메뉴 건너뛰기




Volumn 94, Issue 9, 2012, Pages 1974-1981

Characterization of a series of 4-aminoquinolines that stimulate caspase-7 mediated cleavage of TDP-43 and inhibit its function

Author keywords

Caspase activation; Mixed inhibition; TDP 43

Indexed keywords

4 AMINOQUINOLINE DERIVATIVE; CASPASE 3; CASPASE 7; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; OLIGONUCLEOTIDE; TAR DNA BINDING PROTEIN;

EID: 84864279352     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2012.05.020     Document Type: Article
Times cited : (23)

References (35)
  • 1
    • 38449102667 scopus 로고    scopus 로고
    • Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease
    • DOI 10.2741/2727
    • E. Buratti, and F.E. Baralle Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease Front. Biosci. 13 2008 867 878 (Pubitemid 351594732)
    • (2008) Frontiers in Bioscience , vol.13 , Issue.3 , pp. 867-878
    • Buratti, E.1    Baralle, F.E.2
  • 2
    • 77953890823 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: Emerging roles in RNA processing and neurodegeneration
    • C. Lagier-Tourenne, M. Polymenidou, and D.W. Cleveland TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration Hum. Mol. Genet. 19 2010 R46 R64
    • (2010) Hum. Mol. Genet. , vol.19
    • Lagier-Tourenne, C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 3
    • 64549100193 scopus 로고    scopus 로고
    • Structural insights into TDP-43 in nucleic-acid binding and domain interactions
    • P.H. Kuo, L.G. Doudeva, Y.T. Wang, C.K. Shen, and H.S. Yuan Structural insights into TDP-43 in nucleic-acid binding and domain interactions Nucleic Acids Res. 37 2009 1799 1808
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1799-1808
    • Kuo, P.H.1    Doudeva, L.G.2    Wang, Y.T.3    Shen, C.K.4    Yuan, H.S.5
  • 4
    • 0029066110 scopus 로고
    • Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs
    • S.H. Ou, F. Wu, D. Harrich, L.F. Garcia-Martinez, and R.B. Gaynor Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs J. Virol. 69 1995 3584 3596
    • (1995) J. Virol. , vol.69 , pp. 3584-3596
    • Ou, S.H.1    Wu, F.2    Harrich, D.3    Garcia-Martinez, L.F.4    Gaynor, R.B.5
  • 5
    • 0035965309 scopus 로고    scopus 로고
    • Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9
    • E. Buratti, and F.E. Baralle Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9 J. Biol. Chem. 276 2001 36337 36343
    • (2001) J. Biol. Chem. , vol.276 , pp. 36337-36343
    • Buratti, E.1    Baralle, F.E.2
  • 6
    • 2442676753 scopus 로고    scopus 로고
    • Nuclear factor TDP-43 binds to the polymorphic TG repeats in CFTR intron 8 and causes skipping of exon 9: A functional link with disease penetrance [2]
    • DOI 10.1086/420978
    • E. Buratti, A. Brindisi, F. Pagani, and F.E. Baralle Nuclear factor TDP-43 binds to the polymorphic TG repeats in CFTR intron 8 and causes skipping of exon 9: a functional link with disease penetrance Am. J. Hum. Genet. 74 2004 1322 1325 (Pubitemid 38669335)
    • (2004) American Journal of Human Genetics , vol.74 , Issue.6 , pp. 1322-1325
    • Buratti, E.1    Brindisi, A.2    Pagani, F.3    Baralle, F.E.4
  • 7
    • 0035794665 scopus 로고    scopus 로고
    • Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping
    • DOI 10.1093/emboj/20.7.1774
    • E. Buratti, T. Dork, E. Zuccato, F. Pagani, M. Romano, and F.E. Baralle Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping EMBO J. 20 2001 1774 1784 (Pubitemid 32299413)
    • (2001) EMBO Journal , vol.20 , Issue.7 , pp. 1774-1784
    • Buratti, E.1    Dork, T.2    Zuccato, E.3    Pagani, F.4    Romano, M.5    Baralle, F.E.6
  • 8
    • 32344435621 scopus 로고    scopus 로고
    • TDP43 depletion rescues aberrant CFTR exon 9 skipping
    • DOI 10.1016/j.febslet.2006.01.052, PII S0014579306001050
    • Y.M. Ayala, F. Pagani, and F.E. Baralle TDP43 depletion rescues aberrant CFTR exon 9 skipping FEBS Lett. 580 2006 1339 1344 (Pubitemid 43221997)
    • (2006) FEBS Letters , vol.580 , Issue.5 , pp. 1339-1344
    • Ayala, Y.M.1    Pagani, F.2    Baralle, F.E.3
  • 10
    • 84455169931 scopus 로고    scopus 로고
    • Regulation of autophagy by the neuropathological protein TDP-43
    • J.K. Bose, C.C. Huang, and C.K. Shen Regulation of autophagy by the neuropathological protein TDP-43 J. Biol. Chem. 286 2011 44441 44448
    • (2011) J. Biol. Chem. , vol.286 , pp. 44441-44448
    • Bose, J.K.1    Huang, C.C.2    Shen, C.K.3
  • 11
    • 77958604956 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis-associated proteins TDP-43 and FUS/TLS function in a common biochemical complex to co-regulate HDAC6 mRNA
    • S.H. Kim, N.P. Shanware, M.J. Bowler, and R.S. Tibbetts Amyotrophic lateral sclerosis-associated proteins TDP-43 and FUS/TLS function in a common biochemical complex to co-regulate HDAC6 mRNA J. Biol. Chem. 285 2010 34097 34105
    • (2010) J. Biol. Chem. , vol.285 , pp. 34097-34105
    • Kim, S.H.1    Shanware, N.P.2    Bowler, M.J.3    Tibbetts, R.S.4
  • 15
    • 76149120427 scopus 로고    scopus 로고
    • Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery
    • B.D. Freibaum, R.K. Chitta, A.A. High, and J.P. Taylor Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery J. Proteome Res. 9 2009 1104 1120
    • (2009) J. Proteome Res. , vol.9 , pp. 1104-1120
    • Freibaum, B.D.1    Chitta, R.K.2    High, A.A.3    Taylor, J.P.4
  • 16
    • 34447103093 scopus 로고    scopus 로고
    • TDP-43 proteinopathy: The neuropathology underlying major forms of sporadic and familial frontotemporal lobar degeneration and motor neuron disease
    • DOI 10.1007/s00401-007-0226-5
    • L.K. Kwong, M. Neumann, D.M. Sampathu, V.M. Lee, and J.Q. Trojanowski TDP-43 proteinopathy: the neuropathology underlying major forms of sporadic and familial frontotemporal lobar degeneration and motor neuron disease Acta Neuropathol. 114 2007 63 70 (Pubitemid 47029061)
    • (2007) Acta Neuropathologica , vol.114 , Issue.1 , pp. 63-70
    • Kwong, L.K.1    Neumann, M.2    Sampathu, D.M.3    Lee, V.M.-Y.4    Trojanowski, J.Q.5
  • 17
    • 69549114542 scopus 로고    scopus 로고
    • The molecular links between TDP-43 dysfunction and neurodegeneration
    • E. Buratti, and F.E. Baralle The molecular links between TDP-43 dysfunction and neurodegeneration Adv. Genet. 66 2009 1 34
    • (2009) Adv. Genet. , vol.66 , pp. 1-34
    • Buratti, E.1    Baralle, F.E.2
  • 18
    • 68349125007 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis, frontotemporal dementia and beyond: The TDP-43 diseases
    • F. Geser, M. Martinez-Lage, L.K. Kwong, V.M. Lee, and J.Q. Trojanowski Amyotrophic lateral sclerosis, frontotemporal dementia and beyond: the TDP-43 diseases J. Neurol. 256 2009 1205 1214
    • (2009) J. Neurol. , vol.256 , pp. 1205-1214
    • Geser, F.1    Martinez-Lage, M.2    Kwong, L.K.3    Lee, V.M.4    Trojanowski, J.Q.5
  • 19
    • 54049140363 scopus 로고    scopus 로고
    • The syndromes of frontotemporal dysfunction in amyotrophic lateral sclerosis
    • M.J. Strong The syndromes of frontotemporal dysfunction in amyotrophic lateral sclerosis Amyotroph. Lateral Scler. 9 2008 323 338
    • (2008) Amyotroph. Lateral Scler. , vol.9 , pp. 323-338
    • Strong, M.J.1
  • 20
    • 77953488668 scopus 로고    scopus 로고
    • Current nervous system related drug targets for the treatment of amyotrophic lateral sclerosis
    • A.C. Pawlyk, J.A. Cassel, and A.B. Reitz Current nervous system related drug targets for the treatment of amyotrophic lateral sclerosis Curr. Pharm. Des. 16 2010 2053 2073
    • (2010) Curr. Pharm. Des. , vol.16 , pp. 2053-2073
    • Pawlyk, A.C.1    Cassel, J.A.2    Reitz, A.B.3
  • 21
    • 49249118746 scopus 로고    scopus 로고
    • TDP-43 is a culprit in human neurodegeneration, and not just an innocent bystander
    • G.T. Banks, A. Kuta, A.M. Isaacs, and E.M. Fisher TDP-43 is a culprit in human neurodegeneration, and not just an innocent bystander Mamm. Genome 19 2008 299 305
    • (2008) Mamm. Genome , vol.19 , pp. 299-305
    • Banks, G.T.1    Kuta, A.2    Isaacs, A.M.3    Fisher, E.M.4
  • 22
    • 62149141328 scopus 로고    scopus 로고
    • Rethinking ALS: The FUS about TDP-43
    • C. Lagier-Tourenne, and D.W. Cleveland Rethinking ALS: the FUS about TDP-43 Cell 136 2009 1001 1004
    • (2009) Cell , vol.136 , pp. 1001-1004
    • Lagier-Tourenne, C.1    Cleveland, D.W.2
  • 24
    • 63949083624 scopus 로고    scopus 로고
    • Mimicking aspects of frontotemporal lobar degeneration and Lou Gehrig's disease in rats via TDP-43 overexpression
    • J.B. Tatom, D.B. Wang, R.D. Dayton, O. Skalli, M.L. Hutton, D.W. Dickson, and R.L. Klein Mimicking aspects of frontotemporal lobar degeneration and Lou Gehrig's disease in rats via TDP-43 overexpression Mol. Ther. 17 2009 607 613
    • (2009) Mol. Ther. , vol.17 , pp. 607-613
    • Tatom, J.B.1    Wang, D.B.2    Dayton, R.D.3    Skalli, O.4    Hutton, M.L.5    Dickson, D.W.6    Klein, R.L.7
  • 25
    • 80052967905 scopus 로고    scopus 로고
    • TDP-43: The relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration
    • R.H. Baloh TDP-43: the relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration FEBS J. 278 2011 3539 3549
    • (2011) FEBS J. , vol.278 , pp. 3539-3549
    • Baloh, R.H.1
  • 26
    • 77949910265 scopus 로고    scopus 로고
    • Review: Transactive response DNA-binding protein 43 (TDP-43): Mechanisms of neurodegeneration
    • T.F. Gendron, K.A. Josephs, and L. Petrucelli Review: transactive response DNA-binding protein 43 (TDP-43): mechanisms of neurodegeneration Neuropathol. Appl. Neurobiol. 36 2010 97 112
    • (2010) Neuropathol. Appl. Neurobiol. , vol.36 , pp. 97-112
    • Gendron, T.F.1    Josephs, K.A.2    Petrucelli, L.3
  • 29
    • 73249152831 scopus 로고    scopus 로고
    • TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration
    • I. Wegorzewska, S. Bell, N.J. Cairns, T.M. Miller, and R.H. Baloh TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration Proc. Natl. Acad. Sci. U.S.A. 106 2009 18809 18814
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 18809-18814
    • Wegorzewska, I.1    Bell, S.2    Cairns, N.J.3    Miller, T.M.4    Baloh, R.H.5
  • 30
    • 79953855830 scopus 로고    scopus 로고
    • TDP-43-induced death is associated with altered regulation of BIM and Bcl-xL and attenuated by caspase-mediated TDP-43 cleavage
    • H. Suzuki, K. Lee, and M. Matsuoka TDP-43-induced death is associated with altered regulation of BIM and Bcl-xL and attenuated by caspase-mediated TDP-43 cleavage J. Biol. Chem. 286 2011 13171 13183
    • (2011) J. Biol. Chem. , vol.286 , pp. 13171-13183
    • Suzuki, H.1    Lee, K.2    Matsuoka, M.3
  • 33
    • 78650083095 scopus 로고    scopus 로고
    • Development of a novel nonradiometric assay for nucleic acid binding to TDP-43 suitable for high-throughput screening using AlphaScreen technology
    • J.A. Cassel, B.E. Blass, A.B. Reitz, and A.C. Pawlyk Development of a novel nonradiometric assay for nucleic acid binding to TDP-43 suitable for high-throughput screening using AlphaScreen technology J. Biomol. Screen. 15 2010 1099 1106
    • (2010) J. Biomol. Screen. , vol.15 , pp. 1099-1106
    • Cassel, J.A.1    Blass, B.E.2    Reitz, A.B.3    Pawlyk, A.C.4
  • 35
    • 36249031068 scopus 로고    scopus 로고
    • Recognizing and exploiting differences between RNAi and small-molecule inhibitors
    • DOI 10.1038/nchembio1207-739, PII NCHEMBIO1207739
    • W.A. Weiss, S.S. Taylor, and K.M. Shokat Recognizing and exploiting differences between RNAi and small-molecule inhibitors Nat. Chem. Biol. 3 2007 739 744 (Pubitemid 350126879)
    • (2007) Nature Chemical Biology , vol.3 , Issue.12 , pp. 739-744
    • Weiss, W.A.1    Taylor, S.S.2    Shokat, K.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.