메뉴 건너뛰기




Volumn 55, Issue , 2015, Pages 553-572

Activation and regulation of caspase-6 and its role in neurodegenerative diseases

Author keywords

Alzheimer's disease; Caspase 6; Huntington's disease; Neurodegeneration; Regulation mechanism

Indexed keywords

AMYLOID PRECURSOR PROTEIN; CASPASE 6; CASPASE 6 INHIBITOR; CASPASE INHIBITOR; HUNTINGTIN; UNCLASSIFIED DRUG; HTT PROTEIN, HUMAN; NERVE PROTEIN;

EID: 84920836462     PISSN: 03621642     EISSN: 15454304     Source Type: Book Series    
DOI: 10.1146/annurev-pharmtox-010814-124414     Document Type: Review
Times cited : (78)

References (133)
  • 1
    • 8444220527 scopus 로고    scopus 로고
    • Molecular mechanisms of caspase regulation during apoptosis
    • Riedl SJ, Shi Y. 2004. Molecular mechanisms of caspase regulation during apoptosis. Nat. Rev. Mol. Cell Biol. 5:897-907
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 897-907
    • Riedl, S.J.1    Shi, Y.2
  • 2
    • 28444491105 scopus 로고    scopus 로고
    • Mechanisms of apoptosis through structural biology
    • Yan N, Shi Y. 2005. Mechanisms of apoptosis through structural biology. Annu. Rev. Cell Dev. Biol. 21:35-56
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 35-56
    • Yan, N.1    Shi, Y.2
  • 3
    • 10644282148 scopus 로고    scopus 로고
    • The protein structures that shape caspase activity, specificity, activation and inhibition
    • Fuentes-Prior P, Salvesen GS. 2004. The protein structures that shape caspase activity, specificity, activation and inhibition. Biochem. J. 384:201-32
    • (2004) Biochem. J. , vol.384 , pp. 201-232
    • Fuentes-Prior, P.1    Salvesen, G.S.2
  • 4
    • 0029025549 scopus 로고
    • Mch2, a new member of the apoptotic Ced-3/Ice cysteine protease gene family
    • Fernandes-Alnemri T, Litwack G, Alnemri ES. 1995. Mch2, a new member of the apoptotic Ced-3/Ice cysteine protease gene family. Cancer Res. 55:2737-42
    • (1995) Cancer Res. , vol.55 , pp. 2737-2742
    • Fernandes-Alnemri, T.1    Litwack, G.2    Alnemri, E.S.3
  • 5
    • 0033601746 scopus 로고    scopus 로고
    • Ordering the cytochrome c-initiated caspase cascade: Hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner
    • Slee EA, Harte MT, Kluck RM, Wolf BB, Casiano CA, et al. 1999. Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner. J. Cell Biol. 144:281-92
    • (1999) J. Cell Biol. , vol.144 , pp. 281-292
    • Slee, E.A.1    Harte, M.T.2    Kluck, R.M.3    Wolf, B.B.4    Casiano, C.A.5
  • 6
    • 0032536519 scopus 로고    scopus 로고
    • Caspases are activated in a branched protease cascade and control distinct downstream processes in Fas-induced apoptosis
    • Hirata H, Takahashi A, Kobayashi S, Yonehara S, Sawai H, et al. 1998. Caspases are activated in a branched protease cascade and control distinct downstream processes in Fas-induced apoptosis. J. Exp. Med. 187:587-600
    • (1998) J. Exp. Med. , vol.187 , pp. 587-600
    • Hirata, H.1    Takahashi, A.2    Kobayashi, S.3    Yonehara, S.4    Sawai, H.5
  • 8
    • 0034682825 scopus 로고    scopus 로고
    • Apoptosis induced by the nuclear death domain protein p84N5 is associated with caspase-6 and NF-βB activation
    • Doostzadeh-Cizeron J, Yin S, Goodrich DW. 2000. Apoptosis induced by the nuclear death domain protein p84N5 is associated with caspase-6 and NF-βB activation. J. Biol. Chem. 275:25336-41
    • (2000) J. Biol. Chem. , vol.275 , pp. 25336-25341
    • Doostzadeh-Cizeron, J.1    Yin, S.2    Goodrich, D.W.3
  • 9
    • 0033551738 scopus 로고    scopus 로고
    • Caspase-6 role in apoptosis of human neurons, amyloidogenesis, and Alzheimers disease
    • LeBlanc A, Liu H, Goodyer C, Bergeron C, Hammond J. 1999. Caspase-6 role in apoptosis of human neurons, amyloidogenesis, and Alzheimers disease. J. Biol. Chem. 274:23426-36
    • (1999) J. Biol. Chem. , vol.274 , pp. 23426-23436
    • Leblanc, A.1    Liu, H.2    Goodyer, C.3    Bergeron, C.4    Hammond, J.5
  • 10
    • 60649093275 scopus 로고    scopus 로고
    • Self-activation ofCaspase-6 in vitro and in vivo:Caspase- 6 activation does not induce cell death in HEK293T cells
    • Klaiman G, Champagne N, LeBlanc AC. 2009. Self-activation ofCaspase-6 in vitro and in vivo:Caspase- 6 activation does not induce cell death in HEK293T cells. Biochim. Biophys. Acta 1793:592-601
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 592-601
    • Klaiman, G.1    Champagne, N.2    Leblanc, A.C.3
  • 11
    • 78049347657 scopus 로고    scopus 로고
    • Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation
    • Wang XJ, Cao Q, Liu X, Wang KT, Mi W, et al. 2010. Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation. EMBO Rep. 11:841-47
    • (2010) EMBO Rep. , vol.11 , pp. 841-847
    • Wang, X.J.1    Cao, Q.2    Liu, X.3    Wang, K.T.4    Mi, W.5
  • 12
    • 0029891838 scopus 로고    scopus 로고
    • The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A
    • Orth K, Chinnaiyan AM, Garg M, Froelich CJ, Dixit VM. 1996. The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A. J. Biol. Chem. 271:16443-46
    • (1996) J. Biol. Chem. , vol.271 , pp. 16443-16446
    • Orth, K.1    Chinnaiyan, A.M.2    Garg, M.3    Froelich, C.J.4    Dixit, V.M.5
  • 13
    • 0033174072 scopus 로고    scopus 로고
    • Apoptosis overrides survival signals through a caspase-mediated dominant-negative NF-βB loop
    • Levkau B, Scatena M, Giachelli CM, Ross R, Raines EW. 1999. Apoptosis overrides survival signals through a caspase-mediated dominant-negative NF-βB loop. Nat. Cell Biol. 1:227-33
    • (1999) Nat. Cell Biol. , vol.1 , pp. 227-233
    • Levkau, B.1    Scatena, M.2    Giachelli, C.M.3    Ross, R.4    Raines, E.W.5
  • 14
    • 0034928793 scopus 로고    scopus 로고
    • SATB1 cleavage by caspase 6 disrupts PDZ domain-mediated dimerization, causing detachment from chromatin early in T-cell apoptosis
    • Galande S, Dickinson LA, Mian IS, Sikorska M, Kohwi-Shigematsu T. 2001. SATB1 cleavage by caspase 6 disrupts PDZ domain-mediated dimerization, causing detachment from chromatin early in T-cell apoptosis. Mol. Cell. Biol. 21:5591-604
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5591-5604
    • Galande, S.1    Dickinson, L.A.2    Mian, I.S.3    Sikorska, M.4    Kohwi-Shigematsu, T.5
  • 15
    • 0034954558 scopus 로고    scopus 로고
    • Transcription factor AP-2αis preferentially cleaved by caspase 6 and degraded by proteasome during tumor necrosis factor α-induced apoptosis in breast cancer cells
    • Nyormoi O, Wang Z, Doan D, Ruiz M, McConkey D, Bar-Eli M. 2001. Transcription factor AP-2α is preferentially cleaved by caspase 6 and degraded by proteasome during tumor necrosis factor α-induced apoptosis in breast cancer cells. Mol. Cell. Biol. 21:4856-67
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4856-4867
    • Nyormoi, O.1    Wang, Z.2    Doan, D.3    Ruiz, M.4    McConkey, D.5    Bar-Eli, M.6
  • 16
    • 0347624644 scopus 로고    scopus 로고
    • Critical loss of CBP/p300 histone acetylase activity by caspase-6 during neurodegeneration
    • Rouaux C, Jokic N, Mbebi C, Boutillier S, Loeffler JP, Boutillier AL. 2003. Critical loss of CBP/p300 histone acetylase activity by caspase-6 during neurodegeneration. EMBO J. 22:6537-49
    • (2003) EMBO J. , vol.22 , pp. 6537-6549
    • Rouaux, C.1    Jokic, N.2    Mbebi, C.3    Boutillier, S.4    Loeffler, J.P.5    Boutillier, A.L.6
  • 17
    • 3242811902 scopus 로고    scopus 로고
    • Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimers disease
    • Guo H, Albrecht S, Bourdeau M, Petzke T, Bergeron C, LeBlanc AC. 2004. Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimers disease. Am. J. Pathol. 165:523-31
    • (2004) Am. J. Pathol. , vol.165 , pp. 523-531
    • Guo, H.1    Albrecht, S.2    Bourdeau, M.3    Petzke, T.4    Bergeron, C.5    Leblanc, A.C.6
  • 19
    • 78149487690 scopus 로고    scopus 로고
    • Cleavage at the 586 amino acid caspase-6 site in mutant huntingtin influences caspase-6 activation in vivo
    • Graham RK, Deng Y, Carroll J, Vaid K, Cowan C, et al. 2010. Cleavage at the 586 amino acid caspase-6 site in mutant huntingtin influences caspase-6 activation in vivo. J. Neurosci. 30:15019-29
    • (2010) J. Neurosci. , vol.30 , pp. 15019-15029
    • Graham, R.K.1    Deng, Y.2    Carroll, J.3    Vaid, K.4    Cowan, C.5
  • 20
    • 0036314330 scopus 로고    scopus 로고
    • Cloning and expression of rat caspase-6 and its localization in renal ischemia/reperfusion injury
    • Singh AB, Kaushal V, Megyesi JK, Shah SV, Kaushal GP. 2002. Cloning and expression of rat caspase-6 and its localization in renal ischemia/reperfusion injury. Kidney Int. 62:106-15
    • (2002) Kidney Int. , vol.62 , pp. 106-115
    • Singh, A.B.1    Kaushal, V.2    Megyesi, J.K.3    Shah, S.V.4    Kaushal, G.P.5
  • 21
  • 22
    • 60549089207 scopus 로고    scopus 로고
    • APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
    • Nikolaev A, McLaughlin T, OLeary DD, Tessier-Lavigne M. 2009. APP binds DR6 to trigger axon pruning and neuron death via distinct caspases. Nature 457:981-89
    • (2009) Nature , vol.457 , pp. 981-989
    • Nikolaev, A.1    McLaughlin, T.2    Oleary, D.D.3    Tessier-Lavigne, M.4
  • 23
    • 77951870448 scopus 로고    scopus 로고
    • Axonal degeneration is regulated by the apoptotic machinery or a NAD+-sensitive pathway in insects and mammals
    • Schoenmann Z, Assa-Kunik E, Tiomny S, Minis A, Haklai-Topper L, et al. 2010. Axonal degeneration is regulated by the apoptotic machinery or a NAD+-sensitive pathway in insects and mammals. J. Neurosci. 30:6375-86
    • (2010) J. Neurosci. , vol.30 , pp. 6375-6386
    • Schoenmann, Z.1    Assa-Kunik, E.2    Tiomny, S.3    Minis, A.4    Haklai-Topper, L.5
  • 26
    • 77951667668 scopus 로고    scopus 로고
    • P75NTR-dependent, myelin-mediated axonal degeneration regulates neural connectivity in the adult brain
    • Park KJ, Grosso CA, Aubert I, Kaplan DR, Miller FD. 2010. p75NTR-dependent, myelin-mediated axonal degeneration regulates neural connectivity in the adult brain. Nat. Neurosci. 13:559-66
    • (2010) Nat. Neurosci. , vol.13 , pp. 559-566
    • Park, K.J.1    Grosso, C.A.2    Aubert, I.3    Kaplan, D.R.4    Miller, F.D.5
  • 27
    • 77958026084 scopus 로고    scopus 로고
    • Amyloid precursor protein cleavage-dependent and -independent axonal degeneration programs share a common nicotinamide mononucleotide adenylyltransferase 1-sensitive pathway
    • Vohra BP, Sasaki Y, Miller BR, Chang J, DiAntonio A, Milbrandt J. 2010. Amyloid precursor protein cleavage-dependent and -independent axonal degeneration programs share a common nicotinamide mononucleotide adenylyltransferase 1-sensitive pathway. J. Neurosci. 30:13729-38
    • (2010) J. Neurosci. , vol.30 , pp. 13729-13738
    • Vohra, B.P.1    Sasaki, Y.2    Miller, B.R.3    Chang, J.4    Diantonio, A.5    Milbrandt, J.6
  • 28
    • 79959314865 scopus 로고    scopus 로고
    • Intranasal delivery of caspase-9 inhibitor reduces caspase-6-dependent axon/neuron loss and improves neurological function after stroke
    • Akpan N, Serrano-Saiz E, Zacharia BE, Otten ML, Ducruet AF, et al. 2011. Intranasal delivery of caspase-9 inhibitor reduces caspase-6-dependent axon/neuron loss and improves neurological function after stroke. J. Neurosci. 31:8894-904
    • (2011) J. Neurosci. , vol.31 , pp. 8894-8904
    • Akpan, N.1    Serrano-Saiz, E.2    Zacharia, B.E.3    Otten, M.L.4    Ducruet, A.F.5
  • 29
    • 84859244583 scopus 로고    scopus 로고
    • Rescue from excitotoxicity and axonal degeneration accompanied by age-dependent behavioral and neuroanatomical alterations in caspase-6-deficient mice
    • Uribe V, Wong BK, Graham RK, Cusack CL, Skotte NH, et al. 2012. Rescue from excitotoxicity and axonal degeneration accompanied by age-dependent behavioral and neuroanatomical alterations in caspase-6-deficient mice. Hum. Mol. Genet. 21:1954-67
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 1954-1967
    • Uribe, V.1    Wong, B.K.2    Graham, R.K.3    Cusack, C.L.4    Skotte, N.H.5
  • 30
    • 33745003424 scopus 로고    scopus 로고
    • Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin
    • Graham RK, Deng Y, Slow EJ, Haigh B, Bissada N, et al. 2006. Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin. Cell 125:1179-91
    • (2006) Cell , vol.125 , pp. 1179-1191
    • Graham, R.K.1    Deng, Y.2    Slow, E.J.3    Haigh, B.4    Bissada, N.5
  • 31
    • 11144357398 scopus 로고    scopus 로고
    • Specific caspase interactions and amplification are involved in selective neuronal vulnerability in Huntingtons disease
    • Hermel E, Gafni J, Propp SS, Leavitt BR, Wellington CL, et al. 2004. Specific caspase interactions and amplification are involved in selective neuronal vulnerability in Huntingtons disease. Cell Death Differ. 11:424-38
    • (2004) Cell Death Differ. , vol.11 , pp. 424-438
    • Hermel, E.1    Gafni, J.2    Propp, S.S.3    Leavitt, B.R.4    Wellington, C.L.5
  • 32
    • 65249132310 scopus 로고    scopus 로고
    • Prevention of depressive behaviour in the YAC128 mouse model of Huntington disease by mutation at residue 586 of huntingtin
    • Pouladi MA, Graham RK, Karasinska JM, Xie Y, Santos RD, et al. 2009. Prevention of depressive behaviour in the YAC128 mouse model of Huntington disease by mutation at residue 586 of huntingtin. Brain 132:919-32
    • (2009) Brain , vol.132 , pp. 919-932
    • Pouladi, M.A.1    Graham, R.K.2    Karasinska, J.M.3    Xie, Y.4    Santos, R.D.5
  • 33
    • 74549181538 scopus 로고    scopus 로고
    • Early increase in extrasynapticNMDA receptor signaling and expression contributes to phenotype onset in Huntingtons disease mice
    • Milnerwood AJ, Gladding CM, Pouladi MA, Kaufman AM, Hines RM, et al. 2010. Early increase in extrasynapticNMDA receptor signaling and expression contributes to phenotype onset in Huntingtons disease mice. Neuron 65:178-90
    • (2010) Neuron , vol.65 , pp. 178-190
    • Milnerwood, A.J.1    Gladding, C.M.2    Pouladi, M.A.3    Kaufman, A.M.4    Hines, R.M.5
  • 34
    • 48049092846 scopus 로고    scopus 로고
    • Activated caspase-6 and caspase- 6-cleaved fragments of huntingtin specifically colocalize in the nucleus
    • Warby SC, Doty CN, Graham RK, Carroll JB, Yang YZ, et al. 2008. Activated caspase-6 and caspase- 6-cleaved fragments of huntingtin specifically colocalize in the nucleus. Hum. Mol. Genet. 17:2390-404
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 2390-2404
    • Warby, S.C.1    Doty, C.N.2    Graham, R.K.3    Carroll, J.B.4    Yang, Y.Z.5
  • 35
    • 0033617402 scopus 로고    scopus 로고
    • Involvement of caspases in proteolytic cleavage of Alzheimers amyloid-β precursor protein and amyloidogenic Aβpeptide formation
    • Gervais FG, Xu D, Robertson GS, Vaillancourt JP, Zhu Y, et al. 1999. Involvement of caspases in proteolytic cleavage of Alzheimers amyloid-β precursor protein and amyloidogenic Aβ peptide formation. Cell 97:395-406
    • (1999) Cell , vol.97 , pp. 395-406
    • Gervais, F.G.1    Xu, D.2    Robertson, G.S.3    Vaillancourt, J.P.4    Zhu, Y.5
  • 36
    • 0036064748 scopus 로고    scopus 로고
    • Caspase cleavage of members of the amyloid precursor family of proteins
    • Galvan V, Chen S, Lu D, Logvinova A, Goldsmith P, et al. 2002. Caspase cleavage of members of the amyloid precursor family of proteins. J. Neurochem. 82:283-94
    • (2002) J. Neurochem. , vol.82 , pp. 283-294
    • Galvan, V.1    Chen, S.2    Lu, D.3    Logvinova, A.4    Goldsmith, P.5
  • 37
    • 0034107524 scopus 로고    scopus 로고
    • A second cytotoxic proteolytic peptide derived from amyloid β-protein precursor
    • Lu DC, Rabizadeh S, Chandra S, Shayya RF, Ellerby LM, et al. 2000. A second cytotoxic proteolytic peptide derived from amyloid β-protein precursor. Nat. Med. 6:397-404
    • (2000) Nat. Med. , vol.6 , pp. 397-404
    • Lu, D.C.1    Rabizadeh, S.2    Chandra, S.3    Shayya, R.F.4    Ellerby, L.M.5
  • 38
    • 0347479366 scopus 로고    scopus 로고
    • Accumulation of caspase cleaved amyloid precursor protein represents an early neurodegenerative event in aging and in Alzheimers disease
    • Zhao M, Su J, Head E, Cotman CW. 2003. Accumulation of caspase cleaved amyloid precursor protein represents an early neurodegenerative event in aging and in Alzheimers disease. Neurobiol. Dis. 14:391-403
    • (2003) Neurobiol. Dis. , vol.14 , pp. 391-403
    • Zhao, M.1    Su, J.2    Head, E.3    Cotman, C.W.4
  • 39
    • 33845898816 scopus 로고    scopus 로고
    • Deficits in synaptic transmission and learning in amyloid precursor protein (APP) transgenic mice require C-terminal cleavage of APP
    • Saganich MJ, Schroeder BE, Galvan V, Bredesen DE, Koo EH, Heinemann SF. 2006. Deficits in synaptic transmission and learning in amyloid precursor protein (APP) transgenic mice require C-terminal cleavage of APP. J. Neurosci. 26:13428-36
    • (2006) J. Neurosci. , vol.26 , pp. 13428-13436
    • Saganich, M.J.1    Schroeder, B.E.2    Galvan, V.3    Bredesen, D.E.4    Koo, E.H.5    Heinemann, S.F.6
  • 40
    • 38449120482 scopus 로고    scopus 로고
    • Signal transduction in Alzheimer disease: P21-activated kinase signaling requires C-terminal cleavage of APP at Asp664
    • Nguyen TV, Galvan V, Huang W, Banwait S, Tang H, et al. 2008. Signal transduction in Alzheimer disease: p21-activated kinase signaling requires C-terminal cleavage of APP at Asp664. J. Neurochem. 104:1065-80
    • (2008) J. Neurochem. , vol.104 , pp. 1065-1080
    • Nguyen, T.V.1    Galvan, V.2    Huang, W.3    Banwait, S.4    Tang, H.5
  • 41
    • 33646480747 scopus 로고    scopus 로고
    • Reversal of Alzheimers-like pathology and behavior in human APP transgenic mice by mutation of Asp664
    • Galvan V, Gorostiza OF, Banwait S, Ataie M, Logvinova AV, et al. 2006. Reversal of Alzheimers-like pathology and behavior in human APP transgenic mice by mutation of Asp664. Proc. Natl. Acad. Sci. USA 103:7130-35
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7130-7135
    • Galvan, V.1    Gorostiza, O.F.2    Banwait, S.3    Ataie, M.4    Logvinova, A.V.5
  • 42
    • 84860853336 scopus 로고    scopus 로고
    • Inhibitory mechanism of caspase-6 phosphorylation revealed by crystal structures, molecular dynamics simulations, and biochemical assays
    • Cao Q, Wang XJ, Liu CW, Liu DF, Li LF, et al. 2012. Inhibitory mechanism of caspase-6 phosphorylation revealed by crystal structures, molecular dynamics simulations, and biochemical assays. J. Biol. Chem. 287:15371-79
    • (2012) J. Biol. Chem. , vol.287 , pp. 15371-15379
    • Cao, Q.1    Wang, X.J.2    Liu, C.W.3    Liu, D.F.4    Li, L.F.5
  • 43
    • 84859416412 scopus 로고    scopus 로고
    • Phosphorylation regulates assembly of the caspase-6 substratebinding groove
    • Velazquez-Delgado EM, Hardy JA. 2012. Phosphorylation regulates assembly of the caspase-6 substratebinding groove. Structure 20:742-51
    • (2012) Structure , vol.20 , pp. 742-751
    • Velazquez-Delgado, E.M.1    Hardy, J.A.2
  • 44
    • 84892383815 scopus 로고    scopus 로고
    • The regulatory mechanism of the caspase 6 pro-domain revealed by crystal structure and biochemical assays
    • Cao Q, Wang XJ, Li LF, Su XD. 2014. The regulatory mechanism of the caspase 6 pro-domain revealed by crystal structure and biochemical assays. Acta Crystallogr. D Biol. Crystallogr. 70:58-67
    • (2014) Acta Crystallogr. D Biol. Crystallogr. , vol.70 , pp. 58-67
    • Cao, Q.1    Wang, X.J.2    Li, L.F.3    Su, X.D.4
  • 45
    • 77956069555 scopus 로고    scopus 로고
    • Huntingtons disease
    • Novak MJ, Tabrizi SJ. 2010. Huntingtons disease. BMJ 340:c3109
    • (2010) BMJ , vol.340 , pp. c3109
    • Novak, M.J.1    Tabrizi, S.J.2
  • 46
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntingtons disease chromosomes
    • TheHuntingtons Disease Collaborative Research Group
    • TheHuntingtons Disease Collaborative Research Group. 1993. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntingtons disease chromosomes. Cell 72:971-83
    • (1993) Cell , vol.72 , pp. 971-983
  • 47
    • 0027432418 scopus 로고
    • Widespread expression of the human and rat Huntingtons disease gene in brain and nonneural tissues
    • Strong TV, Tagle DA, Valdes JM, Elmer LW, Boehm K, et al. 1993. Widespread expression of the human and rat Huntingtons disease gene in brain and nonneural tissues. Nat. Genet. 5:259-65
    • (1993) Nat. Genet. , vol.5 , pp. 259-265
    • Strong, T.V.1    Tagle, D.A.2    Valdes, J.M.3    Elmer, L.W.4    Boehm, K.5
  • 48
    • 0029816724 scopus 로고    scopus 로고
    • Subcellular localization of theHuntingtons disease gene product in cell lines by immunofluorescence and biochemical subcellular fractionation
    • De Rooij KE, Dorsman JC, Smoor MA, Den Dunnen JT, VanOmmen GJ. 1996. Subcellular localization of theHuntingtons disease gene product in cell lines by immunofluorescence and biochemical subcellular fractionation. Hum. Mol. Genet. 5:1093-99
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1093-1099
    • De Rooij, K.E.1    Dorsman, J.C.2    Smoor, M.A.3    Den Dunnen, J.T.4    Vanommen, G.J.5
  • 49
    • 0028989602 scopus 로고
    • Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons
    • DiFiglia M, Sapp E, Chase K, Schwarz C, Meloni A, et al. 1995. Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons. Neuron 14:1075-81
    • (1995) Neuron , vol.14 , pp. 1075-1081
    • Difiglia, M.1    Sapp, E.2    Chase, K.3    Schwarz, C.4    Meloni, A.5
  • 51
    • 0041656292 scopus 로고    scopus 로고
    • The hunt for huntingtin function: Interaction partners tell many different stories
    • Harjes P, Wanker EE. 2003. The hunt for huntingtin function: interaction partners tell many different stories. Trends Biochem. Sci. 28:425-33
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 425-433
    • Harjes, P.1    Wanker, E.E.2
  • 52
    • 0035919701 scopus 로고    scopus 로고
    • Loss of huntingtin-mediated BDNF gene transcription in Huntingtons disease
    • Zuccato C, Ciammola A, Rigamonti D, Leavitt BR, Goffredo D, et al. 2001. Loss of huntingtin-mediated BDNF gene transcription in Huntingtons disease. Science 293:493-98
    • (2001) Science , vol.293 , pp. 493-498
    • Zuccato, C.1    Ciammola, A.2    Rigamonti, D.3    Leavitt, B.R.4    Goffredo, D.5
  • 53
    • 80053573543 scopus 로고    scopus 로고
    • Small changes, big impact: Posttranslationalmodifications and function of huntingtin in Huntington disease
    • Ehrnhoefer DE, Sutton L, Hayden MR. 2011. Small changes, big impact: posttranslationalmodifications and function of huntingtin in Huntington disease. Neuroscientist 17:475-92
    • (2011) Neuroscientist , vol.17 , pp. 475-492
    • Ehrnhoefer, D.E.1    Sutton, L.2    Hayden, M.R.3
  • 55
    • 79551655290 scopus 로고    scopus 로고
    • Huntingtons disease: Can mice lead the way to treatment?
    • Crook ZR, Housman D. 2011. Huntingtons disease: Can mice lead the way to treatment? Neuron 69:423-35
    • (2011) Neuron , vol.69 , pp. 423-435
    • Crook, Z.R.1    Housman, D.2
  • 56
    • 30744459353 scopus 로고    scopus 로고
    • Levels of mutant huntingtin influence the phenotypic severity of Huntington disease in YAC128 mouse models
    • Graham RK, Slow EJ, Deng Y, Bissada N, Lu G, et al. 2006. Levels of mutant huntingtin influence the phenotypic severity of Huntington disease in YAC128 mouse models. Neurobiol. Dis. 21:444-55
    • (2006) Neurobiol. Dis. , vol.21 , pp. 444-455
    • Graham, R.K.1    Slow, E.J.2    Deng, Y.3    Bissada, N.4    Lu, G.5
  • 57
    • 0034733607 scopus 로고    scopus 로고
    • Inhibiting caspase cleavage of huntingtin reduces toxicity and aggregate formation in neuronal and nonneuronal cells
    • Wellington CL, Singaraja R, Ellerby L, Savill J, Roy S, et al. 2000. Inhibiting caspase cleavage of huntingtin reduces toxicity and aggregate formation in neuronal and nonneuronal cells. J. Biol. Chem. 275:19831-38
    • (2000) J. Biol. Chem. , vol.275 , pp. 19831-19838
    • Wellington, C.L.1    Singaraja, R.2    Ellerby, L.3    Savill, J.4    Roy, S.5
  • 58
    • 0032502715 scopus 로고    scopus 로고
    • Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract
    • Wellington CL, Ellerby LM, Hackam AS, Margolis RL, Trifiro MA, et al. 1998. Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract. J. Biol. Chem. 273:9158-67
    • (1998) J. Biol. Chem. , vol.273 , pp. 9158-9167
    • Wellington, C.L.1    Ellerby, L.M.2    Hackam, A.S.3    Margolis, R.L.4    Trifiro, M.A.5
  • 59
    • 16044373842 scopus 로고    scopus 로고
    • Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice
    • Mangiarini L, Sathasivam K, Seller M, Cozens B, Harper A, et al. 1996. Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice. Cell 87:493-506
    • (1996) Cell , vol.87 , pp. 493-506
    • Mangiarini, L.1    Sathasivam, K.2    Seller, M.3    Cozens, B.4    Harper, A.5
  • 60
    • 0032101287 scopus 로고    scopus 로고
    • The influence of huntingtin protein size on nuclear localization and cellular toxicity
    • Hackam AS, Singaraja R, Wellington CL, Metzler M, McCutcheon K, et al. 1998. The influence of huntingtin protein size on nuclear localization and cellular toxicity. J. Cell Biol. 141:1097-105
    • (1998) J. Cell Biol. , vol.141 , pp. 1097-1105
    • Hackam, A.S.1    Singaraja, R.2    Wellington, C.L.3    Metzler, M.4    McCutcheon, K.5
  • 61
    • 0037107151 scopus 로고    scopus 로고
    • Caspase cleavage ofmutant huntingtin precedes neurodegeneration in Huntingtons disease
    • Wellington CL, Ellerby LM, Gutekunst CA, Rogers D, Warby S, et al. 2002. Caspase cleavage ofmutant huntingtin precedes neurodegeneration in Huntingtons disease. J. Neurosci. 22:7862-72
    • (2002) J. Neurosci. , vol.22 , pp. 7862-7872
    • Wellington, C.L.1    Ellerby, L.M.2    Gutekunst, C.A.3    Rogers, D.4    Warby, S.5
  • 62
    • 84861630493 scopus 로고    scopus 로고
    • Caspase-6 activity in a BACHD mouse modulates steady-state levels of mutant huntingtin protein but is not necessary for production of a 586 amino acid proteolytic fragment
    • Gafni J, Papanikolaou T, Degiacomo F, Holcomb J, Chen S, et al. 2012. Caspase-6 activity in a BACHD mouse modulates steady-state levels of mutant huntingtin protein but is not necessary for production of a 586 amino acid proteolytic fragment. J. Neurosci. 32:7454-65
    • (2012) J. Neurosci. , vol.32 , pp. 7454-7465
    • Gafni, J.1    Papanikolaou, T.2    Degiacomo, F.3    Holcomb, J.4    Chen, S.5
  • 63
    • 18544410106 scopus 로고    scopus 로고
    • Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation
    • Davies SW, Turmaine M, Cozens BA, DiFiglia M, Sharp AH, et al. 1997. Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 90:537-48
    • (1997) Cell , vol.90 , pp. 537-548
    • Davies, S.W.1    Turmaine, M.2    Cozens, B.A.3    Difiglia, M.4    Sharp, A.H.5
  • 64
    • 0033119123 scopus 로고    scopus 로고
    • Nuclear and neuropil aggregates in Huntingtons disease: Relationship to neuropathology
    • Gutekunst CA, Li SH, Yi H, Mulroy JS, Kuemmerle S, et al. 1999. Nuclear and neuropil aggregates in Huntingtons disease: relationship to neuropathology. J. Neurosci. 19:2522-34
    • (1999) J. Neurosci. , vol.19 , pp. 2522-2534
    • Gutekunst, C.A.1    Li, S.H.2    Yi, H.3    Mulroy, J.S.4    Kuemmerle, S.5
  • 65
    • 29644433445 scopus 로고    scopus 로고
    • Selective degeneration and nuclear localization of mutant huntingtin in the YAC128 mouse model of Huntington disease
    • Van Raamsdonk JM, Murphy Z, Slow EJ, Leavitt BR, Hayden MR. 2005. Selective degeneration and nuclear localization of mutant huntingtin in the YAC128 mouse model of Huntington disease. Hum. Mol. Genet. 14:3823-35
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 3823-3835
    • Van Raamsdonk, J.M.1    Murphy, Z.2    Slow, E.J.3    Leavitt, B.R.4    Hayden, M.R.5
  • 66
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou F, Finkbeiner S, Devys D, Greenberg ME. 1998. Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 95:55-66
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 67
    • 0033081766 scopus 로고    scopus 로고
    • Mutant huntingtin expression in clonal striatal cells: Dissociation of inclusion formation and neuronal survival by caspase inhibition
    • Kim M, Lee HS, LaForet G, McIntyre C, Martin EJ, et al. 1999. Mutant huntingtin expression in clonal striatal cells: dissociation of inclusion formation and neuronal survival by caspase inhibition. J. Neurosci. 19:964-73
    • (1999) J. Neurosci. , vol.19 , pp. 964-973
    • Kim, M.1    Lee, H.S.2    Laforet, G.3    McIntyre, C.4    Martin, E.J.5
  • 68
    • 36048971978 scopus 로고    scopus 로고
    • Automated deformation analysis in the YAC128 Huntington disease mouse model
    • Lerch JP, Carroll JB, Spring S, Bertram LN, Schwab C, et al. 2008. Automated deformation analysis in the YAC128 Huntington disease mouse model. NeuroImage 39:32-39
    • (2008) NeuroImage , vol.39 , pp. 32-39
    • Lerch, J.P.1    Carroll, J.B.2    Spring, S.3    Bertram, L.N.4    Schwab, C.5
  • 69
    • 79959802847 scopus 로고    scopus 로고
    • Transgenic mice expressing caspase-6-derived N-terminal fragments of mutant huntingtin develop neurologic abnormalities with predominant cytoplasmic inclusion pathology composed largely of a smaller proteolytic derivative
    • Tebbenkamp AT, Green C, Xu G, Denovan-Wright EM, Rising AC, et al. 2011. Transgenic mice expressing caspase-6-derived N-terminal fragments of mutant huntingtin develop neurologic abnormalities with predominant cytoplasmic inclusion pathology composed largely of a smaller proteolytic derivative. Hum. Mol. Genet. 20:2770-82
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 2770-2782
    • Tebbenkamp, A.T.1    Green, C.2    Xu, G.3    Denovan-Wright, E.M.4    Rising, A.C.5
  • 70
    • 84855921378 scopus 로고    scopus 로고
    • Transgenic mouse model expressing the caspase 6 fragment of mutant huntingtin
    • Waldron-Roby E, Ratovitski T, Wang X, Jiang M, Watkin E, et al. 2012. Transgenic mouse model expressing the caspase 6 fragment of mutant huntingtin. J. Neurosci. 32:183-93
    • (2012) J. Neurosci. , vol.32 , pp. 183-193
    • Waldron-Roby, E.1    Ratovitski, T.2    Wang, X.3    Jiang, M.4    Watkin, E.5
  • 73
    • 13944276825 scopus 로고    scopus 로고
    • Twenty years of the Alzheimers disease amyloid hypo thesis a genetic perspective
    • Tanzi RE, Bertram L. 2005. Twenty years of the Alzheimers disease amyloid hypothesis: A genetic perspective. Cell 120:545-55
    • (2005) Cell , vol.120 , pp. 545-555
    • Tanzi, R.E.1    Bertram, L.2
  • 74
    • 33750705653 scopus 로고    scopus 로고
    • A century of Alzheimers disease
    • Goedert M, Spillantini MG. 2006. A century of Alzheimers disease. Science 314:777-81
    • (2006) Science , vol.314 , pp. 777-781
    • Goedert, M.1    Spillantini, M.G.2
  • 75
    • 0345276568 scopus 로고    scopus 로고
    • Synaptic pathology in Alzheimers disease: A review of ultrastructural studies
    • Scheff SW, Price DA. 2003. Synaptic pathology in Alzheimers disease: A review of ultrastructural studies. Neurobiol. Aging 24:1029-46
    • (2003) Neurobiol. Aging , vol.24 , pp. 1029-1046
    • Scheff, S.W.1    Price, D.A.2
  • 76
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimers disease
    • Mattson MP. 2004. Pathways towards and away from Alzheimers disease. Nature 430:631-39
    • (2004) Nature , vol.430 , pp. 631-639
    • Mattson, M.P.1
  • 77
    • 24644453571 scopus 로고    scopus 로고
    • The role of apoptotic pathways in Alzheimers disease neurodegeneration and cell death
    • LeBlanc AC. 2005. The role of apoptotic pathways in Alzheimers disease neurodegeneration and cell death. Curr. Alzheimer Res. 2:389-402
    • (2005) Curr. Alzheimer Res. , vol.2 , pp. 389-402
    • Leblanc, A.C.1
  • 79
    • 0036150827 scopus 로고    scopus 로고
    • Alzheimers disease-do tauists and baptists finally shake hands?
    • Mudher A, Lovestone S. 2002. Alzheimers disease-do tauists and baptists finally shake hands? Trends Neurosci. 25:22-26
    • (2002) Trends Neurosci. , vol.25 , pp. 22-26
    • Mudher, A.1    Lovestone, S.2
  • 80
    • 84879247889 scopus 로고    scopus 로고
    • Caspase-6 as a novel early target in the treatment of Alzheimers disease
    • LeBlanc AC. 2013. Caspase-6 as a novel early target in the treatment of Alzheimers disease. Eur. J. Neurosci. 37:2005-18
    • (2013) Eur. J. Neurosci. , vol.37 , pp. 2005-2018
    • Leblanc, A.C.1
  • 82
    • 0037047157 scopus 로고    scopus 로고
    • Apoptotic threshold is lowered by p53 transactivation of caspase-6
    • MacLachlan TK, El-Deiry WS. 2002. Apoptotic threshold is lowered by p53 transactivation of caspase-6. Proc. Natl. Acad. Sci. USA 99:9492-97
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9492-9497
    • Maclachlan, T.K.1    El-Deiry, W.S.2
  • 83
    • 0037336851 scopus 로고    scopus 로고
    • Caspase gene expression in the brain as a function of the clinical progression of Alzheimer disease
    • Pompl PN, Yemul S, Xiang Z, Ho L, Haroutunian V, et al. 2003. Caspase gene expression in the brain as a function of the clinical progression of Alzheimer disease. Arch. Neurol. 60:369-76
    • (2003) Arch. Neurol. , vol.60 , pp. 369-376
    • Pompl, P.N.1    Yemul, S.2    Xiang, Z.3    Ho, L.4    Haroutunian, V.5
  • 85
    • 73349135640 scopus 로고    scopus 로고
    • Caspase-6 activation in familial Alzheimer disease brains carrying amyloid precursor protein or presenilin i or presenilin II mutations
    • Albrecht S, Bogdanovic N, Ghetti B, Winblad B, LeBlanc AC. 2009. Caspase-6 activation in familial Alzheimer disease brains carrying amyloid precursor protein or presenilin I or presenilin II mutations. J. Neuropathol. Exp. Neurol. 68:1282-93
    • (2009) J. Neuropathol. Exp. Neurol. , vol.68 , pp. 1282-1293
    • Albrecht, S.1    Bogdanovic, N.2    Ghetti, B.3    Winblad, B.4    Leblanc, A.C.5
  • 87
    • 14244260622 scopus 로고    scopus 로고
    • Molecular ordering of the caspase activation cascade initiated by the cytotoxic T lymphocyte/natural killer (CTL/NK) protease granzyme B
    • Adrain C, Murphy BM, Martin SJ. 2005. Molecular ordering of the caspase activation cascade initiated by the cytotoxic T lymphocyte/natural killer (CTL/NK) protease granzyme B. J. Biol. Chem. 280:4663-73
    • (2005) J. Biol. Chem. , vol.280 , pp. 4663-4673
    • Adrain, C.1    Murphy, B.M.2    Martin, S.J.3
  • 88
    • 0030025216 scopus 로고    scopus 로고
    • Disappearance of actin-binding protein, drebrin, from hippocampal synapses in Alzheimers disease
    • Harigaya Y, Shoji M, Shirao T, Hirai S. 1996. Disappearance of actin-binding protein, drebrin, from hippocampal synapses in Alzheimers disease. J. Neurosci. Res. 43:87-92
    • (1996) J. Neurosci. Res. , vol.43 , pp. 87-92
    • Harigaya, Y.1    Shoji, M.2    Shirao, T.3    Hirai, S.4
  • 89
    • 77951653609 scopus 로고    scopus 로고
    • Identification of Caspase-6-mediated processing of the valosin containing protein (p97) in Alzheimers disease: A novel link to dysfunction in ubiquitin proteasome system-mediated protein degradation
    • Halawani D, Tessier S, Anzellotti D, Bennett DA, Latterich M, LeBlanc AC. 2010. Identification of Caspase-6-mediated processing of the valosin containing protein (p97) in Alzheimers disease: A novel link to dysfunction in ubiquitin proteasome system-mediated protein degradation. J. Neurosci. 30:6132-42
    • (2010) J. Neurosci. , vol.30 , pp. 6132-6142
    • Halawani, D.1    Tessier, S.2    Anzellotti, D.3    Bennett, D.A.4    Latterich, M.5    Leblanc, A.C.6
  • 90
    • 34248172449 scopus 로고    scopus 로고
    • Structure and functions of the human amyloid precursor protein: The whole is more than the sum of its parts
    • Gralle M, Ferreira ST. 2007. Structure and functions of the human amyloid precursor protein: the whole is more than the sum of its parts. Prog. Neurobiol. 82:11-32
    • (2007) Prog. Neurobiol. , vol.82 , pp. 11-32
    • Gralle, M.1    Ferreira, S.T.2
  • 91
    • 67749139805 scopus 로고    scopus 로고
    • Neurodegeneration in Alzheimers disease: Caspases and synaptic element interdependence
    • Bredesen DE. 2009. Neurodegeneration in Alzheimers disease: caspases and synaptic element interdependence. Mol. Neurodegener. 4:27
    • (2009) Mol. Neurodegener. , vol.4 , pp. 27
    • Bredesen, D.E.1
  • 92
    • 0030849093 scopus 로고    scopus 로고
    • A combinatorial approach defines specificities ofmembers of the caspase family and granzyme B: Functional relationships established for key mediators of apoptosis
    • Thornberry NA, Rano TA, Peterson EP, Rasper DM, Timkey T, et al. 1997. A combinatorial approach defines specificities ofmembers of the caspase family and granzyme B: functional relationships established for key mediators of apoptosis. J. Biol. Chem. 272:17907-11
    • (1997) J. Biol. Chem. , vol.272 , pp. 17907-17911
    • Thornberry, N.A.1    Rano, T.A.2    Peterson, E.P.3    Rasper, D.M.4    Timkey, T.5
  • 93
    • 0033597884 scopus 로고    scopus 로고
    • Alternative, non-secretase processing of Alzheimers β-amyloid precursor protein during apoptosis by caspase-6 and -8
    • Pellegrini L, Passer BJ, Tabaton M, Ganjei JK, DAdamio L. 1999. Alternative, non-secretase processing of Alzheimers β-amyloid precursor protein during apoptosis by caspase-6 and -8. J. Biol. Chem. 274:21011-16
    • (1999) J. Biol. Chem. , vol.274 , pp. 21011-21016
    • Pellegrini, L.1    Passer, B.J.2    Tabaton, M.3    Ganjei, J.K.4    Dadamio, L.5
  • 94
    • 78650662312 scopus 로고    scopus 로고
    • Importance of the caspase cleavage site in amyloid-β protein precursor
    • Bredesen DE, John V, Galvan V. 2010. Importance of the caspase cleavage site in amyloid-β protein precursor. J. Alzheimers Dis. 22:57-63
    • (2010) J. Alzheimers Dis. , vol.22 , pp. 57-63
    • Bredesen, D.E.1    John, V.2    Galvan, V.3
  • 95
    • 40549095365 scopus 로고    scopus 로고
    • C-terminal cleavage of the amyloid-β protein precursor at Asp664: A switch associated with Alzheimers disease
    • Banwait S, Galvan V, Zhang J, Gorostiza OF, Ataie M, et al. 2008. C-terminal cleavage of the amyloid-β protein precursor at Asp664: A switch associated with Alzheimers disease. J. Alzheimers Dis. 13:1-16
    • (2008) J. Alzheimers Dis. , vol.13 , pp. 1-16
    • Banwait, S.1    Galvan, V.2    Zhang, J.3    Gorostiza, O.F.4    Ataie, M.5
  • 97
    • 69249212154 scopus 로고    scopus 로고
    • Mechanism of cytotoxicity mediated by the C31 fragment of the amyloid precursor protein
    • Park SA, Shaked GM, Bredesen DE, Koo EH. 2009. Mechanism of cytotoxicity mediated by the C31 fragment of the amyloid precursor protein. Biochem. Biophys. Res. Commun. 388:450-55
    • (2009) Biochem. Biophys. Res. Commun. , vol.388 , pp. 450-455
    • Park, S.A.1    Shaked, G.M.2    Bredesen, D.E.3    Koo, E.H.4
  • 98
    • 43849090364 scopus 로고    scopus 로고
    • Long-term prevention of Alzheimers disease-like behavioral deficits in PDAPPmice carrying a mutation in Asp664
    • Galvan V, Zhang J, Gorostiza OF, Banwait S, Huang W, et al. 2008. Long-term prevention of Alzheimers disease-like behavioral deficits in PDAPPmice carrying a mutation in Asp664. Behav. Brain Res. 191:246-55
    • (2008) Behav. Brain Res. , vol.191 , pp. 246-255
    • Galvan, V.1    Zhang, J.2    Gorostiza, O.F.3    Banwait, S.4    Huang, W.5
  • 99
    • 70350324313 scopus 로고    scopus 로고
    • Reversal of learning deficits in hAPP transgenic mice carrying a mutation at Asp664: A role for early experience
    • Zhang J, Gorostiza OF, Tang H, Bredesen DE, Galvan V. 2010. Reversal of learning deficits in hAPP transgenic mice carrying a mutation at Asp664: A role for early experience. Behav. Brain Res. 206:202-7
    • (2010) Behav. Brain Res. , vol.206 , pp. 202-207
    • Zhang, J.1    Gorostiza, O.F.2    Tang, H.3    Bredesen, D.E.4    Galvan, V.5
  • 100
    • 74549185678 scopus 로고    scopus 로고
    • Caspase activation in transgenic mice with Alzheimer-like pathology: Results from a pilot study utilizing the caspase inhibitor, Q-VD-OPh
    • Rohn TT, Kokoulina P, Eaton CR, Poon WW. 2009. Caspase activation in transgenic mice with Alzheimer-like pathology: results from a pilot study utilizing the caspase inhibitor, Q-VD-OPh. Int. J. Clin. Exp. Med. 2:300-8
    • (2009) Int. J. Clin. Exp. Med. , vol.2 , pp. 300-308
    • Rohn, T.T.1    Kokoulina, P.2    Eaton, C.R.3    Poon, W.W.4
  • 101
    • 0043135185 scopus 로고    scopus 로고
    • DNAsynthesis and neuronal apoptosis caused by familial Alzheimer disease mutants of the amyloid precursor protein are mediated by the p21 activated kinase PAK3
    • McPhie DL, Coopersmith R, Hines-Peralta A, Chen Y, Ivins KJ, et al. 2003. DNAsynthesis and neuronal apoptosis caused by familial Alzheimer disease mutants of the amyloid precursor protein are mediated by the p21 activated kinase PAK3. J. Neurosci. 23:6914-27
    • (2003) J. Neurosci. , vol.23 , pp. 6914-6927
    • McPhie, D.L.1    Coopersmith, R.2    Hines-Peralta, A.3    Chen, Y.4    Ivins, K.J.5
  • 102
    • 31544476561 scopus 로고    scopus 로고
    • Role of p21-activated kinase pathway defects in the cognitive deficits of Alzheimer disease
    • Zhao L, Ma QL, Calon F, Harris-White ME, Yang F, et al. 2006. Role of p21-activated kinase pathway defects in the cognitive deficits of Alzheimer disease. Nat. Neurosci. 9:234-42
    • (2006) Nat. Neurosci. , vol.9 , pp. 234-242
    • Zhao, L.1    Ma, Q.L.2    Calon, F.3    Harris-White, M.E.4    Yang, F.5
  • 105
    • 0036790423 scopus 로고    scopus 로고
    • Caspase-6 is the direct activator of caspase-8 in the cytochrome c- induced apoptosis pathway: Absolute requirement for removal of caspase-6 prodomain
    • Cowling V, Downward J. 2002. Caspase-6 is the direct activator of caspase-8 in the cytochrome c- induced apoptosis pathway: absolute requirement for removal of caspase-6 prodomain. Cell Death Differ. 9:1046-56
    • (2002) Cell Death Differ. , vol.9 , pp. 1046-1056
    • Cowling, V.1    Downward, J.2
  • 106
    • 0035798361 scopus 로고    scopus 로고
    • Crystal structure of a procaspase-7 zymogen: Mechanisms of activation and substrate binding
    • Chai J, Wu Q, Shiozaki E, Srinivasula SM, Alnemri ES, Shi Y. 2001. Crystal structure of a procaspase-7 zymogen: mechanisms of activation and substrate binding. Cell 107:399-407
    • (2001) Cell , vol.107 , pp. 399-407
    • Chai, J.1    Wu, Q.2    Shiozaki, E.3    Srinivasula, S.M.4    Alnemri, E.S.5    Shi, Y.6
  • 107
    • 84862882878 scopus 로고    scopus 로고
    • Allosteric peptides bind a caspase zymogen and mediate caspase tetramerization
    • Stanger K, Steffek M, Zhou L, Pozniak CD, Quan C, et al. 2012. Allosteric peptides bind a caspase zymogen and mediate caspase tetramerization. Nat. Chem. Biol. 8:655-60
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 655-660
    • Stanger, K.1    Steffek, M.2    Zhou, L.3    Pozniak, C.D.4    Quan, C.5
  • 108
    • 4844222278 scopus 로고    scopus 로고
    • Regulation of caspase-6 and FLIP by the AMPK family member ARK5
    • Suzuki A, Kusakai G, Kishimoto A, Shimojo Y, Miyamoto S, et al. 2004. Regulation of caspase-6 and FLIP by the AMPK family member ARK5. Oncogene 23:7067-75
    • (2004) Oncogene , vol.23 , pp. 7067-7075
    • Suzuki, A.1    Kusakai, G.2    Kishimoto, A.3    Shimojo, Y.4    Miyamoto, S.5
  • 110
    • 0036083379 scopus 로고    scopus 로고
    • The IGF-1/Akt pathway is neuroprotective in Huntingtons disease and involves Huntingtin phosphorylation by Akt
    • Humbert S, Bryson EA, Cordelieres FP, Connors NC, Datta SR, et al. 2002. The IGF-1/Akt pathway is neuroprotective in Huntingtons disease and involves Huntingtin phosphorylation by Akt. Dev. Cell 2:831-37
    • (2002) Dev. Cell , vol.2 , pp. 831-837
    • Humbert, S.1    Bryson, E.A.2    Cordelieres, F.P.3    Connors, N.C.4    Datta, S.R.5
  • 111
    • 20444448900 scopus 로고    scopus 로고
    • Huntingtin phosphorylation on serine 421 is significantly reduced in the striatum and by polyglutamine expansion in vivo
    • Warby SC, Chan EY, Metzler M, Gan L, Singaraja RR, et al. 2005. Huntingtin phosphorylation on serine 421 is significantly reduced in the striatum and by polyglutamine expansion in vivo. Hum. Mol. Genet. 14:1569-77
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 1569-1577
    • Warby, S.C.1    Chan, E.Y.2    Metzler, M.3    Gan, L.4    Singaraja, R.R.5
  • 112
    • 70350107735 scopus 로고    scopus 로고
    • The crystal structure of caspase-6, a selective effector of axonal degeneration
    • Baumgartner R, Meder G, Briand C, Decock A, DArcy A, et al. 2009. The crystal structure of caspase-6, a selective effector of axonal degeneration. Biochem. J. 423:429-39
    • (2009) Biochem. J. , vol.423 , pp. 429-439
    • Baumgartner, R.1    Meder, G.2    Briand, C.3    Decock, A.4    Darcy, A.5
  • 113
    • 84870781145 scopus 로고    scopus 로고
    • Mechanistic and structural understanding of uncompetitive inhibitors of caspase-6
    • Heise CE, Murray J, Augustyn KE, Bravo B, Chugha P, et al. 2012. Mechanistic and structural understanding of uncompetitive inhibitors of caspase-6. PLoS ONE 7:e50864
    • (2012) PLoS ONE , vol.7 , pp. e50864
    • Heise, C.E.1    Murray, J.2    Augustyn, K.E.3    Bravo, B.4    Chugha, P.5
  • 114
    • 80051935810 scopus 로고    scopus 로고
    • Structure of human caspase-6 in complex with Z-VAD-FMK: New peptide binding mode observed for the non-canonical caspase conformation
    • Muller I, Lamers MB, Ritchie AJ, Dominguez C, Munoz-Sanjuan I, Kiselyov A. 2011. Structure of human caspase-6 in complex with Z-VAD-FMK: new peptide binding mode observed for the non-canonical caspase conformation. Bioorg. Med. Chem. Lett. 21:5244-47
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 5244-5247
    • Muller, I.1    Lamers, M.B.2    Ritchie, A.J.3    Dominguez, C.4    Munoz-Sanjuan, I.5    Kiselyov, A.6
  • 115
    • 79958712068 scopus 로고    scopus 로고
    • A new apo-caspase-6 crystal form reveals the active conformation of the apoenzyme
    • Muller I, Lamers MB, Ritchie AJ, Park H, Dominguez C, et al. 2011. A new apo-caspase-6 crystal form reveals the active conformation of the apoenzyme. J. Mol. Biol. 410:307-15
    • (2011) J. Mol. Biol. , vol.410 , pp. 307-315
    • Muller, I.1    Lamers, M.B.2    Ritchie, A.J.3    Park, H.4    Dominguez, C.5
  • 116
    • 79151469464 scopus 로고    scopus 로고
    • Substrate-induced conformational changes occur in all cleaved forms of caspase-6
    • Vaidya S, Velazquez-Delgado EM, Abbruzzese G, Hardy JA. 2011. Substrate-induced conformational changes occur in all cleaved forms of caspase-6. J. Mol. Biol. 406:75-91
    • (2011) J. Mol. Biol. , vol.406 , pp. 75-91
    • Vaidya, S.1    Velazquez-Delgado, E.M.2    Abbruzzese, G.3    Hardy, J.A.4
  • 117
    • 0035932465 scopus 로고    scopus 로고
    • Covalent inhibition revealed by the crystal structure of the caspase-8/p35 complex
    • Xu G, Cirilli M, Huang Y, Rich RL, Myszka DG, Wu H. 2001. Covalent inhibition revealed by the crystal structure of the caspase-8/p35 complex. Nature 410:494-97
    • (2001) Nature , vol.410 , pp. 494-497
    • Xu, G.1    Cirilli, M.2    Huang, Y.3    Rich, R.L.4    Myszka, D.G.5    Wu, H.6
  • 118
    • 77957802330 scopus 로고    scopus 로고
    • Alternatively spliced caspase- 6B isoform inhibits the activation of caspase-6A
    • Lee AW, Champagne N, Wang X, Su XD, Goodyer C, LeBlanc AC. 2010. Alternatively spliced caspase- 6B isoform inhibits the activation of caspase-6A. J. Biol. Chem. 285:31974-84
    • (2010) J. Biol. Chem. , vol.285 , pp. 31974-31984
    • Lee, A.W.1    Champagne, N.2    Wang, X.3    Su, X.D.4    Goodyer, C.5    Leblanc, A.C.6
  • 121
    • 1542328053 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of azapeptide epoxides as selective and potent inhibitors of caspases-1, -3, -6, and -8
    • James KE, Asgian JL, Li ZZ, Ekici OD, Rubin JR, et al. 2004. Design, synthesis, and evaluation of azapeptide epoxides as selective and potent inhibitors of caspases-1, -3, -6, and -8. J. Med. Chem. 47:1553-74
    • (2004) J. Med. Chem. , vol.47 , pp. 1553-1574
    • James, K.E.1    Asgian, J.L.2    Li, Z.Z.3    Ekici, O.D.4    Rubin, J.R.5
  • 122
    • 24644447930 scopus 로고    scopus 로고
    • Synthesis and evaluation of novel dipeptidyl benzoyloxymethyl ketones as caspase inhibitors
    • Nedev HN, Klaiman G, LeBlanc A, Saragovi HU. 2005. Synthesis and evaluation of novel dipeptidyl benzoyloxymethyl ketones as caspase inhibitors. Biochem. Biophys. Res. Commun. 336:397-400
    • (2005) Biochem. Biophys. Res. Commun. , vol.336 , pp. 397-400
    • Nedev, H.N.1    Klaiman, G.2    Leblanc, A.3    Saragovi, H.U.4
  • 123
    • 33748859423 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of aza-peptide Michael acceptors as selective and potent inhibitors of caspases-2, -3, -6, -7, -8, -9, and -10
    • Ekici OD, Li ZZ, Campbell AJ, James KE, Asgian JL, et al. 2006. Design, synthesis, and evaluation of aza-peptide Michael acceptors as selective and potent inhibitors of caspases-2, -3, -6, -7, -8, -9, and -10. J. Med. Chem. 49:5728-49
    • (2006) J. Med. Chem. , vol.49 , pp. 5728-5749
    • Ekici, O.D.1    Li, Z.Z.2    Campbell, A.J.3    James, K.E.4    Asgian, J.L.5
  • 124
    • 33845923917 scopus 로고    scopus 로고
    • Synthesis of novel caspase inhibitors for characterization of the active caspase proteome in vitro and in vivo
    • Henzing AJ, Dodson H, Reid JM, Kaufmann SH, Baxter RL, Earnshaw WC. 2006. Synthesis of novel caspase inhibitors for characterization of the active caspase proteome in vitro and in vivo. J. Med. Chem. 49:7636-45
    • (2006) J. Med. Chem. , vol.49 , pp. 7636-7645
    • Henzing, A.J.1    Dodson, H.2    Reid, J.M.3    Kaufmann, S.H.4    Baxter, R.L.5    Earnshaw, W.C.6
  • 125
    • 38049119903 scopus 로고    scopus 로고
    • Overlapping cleavage motif selectivity of caspases: Implications for analysis of apoptotic pathways
    • McStay GP, Salvesen GS, Green DR. 2008. Overlapping cleavage motif selectivity of caspases: implications for analysis of apoptotic pathways. Cell Death Differ. 15:322-31
    • (2008) Cell Death Differ. , vol.15 , pp. 322-331
    • McStay, G.P.1    Salvesen, G.S.2    Green, D.R.3
  • 126
    • 0035289779 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski CA, Lombardo F, Dominy BW, Feeney PJ. 2001. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv. Drug Deliv. Rev. 46:3-26
    • (2001) Adv. Drug Deliv. Rev. , vol.46 , pp. 3-26
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 127
    • 65249096525 scopus 로고    scopus 로고
    • Synthesis and in vitro evaluation of sulfonamide isatin Michael acceptors as small molecule inhibitors of caspase-6
    • Chu W, Rothfuss J, Chu Y, Zhou D, Mach RH. 2009. Synthesis and in vitro evaluation of sulfonamide isatin Michael acceptors as small molecule inhibitors of caspase-6. J. Med. Chem. 52:2188-91
    • (2009) J. Med. Chem. , vol.52 , pp. 2188-2191
    • Chu, W.1    Rothfuss, J.2    Chu, Y.3    Zhou, D.4    Mach, R.H.5
  • 128
    • 84888832108 scopus 로고    scopus 로고
    • Modulating caspase activity: Beyond the active site
    • Murray J, Renslo AR. 2013. Modulating caspase activity: beyond the active site. Curr. Opin. Struct. Biol. 23:812-19
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 812-819
    • Murray, J.1    Renslo, A.R.2
  • 129
  • 130
    • 84867805315 scopus 로고    scopus 로고
    • Zinc-mediated allosteric inhibition of caspase-6
    • Velazquez-Delgado EM, Hardy JA. 2012. Zinc-mediated allosteric inhibition of caspase-6. J. Biol. Chem. 287:36000-11
    • (2012) J. Biol. Chem. , vol.287 , pp. 36000-36011
    • Velazquez-Delgado, E.M.1    Hardy, J.A.2
  • 131
    • 84862513319 scopus 로고    scopus 로고
    • Mechanism of zinc-mediated inhibition of caspase-9
    • Huber KL, Hardy JA. 2012. Mechanism of zinc-mediated inhibition of caspase-9. Protein Sci. 21:1056-65
    • (2012) Protein Sci. , vol.21 , pp. 1056-1065
    • Huber, K.L.1    Hardy, J.A.2
  • 132
    • 79959832624 scopus 로고    scopus 로고
    • A new role of NUAK1: Directly phosphorylating p53 and regulating cell proliferation
    • Hou X, Liu JE, Liu W, Liu CY, Liu ZY, Sun ZY. 2011. A new role of NUAK1: directly phosphorylating p53 and regulating cell proliferation. Oncogene 30:2933-42
    • (2011) Oncogene , vol.30 , pp. 2933-2942
    • Hou, X.1    Liu, J.E.2    Liu, W.3    Liu, C.Y.4    Liu, Z.Y.5    Sun, Z.Y.6
  • 133
    • 84883856935 scopus 로고    scopus 로고
    • Nanotechnology-based drug delivery systems for targeting, imaging and diagnosis of neurodegenerative diseases
    • Pehlivan SB. 2013. Nanotechnology-based drug delivery systems for targeting, imaging and diagnosis of neurodegenerative diseases. Pharm. Res. 30:2499-511
    • (2013) Pharm. Res. , vol.30 , pp. 2499-2511
    • Pehlivan, S.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.