메뉴 건너뛰기




Volumn 5, Issue 9, 2014, Pages 823-829

Proteasome activation is a mechanism for pyrazolone small molecules displaying therapeutic potential in amyotrophic lateral sclerosis

Author keywords

Amyotrophic lateral sclerosis; Drug discovery; Neurodegeneration; Proteasome activator; Pyrazolone; Target identification

Indexed keywords

26S PROTEASOME REGULATORY SUBUNIT 4; 26S PROTEASOME REGULATORY SUBUNIT 6B; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; CHAPERONIN CONTAINING TCP1; NEUROPROTECTIVE AGENT; PROTEASOME; PROTEASOME INHIBITOR; PYRAZOLONE DERIVATIVE; UNCLASSIFIED DRUG; BENZYLOXYCARBONYLLEUCYL-LEUCYL-LEUCINE ALDEHYDE; CELL CYCLE PROTEIN; CYSTEINE PROTEINASE INHIBITOR; LEUPEPTIN; NONSTEROID ANTIINFLAMMATORY AGENT; PHOTOPROTEIN; PYRAZOLONE; SOD1 G93A PROTEIN; SUPEROXIDE DISMUTASE; UBIQUITIN; UBQLN2 PROTEIN, HUMAN;

EID: 84924980848     PISSN: None     EISSN: 19487193     Source Type: Journal    
DOI: 10.1021/cn500147v     Document Type: Article
Times cited : (45)

References (38)
  • 2
    • 33747605320 scopus 로고    scopus 로고
    • Molecular biology of amyotrophic lateral sclerosis: Insights from genetics
    • Pasinelli, P., and Brown, R. H. (2006) Molecular biology of amyotrophic lateral sclerosis: insights from genetics. Nat. Rev. Neurosci. 7, 710-723.
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 710-723
    • Pasinelli, P.1    Brown, R.H.2
  • 5
    • 60849093466 scopus 로고    scopus 로고
    • Current hypotheses for the underlying biology of amyotrophic lateral sclerosis
    • Rothstein, J. D. (2009) Current hypotheses for the underlying biology of amyotrophic lateral sclerosis. Ann. Neurol. 65 (Suppl 1), S3-9.
    • (2009) Ann. Neurol. , vol.65 , pp. S3-S9
    • Rothstein, J.D.1
  • 6
    • 77953028624 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis is a non-amyloid disease in which extensive misfolding of SOD1 is unique to the familial form
    • Kerman, A., Liu, H. N., Croul, S., Bilbao, J., Rogaeva, E., Zinman, L., Robertson, J., and Chakrabartty, A. (2010) Amyotrophic lateral sclerosis is a non-amyloid disease in which extensive misfolding of SOD1 is unique to the familial form. Acta Neuropathol. 119, 335-344.
    • (2010) Acta Neuropathol. , vol.119 , pp. 335-344
    • Kerman, A.1    Liu, H.N.2    Croul, S.3    Bilbao, J.4    Rogaeva, E.5    Zinman, L.6    Robertson, J.7    Chakrabartty, A.8
  • 9
    • 77950867149 scopus 로고    scopus 로고
    • TAR DNA-binding protein 43 in neurodegenerative disease
    • Chen-Plotkin, A. S., Lee, V. M., and Trojanowski, J. Q. (2010) TAR DNA-binding protein 43 in neurodegenerative disease. Nat. Rev. Neurol. 6, 211-220.
    • (2010) Nat. Rev. Neurol. , vol.6 , pp. 211-220
    • Chen-Plotkin, A.S.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 11
    • 84859512071 scopus 로고    scopus 로고
    • Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosis
    • Pokrishevsky, E., Grad, L. I., Yousefi, M., Wang, J., Mackenzie, I. R., and Cashman, N. R. (2012) Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosis. PloS One 7, e35050.
    • (2012) PloS One , vol.7 , pp. e35050
    • Pokrishevsky, E.1    Grad, L.I.2    Yousefi, M.3    Wang, J.4    Mackenzie, I.R.5    Cashman, N.R.6
  • 12
    • 39049126210 scopus 로고    scopus 로고
    • Protein misfolding and neurodegeneration
    • Soto, C., and Estrada, L. D. (2008) Protein misfolding and neurodegeneration. Arch. Neurol. 65, 184-189.
    • (2008) Arch. Neurol. , vol.65 , pp. 184-189
    • Soto, C.1    Estrada, L.D.2
  • 14
    • 84862907505 scopus 로고    scopus 로고
    • ADME-guided design and synthesis of aryloxanyl pyrazolone derivatives to block mutant superoxide dismutase 1 (SOD1) cytotoxicity and protein aggregation: Potential application for the treatment of amyotrophic lateral sclerosis
    • Chen, T., Benmohamed, R., Kim, J., Smith, K., Amante, D., Morimoto, R. I., Kirsch, D. R., Ferrante, R. J., and Silverman, R. B. (2012) ADME-guided design and synthesis of aryloxanyl pyrazolone derivatives to block mutant superoxide dismutase 1 (SOD1) cytotoxicity and protein aggregation: potential application for the treatment of amyotrophic lateral sclerosis. J. Med. Chem. 55, 515-527.
    • (2012) J. Med. Chem. , vol.55 , pp. 515-527
    • Chen, T.1    Benmohamed, R.2    Kim, J.3    Smith, K.4    Amante, D.5    Morimoto, R.I.6    Kirsch, D.R.7    Ferrante, R.J.8    Silverman, R.B.9
  • 16
    • 33645106746 scopus 로고    scopus 로고
    • Loss of metabotropic glutamate receptor-mediated regulation of glutamate transport in chemically activated astrocytes in a rat model of amyotrophic lateral sclerosis
    • Vermeiren, C., Hemptinne, I., Vanhoutte, N., Tilleux, S., Maloteaux, J. M., and Hermans, E. (2006) Loss of metabotropic glutamate receptor-mediated regulation of glutamate transport in chemically activated astrocytes in a rat model of amyotrophic lateral sclerosis. J. Neurochem 96, 719-731.
    • (2006) J. Neurochem , vol.96 , pp. 719-731
    • Vermeiren, C.1    Hemptinne, I.2    Vanhoutte, N.3    Tilleux, S.4    Maloteaux, J.M.5    Hermans, E.6
  • 17
    • 26444471905 scopus 로고    scopus 로고
    • Structural properties and neuronal toxicity of amyotrophic lateral sclerosis-associated Cu/Zn superoxide dismutase 1 aggregates
    • Matsumoto, G., Stojanovic, A., Holmberg, C. I., Kim, S., and Morimoto, R. I. (2005) Structural properties and neuronal toxicity of amyotrophic lateral sclerosis-associated Cu/Zn superoxide dismutase 1 aggregates. J. Cell Biol. 171, 75-85.
    • (2005) J. Cell Biol. , vol.171 , pp. 75-85
    • Matsumoto, G.1    Stojanovic, A.2    Holmberg, C.I.3    Kim, S.4    Morimoto, R.I.5
  • 18
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • Morimoto, R. I. (2008) Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev. 22, 1427-1438.
    • (2008) Genes Dev. , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 20
    • 84873841667 scopus 로고    scopus 로고
    • Synthetic strategies for the biotinylation of bioactive small molecules
    • Trippier, P. C. (2013) Synthetic strategies for the biotinylation of bioactive small molecules. Chem Med Chem 8, 190-203.
    • (2013) Chem Med Chem , vol.8 , pp. 190-203
    • Trippier, P.C.1
  • 21
    • 77953708147 scopus 로고    scopus 로고
    • Biochemical target isolation for novices: Affinity-based strategies
    • Sato, S., Murata, A., Shirakawa, T., and Uesugi, M. (2010) Biochemical target isolation for novices: affinity-based strategies. Chem. Biol. 17, 616-623.
    • (2010) Chem. Biol. , vol.17 , pp. 616-623
    • Sato, S.1    Murata, A.2    Shirakawa, T.3    Uesugi, M.4
  • 22
    • 84867582469 scopus 로고    scopus 로고
    • Substituted pyrazolones require N(2) hydrogen bond donating ability to protect against cytotoxicity from protein aggregation of mutant superoxide dismutase 1
    • Trippier, P. C., Benmohammed, R., Kirsch, D. R., and Silverman, R. B. (2012) Substituted pyrazolones require N(2) hydrogen bond donating ability to protect against cytotoxicity from protein aggregation of mutant superoxide dismutase 1. Bioorg. Med. Chem. Lett. 22, 6647-6650.
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , pp. 6647-6650
    • Trippier, P.C.1    Benmohammed, R.2    Kirsch, D.R.3    Silverman, R.B.4
  • 23
    • 45749158648 scopus 로고    scopus 로고
    • Identification of the cellular targets of bioactive small organic molecules using affinity reagents
    • Leslie, B. J., and Hergenrother, P. J. (2008) Identification of the cellular targets of bioactive small organic molecules using affinity reagents. Chem. Soc. Rev. 37, 1347-1360.
    • (2008) Chem. Soc. Rev. , vol.37 , pp. 1347-1360
    • Leslie, B.J.1    Hergenrother, P.J.2
  • 25
    • 0018720271 scopus 로고
    • A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gels
    • Switzer, R. C., 3rd, Merril, C. R., and Shifrin, S. (1979) A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gels. Anal. Biochem. 98, 231-237.
    • (1979) Anal. Biochem. , vol.98 , pp. 231-237
    • Switzer, R.C.1    Merril, C.R.2    Shifrin, S.3
  • 26
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R., and Mann, M. (2003) Mass spectrometry-based proteomics. Nature 422, 198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 27
    • 3042515545 scopus 로고    scopus 로고
    • Focal dysfunction of the proteasome: A pathogenic factor in a mouse model of amyotrophic lateral sclerosis
    • Kabashi, E., Agar, J. N., Taylor, D. M., Minotti, S., and Durham, H. D. (2004) Focal dysfunction of the proteasome: a pathogenic factor in a mouse model of amyotrophic lateral sclerosis. J. Neurochem. 89, 1325-1335.
    • (2004) J. Neurochem. , vol.89 , pp. 1325-1335
    • Kabashi, E.1    Agar, J.N.2    Taylor, D.M.3    Minotti, S.4    Durham, H.D.5
  • 28
    • 45549084712 scopus 로고    scopus 로고
    • Cytoplasmic dynein could be key to understanding neurodegeneration
    • Banks, G. T., and Fisher, E. M. (2008) Cytoplasmic dynein could be key to understanding neurodegeneration. Genome Biol. 9, 214.
    • (2008) Genome Biol. , vol.9 , pp. 214
    • Banks, G.T.1    Fisher, E.M.2
  • 29
    • 7444231693 scopus 로고    scopus 로고
    • Mechanism of the eukaryotic chaperonin: Protein folding in the chamber of secrets
    • Spiess, C., Meyer, A. S., Reissmann, S., and Frydman, J. (2004) Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets. Trends Cell Biol. 14, 598-604.
    • (2004) Trends Cell Biol. , vol.14 , pp. 598-604
    • Spiess, C.1    Meyer, A.S.2    Reissmann, S.3    Frydman, J.4
  • 32
    • 84855199977 scopus 로고    scopus 로고
    • Proteasomal AAAA-TPases: Structure and function
    • Bar-Nun, S., and Glickman, M. H. (2012) Proteasomal AAAA-TPases: structure and function. Biochim. Biophys. Acta 1823, 67-82.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 67-82
    • Bar-Nun, S.1    Glickman, M.H.2
  • 33
    • 51749093587 scopus 로고    scopus 로고
    • Characterization of the proteasome interaction network using a QTAX-based tag-team strategy and protein interaction network analysis
    • Guerrero, C., Milenkovic, T., Przulj, N., Kaiser, P., and Huang, L. (2008) Characterization of the proteasome interaction network using a QTAX-based tag-team strategy and protein interaction network analysis. Proc. Natl. Acad. Sci. U.S.A. 105, 13333-13338.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 13333-13338
    • Guerrero, C.1    Milenkovic, T.2    Przulj, N.3    Kaiser, P.4    Huang, L.5
  • 34
  • 36
    • 65649124922 scopus 로고    scopus 로고
    • Proteasome regulators: Activators and inhibitors
    • Huang, L., and Chen, C. H. (2009) Proteasome regulators: activators and inhibitors. Curr. Med. Chem. 16, 931-939.
    • (2009) Curr. Med. Chem. , vol.16 , pp. 931-939
    • Huang, L.1    Chen, C.H.2
  • 37
    • 34948845308 scopus 로고    scopus 로고
    • Proteasome activator enhances survival of Huntington' s disease neuronal model cells
    • Seo, H., Sonntag, K. C., Kim, W., Cattaneo, E., and Isacson, O. (2007) Proteasome activator enhances survival of Huntington' s disease neuronal model cells. PloS One 2, e238.
    • (2007) PloS One , vol.2 , pp. e238
    • Seo, H.1    Sonntag, K.C.2    Kim, W.3    Cattaneo, E.4    Isacson, O.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.