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Volumn 30, Issue 2, 2012, Pages 393-405

AβPP intracellular C-terminal domain function is related to its degradation processes

Author keywords

AICD; A PP; Fe65; IDE; proteasome; Tip60

Indexed keywords

AMYLOID PRECURSOR PROTEIN; AMYLOID PRECURSOR PROTEIN INTRACELLULAR C TERMINAL DOMAIN; INSULINASE; METALLOPROTEINASE INHIBITOR; PROTEASOME; PROTEIN FE65; TIP60 PROTEIN; UNCLASSIFIED DRUG;

EID: 84861515874     PISSN: 13872877     EISSN: 18758908     Source Type: Journal    
DOI: 10.3233/JAD-2012-111961     Document Type: Article
Times cited : (12)

References (55)
  • 3
    • 27544442991 scopus 로고    scopus 로고
    • Activation of GSK-3 and phosphorylation of CRMP2 in transgenic mice expressing APP intracellular domain
    • DOI 10.1083/jcb.200505078
    • Ryan KA, Pimplikar SW (2005) Activation of GSK-3 and phosphorylation of CRMP2 in transgenic mice expressing APP intracellular domain. J Cell Biol 171, 327-335. (Pubitemid 41540024)
    • (2005) Journal of Cell Biology , vol.171 , Issue.2 , pp. 327-335
    • Ryan, K.A.1    Pimplikar, S.W.2
  • 4
    • 0035955693 scopus 로고    scopus 로고
    • The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notchlike manner
    • Kimberly WT, Zheng JB, Guénette SY, Selkoe DJ (2001) The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notchlike manner. J Biol Chem 276, 40288-40292.
    • (2001) J Biol Chem , vol.276 , pp. 40288-40292
    • Kimberly, W.T.1    Zheng, J.B.2    Guénette, S.Y.3    Selkoe, D.J.4
  • 5
    • 0033617522 scopus 로고    scopus 로고
    • Notch signaling: Cell fate control and signal integration in development
    • DOI 10.1126/science.284.5415.770
    • Artavanis-Tsakonas S, Rand MD, Lake RJ (1999) Notch signaling: Cell fate control and signal integrationindevelopment. Science 284, 770-776. (Pubitemid 29291335)
    • (1999) Science , vol.284 , Issue.5415 , pp. 770-776
    • Artavanis-Tsakonas, S.1    Rand, M.D.2    Lake, R.J.3
  • 7
    • 0032574993 scopus 로고    scopus 로고
    • Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain
    • DOI 10.1038/30756
    • Schroeter EH, Kisslinger JA, Kopan R (1998) Notch-1 signalling requires ligand-induced proteolytic release of intra-cellular domain. Nature 393, 382-386. (Pubitemid 28269713)
    • (1998) Nature , vol.393 , Issue.6683 , pp. 382-386
    • Schroeter, E.H.1    Kisslinger, J.A.2    Kopan, R.3
  • 8
    • 0030592773 scopus 로고    scopus 로고
    • The intracellular cytoplasmic domain of the Alzheimer's disease amyloid precursor protein interacts with phosphotyrosine-binding domain proteins in the yeast two-hybrid system
    • DOI 10.1016/S0014-5793(96)01128-3, PII S0014579396011283
    • McLoughlin DM, Miller CC (1996) The intracellular cyto-plasmic domainof the Alzheimer's disease amyloid precursor protein interacts with phosphotyrosine-binding domain proteins in the yeast two-hybrid system. FEBS Lett 397, 197-200. (Pubitemid 26414016)
    • (1996) FEBS Letters , vol.397 , Issue.2-3 , pp. 197-200
    • McLoughlin, D.M.1    Miller, C.C.J.2
  • 9
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptivety active complex of APP with Fe65 and histone acetyltransferase Tip60
    • DOI 10.1126/science.1058783
    • Cao X, Sudhof TC (2001) A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 293, 115-120. (Pubitemid 32625507)
    • (2001) Science , vol.293 , Issue.5527 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 10
    • 5444275067 scopus 로고    scopus 로고
    • The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor
    • DOI 10.1242/jcs.01323
    • Von Rotz RC, Kohli BM, Bosset J, Meier M, Suzuki T, Nitsch RM, Konietzko U (2004) The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor. J Cell Sci 117, 4435-4448. (Pubitemid 39360070)
    • (2004) Journal of Cell Science , vol.117 , Issue.19 , pp. 4435-4448
    • Von Rotz, R.C.1    Kohli, B.M.2    Bosset, J.3    Meier, M.4    Suzuki, T.5    Nitsch, R.M.6    Konietzko, U.7
  • 14
    • 0029952441 scopus 로고    scopus 로고
    • In vivoubiquiti-nation and proteasome-mediated degradation of p53
    • Maki CG, Huibregtse JM, Howley PM (1996) In vivoubiquiti-nation and proteasome-mediated degradation of p53. Cancer Res 56, 649-2654.
    • (1996) Cancer Res , vol.56 , pp. 649-2654
    • Maki, C.G.1    Huibregtse, J.M.2    Howley, P.M.3
  • 15
    • 0036240701 scopus 로고    scopus 로고
    • The proteasome: A target novel for cancer chemotherapy
    • DOI 10.1038/sj/leu/2402417
    • Almond JB, Cohen GM (2002) The proteasome: A novel target for cancer chemotherapy. Leukemia 16, 433-443. (Pubitemid 34449723)
    • (2002) Leukemia , vol.16 , Issue.4 , pp. 433-443
    • Almond, J.B.1    Cohen, G.M.2
  • 16
    • 33845994064 scopus 로고    scopus 로고
    • P53 mediates nontranscriptional cell death in dopaminergic cells in response to proteasome inhibition
    • DOI 10.1074/jbc.M603950200
    • Nair VD, McNaught KS, González-Maeso J, Sealfon SC, Olanow CW (2006) p53 mediates nontranscriptional cell death in dopaminergic cells in response to proteasome inhibition. J Biol Chem 281, 39550-39560. (Pubitemid 46041915)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.51 , pp. 39550-39560
    • Nair, V.D.1    McNaught, K.St.P.2    Gonzalez-Maeso, J.3    Sealfon, S.C.4    Olanow, C.W.5
  • 17
    • 48349085043 scopus 로고    scopus 로고
    • The amyloid precursor protein intracellular domain (AICD) as modulator of gene expression, apoptosis, and cytoskeletal dynamics-relevance for Alzheimer's disease
    • Müller T, Meyer HE, Egensperger R, Marcus K (2008) The amyloid precursor protein intracellular domain (AICD) as modulator of gene expression, apoptosis, and cytoskeletal dynamics-relevance for Alzheimer's disease. Prog Neurobiol 85, 393-406.
    • (2008) Prog Neurobiol , vol.85 , pp. 393-406
    • Müller, T.1    Meyer, H.E.2    Egensperger, R.3    Marcus, K.4
  • 18
    • 2642582435 scopus 로고    scopus 로고
    • Dissection of amyloid-β precursor protein-dependent transcriptional transactivation
    • DOI 10.1074/jbc.M402248200
    • Cao X, Südhof TC (2004) Dissection of amyloid-beta precursor protein-dependent transcriptional transactivation. J Biol Chem 279, 24601-24611. (Pubitemid 38725327)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.23 , pp. 24601-24611
    • Cao, X.1    Sudhof, T.C.2
  • 19
    • 33646732989 scopus 로고    scopus 로고
    • Role of APP phosphorylation in FE65-dependent gene transactivation mediated by AICD
    • DOI 10.1111/j.1365-2443.2006.00968.x
    • Nakaya T, Suzuki T (2006) Role of APP phosphorylation in Fe65-dependent gene transactivation mediated by AICD. Genes Cells 11, 633-645. (Pubitemid 43744814)
    • (2006) Genes to Cells , vol.11 , Issue.6 , pp. 633-645
    • Nakaya, T.1    Suzuki, T.2
  • 21
    • 52049112089 scopus 로고    scopus 로고
    • Evidence that the Amyloid beta Precursor Protein-intracellular domain lowers the stress threshold of neurons and has a "regulated" transcriptional role
    • Giliberto L, Zhou D, Weldon R, Tamagno E, De Luca P, Tabaton M, D'Adamio L (2008) Evidence that the Amyloid beta Precursor Protein-intracellular domain lowers the stress threshold of neurons and has a "regulated" transcriptional role. Mol Neurodegener 2, 3-12.
    • (2008) Mol Neurodegener , vol.2 , pp. 3-12
    • Giliberto, L.1    Zhou, D.2    Weldon, R.3    Tamagno, E.4    De Luca, P.5    Tabaton, M.6    D'Adamio, L.7
  • 22
    • 12844282223 scopus 로고    scopus 로고
    • Proteasome-mediated effects on amyloid precursor protein processing at the γ-secretase site
    • DOI 10.1042/BJ20041145
    • Flood F, Murphy S, Cowburn RF, Lannfelt L, Walker B, Johnston JA (2005) Proteasome-mediated effects on amyloid precursor protein processing at the gamma-secretase site. Biochem J 385, 545-550. (Pubitemid 40165088)
    • (2005) Biochemical Journal , vol.385 , Issue.2 , pp. 545-550
    • Flood, F.1    Murphy, S.2    Cowburn, R.F.3    Lannfelt, L.4    Walkers, B.5    Johnston, J.A.6
  • 23
    • 0034142022 scopus 로고    scopus 로고
    • A distinct ER/IC γ-secretase competes with the proteasome for cleavage of APP
    • DOI 10.1021/bi991728z
    • Skovronsky DM, Pijak DS, Doms RW, Lee VM (2000) Adis-tinct ER/IC gamma-secretase competes with the proteasome for cleavage of APP. Biochemistry 39, 810-817. (Pubitemid 30065051)
    • (2000) Biochemistry , vol.39 , Issue.4 , pp. 810-817
    • Skovronsky, D.M.1    Pijak, D.S.2    Doms, R.W.3    Lee, V.M.-Y.4
  • 24
    • 0034797234 scopus 로고    scopus 로고
    • The C-terminal fragment of the Alzheimer's disease amyloid protein precursor is degraded by a proteasome-dependent mechanism distinct from γ-secretase
    • DOI 10.1046/j.0014-2956.2001.02465.x
    • Nunan J, Shearman MS, Checler F, Cappai R, Evin G, Beyreuther K, Masters CL, Small DH (2001) The C-terminal fragment of the Alzheimer's disease amyloid protein precursor is degraded by a proteasome-dependent mechanism distinct from gamma-secretase. Eur J Biochem 268, 5329-5336. (Pubitemid 32948359)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.20 , pp. 5329-5336
    • Nunan, J.1    Shearman, M.S.2    Checler, F.3    Cappai, R.4    Evin, G.5    Beyreuther, K.6    Masters, C.L.7    Small, D.H.8
  • 25
    • 0242330370 scopus 로고    scopus 로고
    • Proteasome-Mediated Degradation of the C-terminus of the Alzheimer's Disease β-Amyloid Protein Precursor: Effect of C-Terminal Truncation on Production of β-Amyloid Protein
    • DOI 10.1002/jnr.10646
    • Nunan J, Williamson NA, Hill AF, Sernee MF, Masters CL, Small DH (2003) Proteasome-mediated degradation of the C-terminus of the Alzheimer's disease beta-amyloid protein precursor: Effect of C-terminal truncation on production of beta-amyloid protein. J Neurosci Res 74, 378-385. (Pubitemid 37362814)
    • (2003) Journal of Neuroscience Research , vol.74 , Issue.3 , pp. 378-385
    • Nunan, J.1    Williamson, N.A.2    Hill, A.F.3    Sernee, M.F.4    Masters, C.L.5    Small, D.H.6
  • 26
    • 18744405422 scopus 로고    scopus 로고
    • Cytoplasmic domain of the β-amyloid protein precursor of Alzheimer's disease: Function, regulation of proteolysis, and implications for drug development
    • DOI 10.1002/jnr.20408
    • Kerr ML, Small DH (2005) Cytoplasmic domain of the beta-amyloid protein precursor of Alzheimer's disease: Function, regulation of proteolysis, and implications for drug development. J Neurosci Res 80, 151-159. (Pubitemid 40676299)
    • (2005) Journal of Neuroscience Research , vol.80 , Issue.2 , pp. 151-159
    • Kerr, M.L.1    Small, D.H.2
  • 27
    • 0018389336 scopus 로고
    • The effect of age on insulin-degrading activity in rat tissue
    • Runyan K, Duckworth WC, Kitabchi AE, Huff G (1979) The effect of age on insulin-degrading activity in rat tissue. Diabetes 28, 324-325. (Pubitemid 9176781)
    • (1979) Diabetes , vol.28 , Issue.4 , pp. 324-325
    • Runyan, K.1    Duckworth, W.C.2    Kitabchi, A.E.3    Huff, G.4
  • 29
    • 0028176821 scopus 로고
    • Alzheimer's beta-amyloid peptide specifically interacts with and is degraded by insulin-degrading enzyme
    • Kurochkin IV, Goto S (1994) Alzheimer's beta-amyloid peptide specifically interacts with and is degraded by insulin-degrading enzyme. FEBS Lett 345, 33-37.
    • (1994) FEBS Lett , vol.345 , pp. 33-37
    • Kurochkin, I.V.1    Goto, S.2
  • 30
    • 0034551718 scopus 로고    scopus 로고
    • Insulysinhydrolyzes amyloid beta peptides to products that are neither neurotoxic nor deposit on amyloid plaques
    • Mukherjee A, Song E, Kihiko-Ehmann M, Goodman JP Jr, Pyrek JS, Estus S, Hersh LB (2000) Insulysinhydrolyzes amyloid beta peptides to products that are neither neurotoxic nor deposit on amyloid plaques. J Neurosci 20, 8745-8749.
    • (2000) J Neurosci , vol.20 , pp. 8745-8749
    • Mukherjee, A.1    Song, E.2    Kihiko-Ehmann, M.3    Goodman Jr., J.P.4    Pyrek, J.S.5    Estus, S.6    Hersh, L.B.7
  • 31
    • 35848951410 scopus 로고    scopus 로고
    • Insulysin cleaves the APP cytoplasmic fragment at multiple sites
    • DOI 10.1007/s11064-007-9449-z
    • Venugopal C, Pappolla MA, Sambamurti K (2007) Insulysin cleaves the APP Cytoplasmic Fragment atmultiple sites. Neurochem Res 32, 2225-2234. (Pubitemid 350059868)
    • (2007) Neurochemical Research , vol.32 , Issue.12 , pp. 2225-2234
    • Venugopal, C.1    Pappolla, M.A.2    Sambamurti, K.3
  • 33
    • 0029811040 scopus 로고    scopus 로고
    • Association of insulin-degrading enzyme with a 70 kDa cytosolic protein in hepatoma cells
    • Authier F, Cameron PH, Taupin V (1996) Association of insulin-degrading enzyme with a 70kDa cytosolic protein in hepatoma cells. Biochem J 319, 149-158. (Pubitemid 26394752)
    • (1996) Biochemical Journal , vol.319 , Issue.1 , pp. 149-158
    • Authier, F.1    Cameron, P.H.2    Taupin, V.3
  • 34
    • 0031044352 scopus 로고    scopus 로고
    • Degradation of Alzheimer's beta-amyloid protein by human and rat brain peptidases: Involvement of insulin-degrading enzyme
    • McDermott JR, Gibson AM (1997) Degradation of Alzheimer's beta-amyloid protein by human and rat brain peptidases: Involvement of insulin-degrading enzyme. Neurochem Res 22, 49-56.
    • (1997) Neurochem Res , vol.22 , pp. 49-56
    • McDermott, J.R.1    Gibson, A.M.2
  • 35
    • 0034038036 scopus 로고    scopus 로고
    • Degradation of soluble amyloid β-peptides 1-40, 1-42, and the Dutch variant 1-40Q by insulin degrading enzyme from Alzheimer disease and control brains
    • DOI 10.1023/A:1007527721160
    • Pérez A, Morelli L, Cresto JC, Castano EM (2000) Degrada-tionofsolubleamyloid beta-peptides 1-40, 1-42 andthe Dutch variant 1-40 Q by insulin degrading enzyme from Alzheimer disease and control brains. Neurochem Res 25, 247-255. (Pubitemid 30210091)
    • (2000) Neurochemical Research , vol.25 , Issue.2 , pp. 247-255
    • Perez, A.1    Morelli, L.2    Cresto, J.C.3    Castano, E.M.4
  • 36
    • 77955270739 scopus 로고    scopus 로고
    • Beta-Amyloid precursor protein metabolism: Focus on the functions and degradation of its intracellular domain
    • Buoso E, Lanni C, Schettini G, Govoni S, Racchi M (2010) beta-Amyloid precursor protein metabolism: Focus on the functions and degradation of its intracellular domain. Pharmacol Res 62, 308-317.
    • (2010) Pharmacol Res , vol.62 , pp. 308-317
    • Buoso, E.1    Lanni, C.2    Schettini, G.3    Govoni, S.4    Racchi, M.5
  • 37
    • 70450235497 scopus 로고    scopus 로고
    • Alzheimer's disease-like pathological features in transgenic mice expressing the APP intracellular domain
    • Ghosal K, Vogt DL, Liang M, Shen Y, Lamb BT, Pimplikar SW (2009) Alzheimer's disease-like pathological features in transgenic mice expressing the APP intracellular domain. Proc Natl Acad Sci USA 106, 18367-18372.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 18367-18372
    • Ghosal, K.1    Vogt, D.L.2    Liang, M.3    Shen, Y.4    Lamb, B.T.5    Pimplikar, S.W.6
  • 38
    • 79960133399 scopus 로고    scopus 로고
    • Abnormal neuronal networks and seizure susceptibility in mice overexpressing the APP intracellular domain
    • Vogt DL, Thomas D, Galvan V, Bredesen DE, Lamb BT, Pim-plikar SW (2009) Abnormal neuronal networks and seizure susceptibility in mice overexpressing the APP intracellular domain. Neurobiol Aging 32, 1725-1729.
    • (2009) Neurobiol Aging , vol.32 , pp. 1725-1729
    • Vogt, D.L.1    Thomas, D.2    Galvan, V.3    Bredesen, D.E.4    Lamb, B.T.5    Pim-Plikar, S.W.6
  • 39
    • 51349120462 scopus 로고    scopus 로고
    • The intracellular domain of amyloid precursor protein induces neuron-specific apoptosis
    • Nakayama K, Ohkawara T, Hiratochi M, Koh CS, Nagase H (2008) The intracellular domain of amyloid precursor protein induces neuron-specific apoptosis. Neurosci Lett 444, 127-131.
    • (2008) Neurosci Lett , vol.444 , pp. 127-131
    • Nakayama, K.1    Ohkawara, T.2    Hiratochi, M.3    Koh, C.S.4    Nagase, H.5
  • 40
    • 79952004107 scopus 로고    scopus 로고
    • The amyloid precursor protein intracellular domain alters gene expression and induces neuron-specific apoptosis
    • Ohkawara T, Nagase H, Koh CS, Nakayama K (2011) The amyloid precursor protein intracellular domain alters gene expression and induces neuron-specific apoptosis. Gene 475, 1-9.
    • (2011) Gene , vol.475 , pp. 1-9
    • Ohkawara, T.1    Nagase, H.2    Koh, C.S.3    Nakayama, K.4
  • 41
    • 42349089604 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in Alzheimer's disease
    • DOI 10.1111/j.1582-4934.2008.00276.x
    • Oddo S (2008) The ubiquitin-proteasome system in Alzheimer's disease. J Cell Mol Med 12, 363-373. (Pubitemid 351555121)
    • (2008) Journal of Cellular and Molecular Medicine , vol.12 , Issue.2 , pp. 363-373
    • Oddo, S.1
  • 42
    • 0029905596 scopus 로고    scopus 로고
    • The carboxyl termini of β-amyloid peptides 1-40 and 1-42 are generated by distinct γ-secretase activities
    • DOI 10.1074/jbc.271.45.28655
    • Klafki H, Abramowski D, Swoboda R, Paganetti PA, Staufen-biel M (1996) The carboxyl termini of beta-amyloid peptides 1-40 and 1-42 are generated by distinct gamma-secretase activities. J Biol Chem 271, 28655-28659. (Pubitemid 26374693)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.45 , pp. 28655-28659
    • Klafki, H.-W.1    Abramowski, D.2    Swoboda, R.3    Paganetti, P.A.4    Staufenbiel, M.5
  • 45
    • 0037134505 scopus 로고    scopus 로고
    • Insulin-degrading enzyme rapidly removes the β-amyloid precursor protein intracellular domain (AICD)
    • DOI 10.1074/jbc.M111571200
    • Edbauer D, Willem M, Lammich S, Steiner H, Haass C (2002) Insulin-degrading enzyme rapidly removes the fj-amyloid precursor protein intracellular domain (AICD). J Biol Chem 277, 13389-13393. (Pubitemid 34967931)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.16 , pp. 13389-13393
    • Edbauer, D.1    Willem, M.2    Lammich, S.3    Steiner, H.4    Haass, C.5
  • 47
    • 0033214675 scopus 로고    scopus 로고
    • Presenilins: Molecular switches between proteolysis and signal transduction
    • DOI 10.1016/S0166-2236(99)01455-1, PII S0166223699014551
    • Annaert W, De Strooper B (1999) Presenilins: Molecular switches between proteolysis and signal transduction. Trends Neurosci 22, 439-443. (Pubitemid 29447727)
    • (1999) Trends in Neurosciences , vol.22 , Issue.10 , pp. 439-443
    • Annaert, W.1    De Strooper, B.2
  • 49
    • 33745584643 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis of amyloid precursor protein and regulation of expression of putative target genes
    • DOI 10.1038/sj.embor.7400704, PII 7400704
    • Hebert SS, Serneels L, Tolia A, Craessaerts K, Derks C, Filippov MA, Müller U, De Strooper B (2006) Regulated intramembrane proteolysis of amyloid precursor protein and regulation of expression of putative target genes. EMBO Rep 7, 739-745. (Pubitemid 43986273)
    • (2006) EMBO Reports , vol.7 , Issue.7 , pp. 739-745
    • Hebert, S.S.1    Serneels, L.2    Tolia, A.3    Craessaerts, K.4    Derks, C.5    Filippov, M.A.6    Muller, U.7    De Strooper, B.8
  • 51
    • 78650669822 scopus 로고    scopus 로고
    • The transcriptionally active amyloid precursor protein (APP) intracellular domain is preferentially produced from the 695 isoform of APP in a {beta}-secretase-dependent pathway
    • Belyaev ND, Kellett KA, Beckett C, Makova NZ, Revett TJ, Nalivaeva NN, Hooper NM, Turner AJ (2010) The transcriptionally active amyloid precursor protein (APP) intracellular domain is preferentially produced from the 695 isoform of APP in a {beta}-secretase-dependent pathway. J Biol Chem 285, 41443-41454.
    • (2010) J Biol Chem , vol.285 , pp. 41443-41454
    • Belyaev, N.D.1    Kellett, K.A.2    Beckett, C.3    Makova, N.Z.4    Revett, T.J.5    Nalivaeva, N.N.6    Hooper, N.M.7    Turner, A.J.8
  • 52
    • 0034131044 scopus 로고    scopus 로고
    • Impaired proteasome function in Alzheimer's disease
    • DOI 10.1046/j.1471-4159.2000.0750436.x
    • Keller JN, Hanni KB, Markesbery WR (2000) Impaired pro-teasome function in Alzheimer's disease. J Neurochem 75, 436-439. (Pubitemid 30418211)
    • (2000) Journal of Neurochemistry , vol.75 , Issue.1 , pp. 436-439
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 55
    • 85027919079 scopus 로고    scopus 로고
    • Y-secretase-regulated mechanisms similar to notch signaling may play a role in signaling events, including APP signaling, which leads to Alzheimer's disease
    • Nakayama K, Nagase H, Koh CS, Ohkawara T (2011)-y-secretase-regulated mechanisms similar to notch signaling may play a role in signaling events, including APP signaling, which leads to Alzheimer's disease. Cell Mol Neurobiol 31, 887-900.
    • (2011) Cell Mol Neurobiol , vol.31 , pp. 887-900
    • Nakayama, K.1    Nagase, H.2    Koh, C.S.3    Ohkawara, T.4


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