by an oncogenic herpesvirus Am. J. Cancer Res. 1 2011 687 700
    • (2011) Am. J. Cancer Res. , vol.1 , pp. 687-700
    • Defee, M.R.1    Qin, Z.2    Dai, L.3    Toole, B.P.4    Isaacs, J.S.5    Parsons, C.H.6
  • 27
    • 84899578167 scopus 로고    scopus 로고
    • Identification of novel Hsp90alpha/beta isoform selective inhibitors using structure-based drug design. Demonstration of potential utility in treating CNS disorders such as Huntington's disease
    • J.T. Ernst, T. Neubert, M. Liu, S. Sperry, H. Zuccola, A. Turnbull, B. Fleck, W. Kargo, L. Woody, P. Chiang, and et al. Identification of novel Hsp90alpha/beta isoform selective inhibitors using structure-based drug design. Demonstration of potential utility in treating CNS disorders such as Huntington's disease J. Med. Chem. 57 2014 3382 3400
    • (2014) J. Med. Chem. , vol.57 , pp. 3382-3400
    • Ernst, J.T.1    Neubert, T.2    Liu, M.3    Sperry, S.4    Zuccola, H.5    Turnbull, A.6    Fleck, B.7    Kargo, W.8    Woody, L.9    Chiang, P.10
  • 29
    • 84883049362 scopus 로고    scopus 로고
    • Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis
    • A. Finka, and P. Goloubinoff Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis Cell Stress Chaperones 18 2013 591 605
    • (2013) Cell Stress Chaperones , vol.18 , pp. 591-605
    • Finka, A.1    Goloubinoff, P.2
  • 30
    • 84857049091 scopus 로고    scopus 로고
    • Broad action of Hsp90 as a host chaperone required for viral replication
    • R. Geller, S. Taguwa, and J. Frydman Broad action of Hsp90 as a host chaperone required for viral replication Biochim. Biophys. Acta 1823 2012 698 706
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 698-706
    • Geller, R.1    Taguwa, S.2    Frydman, J.3
  • 33
    • 84908571827 scopus 로고    scopus 로고
    • Alternative approaches to Hsp90 modulation for the treatment of cancer
    • J.A. Hall, L.K. Forsberg, and B.S. Blagg Alternative approaches to Hsp90 modulation for the treatment of cancer Future Med. Chem. 6 2014 1587 1605
    • (2014) Future Med. Chem. , vol.6 , pp. 1587-1605
    • Hall, J.A.1    Forsberg, L.K.2    Blagg, B.S.3
  • 34
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • F.U. Hartl, A. Bracher, and M. Hayer-Hartl Molecular chaperones in protein folding and proteostasis Nature 475 2011 324 332
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 35
    • 0037064023 scopus 로고    scopus 로고
    • The assembly and intermolecular properties of the Hsp70-Hop-Hsp90 molecular chaperone complex
    • M.P. Hernandez, W.P. Sullivan, and D.O. Toft The assembly and intermolecular properties of the Hsp70-Hop-Hsp90 molecular chaperone complex J. Biol. Chem. 277 2002 38294 38304
    • (2002) J. Biol. Chem. , vol.277 , pp. 38294-38304
    • Hernandez, M.P.1    Sullivan, W.P.2    Toft, D.O.3
  • 36
    • 84880065073 scopus 로고    scopus 로고
    • Alpha 7 helix region of alpha I domain is crucial for integrin binding to endoplasmic reticulum chaperone gp96: A potential therapeutic target for cancer metastasis
    • F. Hong, B. Liu, G. Chiosis, D.T. Gewirth, and Z. Li Alpha 7 helix region of alpha I domain is crucial for integrin binding to endoplasmic reticulum chaperone gp96: a potential therapeutic target for cancer metastasis J. Biol. Chem. 288 2013 18243 18248
    • (2013) J. Biol. Chem. , vol.288 , pp. 18243-18248
    • Hong, F.1    Liu, B.2    Chiosis, G.3    Gewirth, D.T.4    Li, Z.5
  • 38
    • 80053620191 scopus 로고    scopus 로고
    • Heat shock protein 90 (Hsp90) contributes to cytosolic translocation of extracellular antigen for cross-presentation by dendritic cells
    • T. Imai, Y. Kato, C. Kajiwara, S. Mizukami, I. Ishige, T. Ichiyanagi, M. Hikida, J.Y. Wang, and H. Udono Heat shock protein 90 (Hsp90) contributes to cytosolic translocation of extracellular antigen for cross-presentation by dendritic cells Proc. Natl. Acad. Sci. USA 108 2011 16363 16368
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 16363-16368
    • Imai, T.1    Kato, Y.2    Kajiwara, C.3    Mizukami, S.4    Ishige, I.5    Ichiyanagi, T.6    Hikida, M.7    Wang, J.Y.8    Udono, H.9
  • 40
  • 41
    • 77954947810 scopus 로고    scopus 로고
    • The Hsp70 chaperone machinery: J proteins as drivers of functional specificity
    • H.H. Kampinga, and E.A. Craig The Hsp70 chaperone machinery: J proteins as drivers of functional specificity Nat. Rev. Mol. Cell Biol. 11 2010 579 592
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 44
    • 84871689599 scopus 로고    scopus 로고
    • Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones
    • R. Kityk, J. Kopp, I. Sinning, and M.P. Mayer Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones Mol. Cell 48 2012 863 874
    • (2012) Mol. Cell , vol.48 , pp. 863-874
    • Kityk, R.1    Kopp, J.2    Sinning, I.3    Mayer, M.P.4
  • 46
    • 0030064081 scopus 로고    scopus 로고
    • Mkt-077, a novel rhodacyanine dye in clinical trials, exhibits anticarcinoma activity in preclinical studies based on selective mitochondrial accumulation
    • K. Koya, Y. Li, H. Wang, T. Ukai, N. Tatsuta, M. Kawakami, Shishido, and L.B. Chen Mkt-077, a novel rhodacyanine dye in clinical trials, exhibits anticarcinoma activity in preclinical studies based on selective mitochondrial accumulation Cancer Res. 56 1996 538 543
    • (1996) Cancer Res. , vol.56 , pp. 538-543
    • Koya, K.1    Li, Y.2    Wang, H.3    Ukai, T.4    Tatsuta, N.5    Kawakami, M.6    Shishido7    Chen, L.B.8
  • 49
  • 50
    • 79960694363 scopus 로고    scopus 로고
    • Hsp70 inhibition by the small-molecule 2-phenylethynesulfonamide impairs protein clearance pathways in tumor cells
    • J.I.J. Leu, J. Pimkina, P. Pandey, M.E. Murphy, and D.L. George Hsp70 inhibition by the small-molecule 2-phenylethynesulfonamide impairs protein clearance pathways in tumor cells Mol. Cancer Res. 9 2011 936 947
    • (2011) Mol. Cancer Res. , vol.9 , pp. 936-947
    • Leu, J.I.J.1    Pimkina, J.2    Pandey, P.3    Murphy, M.E.4    George, D.L.5
  • 51
    • 84857042271 scopus 로고    scopus 로고
    • The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones
    • J. Li, J. Soroka, and J. Buchner The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones Biochim. Biophys. Acta 1823 2012 624 635
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 624-635
    • Li, J.1    Soroka, J.2    Buchner, J.3
  • 53
    • 84929512660 scopus 로고    scopus 로고
    • Cell membrane gp96 facilitates HER2 dimerization and serves as a novel target in breast cancer
    • X. Li, L. Sun, J. Hou, M. Gui, J. Ying, H. Zhao, N. Lv, and S. Meng Cell membrane gp96 facilitates HER2 dimerization and serves as a novel target in breast cancer Int. J. Cancer 137 2015 512 524
    • (2015) Int. J. Cancer , vol.137 , pp. 512-524
    • Li, X.1    Sun, L.2    Hou, J.3    Gui, M.4    Ying, J.5    Zhao, H.6    Lv, N.7    Meng, S.8
  • 55
    • 84908126700 scopus 로고    scopus 로고
    • Egress of budded virions of Autographa californica nucleopolyhedrovirus does not require activity of Spodoptera frugiperda HSP/HSC70 chaperones
    • Y.V. Lyupina, O.V. Orlova, S.B. Abaturova, S.N. Beljelarskaya, A.N. Lavrov, and V.S. Mikhailov Egress of budded virions of Autographa californica nucleopolyhedrovirus does not require activity of Spodoptera frugiperda HSP/HSC70 chaperones Virus Res. 192 2014 1 5
    • (2014) Virus Res. , vol.192 , pp. 1-5
    • Lyupina, Y.V.1    Orlova, O.V.2    Abaturova, S.B.3    Beljelarskaya, S.N.4    Lavrov, A.N.5    Mikhailov, V.S.6
  • 57
    • 84857053996 scopus 로고    scopus 로고
    • Grp94: An Hsp90-like protein specialized for protein folding and quality control in the endoplasmic reticulum
    • M. Marzec, D. Eletto, and Y. Argon Grp94: an Hsp90-like protein specialized for protein folding and quality control in the endoplasmic reticulum Biochim. Biophys. Acta 1823 2012 774 787
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 774-787
    • Marzec, M.1    Eletto, D.2    Argon, Y.3
  • 59
    • 84910018393 scopus 로고    scopus 로고
    • Cell death induced by 2-phenylethynesulfonamide uncovers a pro-survival function of BAX
    • P. Mattiolo, A. Barbero-Farran, J. Amigo, M. Ripamonti, J. Ribas, and J. Boix Cell death induced by 2-phenylethynesulfonamide uncovers a pro-survival function of BAX Cancer Lett. 354 2014 115 121
    • (2014) Cancer Lett. , vol.354 , pp. 115-121
    • Mattiolo, P.1    Barbero-Farran, A.2    Amigo, J.3    Ripamonti, M.4    Ribas, J.5    Boix, J.6
  • 61
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • M.P. Mayer, and B. Bukau Hsp70 chaperones: cellular functions and molecular mechanism Cell Mol. Life Sci. 62 2005 670 684
    • (2005) Cell Mol. Life Sci. , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 62
    • 84963690768 scopus 로고    scopus 로고
    • Insights into the molecular mechanism of allostery in Hsp70s
    • M.P. Mayer, and R. Kityk Insights into the molecular mechanism of allostery in Hsp70s Front. Mol. Biosci. 2 2015 58
    • (2015) Front. Mol. Biosci. , vol.2 , pp. 58
    • Mayer, M.P.1    Kityk, R.2
  • 63
    • 84901189858 scopus 로고    scopus 로고
    • An impermeant ganetespib analog inhibits extracellular Hsp90-mediated cancer cell migration that involves lysyl oxidase 2-like protein
    • Basel
    • J. McCready, D.S. Wong, J.A. Burlison, W. Ying, and D.G. Jay An impermeant ganetespib analog inhibits extracellular Hsp90-mediated cancer cell migration that involves lysyl oxidase 2-like protein Cancers (Basel) 6 2014 1031 1046
    • (2014) Cancers , vol.6 , pp. 1031-1046
    • McCready, J.1    Wong, D.S.2    Burlison, J.A.3    Ying, W.4    Jay, D.G.5
  • 64
    • 84857044092 scopus 로고    scopus 로고
    • Post-translational modifications of Hsp90 and their contributions to chaperone regulation
    • M. Mollapour, and L. Neckers Post-translational modifications of Hsp90 and their contributions to chaperone regulation Biochim. Biophys. Acta 1823 2012 648 655
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 648-655
    • Mollapour, M.1    Neckers, L.2
  • 66
    • 84876477696 scopus 로고    scopus 로고
    • The Hsp70 and autophagy inhibitor pifithrin-mu enhances the antitumor effects of trail on human pancreatic cancer
    • H. Monma, N. Harashima, T. Inao, S. Okano, Y. Tajima, and M. Harada The Hsp70 and autophagy inhibitor pifithrin-mu enhances the antitumor effects of trail on human pancreatic cancer Mol. Cancer Ther. 12 2013 341 351
    • (2013) Mol. Cancer Ther. , vol.12 , pp. 341-351
    • Monma, H.1    Harashima, N.2    Inao, T.3    Okano, S.4    Tajima, Y.5    Harada, M.6
  • 68
    • 84879412911 scopus 로고    scopus 로고
    • C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones Chip and Hop to determine cellular protein folding/degradation balances
    • P. Muller, E. Ruckova, P. Halada, P.J. Coates, R. Hrstka, D.P. Lane, and B. Vojtesek C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones Chip and Hop to determine cellular protein folding/degradation balances Oncogene 32 2013 3101 3110
    • (2013) Oncogene , vol.32 , pp. 3101-3110
    • Muller, P.1    Ruckova, E.2    Halada, P.3    Coates, P.J.4    Hrstka, R.5    Lane, D.P.6    Vojtesek, B.7
  • 70
    • 33645975518 scopus 로고    scopus 로고
    • Chaperoning oncogenes: Hsp90 as a target of geldanamycin
    • L. Neckers Chaperoning oncogenes: Hsp90 as a target of geldanamycin Handb. Exp. Pharmacol. 2006 259 277
    • (2006) Handb. Exp. Pharmacol. , pp. 259-277
    • Neckers, L.1
  • 71
    • 0033502429 scopus 로고    scopus 로고
    • Geldanamycin as a potential anti-cancer agent: Its molecular target and biochemical activity
    • L. Neckers, T.W. Schulte, and E. Mimnaugh Geldanamycin as a potential anti-cancer agent: its molecular target and biochemical activity Invest. New Drugs 17 1999 361 373
    • (1999) Invest. New Drugs , vol.17 , pp. 361-373
    • Neckers, L.1    Schulte, T.W.2    Mimnaugh, E.3
  • 73
    • 84903215565 scopus 로고    scopus 로고
    • Mitochondrial Hsp90s suppress calcium-mediated stress signals propagating from mitochondria to the ER in cancer cells
    • H.K. Park, J.E. Lee, J. Lim, and B.H. Kang Mitochondrial Hsp90s suppress calcium-mediated stress signals propagating from mitochondria to the ER in cancer cells Mol. Cancer 13 2014 148
    • (2014) Mol. Cancer , vol.13 , pp. 148
    • Park, H.K.1    Lee, J.E.2    Lim, J.3    Kang, B.H.4
  • 74
    • 79955432735 scopus 로고    scopus 로고
    • Advances in the discovery and development of heat-shock protein 90 inhibitors for cancer treatment
    • H.J. Patel, S. Modi, G. Chiosis, and T. Taldone Advances in the discovery and development of heat-shock protein 90 inhibitors for cancer treatment Expert Opin. Drug Discov. 6 2011 559 587
    • (2011) Expert Opin. Drug Discov. , vol.6 , pp. 559-587
    • Patel, H.J.1    Modi, S.2    Chiosis, G.3    Taldone, T.4
  • 76
    • 84929315274 scopus 로고    scopus 로고
    • Structure-activity relationship in a purine-scaffold compound series with selectivity for the endoplasmic reticulum Hsp90 paralog Grp94
    • H.J. Patel, P.D. Patel, S.O. Ochiana, P. Yan, W. Sun, M.R. Patel, S.K. Shah, E. Tramentozzi, J. Brooks, A. Bolaender, and et al. Structure-activity relationship in a purine-scaffold compound series with selectivity for the endoplasmic reticulum Hsp90 paralog Grp94 J. Med. Chem. 58 2015 3922 3943
    • (2015) J. Med. Chem. , vol.58 , pp. 3922-3943
    • Patel, H.J.1    Patel, P.D.2    Ochiana, S.O.3    Yan, P.4    Sun, W.5    Patel, M.R.6    Shah, S.K.7    Tramentozzi, E.8    Brooks, J.9    Bolaender, A.10
  • 77
    • 82955169612 scopus 로고    scopus 로고
    • A compound that inhibits the Hop-Hsp90 complex formation and has unique killing effects in breast cancer cell lines
    • G. Pimienta, K.M. Herbert, and L. Regan A compound that inhibits the Hop-Hsp90 complex formation and has unique killing effects in breast cancer cell lines Mol. Pharm. 8 2011 2252 2261
    • (2011) Mol. Pharm. , vol.8 , pp. 2252-2261
    • Pimienta, G.1    Herbert, K.M.2    Regan, L.3
  • 78
    • 84910031803 scopus 로고    scopus 로고
    • Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases
    • W.B. Pratt, J.E. Gestwicki, Y. Osawa, and A.P. Lieberman Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases Annu. Rev. Pharmacol. Toxicol. 55 2015 353 371
    • (2015) Annu. Rev. Pharmacol. Toxicol. , vol.55 , pp. 353-371
    • Pratt, W.B.1    Gestwicki, J.E.2    Osawa, Y.3    Lieberman, A.P.4
  • 79
    • 84950335560 scopus 로고    scopus 로고
    • Client proteins and small molecule inhibitors display distinct binding preferences for constitutive and stress-induced Hsp90 isoforms and their conformationally restricted mutants
    • T.L. Prince, T. Kijima, M. Tatokoro, S. Lee, S. Tsutsumi, K. Yim, C. Rivas, S. Alarcon, H. Schwartz, K. Khamit-Kush, and et al. Client proteins and small molecule inhibitors display distinct binding preferences for constitutive and stress-induced Hsp90 isoforms and their conformationally restricted mutants PLoS One 10 2015 e0141786
    • (2015) PLoS One , vol.10
    • Prince, T.L.1    Kijima, T.2    Tatokoro, M.3    Lee, S.4    Tsutsumi, S.5    Yim, K.6    Rivas, C.7    Alarcon, S.8    Schwartz, H.9    Khamit-Kush, K.10
  • 80
    • 84857051938 scopus 로고    scopus 로고
    • The 'active life' of Hsp90 complexes
    • C. Prodromou The 'active life' of Hsp90 complexes Biochim. Biophys. Acta 1823 2012 614 623
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 614-623
    • Prodromou, C.1
  • 81
    • 84855928022 scopus 로고    scopus 로고
    • Inhibition of RPE cell sterile inflammatory responses and endotoxin-induced uveitis by a cell-impermeable Hsp90 inhibitor
    • S. Qin, M. Ni, X. Wang, F. Maurier-Mahe, D.L. Shurland, and G.A. Rodrigues Inhibition of RPE cell sterile inflammatory responses and endotoxin-induced uveitis by a cell-impermeable Hsp90 inhibitor Exp. Eye Res. 93 2011 889 897
    • (2011) Exp. Eye Res. , vol.93 , pp. 889-897
    • Qin, S.1    Ni, M.2    Wang, X.3    Maurier-Mahe, F.4    Shurland, D.L.5    Rodrigues, G.A.6
  • 83
    • 84890860170 scopus 로고    scopus 로고
    • Identification of an allosteric pocket on human Hsp70 reveals a mode of inhibition of this therapeutically important protein
    • A. Rodina, P.D. Patel, Y. Kang, Y. Patel, I. Baaklini, M.J. Wong, T. Taldone, P. Yan, C. Yang, R. Maharaj, and et al. Identification of an allosteric pocket on human Hsp70 reveals a mode of inhibition of this therapeutically important protein Chem. Biol. 20 2013 1469 1480
    • (2013) Chem. Biol. , vol.20 , pp. 1469-1480
    • Rodina, A.1    Patel, P.D.2    Kang, Y.3    Patel, Y.4    Baaklini, I.5    Wong, M.J.6    Taldone, T.7    Yan, P.8    Yang, C.9    Maharaj, R.10
  • 85
    • 0034725640 scopus 로고    scopus 로고
    • Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, Grp94. I. Evidence for allosteric regulation of ligand binding
    • M.F. Rosser, and C.V. Nicchitta Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, Grp94. I. Evidence for allosteric regulation of ligand binding J. Biol. Chem. 275 2000 22798 22805
    • (2000) J. Biol. Chem. , vol.275 , pp. 22798-22805
    • Rosser, M.F.1    Nicchitta, C.V.2
  • 87
    • 0032569851 scopus 로고    scopus 로고
    • Hsp90 as a capacitor for morphological evolution
    • S.L. Rutherford, and S. Lindquist Hsp90 as a capacitor for morphological evolution Nature 396 1998 336 342
    • (1998) Nature , vol.396 , pp. 336-342
    • Rutherford, S.L.1    Lindquist, S.2
  • 88
    • 84860352218 scopus 로고    scopus 로고
    • The expanding proteome of the molecular chaperone Hsp90
    • R.S. Samant, P.A. Clarke, and P. Workman The expanding proteome of the molecular chaperone Hsp90 Cell Cycle 11 2012 1301 1308
    • (2012) Cell Cycle , vol.11 , pp. 1301-1308
    • Samant, R.S.1    Clarke, P.A.2    Workman, P.3
  • 89
    • 1842782331 scopus 로고    scopus 로고
    • Under cover: Causes, effects and implications of Hsp90-mediated genetic capacitance
    • T.A. Sangster, S. Lindquist, and C. Queitsch Under cover: causes, effects and implications of Hsp90-mediated genetic capacitance Bioessays 26 2004 348 362
    • (2004) Bioessays , vol.26 , pp. 348-362
    • Sangster, T.A.1    Lindquist, S.2    Queitsch, C.3
  • 92
    • 84946053539 scopus 로고    scopus 로고
    • Hsp90 and Hsp70: Implication in inflammation processes and therapeutic approaches for myeloproliferative neoplasms
    • M. Sevin, F. Girodon, C. Garrido, and A. De Thonel Hsp90 and Hsp70: implication in inflammation processes and therapeutic approaches for myeloproliferative neoplasms Mediators Inflamm. 2015 2015 970242
    • (2015) Mediators Inflamm. , vol.2015
    • Sevin, M.1    Girodon, F.2    Garrido, C.3    De Thonel, A.4
  • 93
    • 84857943078 scopus 로고    scopus 로고
    • Quantitative proteomics reveals that Hsp90 inhibition preferentially targets kinases and the DNA damage response
    • K. Sharma, R.M. Vabulas, B. Macek, S. Pinkert, J. Cox, M. Mann, and F.U. Hartl Quantitative proteomics reveals that Hsp90 inhibition preferentially targets kinases and the DNA damage response Mol. Cell Proteomics 11 2012 M111 014654
    • (2012) Mol. Cell Proteomics , vol.11 , Issue.M111
    • Sharma, K.1    Vabulas, R.M.2    Macek, B.3    Pinkert, S.4    Cox, J.5    Mann, M.6    Hartl, F.U.7
  • 94
    • 84938974589 scopus 로고    scopus 로고
    • Hsp70 in cancer: Back to the future
    • M.Y. Sherman, and V.L. Gabai Hsp70 in cancer: back to the future Oncogene 34 2015 4153 4161
    • (2015) Oncogene , vol.34 , pp. 4153-4161
    • Sherman, M.Y.1    Gabai, V.L.2
  • 95
    • 0348111450 scopus 로고    scopus 로고
    • Structure of the N-terminal domain of Grp94. Basis for ligand specificity and regulation
    • K.L. Soldano, A. Jivan, C.V. Nicchitta, and D.T. Gewirth Structure of the N-terminal domain of Grp94. Basis for ligand specificity and regulation J. Biol. Chem. 278 2003 48330 48338
    • (2003) J. Biol. Chem. , vol.278 , pp. 48330-48338
    • Soldano, K.L.1    Jivan, A.2    Nicchitta, C.V.3    Gewirth, D.T.4
  • 96
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • C.E. Stebbins, A.A. Russo, C. Schneider, N. Rosen, F.U. Hartl, and N.P. Pavletich Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent Cell 89 1997 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
  • 98
    • 79953308070 scopus 로고    scopus 로고
    • Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone
    • T.O. Street, L.A. Lavery, and D.A. Agard Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone Mol. Cell 42 2011 96 105
    • (2011) Mol. Cell , vol.42 , pp. 96-105
    • Street, T.O.1    Lavery, L.A.2    Agard, D.A.3
  • 99
    • 84870050994 scopus 로고    scopus 로고
    • Glucose-regulated protein 94 triage of mutant myocilin through endoplasmic reticulum-associated degradation subverts a more efficient autophagic clearance mechanism
    • A. Suntharalingam, J.F. Abisambra, J.C. O'Leary 3rd, J. Koren 3rd, B. Zhang, M.K. Joe, L.J. Blair, S.E. Hill, U.K. Jinwal, M. Cockman, and et al. Glucose-regulated protein 94 triage of mutant myocilin through endoplasmic reticulum-associated degradation subverts a more efficient autophagic clearance mechanism J. Biol. Chem. 287 2012 40661 40669
    • (2012) J. Biol. Chem. , vol.287 , pp. 40661-40669
    • Suntharalingam, A.1    Abisambra, J.F.2    O'Leary, J.C.3    Koren, J.4    Zhang, B.5    Joe, M.K.6    Blair, L.J.7    Hill, S.E.8    Jinwal, U.K.9    Cockman, M.10
  • 103
    • 84896815426 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibitors. 2. 2,5′-thiodipyrimidines, 5-(phenylthio)pyrimidines, 2-(pyridin-3-ylthio)pyrimidines, and 3-(phenylthio)pyridines as reversible binders to an allosteric site on heat shock protein 70
    • T. Taldone, Y. Kang, H.J. Patel, M.R. Patel, P.D. Patel, A. Rodina, Y. Patel, A. Gozman, R. Maharaj, C.C. Clement, and et al. Heat shock protein 70 inhibitors. 2. 2,5′-thiodipyrimidines, 5-(phenylthio)pyrimidines, 2-(pyridin-3-ylthio)pyrimidines, and 3-(phenylthio)pyridines as reversible binders to an allosteric site on heat shock protein 70 J. Med. Chem. 57 2014 1208 1224
    • (2014) J. Med. Chem. , vol.57 , pp. 1208-1224
    • Taldone, T.1    Kang, Y.2    Patel, H.J.3    Patel, M.R.4    Patel, P.D.5    Rodina, A.6    Patel, Y.7    Gozman, A.8    Maharaj, R.9    Clement, C.C.10
  • 104
    • 84908372066 scopus 로고    scopus 로고
    • Selective targeting of the stress chaperome as a therapeutic strategy
    • T. Taldone, S.O. Ochiana, P.D. Patel, and G. Chiosis Selective targeting of the stress chaperome as a therapeutic strategy Trends Pharmacol. Sci. 35 2014 592 603
    • (2014) Trends Pharmacol. Sci. , vol.35 , pp. 592-603
    • Taldone, T.1    Ochiana, S.O.2    Patel, P.D.3    Chiosis, G.4
  • 106
    • 34548189523 scopus 로고    scopus 로고
    • Extracellular heat shock protein 90: A role for a molecular chaperone in cell motility and cancer metastasis
    • S. Tsutsumi, and L. Neckers Extracellular heat shock protein 90: a role for a molecular chaperone in cell motility and cancer metastasis Cancer Sci. 98 2007 1536 1539
    • (2007) Cancer Sci. , vol.98 , pp. 1536-1539
    • Tsutsumi, S.1    Neckers, L.2
  • 110
    • 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
    • L. Whitesell, E.G. Mimnaugh, B. De Costa, C.E. Myers, and L.M. Neckers 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 91 1994 8324 8328
    • (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
  • 112
  • 114
    • 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
    • W. Xu, and L. Neckers Targeting the molecular chaperone heat shock protein 90 provides a multifaceted effect on diverse cell signaling pathways of cancer cells Clin. Cancer Res. 13 2007 1625 1629
    • (2007) Clin. Cancer Res. , vol.13 , pp. 1625-1629
    • Xu, W.1    Neckers, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.