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Volumn 74, Issue 5, 2013, Pages 367-374

Allosteric heat shock protein 70 inhibitors rapidly rescue synaptic plasticity deficits by reducing aberrant tau

Author keywords

Alzheimer's disease; chaperones; Hsc70; rhodacyanine; tau; YM 01

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; TAU PROTEIN;

EID: 84882250523     PISSN: 00063223     EISSN: 18732402     Source Type: Journal    
DOI: 10.1016/j.biopsych.2013.02.027     Document Type: Article
Times cited : (95)

References (60)
  • 1
    • 0022457104 scopus 로고
    • A neuronal antigen in the brains of Alzheimer patients
    • B.L. Wolozin, A. Pruchnicki, D.W. Dickson, and P. Davies A neuronal antigen in the brains of Alzheimer patients Science 232 1986 648 650
    • (1986) Science , vol.232 , pp. 648-650
    • Wolozin, B.L.1    Pruchnicki, A.2    Dickson, D.W.3    Davies, P.4
  • 3
    • 0032543684 scopus 로고    scopus 로고
    • Association of missense and 5'-splice-site mutations in tau with the inherited dementia FTDP-17
    • M. Hutton, C.L. Lendon, P. Rizzu, M. Baker, S. Froelich, and H. Houlden Association of missense and 5'-splice-site mutations in tau with the inherited dementia FTDP-17 Nature 393 1998 702 705
    • (1998) Nature , vol.393 , pp. 702-705
    • Hutton, M.1    Lendon, C.L.2    Rizzu, P.3    Baker, M.4    Froelich, S.5    Houlden, H.6
  • 5
    • 79959689333 scopus 로고    scopus 로고
    • Identification of common variants influencing risk of the tauopathy progressive supranuclear palsy
    • G.U. Hoglinger, N.M. Melhem, D.W. Dickson, P.M. Sleiman, L.S. Wang, and L. Klei Identification of common variants influencing risk of the tauopathy progressive supranuclear palsy Nat Genet 43 2011 699 705
    • (2011) Nat Genet , vol.43 , pp. 699-705
    • Hoglinger, G.U.1    Melhem, N.M.2    Dickson, D.W.3    Sleiman, P.M.4    Wang, L.S.5    Klei, L.6
  • 6
    • 7344220963 scopus 로고    scopus 로고
    • Segregation of a missense mutation in the microtubule-associated protein tau gene with familial frontotemporal dementia and parkinsonism
    • C. Dumanchin, A. Camuzat, D. Campion, P. Verpillat, D. Hannequin, and B. Dubois Segregation of a missense mutation in the microtubule-associated protein tau gene with familial frontotemporal dementia and parkinsonism Hum Mol Genet 7 1998 1825 1829
    • (1998) Hum Mol Genet , vol.7 , pp. 1825-1829
    • Dumanchin, C.1    Camuzat, A.2    Campion, D.3    Verpillat, P.4    Hannequin, D.5    Dubois, B.6
  • 7
    • 84863762839 scopus 로고    scopus 로고
    • Prion-like behaviour and tau-dependent cytotoxicity of pyroglutamylated amyloid-beta
    • J.M. Nussbaum, S. Schilling, H. Cynis, A. Silva, E. Swanson, and T. Wangsanut Prion-like behaviour and tau-dependent cytotoxicity of pyroglutamylated amyloid-beta Nature 485 2012 651 655
    • (2012) Nature , vol.485 , pp. 651-655
    • Nussbaum, J.M.1    Schilling, S.2    Cynis, H.3    Silva, A.4    Swanson, E.5    Wangsanut, T.6
  • 8
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model
    • E.D. Roberson, K. Scearce-Levie, J.J. Palop, F. Yan, I.H. Cheng, and T. Wu Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer's disease mouse model Science 316 2007 750 754
    • (2007) Science , vol.316 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3    Yan, F.4    Cheng, I.H.5    Wu, T.6
  • 9
    • 15144347942 scopus 로고    scopus 로고
    • Emergence of immunoreactivities for phosphorylated tau and amyloid-beta protein in chronic stage of fluid percussion injury in rat brain
    • S. Hoshino, A. Tamaoka, M. Takahashi, S. Kobayashi, T. Furukawa, and Y. Oaki Emergence of immunoreactivities for phosphorylated tau and amyloid-beta protein in chronic stage of fluid percussion injury in rat brain Neuroreport 9 1998 1879 1883
    • (1998) Neuroreport , vol.9 , pp. 1879-1883
    • Hoshino, S.1    Tamaoka, A.2    Takahashi, M.3    Kobayashi, S.4    Furukawa, T.5    Oaki, Y.6
  • 10
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • H. Braak, and E. Braak Neuropathological stageing of Alzheimer-related changes Acta Neuropathol 82 1991 239 259
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 12
    • 77955322042 scopus 로고    scopus 로고
    • Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models
    • L.M. Ittner, Y.D. Ke, F. Delerue, M. Bi, A. Gladbach, and J. van Eersel Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models Cell 142 2010 387 397
    • (2010) Cell , vol.142 , pp. 387-397
    • Ittner, L.M.1    Ke, Y.D.2    Delerue, F.3    Bi, M.4    Gladbach, A.5    Van Eersel, J.6
  • 13
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • G.M. Shankar, B.L. Bloodgood, M. Townsend, D.M. Walsh, D.J. Selkoe, and B.L. Sabatini Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway J Neurosci 27 2007 2866 2875
    • (2007) J Neurosci , vol.27 , pp. 2866-2875
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.L.6
  • 15
    • 0037775776 scopus 로고    scopus 로고
    • Selectively reduced expression of synaptic plasticity-related genes in APP+PS1 transgenic mice
    • C.A. Dickey, J.F. Loring, P.S. Eastman, J.R. Montgomery, M. Gordon, and D.G. Morgan Selectively reduced expression of synaptic plasticity-related genes in APP+PS1 transgenic mice J Neurosci 23 2003 5219 5226
    • (2003) J Neurosci , vol.23 , pp. 5219-5226
    • Dickey, C.A.1    Loring, J.F.2    Eastman, P.S.3    Montgomery, J.R.4    Gordon, M.5    Morgan, D.G.6
  • 16
    • 4043167747 scopus 로고    scopus 로고
    • Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome
    • S. Oddo, L. Billings, J.P. Kesslak, D.H. Cribbs, and F.M. LaFerla Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome Neuron 43 2004 321 332
    • (2004) Neuron , vol.43 , pp. 321-332
    • Oddo, S.1    Billings, L.2    Kesslak, J.P.3    Cribbs, D.H.4    Laferla, F.M.5
  • 17
    • 77958566761 scopus 로고    scopus 로고
    • Phenothiazine-mediated rescue of cognition in tau transgenic mice requires neuroprotection and reduced soluble tau burden
    • J.C. O'Leary 3rd, Q. Li, P. Marinec, L.J. Blair, E.E. Congdon, and A.G. Johnson Phenothiazine-mediated rescue of cognition in tau transgenic mice requires neuroprotection and reduced soluble tau burden Mol Neurodegener 5 2010 45
    • (2010) Mol Neurodegener , vol.5 , pp. 45
    • O'Leary III, J.C.1    Li, Q.2    Marinec, P.3    Blair, L.J.4    Congdon, E.E.5    Johnson, A.G.6
  • 18
  • 19
    • 69449093036 scopus 로고    scopus 로고
    • Age-dependent impairment of cognitive and synaptic function in the htau mouse model of tau pathology
    • M. Polydoro, C.M. Acker, K. Duff, P.E. Castillo, and P. Davies Age-dependent impairment of cognitive and synaptic function in the htau mouse model of tau pathology J Neurosci 29 2009 10741 10749
    • (2009) J Neurosci , vol.29 , pp. 10741-10749
    • Polydoro, M.1    Acker, C.M.2    Duff, K.3    Castillo, P.E.4    Davies, P.5
  • 20
    • 78449254717 scopus 로고    scopus 로고
    • Phosphorylation dynamics regulate Hsp27-mediated rescue of neuronal plasticity deficits in tau transgenic mice
    • J.F. Abisambra, L.J. Blair, S.E. Hill, J. Jones, C. Kraft, and J. Rogers Phosphorylation dynamics regulate Hsp27-mediated rescue of neuronal plasticity deficits in tau transgenic mice J Neurosci 30 2010 15374 15382
    • (2010) J Neurosci , vol.30 , pp. 15374-15382
    • Abisambra, J.F.1    Blair, L.J.2    Hill, S.E.3    Jones, J.4    Kraft, C.5    Rogers, J.6
  • 21
    • 33847369469 scopus 로고    scopus 로고
    • The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins
    • C.A. Dickey, A. Kamal, K. Lundgren, N. Klosak, R.M. Bailey, and J. Dunmore The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins J Clin Invest 117 2007 648 658
    • (2007) J Clin Invest , vol.117 , pp. 648-658
    • Dickey, C.A.1    Kamal, A.2    Lundgren, K.3    Klosak, N.4    Bailey, R.M.5    Dunmore, J.6
  • 23
    • 84875755553 scopus 로고    scopus 로고
    • Imbalance of Hsp70 family variants fosters tau accumulation [published online ahead of print December 27]
    • Jinwal UK, Akoury E, Abisambra JF, O'Leary JC, Thompson AD, Blair LJ, et al. (2012): Imbalance of Hsp70 family variants fosters tau accumulation [published online ahead of print December 27]. FASEB J 27:1450-1459.
    • (2012) FASEB J , vol.27 , pp. 1450-1459
    • Jinwal, U.K.1    Akoury, E.2    Abisambra, J.F.3    O'Leary, J.C.4    Thompson, A.D.5    Blair, L.J.6
  • 24
    • 84867809427 scopus 로고    scopus 로고
    • Analysis of the tau-associated proteome reveals that exchange of Hsp70 for Hsp90 is involved in tau degradation
    • A.D. Thompson, K.M. Scaglione, J. Prensner, A.T. Gillies, A. Chinnaiyan, and H.L. Paulson Analysis of the tau-associated proteome reveals that exchange of Hsp70 for Hsp90 is involved in tau degradation ACS Chem Biol 7 2012 1677 1686
    • (2012) ACS Chem Biol , vol.7 , pp. 1677-1686
    • Thompson, A.D.1    Scaglione, K.M.2    Prensner, J.3    Gillies, A.T.4    Chinnaiyan, A.5    Paulson, H.L.6
  • 25
    • 84869988993 scopus 로고    scopus 로고
    • Cysteine reactivity distinguishes redox sensing by the heat-inducible and constitutive forms of heat shock protein 70
    • Y. Miyata, J.N. Rauch, U.K. Jinwal, A.D. Thompson, S. Srinivasan, C.A. Dickey, and J.E. Gestwicki Cysteine reactivity distinguishes redox sensing by the heat-inducible and constitutive forms of heat shock protein 70 Chem Biol 19 2012 1391 1399
    • (2012) Chem Biol , vol.19 , pp. 1391-1399
    • Miyata, Y.1    Rauch, J.N.2    Jinwal, U.K.3    Thompson, A.D.4    Srinivasan, S.5    Dickey, C.A.6    Gestwicki, J.E.7
  • 26
    • 84862281225 scopus 로고    scopus 로고
    • Methylthioninium chloride (methylene blue) induces autophagy and attenuates tauopathy in vitro and in vivo
    • E.E. Congdon, J.W. Wu, N. Myeku, Y.H. Figueroa, M. Herman, and P.S. Marinec Methylthioninium chloride (methylene blue) induces autophagy and attenuates tauopathy in vitro and in vivo Autophagy 8 2012 609 622
    • (2012) Autophagy , vol.8 , pp. 609-622
    • Congdon, E.E.1    Wu, J.W.2    Myeku, N.3    Figueroa, Y.H.4    Herman, M.5    Marinec, P.S.6
  • 27
    • 0034671731 scopus 로고    scopus 로고
    • Selective toxicity of MKT-077 to cancer cells is mediated by its binding to the hsp70 family protein mot-2 and reactivation of p53 function
    • R. Wadhwa, T. Sugihara, A. Yoshida, H. Nomura, R.R. Reddel, and R. Simpson Selective toxicity of MKT-077 to cancer cells is mediated by its binding to the hsp70 family protein mot-2 and reactivation of p53 function Cancer Res 60 2000 6818 6821
    • (2000) Cancer Res , vol.60 , pp. 6818-6821
    • Wadhwa, R.1    Sugihara, T.2    Yoshida, A.3    Nomura, H.4    Reddel, R.R.5    Simpson, R.6
  • 29
    • 79960927001 scopus 로고    scopus 로고
    • Allosteric drugs: The interaction of antitumor compound MKT-077 with human Hsp70 chaperones
    • A. Rousaki, Y. Miyata, U.K. Jinwal, C.A. Dickey, J.E. Gestwicki, and E.R. Zuiderweg Allosteric drugs: The interaction of antitumor compound MKT-077 with human Hsp70 chaperones J Mol Biol 411 2011 614 632
    • (2011) J Mol Biol , vol.411 , pp. 614-632
    • Rousaki, A.1    Miyata, Y.2    Jinwal, U.K.3    Dickey, C.A.4    Gestwicki, J.E.5    Zuiderweg, E.R.6
  • 30
    • 84872680675 scopus 로고    scopus 로고
    • Activation of Hsp70 reduces neurotoxicity by promoting polyglutamine protein degradation
    • A.M. Wang, Y. Miyata, S. Klinedinst, H.-M. Peng, J.C. Chua, and T. Komiyama Activation of Hsp70 reduces neurotoxicity by promoting polyglutamine protein degradation Nat Chem Biol 9 2013 112 118
    • (2013) Nat Chem Biol , vol.9 , pp. 112-118
    • Wang, A.M.1    Miyata, Y.2    Klinedinst, S.3    Peng, H.-M.4    Chua, J.C.5    Komiyama, T.6
  • 31
    • 84860369416 scopus 로고    scopus 로고
    • Rhodacyanine derivative selectively targets cancer cells and overcomes tamoxifen resistance
    • J. Koren 3rd, Y. Miyata, J. Kiray, J.C. O'Leary, L. Nguyen, and J. Guo Rhodacyanine derivative selectively targets cancer cells and overcomes tamoxifen resistance PloS One 7 2012 e35566
    • (2012) PloS One , vol.7 , pp. 35566
    • Koren III, J.1    Miyata, Y.2    Kiray, J.3    O'Leary, J.C.4    Nguyen, L.5    Guo, J.6
  • 33
    • 6344275303 scopus 로고    scopus 로고
    • Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast
    • R.T. Youker, P. Walsh, T. Beilharz, T. Lithgow, and J.L. Brodsky Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast Mol Biol Cell 15 2004 4787 4797
    • (2004) Mol Biol Cell , vol.15 , pp. 4787-4797
    • Youker, R.T.1    Walsh, P.2    Beilharz, T.3    Lithgow, T.4    Brodsky, J.L.5
  • 35
  • 38
    • 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
  • 39
    • 0035152814 scopus 로고    scopus 로고
    • Neurotrophins are required for nerve growth during development
    • K.L. Tucker, M. Meyer, and Y.A. Barde Neurotrophins are required for nerve growth during development Nat Neurosci 4 2001 29 37
    • (2001) Nat Neurosci , vol.4 , pp. 29-37
    • Tucker, K.L.1    Meyer, M.2    Barde, Y.A.3
  • 40
    • 33748300645 scopus 로고    scopus 로고
    • Microdeletion encompassing MAPT at chromosome 17q21.3 is associated with developmental delay and learning disability
    • C. Shaw-Smith, A.M. Pittman, L. Willatt, H. Martin, L. Rickman, and S. Gribble Microdeletion encompassing MAPT at chromosome 17q21.3 is associated with developmental delay and learning disability Nat Genet 38 2006 1032 1037
    • (2006) Nat Genet , vol.38 , pp. 1032-1037
    • Shaw-Smith, C.1    Pittman, A.M.2    Willatt, L.3    Martin, H.4    Rickman, L.5    Gribble, S.6
  • 41
    • 84856708923 scopus 로고    scopus 로고
    • Tau deficiency induces parkinsonism with dementia by impairing APP-mediated iron export
    • P. Lei, S. Ayton, D.I. Finkelstein, L. Spoerri, G.D. Ciccotosto, and D.K. Wright Tau deficiency induces parkinsonism with dementia by impairing APP-mediated iron export Nat Med 18 2012 291 295
    • (2012) Nat Med , vol.18 , pp. 291-295
    • Lei, P.1    Ayton, S.2    Finkelstein, D.I.3    Spoerri, L.4    Ciccotosto, G.D.5    Wright, D.K.6
  • 43
    • 77952081276 scopus 로고    scopus 로고
    • Discovery of brain-penetrant, orally bioavailable aminothienopyridazine inhibitors of tau aggregation
    • C. Ballatore, K.R. Brunden, F. Piscitelli, M.J. James, A. Crowe, and Y. Yao Discovery of brain-penetrant, orally bioavailable aminothienopyridazine inhibitors of tau aggregation J Med Chem 53 2010 3739 3747
    • (2010) J Med Chem , vol.53 , pp. 3739-3747
    • Ballatore, C.1    Brunden, K.R.2    Piscitelli, F.3    James, M.J.4    Crowe, A.5    Yao, Y.6
  • 44
    • 65249128503 scopus 로고    scopus 로고
    • Challenges in the conduct of disease-modifying trials in AD: Practical experience from a phase 2 trial of Tau-aggregation inhibitor therapy
    • C. Wischik, and R. Staff Challenges in the conduct of disease-modifying trials in AD: Practical experience from a phase 2 trial of Tau-aggregation inhibitor therapy J Nutr Health Aging 13 2009 367 369
    • (2009) J Nutr Health Aging , vol.13 , pp. 367-369
    • Wischik, C.1    Staff, R.2
  • 45
    • 0035808457 scopus 로고    scopus 로고
    • Indirubins inhibit glycogen synthase kinase-3 beta and CDK5/p25, two protein kinases involved in abnormal tau phosphorylation in Alzheimer's disease. A property common to most cyclin-dependent kinase inhibitors?
    • S. Leclerc, M. Garnier, R. Hoessel, D. Marko, J.A. Bibb, and G.L. Snyder Indirubins inhibit glycogen synthase kinase-3 beta and CDK5/p25, two protein kinases involved in abnormal tau phosphorylation in Alzheimer's disease. A property common to most cyclin-dependent kinase inhibitors? J Biol Chem 276 2001 251 260
    • (2001) J Biol Chem , vol.276 , pp. 251-260
    • Leclerc, S.1    Garnier, M.2    Hoessel, R.3    Marko, D.4    Bibb, J.A.5    Snyder, G.L.6
  • 46
    • 0038689162 scopus 로고    scopus 로고
    • Cdk5 is a key factor in tau aggregation and tangle formation in vivo
    • W. Noble, V. Olm, K. Takata, E. Casey, O. Mary, and J. Meyerson Cdk5 is a key factor in tau aggregation and tangle formation in vivo Neuron 38 2003 555 565
    • (2003) Neuron , vol.38 , pp. 555-565
    • Noble, W.1    Olm, V.2    Takata, K.3    Casey, E.4    Mary, O.5    Meyerson, J.6
  • 47
    • 21044449225 scopus 로고    scopus 로고
    • Inhibition of glycogen synthase kinase-3 by lithium correlates with reduced tauopathy and degeneration in vivo
    • W. Noble, E. Planel, C. Zehr, V. Olm, J. Meyerson, and F. Suleman Inhibition of glycogen synthase kinase-3 by lithium correlates with reduced tauopathy and degeneration in vivo Proc Natl Acad Sci U S A 102 2005 6990 6995
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 6990-6995
    • Noble, W.1    Planel, E.2    Zehr, C.3    Olm, V.4    Meyerson, J.5    Suleman, F.6
  • 48
    • 0345405447 scopus 로고    scopus 로고
    • Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles
    • J.C. Cruz, H.C. Tseng, J.A. Goldman, H. Shih, and L.H. Tsai Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles Neuron 40 2003 471 483
    • (2003) Neuron , vol.40 , pp. 471-483
    • Cruz, J.C.1    Tseng, H.C.2    Goldman, J.A.3    Shih, H.4    Tsai, L.H.5
  • 49
    • 57049139853 scopus 로고    scopus 로고
    • Two motifs within the tau microtubule-binding domain mediate its association with the hsc70 molecular chaperone
    • M. Sarkar, J. Kuret, and G. Lee Two motifs within the tau microtubule-binding domain mediate its association with the hsc70 molecular chaperone J Neurosci Res 86 2008 2763 2773
    • (2008) J Neurosci Res , vol.86 , pp. 2763-2773
    • Sarkar, M.1    Kuret, J.2    Lee, G.3
  • 50
    • 33745959291 scopus 로고    scopus 로고
    • Deletion of the ubiquitin ligase CHIP leads to the accumulation, but not the aggregation, of both endogenous phospho- and caspase-3-cleaved tau species
    • C.A. Dickey, M. Yue, W.L. Lin, D.W. Dickson, J.H. Dunmore, and W.C. Lee Deletion of the ubiquitin ligase CHIP leads to the accumulation, but not the aggregation, of both endogenous phospho- and caspase-3-cleaved tau species J Neurosci 26 2006 6985 6996
    • (2006) J Neurosci , vol.26 , pp. 6985-6996
    • Dickey, C.A.1    Yue, M.2    Lin, W.L.3    Dickson, D.W.4    Dunmore, J.H.5    Lee, W.C.6
  • 52
    • 0028151509 scopus 로고
    • The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE
    • A. Szabo, T. Langer, H. Schroder, J. Flanagan, B. Bukau, and F.U. Hartl The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE Proc Natl Acad Sci U S A 91 1994 10345 10349
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 10345-10349
    • Szabo, A.1    Langer, T.2    Schroder, H.3    Flanagan, J.4    Bukau, B.5    Hartl, F.U.6
  • 53
    • 33750842131 scopus 로고    scopus 로고
    • Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis
    • X. Wang, J. Venable, P. LaPointe, D.M. Hutt, A.V. Koulov, and J. Coppinger Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis Cell 127 2006 803 815
    • (2006) Cell , vol.127 , pp. 803-815
    • Wang, X.1    Venable, J.2    Lapointe, P.3    Hutt, D.M.4    Koulov, A.V.5    Coppinger, J.6
  • 54
    • 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, and M. Kawakami 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
  • 55
    • 0032834594 scopus 로고    scopus 로고
    • Phase i trial of the selective mitochondrial toxin MKT077 in chemo-resistant solid tumours
    • D.J. Propper, J.P. Braybrooke, D.J. Taylor, R. Lodi, P. Styles, and J.A. Cramer Phase I trial of the selective mitochondrial toxin MKT077 in chemo-resistant solid tumours Ann Oncol 10 1999 923 927
    • (1999) Ann Oncol , vol.10 , pp. 923-927
    • Propper, D.J.1    Braybrooke, J.P.2    Taylor, D.J.3    Lodi, R.4    Styles, P.5    Cramer, J.A.6
  • 56
    • 0030823337 scopus 로고    scopus 로고
    • Synthesis and evaluation of novel rhodacyanine dyes that exhibit antitumor activity
    • M. Kawakami, K. Koya, T. Ukai, N. Tatsuta, A. Ikegawa, and K. Ogawa Synthesis and evaluation of novel rhodacyanine dyes that exhibit antitumor activity J Med Chem 40 1997 3151 3160
    • (1997) J Med Chem , vol.40 , pp. 3151-3160
    • Kawakami, M.1    Koya, K.2    Ukai, T.3    Tatsuta, N.4    Ikegawa, A.5    Ogawa, K.6
  • 58
    • 84989996390 scopus 로고
    • Chemistry of the cyanine dyes
    • L.G. Brooker Chemistry of the cyanine dyes Ann N Y Acad Sci 50 1948 108
    • (1948) Ann N y Acad Sci , vol.50 , pp. 108
    • Brooker, L.G.1
  • 59
    • 0013945751 scopus 로고
    • The chemical, spectral, and biological properties of monomethine cyanine dyes containing 1,3-benzoxazine and quinazoline nuclei
    • R.W. Carney, J. Wojtkunski, E.A. Konopka, and G. deStevens The chemical, spectral, and biological properties of monomethine cyanine dyes containing 1,3-benzoxazine and quinazoline nuclei J Med Chem 9 1966 758 762
    • (1966) J Med Chem , vol.9 , pp. 758-762
    • Carney, R.W.1    Wojtkunski, J.2    Konopka, E.A.3    Destevens, G.4
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