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Volumn 1262, Issue , 2009, Pages 89-99

γ-secretase processing of APLP1 leads to the production of a p3-like peptide that does not aggregate and is not toxic to neurons

Author keywords

Aggregation; Alzheimer's disease; Amyloid protein; Amyloid precursor like protein 1; Fibrillogenesis; Neurotoxicity

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR LIKE PROTEIN 1; AMYLOID PRECURSOR LIKE PROTEIN 1 DERIVED PEPTIDE; AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; GAMMA SECRETASE; PROTEIN ANTIBODY; UNCLASSIFIED DRUG;

EID: 62249105153     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.brainres.2009.01.008     Document Type: Article
Times cited : (17)

References (58)
  • 1
    • 32444443485 scopus 로고    scopus 로고
    • Involvement of amyloid beta precursor protein (AbetaPP) modulated copper homeostasis in Alzheimer's disease
    • discussion 209-215
    • Bayer T.A., and Multhaup G. Involvement of amyloid beta precursor protein (AbetaPP) modulated copper homeostasis in Alzheimer's disease. J. Alzheimers Dis. 8 (2005) 201-206 discussion 209-215
    • (2005) J. Alzheimers Dis. , vol.8 , pp. 201-206
    • Bayer, T.A.1    Multhaup, G.2
  • 3
    • 0032760270 scopus 로고    scopus 로고
    • It all sticks together-the APP-related family of proteins and Alzheimer's disease
    • Bayer T.A., Cappai R., Masters C.L., Beyreuther K., and Multhaup G. It all sticks together-the APP-related family of proteins and Alzheimer's disease. Mol. Psychiatry 4 (1999) 524-528
    • (1999) Mol. Psychiatry , vol.4 , pp. 524-528
    • Bayer, T.A.1    Cappai, R.2    Masters, C.L.3    Beyreuther, K.4    Multhaup, G.5
  • 4
    • 0030614752 scopus 로고    scopus 로고
    • Increased gene expression of beta-amyloid precursor protein and its homologues APLP1 and APLP2 in human neuroblastoma cells in response to retinoic acid
    • Beckman M., and Iverfeldt K. Increased gene expression of beta-amyloid precursor protein and its homologues APLP1 and APLP2 in human neuroblastoma cells in response to retinoic acid. Neurosci. Lett. 221 (1997) 73-76
    • (1997) Neurosci. Lett. , vol.221 , pp. 73-76
    • Beckman, M.1    Iverfeldt, K.2
  • 5
    • 49549098365 scopus 로고    scopus 로고
    • Aggregation and catabolism of disease-associated intra-Aβ mutations: reduced proteolysis of AβA21G by neprilysin
    • Betts V., Leissring M.L., Dolios G., Wang R., Selkoe D.J., and Walsh D.M. Aggregation and catabolism of disease-associated intra-Aβ mutations: reduced proteolysis of AβA21G by neprilysin. Neurobiol. Dis. 31 (2008) 442-450
    • (2008) Neurobiol. Dis. , vol.31 , pp. 442-450
    • Betts, V.1    Leissring, M.L.2    Dolios, G.3    Wang, R.4    Selkoe, D.J.5    Walsh, D.M.6
  • 7
    • 0033972608 scopus 로고    scopus 로고
    • What the evolution of the amyloid protein precursor supergene family tells us about its function
    • Coulson E.J., Paliga K., Beyreuther K., and Masters C.L. What the evolution of the amyloid protein precursor supergene family tells us about its function. Neurochem. Int. 36 (2000) 175-184
    • (2000) Neurochem. Int. , vol.36 , pp. 175-184
    • Coulson, E.J.1    Paliga, K.2    Beyreuther, K.3    Masters, C.L.4
  • 8
    • 0027333449 scopus 로고
    • Apl-1, a C. elegans gene encoding a protein related to the human β-amyloid protein precursor
    • Daigle I., and Li C. Apl-1, a C. elegans gene encoding a protein related to the human β-amyloid protein precursor. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 12045-12049
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 12045-12049
    • Daigle, I.1    Li, C.2
  • 9
    • 0033017690 scopus 로고    scopus 로고
    • Age-related cognitive deficits, impaired long-term potentiation and reduction in synaptic marker density in mice lacking the beta-amyloid precursor protein
    • Dawson G.R., Seabrook G.R., Zheng H., Smith D.W., Graham S., O'Dowd G., Bowery B.J., Boyce S., Trumbauer M.E., Chen H.Y., et al. Age-related cognitive deficits, impaired long-term potentiation and reduction in synaptic marker density in mice lacking the beta-amyloid precursor protein. Neuroscience 90 (1999) 1-13
    • (1999) Neuroscience , vol.90 , pp. 1-13
    • Dawson, G.R.1    Seabrook, G.R.2    Zheng, H.3    Smith, D.W.4    Graham, S.5    O'Dowd, G.6    Bowery, B.J.7    Boyce, S.8    Trumbauer, M.E.9    Chen, H.Y.10
  • 10
    • 33745268224 scopus 로고    scopus 로고
    • Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons
    • Deshpande A., Mina E., Glabe C., and Busciglio J. Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons. J. Neurosci. 26 (2006) 6011-6018
    • (2006) J. Neurosci. , vol.26 , pp. 6011-6018
    • Deshpande, A.1    Mina, E.2    Glabe, C.3    Busciglio, J.4
  • 11
    • 2442592973 scopus 로고    scopus 로고
    • The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves alpha-, beta-, gamma-, and epsilon-like cleavages: modulation of APLP-1 processing by n-glycosylation
    • Eggert S., Paliga K., Soba P., Evin G., Masters C.L., Weidemann A., and Beyreuther K. The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves alpha-, beta-, gamma-, and epsilon-like cleavages: modulation of APLP-1 processing by n-glycosylation. J. Biol. Chem. 279 (2004) 18146-18156
    • (2004) J. Biol. Chem. , vol.279 , pp. 18146-18156
    • Eggert, S.1    Paliga, K.2    Soba, P.3    Evin, G.4    Masters, C.L.5    Weidemann, A.6    Beyreuther, K.7
  • 12
    • 0024317904 scopus 로고
    • Prevalence of Alzheimer's disease in a community population of older persons. Higher than previously reported
    • Evans D.A., Funkenstein H.H., Albert M.S., et al. Prevalence of Alzheimer's disease in a community population of older persons. Higher than previously reported. JAMA 262 (1989) 2551
    • (1989) JAMA , vol.262 , pp. 2551
    • Evans, D.A.1    Funkenstein, H.H.2    Albert, M.S.3
  • 13
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • Glabe C.G. Structural classification of toxic amyloid oligomers. J. Biol. Chem. 283 (2008) 29639-29643
    • (2008) J. Biol. Chem. , vol.283 , pp. 29639-29643
    • Glabe, C.G.1
  • 16
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley D.M., Walsh D.M., Ye C.P., Diehl T., Vasquez S., Vassilev P.M., Teplow D.B., and Selkoe D.J. Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J. Neurosci. 19 (1999) 8876-8884
    • (1999) J. Neurosci. , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6    Teplow, D.B.7    Selkoe, D.J.8
  • 18
    • 8144230876 scopus 로고    scopus 로고
    • Cortical dysplasia resembling human type 2 lissencephaly in mice lacking all three APP family members
    • Herms J., Anliker B., Heber S., Ring S., Fuhrmann M., Kretzschmar H., Sisodia S., and Muller U. Cortical dysplasia resembling human type 2 lissencephaly in mice lacking all three APP family members. EMBO J. 23 (2004) 4106-4115
    • (2004) EMBO J. , vol.23 , pp. 4106-4115
    • Herms, J.1    Anliker, B.2    Heber, S.3    Ring, S.4    Fuhrmann, M.5    Kretzschmar, H.6    Sisodia, S.7    Muller, U.8
  • 19
    • 0037975676 scopus 로고    scopus 로고
    • Spherical aggregates of beta-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3beta
    • Hoshi M., Sato M., Matsumoto S., Noguchi A., Yasutake K., Yoshida N., and Sato K. Spherical aggregates of beta-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3beta. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 6370-6375
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 6370-6375
    • Hoshi, M.1    Sato, M.2    Matsumoto, S.3    Noguchi, A.4    Yasutake, K.5    Yoshida, N.6    Sato, K.7
  • 20
    • 0029661424 scopus 로고    scopus 로고
    • Analysis of heterogeneous A4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay
    • Ida N., Hartmann T., Pantel J., Schroder J., Zerfass R., Forstl H., Sandbrink R., Masters C.L., and Beyreuther K. Analysis of heterogeneous A4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay. J. Biol. Chem. 271 (1996) 22908-22914
    • (1996) J. Biol. Chem. , vol.271 , pp. 22908-22914
    • Ida, N.1    Hartmann, T.2    Pantel, J.3    Schroder, J.4    Zerfass, R.5    Forstl, H.6    Sandbrink, R.7    Masters, C.L.8    Beyreuther, K.9
  • 21
    • 0029093437 scopus 로고
    • Cell recognition, signal induction, and symmetrical gene activation at the dorsal-ventral boundary of the developing Drosophila wing
    • Kim J., Irvine K.D., and Carroll S.B. Cell recognition, signal induction, and symmetrical gene activation at the dorsal-ventral boundary of the developing Drosophila wing. Cell 82 (1995) 795-802
    • (1995) Cell , vol.82 , pp. 795-802
    • Kim, J.1    Irvine, K.D.2    Carroll, S.B.3
  • 23
    • 1642345964 scopus 로고    scopus 로고
    • Cleavage of amyloid-beta precursor protein and amyloid-beta precursor-like protein by BACE 1
    • Li Q., and Sudhof T.C. Cleavage of amyloid-beta precursor protein and amyloid-beta precursor-like protein by BACE 1. J. Biol. Chem. 279 (2004) 10542-10550
    • (2004) J. Biol. Chem. , vol.279 , pp. 10542-10550
    • Li, Q.1    Sudhof, T.C.2
  • 24
    • 0028914672 scopus 로고
    • Expression in mouse embryos and in adult mouse brain of three members of the amyloid precursor protein family, of the alpha-2-macroglobulin receptor/low density lipoprotein receptor-related protein and of its ligands apolipoprotein E, lipoprotein lipase, alpha-2-macroglobulin and the 40,000 molecular weight receptor-associated protein
    • Lorent K., Overbergh L., Moechars D., De Strooper B., Van Leuven F., and Van den Berghe H. Expression in mouse embryos and in adult mouse brain of three members of the amyloid precursor protein family, of the alpha-2-macroglobulin receptor/low density lipoprotein receptor-related protein and of its ligands apolipoprotein E, lipoprotein lipase, alpha-2-macroglobulin and the 40,000 molecular weight receptor-associated protein. Neuroscience 65 (1995) 1009-1025
    • (1995) Neuroscience , vol.65 , pp. 1009-1025
    • Lorent, K.1    Overbergh, L.2    Moechars, D.3    De Strooper, B.4    Van Leuven, F.5    Van den Berghe, H.6
  • 27
    • 0036848056 scopus 로고    scopus 로고
    • A novel beta-sheet breaker, RS-0406, reverses amyloid beta-induced cytotoxicity and impairment of long-term potentiation in vitro
    • Nakagami Y., Nishimura S., Murasugi T., Kaneko I., Meguro M., Marumoto S., Kogen H., Koyama K., and Oda T. A novel beta-sheet breaker, RS-0406, reverses amyloid beta-induced cytotoxicity and impairment of long-term potentiation in vitro. Br. J. Pharmacol. 137 (2002) 676-682
    • (2002) Br. J. Pharmacol. , vol.137 , pp. 676-682
    • Nakagami, Y.1    Nishimura, S.2    Murasugi, T.3    Kaneko, I.4    Meguro, M.5    Marumoto, S.6    Kogen, H.7    Koyama, K.8    Oda, T.9
  • 29
    • 33646349010 scopus 로고    scopus 로고
    • Amyloid precursor-like protein 1 influences endocytosis and proteolytic processing of the amyloid precursor protein
    • Neumann S., Schobel S., Jager S., Trautwein A., Haass C., Pietrzik C.U., and Lichtenthaler S.F. Amyloid precursor-like protein 1 influences endocytosis and proteolytic processing of the amyloid precursor protein. J. Biol. Chem. 281 (2006) 7583-7594
    • (2006) J. Biol. Chem. , vol.281 , pp. 7583-7594
    • Neumann, S.1    Schobel, S.2    Jager, S.3    Trautwein, A.4    Haass, C.5    Pietrzik, C.U.6    Lichtenthaler, S.F.7
  • 30
    • 0031437769 scopus 로고    scopus 로고
    • Human amyloid precursor-like protein 1-cDNA cloning, ectopic expression in COS-7 cells and identification of soluble forms in the cerebrospinal fluid
    • Paliga K., Peraus G., Kreger S., Durrwang U., Hesse L., Multhaup G., Masters C.L., Beyreuther K., and Weidemann A. Human amyloid precursor-like protein 1-cDNA cloning, ectopic expression in COS-7 cells and identification of soluble forms in the cerebrospinal fluid. Eur. J. Biochem. 250 (1997) 354-363
    • (1997) Eur. J. Biochem. , vol.250 , pp. 354-363
    • Paliga, K.1    Peraus, G.2    Kreger, S.3    Durrwang, U.4    Hesse, L.5    Multhaup, G.6    Masters, C.L.7    Beyreuther, K.8    Weidemann, A.9
  • 32
    • 0012194808 scopus 로고
    • A Drosophila gene encoding a protein resembling the human β-amyloid precursor protein
    • Rosen D.R., Martin-Morris L., Luo L., and White K. A Drosophila gene encoding a protein resembling the human β-amyloid precursor protein. Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 2478-2482
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 2478-2482
    • Rosen, D.R.1    Martin-Morris, L.2    Luo, L.3    White, K.4
  • 33
    • 0035954426 scopus 로고    scopus 로고
    • The Alzheimer amyloid precursor protein (APP) and FE65, an APP-binding protein, regulate cell movement
    • Sabo S.L., Ikin A.F., Buxbaum J.D., and Greengard P. The Alzheimer amyloid precursor protein (APP) and FE65, an APP-binding protein, regulate cell movement. J. Cell Biol. 153 (2001) 1403-1414
    • (2001) J. Cell Biol. , vol.153 , pp. 1403-1414
    • Sabo, S.L.1    Ikin, A.F.2    Buxbaum, J.D.3    Greengard, P.4
  • 34
    • 33750342540 scopus 로고    scopus 로고
    • Gene silencing analyses against amyloid precursor protein (APP) gene family by RNA interference
    • Sakai T., and Hohjoh H. Gene silencing analyses against amyloid precursor protein (APP) gene family by RNA interference. Cell Biol. Int. 30 (2006) 952-956
    • (2006) Cell Biol. Int. , vol.30 , pp. 952-956
    • Sakai, T.1    Hohjoh, H.2
  • 35
    • 0037114010 scopus 로고    scopus 로고
    • Processing of beta-amyloid precursor-like protein-1 and -2 by gamma-secretase regulates transcription
    • Scheinfeld M.H., Ghersi E., Laky K., Fowlkes B.J., and D'Adamio L. Processing of beta-amyloid precursor-like protein-1 and -2 by gamma-secretase regulates transcription. J. Biol. Chem. 277 (2002) 44195-44201
    • (2002) J. Biol. Chem. , vol.277 , pp. 44195-44201
    • Scheinfeld, M.H.1    Ghersi, E.2    Laky, K.3    Fowlkes, B.J.4    D'Adamio, L.5
  • 36
    • 0028033810 scopus 로고
    • Alzheimer's disease beyond 1994: the path to therapeutics
    • Selkoe D.J. Alzheimer's disease beyond 1994: the path to therapeutics. Neurobiol. Aging 15 (1994) S131-S133
    • (1994) Neurobiol. Aging , vol.15
    • Selkoe, D.J.1
  • 37
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimer's disease
    • Selkoe D.J. Translating cell biology into therapeutic advances in Alzheimer's disease. Nature 399 Supp (1999) A23-A31
    • (1999) Nature , vol.399 , Issue.SUPPL
    • Selkoe, D.J.1
  • 41
    • 0026721943 scopus 로고
    • β-amyloid precursor protein cleavage by a membrane-bound protease
    • Sisodia S.S. β-amyloid precursor protein cleavage by a membrane-bound protease. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 6075-6079
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 6075-6079
    • Sisodia, S.S.1
  • 42
    • 0028059841 scopus 로고
    • Expression of a ubiquitous, cross-reactive homologue of the mouse β-amyloid precursor protein (APP)
    • Slunt H.H., Thinakaran G., Von Koch C., Lo A.C.Y., Tanzi R.E., and Sisodia S.S. Expression of a ubiquitous, cross-reactive homologue of the mouse β-amyloid precursor protein (APP). J. Biol. Chem. 269 (1994) 2637-2644
    • (1994) J. Biol. Chem. , vol.269 , pp. 2637-2644
    • Slunt, H.H.1    Thinakaran, G.2    Von Koch, C.3    Lo, A.C.Y.4    Tanzi, R.E.5    Sisodia, S.S.6
  • 46
    • 34248190279 scopus 로고    scopus 로고
    • A beta oligomers - a decade of discovery
    • Walsh D.M., and Selkoe D.J. A beta oligomers - a decade of discovery. J. Neurochem. 101 (2007) 1172-1184
    • (2007) J. Neurochem. , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 47
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis: detection of a protofibrillar intermediate
    • Walsh D.M., Lomakin A., Benedek G.B., Condron M.M., and Teplow D.B. Amyloid β-protein fibrillogenesis: detection of a protofibrillar intermediate. J. Biol. Chem. 272 (1997) 22364-22374
    • (1997) J. Biol. Chem. , vol.272 , pp. 22364-22374
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 48
    • 0034609516 scopus 로고    scopus 로고
    • Detection of intracellular oligomers of amyloid β-protein in cells derived from human brain
    • Walsh D.M., Tseng B.P., Rydel R.E., Podlisny M.B., and Selkoe D.J. Detection of intracellular oligomers of amyloid β-protein in cells derived from human brain. Biochemistry 39 (2000) 10831-10839
    • (2000) Biochemistry , vol.39 , pp. 10831-10839
    • Walsh, D.M.1    Tseng, B.P.2    Rydel, R.E.3    Podlisny, M.B.4    Selkoe, D.J.5
  • 49
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of the Alzheimer amyloid β-protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh D., Klyubin I., Fadeeva J., William K., Cullen W., Anwyl R., Wolfe M., Rowan M., and Selkoe D. Naturally secreted oligomers of the Alzheimer amyloid β-protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416 (2002) 535-539
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.1    Klyubin, I.2    Fadeeva, J.3    William, K.4    Cullen, W.5    Anwyl, R.6    Wolfe, M.7    Rowan, M.8    Selkoe, D.9
  • 50
    • 0038322593 scopus 로고    scopus 로고
    • gamma-Secretase cleavage and binding to FE65 regulate the nuclear translocation of the intracellular C-terminal domain (ICD) of the APP family of proteins
    • Walsh D.M., Fadeeva J.V., LaVoie M.J., Paliga K., Eggert S., Kimberly W.T., Wasco W., and Selkoe D.J. gamma-Secretase cleavage and binding to FE65 regulate the nuclear translocation of the intracellular C-terminal domain (ICD) of the APP family of proteins. Biochemistry 42 (2003) 6664-6673
    • (2003) Biochemistry , vol.42 , pp. 6664-6673
    • Walsh, D.M.1    Fadeeva, J.V.2    LaVoie, M.J.3    Paliga, K.4    Eggert, S.5    Kimberly, W.T.6    Wasco, W.7    Selkoe, D.J.8
  • 51
    • 14944378094 scopus 로고    scopus 로고
    • Certain inhibitors of synthetic amyloid beta-peptide (Abeta) fibrillogenesis block oligomerization of natural Abeta and thereby rescue long-term potentiation
    • Walsh D.M., Townsend M., Podlisny M.B., Shankar G.M., Fadeeva J.V., Agnaf O.E., Hartley D.M., and Selkoe D.J. Certain inhibitors of synthetic amyloid beta-peptide (Abeta) fibrillogenesis block oligomerization of natural Abeta and thereby rescue long-term potentiation. J. Neurosci. 25 (2005) 2455-2462
    • (2005) J. Neurosci. , vol.25 , pp. 2455-2462
    • Walsh, D.M.1    Townsend, M.2    Podlisny, M.B.3    Shankar, G.M.4    Fadeeva, J.V.5    Agnaf, O.E.6    Hartley, D.M.7    Selkoe, D.J.8
  • 52
    • 60349100306 scopus 로고    scopus 로고
    • A facile method for expression and purification of the Alzheimer's disease-associated amyloid b-peptide
    • submitted for publication, Jan 27, doi:10.1111/j.1742-4658.2008.06862.x
    • Walsh, D.M., Thulin, E., Minogue, A.M., Gustavsson, N., Pang, E., Teplow, D.B., Linse, S., submitted for publication. A facile method for expression and purification of the Alzheimer's disease-associated amyloid b-peptide. FEBS Journal Published Online: Jan 27 2009 12:02PM. doi:10.1111/j.1742-4658.2008.06862.x.
    • (2009) FEBS Journal Published Online , vol.12
    • Walsh, D.M.1    Thulin, E.2    Minogue, A.M.3    Gustavsson, N.4    Pang, E.5    Teplow, D.B.6    Linse, S.7
  • 53
    • 0026442891 scopus 로고
    • Identification of a mouse brain cDNA that encodes a protein related to the Alzheimer disease-associated amyloid β-protein precursor
    • Wasco W., Bupp K., Magendantz M., Gusella J., Tanzi R.E., and Solomon F. Identification of a mouse brain cDNA that encodes a protein related to the Alzheimer disease-associated amyloid β-protein precursor. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 10758-10762
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 10758-10762
    • Wasco, W.1    Bupp, K.2    Magendantz, M.3    Gusella, J.4    Tanzi, R.E.5    Solomon, F.6
  • 54
    • 0027499514 scopus 로고
    • The amyloid precursor-like protein (APLP) gene maps to the long arm of chromosome 19
    • Wasco W., Brook D.J., and Tanzi R.E. The amyloid precursor-like protein (APLP) gene maps to the long arm of chromosome 19. Genomics 15 (1993) 237-239
    • (1993) Genomics , vol.15 , pp. 237-239
    • Wasco, W.1    Brook, D.J.2    Tanzi, R.E.3
  • 55
    • 0027240503 scopus 로고
    • Isolation and characterization of the human APLP2 gene encoding a homologue of the Alzheimer's associated amyloid β protein precursor
    • Wasco W., Gurubhagavatula S., Paradis M.D., Romano D.M., Sisodia S.S., Hyman B.T., Neve R.L., and Tanzi R.E. Isolation and characterization of the human APLP2 gene encoding a homologue of the Alzheimer's associated amyloid β protein precursor. Nat. Genet. 5 (1993) 95-99
    • (1993) Nat. Genet. , vol.5 , pp. 95-99
    • Wasco, W.1    Gurubhagavatula, S.2    Paradis, M.D.3    Romano, D.M.4    Sisodia, S.S.5    Hyman, B.T.6    Neve, R.L.7    Tanzi, R.E.8
  • 57
    • 37549040612 scopus 로고    scopus 로고
    • A critical function for beta-amyloid precursor protein in neuronal migration revealed by in utero RNA interference
    • Young-Pearse T.L., Bai J., Chang R., Zheng J.B., LoTurco J.J., and Selkoe D.J. A critical function for beta-amyloid precursor protein in neuronal migration revealed by in utero RNA interference. J. Neurosci. 27 (2007) 14459-14469
    • (2007) J. Neurosci. , vol.27 , pp. 14459-14469
    • Young-Pearse, T.L.1    Bai, J.2    Chang, R.3    Zheng, J.B.4    LoTurco, J.J.5    Selkoe, D.J.6


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