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Volumn 1780, Issue 4, 2008, Pages 696-708

Both the N-terminal fragment and the protein-protein interaction domain (PDZ domain) are required for the pro-apoptotic activity of presenilin-associated protein PSAP

Author keywords

Alzheimer's disease; Apoptosis; Caspase; Cell death; Cytochrome c; Mitochondria

Indexed keywords

ADENOSINE; ANTIBODY; CASPASE; CYTOCHROME C; GUANINE; ISOPROTEIN; PDZ PROTEIN; PRESENILIN; PRESENILIN ASSOCIATED PROTEIN; PROTEIN; THYMINE; UNCLASSIFIED DRUG;

EID: 40949133264     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2008.01.013     Document Type: Article
Times cited : (9)

References (27)
  • 1
    • 0029245289 scopus 로고
    • A potential role for apoptosis in neurodegeneration and Alzheimer's disease
    • Cotman C.W., and Anderson A.J. A potential role for apoptosis in neurodegeneration and Alzheimer's disease. Mol. Neurobiol. 10 (1995) 19-45
    • (1995) Mol. Neurobiol. , vol.10 , pp. 19-45
    • Cotman, C.W.1    Anderson, A.J.2
  • 2
    • 0029912056 scopus 로고    scopus 로고
    • Mechanisms of neuronal death in Alzheimer's disease
    • Cotman C.W., and Su J.H. Mechanisms of neuronal death in Alzheimer's disease. Brain Pathol. 6 (1996) 493-506
    • (1996) Brain Pathol. , vol.6 , pp. 493-506
    • Cotman, C.W.1    Su, J.H.2
  • 3
    • 0031760611 scopus 로고    scopus 로고
    • Caspase dependent DNA fragmentation might be associated with excitotoxicity in Alzheimer disease
    • Masliah E., Mallory M., Alford M., Tanaka S., and Hansen L.A. Caspase dependent DNA fragmentation might be associated with excitotoxicity in Alzheimer disease. J. Neuropathol. Exp. Neurol. 57 (1998) 1041-1052
    • (1998) J. Neuropathol. Exp. Neurol. , vol.57 , pp. 1041-1052
    • Masliah, E.1    Mallory, M.2    Alford, M.3    Tanaka, S.4    Hansen, L.A.5
  • 5
    • 0034864628 scopus 로고    scopus 로고
    • Apoptosis in amyotrophic lateral sclerosis: a review of the evidence
    • Sathasivam S., Ince P.G., and Shaw P.J. Apoptosis in amyotrophic lateral sclerosis: a review of the evidence. Neuropathol. Appl. Neurobiol. 27 (2001) 257-274
    • (2001) Neuropathol. Appl. Neurobiol. , vol.27 , pp. 257-274
    • Sathasivam, S.1    Ince, P.G.2    Shaw, P.J.3
  • 6
    • 0035917831 scopus 로고    scopus 로고
    • Activated caspase-3 expression in Alzheimer's and aged control brain: correlation with Alzheimer pathology
    • Su J.H., Zhao M., Anderson A.J., Srinivasan A., and Cotman C.W. Activated caspase-3 expression in Alzheimer's and aged control brain: correlation with Alzheimer pathology. Brain Res. 898 (2001) 350-357
    • (2001) Brain Res. , vol.898 , pp. 350-357
    • Su, J.H.1    Zhao, M.2    Anderson, A.J.3    Srinivasan, A.4    Cotman, C.W.5
  • 7
    • 0038079348 scopus 로고    scopus 로고
    • Fas and Fas ligand are associated with neuritic degeneration in the AD brain and participate in beta-amyloid-induced neuronal death
    • Su J.H., Anderson A.J., Cribbs D.H., Tu C., Tong L., Kesslack P., and Cotman C.W. Fas and Fas ligand are associated with neuritic degeneration in the AD brain and participate in beta-amyloid-induced neuronal death. Neurobiol. Dis. 12 (2003) 182-193
    • (2003) Neurobiol. Dis. , vol.12 , pp. 182-193
    • Su, J.H.1    Anderson, A.J.2    Cribbs, D.H.3    Tu, C.4    Tong, L.5    Kesslack, P.6    Cotman, C.W.7
  • 8
    • 0029671219 scopus 로고    scopus 로고
    • Interfering with apoptosis: Ca(2+)-binding protein ALG-2 and Alzheimer's disease gene ALG-3
    • Vito P., Lacana E., and D'Adamio L. Interfering with apoptosis: Ca(2+)-binding protein ALG-2 and Alzheimer's disease gene ALG-3. Science 271 (1996) 521-525
    • (1996) Science , vol.271 , pp. 521-525
    • Vito, P.1    Lacana, E.2    D'Adamio, L.3
  • 9
    • 0033583253 scopus 로고    scopus 로고
    • Overexpression of a C-terminal fragment of presenilin 1 delays anti-Fas induced apoptosis in Jurkat cells
    • Vezina J., Tschopp C., Andersen E., and Muller K. Overexpression of a C-terminal fragment of presenilin 1 delays anti-Fas induced apoptosis in Jurkat cells. Neurosci. Lett. 263 (1999) 65-68
    • (1999) Neurosci. Lett. , vol.263 , pp. 65-68
    • Vezina, J.1    Tschopp, C.2    Andersen, E.3    Muller, K.4
  • 10
    • 0032755247 scopus 로고    scopus 로고
    • Identification of a novel PSD-95/Dlg/ZO-1 (PDZ)-like protein interacting with the C terminus of presenilin-1
    • Xu X., Shi Y., Wu X., Gambetti P., Sui D., and Cui M.Z. Identification of a novel PSD-95/Dlg/ZO-1 (PDZ)-like protein interacting with the C terminus of presenilin-1. J. Biol. Chem. 274 (1999) 32543-32546
    • (1999) J. Biol. Chem. , vol.274 , pp. 32543-32546
    • Xu, X.1    Shi, Y.2    Wu, X.3    Gambetti, P.4    Sui, D.5    Cui, M.Z.6
  • 14
    • 0029980402 scopus 로고    scopus 로고
    • Biochemical and functional differences in rat liver mitochondrial subpopulations obtained at different gravitational forces
    • Lanni A., Moreno M., Lombardi A., and Goglia F. Biochemical and functional differences in rat liver mitochondrial subpopulations obtained at different gravitational forces. Int. J. Biochem. Cell Biol. 28 (1996) 337-343
    • (1996) Int. J. Biochem. Cell Biol. , vol.28 , pp. 337-343
    • Lanni, A.1    Moreno, M.2    Lombardi, A.3    Goglia, F.4
  • 15
    • 27844441278 scopus 로고    scopus 로고
    • g-Cleavage is dependent on z-cleavage during the proteolytic processing of amyloid precursor protein within its transmembrane domain
    • Zhao G., Cui M.Z., Mao G., Dong Y., Tan J., Sun L., and Xu X. g-Cleavage is dependent on z-cleavage during the proteolytic processing of amyloid precursor protein within its transmembrane domain. J. Biol. Chem. 280 (2005) 37689-37697
    • (2005) J. Biol. Chem. , vol.280 , pp. 37689-37697
    • Zhao, G.1    Cui, M.Z.2    Mao, G.3    Dong, Y.4    Tan, J.5    Sun, L.6    Xu, X.7
  • 16
    • 0025096719 scopus 로고
    • Bacteriophage P1 cloning system for the isolation, amplification, and recovery of DNA fragments as large as 100 kilobase pairs
    • Sternberg N. Bacteriophage P1 cloning system for the isolation, amplification, and recovery of DNA fragments as large as 100 kilobase pairs. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 103-107
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 103-107
    • Sternberg, N.1
  • 18
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • Tusnady G.E., and Simon I. The HMMTOP transmembrane topology prediction server. Bioinformatics 17 (2001) 849-850
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusnady, G.E.1    Simon, I.2
  • 19
    • 0032561132 scopus 로고    scopus 로고
    • Principles governing amino acid composition of integral membrane proteins: application to topology prediction
    • Tusnady G.E., and Simon I. Principles governing amino acid composition of integral membrane proteins: application to topology prediction. J. Mol. Biol. 283 (1998) 489-506
    • (1998) J. Mol. Biol. , vol.283 , pp. 489-506
    • Tusnady, G.E.1    Simon, I.2
  • 20
    • 1842455284 scopus 로고    scopus 로고
    • Disulfide connectivity prediction using recursive neural networks and evolutionary information
    • Vullo A., and Frasconi P. Disulfide connectivity prediction using recursive neural networks and evolutionary information. Bioinformatics 20 (2004) 653-659
    • (2004) Bioinformatics , vol.20 , pp. 653-659
    • Vullo, A.1    Frasconi, P.2
  • 21
    • 7244240818 scopus 로고    scopus 로고
    • POLYVIEW: a flexible visualization tool for structural and functional annotations of proteins
    • Porollo A.A., Adamczak R., and Meller J. POLYVIEW: a flexible visualization tool for structural and functional annotations of proteins. Bioinformatics 20 (2004) 2460-2462
    • (2004) Bioinformatics , vol.20 , pp. 2460-2462
    • Porollo, A.A.1    Adamczak, R.2    Meller, J.3
  • 22
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signaling domains
    • Schultz J., Milpetz F., Bork P., and Ponting C.P. SMART, a simple modular architecture research tool: Identification of signaling domains. PNAS 95 (1998) 5857-5864
    • (1998) PNAS , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 23
    • 0029853389 scopus 로고    scopus 로고
    • Pivotal role of a DEVD-sensitive step in etoposide-induced and Fas-mediated apoptotic pathways
    • Dubrez L., Savoy I., Hamman A., and Solary E. Pivotal role of a DEVD-sensitive step in etoposide-induced and Fas-mediated apoptotic pathways. EMBO J. 15 (1996) 5504-5512
    • (1996) EMBO J. , vol.15 , pp. 5504-5512
    • Dubrez, L.1    Savoy, I.2    Hamman, A.3    Solary, E.4
  • 24
    • 1242317666 scopus 로고    scopus 로고
    • The mitochondrial transporter family (SLC25): physiological and pathological implications
    • Palmieri F. The mitochondrial transporter family (SLC25): physiological and pathological implications. Pflugers Arch. 447 (2004) 689-709
    • (2004) Pflugers Arch. , vol.447 , pp. 689-709
    • Palmieri, F.1
  • 25
    • 0031171361 scopus 로고    scopus 로고
    • PDZ domains: targeting signalling molecules to sub-membranous sites
    • Ponting C.P., Phillips C., Davies K.E., and Blake D.J. PDZ domains: targeting signalling molecules to sub-membranous sites. Bioessays 19 (1997) 469-479
    • (1997) Bioessays , vol.19 , pp. 469-479
    • Ponting, C.P.1    Phillips, C.2    Davies, K.E.3    Blake, D.J.4
  • 26
    • 0037155199 scopus 로고    scopus 로고
    • PDZ domains: structural modules for protein complex assembly
    • Hung A.Y., and Sheng M. PDZ domains: structural modules for protein complex assembly. J. Biol. Chem. 277 (2002) 5699-5702
    • (2002) J. Biol. Chem. , vol.277 , pp. 5699-5702
    • Hung, A.Y.1    Sheng, M.2
  • 27
    • 0020050314 scopus 로고
    • A catalogue of splice junction sequences
    • Mount S.M. A catalogue of splice junction sequences. Nucleic Acids Res 10 (1982) 459-472
    • (1982) Nucleic Acids Res , vol.10 , pp. 459-472
    • Mount, S.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.