메뉴 건너뛰기




Volumn 11, Issue 7, 2016, Pages 2041-2048

Inhibition of Both Hsp70 Activity and Tau Aggregation in Vitro Best Predicts Tau Lowering Activity of Small Molecules

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DERIVATIVE; AMINOTHIENOPYRIDAZINE; ANTHRAQUINONE; CARBOCYANINE; DIHYDROPYRIMIDINE; FLAVONOL; HEAT SHOCK PROTEIN 70; PHENOTHIAZINE; PHENOXY N ARYLACETAMIDE; PIPERIDINE 3 CARBOXAMIDE; POLYPHENOL; PROTEIN INHIBITOR; RHODACYANINE; RHODANINE; SULFONAMIDE; TAU PROTEIN; UNCLASSIFIED DRUG; MAPT PROTEIN, HUMAN; MOLECULAR LIBRARY;

EID: 84978715674     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/acschembio.6b00223     Document Type: Article
Times cited : (14)

References (50)
  • 1
    • 33745018376 scopus 로고    scopus 로고
    • The genetics of neurodegenerative diseases
    • Hardy, J. and Orr, H. (2006) The genetics of neurodegenerative diseases J. Neurochem. 97, 1690-1699 10.1111/j.1471-4159.2006.03979.x
    • (2006) J. Neurochem. , vol.97 , pp. 1690-1699
    • Hardy, J.1    Orr, H.2
  • 3
    • 84924980333 scopus 로고    scopus 로고
    • Advances in Therapeutics for Neurodegenerative Tauopathies: Moving toward the Specific Targeting of the Most Toxic Tau Species
    • Gerson, J. E., Castillo-Carranza, D. L., and Kayed, R. (2014) Advances in Therapeutics for Neurodegenerative Tauopathies: Moving toward the Specific Targeting of the Most Toxic Tau Species ACS Chem. Neurosci. 5, 752-769 10.1021/cn500143n
    • (2014) ACS Chem. Neurosci. , vol.5 , pp. 752-769
    • Gerson, J.E.1    Castillo-Carranza, D.L.2    Kayed, R.3
  • 7
    • 70349638299 scopus 로고    scopus 로고
    • Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies
    • Brunden, K. R., Trojanowski, J. Q., and Lee, V. M. (2009) Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies Nat. Rev. Drug Discovery 8, 783-793 10.1038/nrd2959
    • (2009) Nat. Rev. Drug Discovery , vol.8 , pp. 783-793
    • Brunden, K.R.1    Trojanowski, J.Q.2    Lee, V.M.3
  • 12
    • 20844450734 scopus 로고    scopus 로고
    • Development of a high throughput drug screening assay for the detection of changes in tau levels - Proof of concept with HSP90 inhibitors
    • Dickey, C. A., Eriksen, J., Kamal, A., Burrows, F., Kasibhatla, S., Eckman, C. B., Hutton, M., and Petrucelli, L. (2005) Development of a high throughput drug screening assay for the detection of changes in tau levels - proof of concept with HSP90 inhibitors Curr. Alzheimer Res. 2, 231-238 10.2174/1567205053585927
    • (2005) Curr. Alzheimer Res. , vol.2 , pp. 231-238
    • Dickey, C.A.1    Eriksen, J.2    Kamal, A.3    Burrows, F.4    Kasibhatla, S.5    Eckman, C.B.6    Hutton, M.7    Petrucelli, L.8
  • 16
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T., and Sulzer, D. (2004) Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy Science 305, 1292-1295 10.1126/science.1101738
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 17
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease
    • Auluck, P. K., Chan, H. Y., Trojanowski, J. Q., Lee, V. M., and Bonini, N. M. (2002) Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease Science 295, 865-868 10.1126/science.1067389
    • (2002) Science , vol.295 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.2    Trojanowski, J.Q.3    Lee, V.M.4    Bonini, N.M.5
  • 21
    • 36148989163 scopus 로고    scopus 로고
    • High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK
    • Chang, L., Bertelsen, E. B., Wisen, S., Larsen, E. M., Zuiderweg, E. R., and Gestwicki, J. E. (2008) High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK Anal. Biochem. 372, 167-176 10.1016/j.ab.2007.08.020
    • (2008) Anal. Biochem. , vol.372 , pp. 167-176
    • Chang, L.1    Bertelsen, E.B.2    Wisen, S.3    Larsen, E.M.4    Zuiderweg, E.R.5    Gestwicki, J.E.6
  • 22
    • 84869988993 scopus 로고    scopus 로고
    • Cysteine reactivity distinguishes redox sensing by the heat-inducible and constitutive forms of heat shock protein 70
    • Miyata, Y., Rauch, J. N., Jinwal, U. K., Thompson, A. D., Srinivasan, S., Dickey, C. A., and Gestwicki, J. E. (2012) Cysteine reactivity distinguishes redox sensing by the heat-inducible and constitutive forms of heat shock protein 70 Chem. Biol. 19, 1391-1399 10.1016/j.chembiol.2012.07.026
    • (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
  • 24
    • 84896860139 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibitors. 1. 2,5′-thiodipyrimidine and 5-(phenylthio)pyrimidine acrylamides as irreversible binders to an allosteric site on heat shock protein 70
    • Kang, Y., Taldone, T., Patel, H. J., Patel, P. D., Rodina, A., Gozman, A., Maharaj, R., Clement, C. C., Patel, M. R., Brodsky, J. L., Young, J. C., and Chiosis, G. (2014) Heat shock protein 70 inhibitors. 1. 2,5′-thiodipyrimidine and 5-(phenylthio)pyrimidine acrylamides as irreversible binders to an allosteric site on heat shock protein 70 J. Med. Chem. 57, 1188-1207 10.1021/jm401551n
    • (2014) J. Med. Chem. , vol.57 , pp. 1188-1207
    • Kang, Y.1    Taldone, T.2    Patel, H.J.3    Patel, P.D.4    Rodina, A.5    Gozman, A.6    Maharaj, R.7    Clement, C.C.8    Patel, M.R.9    Brodsky, J.L.10    Young, J.C.11    Chiosis, G.12
  • 25
    • 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
    • Taldone, T., Kang, Y., Patel, H. J., Patel, M. R., Patel, P. D., Rodina, A., Patel, Y., Gozman, A., Maharaj, R., Clement, C. C., Lu, A., Young, J. C., and Chiosis, G. (2014) 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, 1208-1224 10.1021/jm401552y
    • (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    Lu, A.11    Young, J.C.12    Chiosis, G.13
  • 26
    • 84861182695 scopus 로고    scopus 로고
    • Novel inhibitors of heat shock protein Hsp70-mediated luciferase refolding that bind to DnaJ
    • Cassel, J. A., Ilyin, S., McDonnell, M. E., and Reitz, A. B. (2012) Novel inhibitors of heat shock protein Hsp70-mediated luciferase refolding that bind to DnaJ Bioorg. Med. Chem. 20, 3609-3614 10.1016/j.bmc.2012.03.067
    • (2012) Bioorg. Med. Chem. , vol.20 , pp. 3609-3614
    • Cassel, J.A.1    Ilyin, S.2    McDonnell, M.E.3    Reitz, A.B.4
  • 27
    • 70349768075 scopus 로고    scopus 로고
    • A small molecule inhibitor of inducible heat shock protein 70
    • Leu, J. I., Pimkina, J., Frank, A., Murphy, M. E., and George, D. L. (2009) A small molecule inhibitor of inducible heat shock protein 70 Mol. Cell 36, 15-27 10.1016/j.molcel.2009.09.023
    • (2009) Mol. Cell , vol.36 , pp. 15-27
    • Leu, J.I.1    Pimkina, J.2    Frank, A.3    Murphy, M.E.4    George, D.L.5
  • 29
    • 84876588286 scopus 로고    scopus 로고
    • Aminothienopyridazines and methylene blue affect Tau fibrillization via cysteine oxidation
    • Crowe, A., James, M. J., Lee, V. M., Smith, A. B., 3rd, Trojanowski, J. Q., Ballatore, C., and Brunden, K. R. (2013) Aminothienopyridazines and methylene blue affect Tau fibrillization via cysteine oxidation J. Biol. Chem. 288, 11024-11037 10.1074/jbc.M112.436006
    • (2013) J. Biol. Chem. , vol.288 , pp. 11024-11037
    • Crowe, A.1    James, M.J.2    Lee, V.M.3    Smith, A.B.4    Trojanowski, J.Q.5    Ballatore, C.6    Brunden, K.R.7
  • 32
    • 84858595119 scopus 로고    scopus 로고
    • Using intramolecular disulfide bonds in tau protein to deduce structural features of aggregation-resistant conformations
    • Walker, S., Ullman, O., and Stultz, C. M. (2012) Using intramolecular disulfide bonds in tau protein to deduce structural features of aggregation-resistant conformations J. Biol. Chem. 287, 9591-9600 10.1074/jbc.M111.336107
    • (2012) J. Biol. Chem. , vol.287 , pp. 9591-9600
    • Walker, S.1    Ullman, O.2    Stultz, C.M.3
  • 33
    • 0033155997 scopus 로고    scopus 로고
    • Disulfide-cross-linked tau and MAP2 homodimers readily promote microtubule assembly
    • Di Noto, L., DeTure, M. A., and Purich, D. L. (1999) Disulfide-cross-linked tau and MAP2 homodimers readily promote microtubule assembly Mol. Cell Biol. Res. Commun. 2, 71-76 10.1006/mcbr.1999.0153
    • (1999) Mol. Cell Biol. Res. Commun. , vol.2 , pp. 71-76
    • Di Noto, L.1    DeTure, M.A.2    Purich, D.L.3
  • 34
    • 0029742937 scopus 로고    scopus 로고
    • Selective inhibition of Alzheimer disease-like tau aggregation by phenothiazines
    • Wischik, C. M., Edwards, P. C., Lai, R. Y., Roth, M., and Harrington, C. R. (1996) Selective inhibition of Alzheimer disease-like tau aggregation by phenothiazines Proc. Natl. Acad. Sci. U. S. A. 93, 11213-11218 10.1073/pnas.93.20.11213
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 11213-11218
    • Wischik, C.M.1    Edwards, P.C.2    Lai, R.Y.3    Roth, M.4    Harrington, C.R.5
  • 37
    • 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
    • Wischik, C. and Staff, R. (2009) 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, 367-369 10.1007/s12603-009-0046-5
    • (2009) J. Nutr., Health Aging , vol.13 , pp. 367-369
    • Wischik, C.1    Staff, R.2
  • 38
    • 84898059466 scopus 로고    scopus 로고
    • Tau-aggregation inhibitor therapy for Alzheimer's disease
    • Wischik, C. M., Harrington, C. R., and Storey, J. M. (2013) Tau-aggregation inhibitor therapy for Alzheimer's disease Biochem. Pharmacol. 88, 529 10.1016/j.bcp.2013.12.008
    • (2013) Biochem. Pharmacol. , vol.88 , pp. 529
    • Wischik, C.M.1    Harrington, C.R.2    Storey, J.M.3
  • 43
    • 84956696088 scopus 로고    scopus 로고
    • Pan Assay Interference Compounds (PAINS) and Other Promiscuous Compounds in Antifungal Research
    • Pouliot, M. and Jeanmart, S. (2016) Pan Assay Interference Compounds (PAINS) and Other Promiscuous Compounds in Antifungal Research J. Med. Chem. 59, 497-503 10.1021/acs.jmedchem.5b00361
    • (2016) J. Med. Chem. , vol.59 , pp. 497-503
    • Pouliot, M.1    Jeanmart, S.2
  • 44
    • 77950571108 scopus 로고    scopus 로고
    • New substructure filters for removal of pan assay interference compounds (PAINS) from screening libraries and for their exclusion in bioassays
    • Baell, J. B. and Holloway, G. A. (2010) New substructure filters for removal of pan assay interference compounds (PAINS) from screening libraries and for their exclusion in bioassays J. Med. Chem. 53, 2719-2740 10.1021/jm901137j
    • (2010) J. Med. Chem. , vol.53 , pp. 2719-2740
    • Baell, J.B.1    Holloway, G.A.2
  • 45
    • 34248222543 scopus 로고    scopus 로고
    • Pharmacologic reductions of total tau levels; Implications for the role of microtubule dynamics in regulating tau expression
    • Dickey, C. A., Ash, P., Klosak, N., Lee, W. C., Petrucelli, L., Hutton, M., and Eckman, C. B. (2006) Pharmacologic reductions of total tau levels; implications for the role of microtubule dynamics in regulating tau expression Mol. Neurodegener. 1, 6 10.1186/1750-1326-1-6
    • (2006) Mol. Neurodegener. , vol.1 , pp. 6
    • Dickey, C.A.1    Ash, P.2    Klosak, N.3    Lee, W.C.4    Petrucelli, L.5    Hutton, M.6    Eckman, C.B.7
  • 47
    • 84920928078 scopus 로고    scopus 로고
    • Screening strategies to identify HSP70 modulators to treat Alzheimer's disease
    • Repalli, J. and Meruelo, D. (2015) Screening strategies to identify HSP70 modulators to treat Alzheimer's disease Drug Des., Dev. Ther. 9, 321-331 10.2147/DDDT.S72165
    • (2015) Drug Des., Dev. Ther. , vol.9 , pp. 321-331
    • Repalli, J.1    Meruelo, D.2
  • 48
    • 31544477481 scopus 로고    scopus 로고
    • Novel tacrine-melatonin hybrids as dual-acting drugs for Alzheimer disease, with improved acetylcholinesterase inhibitory and antioxidant properties
    • Rodriguez-Franco, M. I., Fernandez-Bachiller, M. I., Perez, C., Hernandez-Ledesma, B., and Bartolome, B. (2006) Novel tacrine-melatonin hybrids as dual-acting drugs for Alzheimer disease, with improved acetylcholinesterase inhibitory and antioxidant properties J. Med. Chem. 49, 459-462 10.1021/jm050746d
    • (2006) J. Med. Chem. , vol.49 , pp. 459-462
    • Rodriguez-Franco, M.I.1    Fernandez-Bachiller, M.I.2    Perez, C.3    Hernandez-Ledesma, B.4    Bartolome, B.5
  • 49
    • 84935857252 scopus 로고    scopus 로고
    • Novel Bioactive Hybrid Compound Dual Targeting Estrogen Receptor and Histone Deacetylase for the Treatment of Breast Cancer
    • Tang, C., Li, C., Zhang, S., Hu, Z., Wu, J., Dong, C., Huang, J., and Zhou, H. B. (2015) Novel Bioactive Hybrid Compound Dual Targeting Estrogen Receptor and Histone Deacetylase for the Treatment of Breast Cancer J. Med. Chem. 58, 4550-4572 10.1021/acs.jmedchem.5b00099
    • (2015) J. Med. Chem. , vol.58 , pp. 4550-4572
    • Tang, C.1    Li, C.2    Zhang, S.3    Hu, Z.4    Wu, J.5    Dong, C.6    Huang, J.7    Zhou, H.B.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.