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Volumn 7, Issue 6, 2012, Pages

Altering APP proteolysis: Increasing sAPPalpha production by targeting dimerization of the APP Ectodomain

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; DISULFIRAM; OLIGOMER; SULFIRAM; TRYPTOPHAN;

EID: 84863111022     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0040027     Document Type: Article
Times cited : (14)

References (56)
  • 1
    • 13044287361 scopus 로고    scopus 로고
    • Plaque-independent disruption of neural circuits in Alzheimer's disease mouse models
    • Hsia AY, Masliah E, McConlogue L, Yu GQ, Tatsuno G, et al. (1999) Plaque-independent disruption of neural circuits in Alzheimer's disease mouse models. Proc Natl Acad Sci U S A 96: 3228-3233.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 3228-3233
    • Hsia, A.Y.1    Masliah, E.2    McConlogue, L.3    Yu, G.Q.4    Tatsuno, G.5
  • 2
    • 36348935683 scopus 로고    scopus 로고
    • Soluble Abeta inhibits specific signal transduction cascades common to the insulin receptor pathway
    • Townsend M, Mehta T, Selkoe DJ, (2007) Soluble Abeta inhibits specific signal transduction cascades common to the insulin receptor pathway. J Biol Chem 282: 33305-33312.
    • (2007) J Biol Chem , vol.282 , pp. 33305-33312
    • Townsend, M.1    Mehta, T.2    Selkoe, D.J.3
  • 3
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, et al. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300: 486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5
  • 5
    • 0035159785 scopus 로고    scopus 로고
    • Intracellular mechanisms of amyloid accumulation and pathogenesis in Alzheimer's disease
    • Glabe C, (2001) Intracellular mechanisms of amyloid accumulation and pathogenesis in Alzheimer's disease. J Mol Neurosci 17: 137-145.
    • (2001) J Mol Neurosci , vol.17 , pp. 137-145
    • Glabe, C.1
  • 6
    • 43049150678 scopus 로고    scopus 로고
    • Metals in Alzheimer's and Parkinson's diseases
    • Barnham KJ, Bush AI, (2008) Metals in Alzheimer's and Parkinson's diseases. Curr Opin Chem Biol 12: 222-228.
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 222-228
    • Barnham, K.J.1    Bush, A.I.2
  • 7
    • 0344824654 scopus 로고    scopus 로고
    • Amyloid beta-peptide [1-42]-associated free radical-induced oxidative stress and neurodegeneration in Alzheimer's disease brain: mechanisms and consequences
    • Butterfield DA, (2003) Amyloid beta-peptide [1-42]-associated free radical-induced oxidative stress and neurodegeneration in Alzheimer's disease brain: mechanisms and consequences. Curr Med Chem 10: 2651-2659.
    • (2003) Curr Med Chem , vol.10 , pp. 2651-2659
    • Butterfield, D.A.1
  • 8
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins
    • Lambert MP, Barlow AK, Chromy BA, Edwards C, Freed R, et al. (1998) Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci U S A 95: 6448-6453.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3    Edwards, C.4    Freed, R.5
  • 9
    • 33646480747 scopus 로고    scopus 로고
    • Reversal of Alzheimer's-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 Alzheimer's-like pathology and behavior in human APP transgenic mice by mutation of Asp664. Proc Natl Acad Sci U S A 103: 7130-7135.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 7130-7135
    • Galvan, V.1    Gorostiza, O.F.2    Banwait, S.3    Ataie, M.4    Logvinova, A.V.5
  • 10
    • 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: 1065-1080.
    • (2008) J Neurochem , vol.104 , pp. 1065-1080
    • Nguyen, T.V.1    Galvan, V.2    Huang, W.3    Banwait, S.4    Tang, H.5
  • 11
    • 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: 234-242.
    • (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
  • 12
    • 45549102847 scopus 로고    scopus 로고
    • Adaptor protein sorting nexin 17 regulates amyloid precursor protein trafficking and processing in the early endosomes
    • Lee J, Retamal C, Cuitino L, Caruano-Yzermans A, Shin JE, et al. (2008) Adaptor protein sorting nexin 17 regulates amyloid precursor protein trafficking and processing in the early endosomes. J Biol Chem 283: 11501-11508.
    • (2008) J Biol Chem , vol.283 , pp. 11501-11508
    • Lee, J.1    Retamal, C.2    Cuitino, L.3    Caruano-Yzermans, A.4    Shin, J.E.5
  • 13
    • 67349109401 scopus 로고    scopus 로고
    • Netrin-1 interacts with amyloid precursor protein and regulates amyloid-beta production
    • Lourenco FC, Galvan V, Fombonne J, Corset V, Llambi F, et al. (2009) Netrin-1 interacts with amyloid precursor protein and regulates amyloid-beta production. Cell Death Differ 16: 655-663.
    • (2009) Cell Death Differ , vol.16 , pp. 655-663
    • Lourenco, F.C.1    Galvan, V.2    Fombonne, J.3    Corset, V.4    Llambi, F.5
  • 14
    • 60549089207 scopus 로고    scopus 로고
    • APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
    • Nikolaev A, McLaughlin T, O'Leary DD, Tessier-Lavigne M, (2009) APP binds DR6 to trigger axon pruning and neuron death via distinct caspases. Nature 457: 981-989.
    • (2009) Nature , vol.457 , pp. 981-989
    • Nikolaev, A.1    McLaughlin, T.2    O'Leary, D.D.3    Tessier-Lavigne, M.4
  • 15
    • 67749139805 scopus 로고    scopus 로고
    • Neurodegeneration in Alzheimer's disease: caspases and synaptic element interdependence
    • Bredesen DE, (2009) Neurodegeneration in Alzheimer's disease: caspases and synaptic element interdependence. Mol Neurodegener 4: 27.
    • (2009) Mol Neurodegener , vol.4 , pp. 27
    • Bredesen, D.E.1
  • 16
    • 0142179222 scopus 로고    scopus 로고
    • Caspase cleavage of the amyloid precursor protein modulates amyloid beta-protein toxicity
    • Lu DC, Soriano S, Bredesen DE, Koo EH, (2003) Caspase cleavage of the amyloid precursor protein modulates amyloid beta-protein toxicity. J Neurochem 87: 733-741.
    • (2003) J Neurochem , vol.87 , pp. 733-741
    • Lu, D.C.1    Soriano, S.2    Bredesen, D.E.3    Koo, E.H.4
  • 17
    • 33845661843 scopus 로고    scopus 로고
    • Abeta induces cell death by direct interaction with its cognate extracellular domain on APP (APP 597-624)
    • Shaked GM, Kummer MP, Lu DC, Galvan V, Bredesen DE, et al. (2006) Abeta induces cell death by direct interaction with its cognate extracellular domain on APP (APP 597-624). Faseb J 20: 1254-1256.
    • (2006) Faseb J , vol.20 , pp. 1254-1256
    • Shaked, G.M.1    Kummer, M.P.2    Lu, D.C.3    Galvan, V.4    Bredesen, D.E.5
  • 18
    • 79960807184 scopus 로고    scopus 로고
    • Structural and Functional Alterations in Amyloid-beta Protein Precursor Induced by Amyloid-beta Peptides
    • Libeu CP, Poksay KS, John V, Bredesen DE, (2011) Structural and Functional Alterations in Amyloid-beta Protein Precursor Induced by Amyloid-beta Peptides. J Alzheimers Dis 25: 547-566.
    • (2011) J Alzheimers Dis , vol.25 , pp. 547-566
    • Libeu, C.P.1    Poksay, K.S.2    John, V.3    Bredesen, D.E.4
  • 19
    • 39049103989 scopus 로고    scopus 로고
    • Alzheimer's disease sends the wrong signals-a perspective
    • Neve RL, (2008) Alzheimer's disease sends the wrong signals-a perspective. Amyloid 15: 1-4.
    • (2008) Amyloid , vol.15 , pp. 1-4
    • Neve, R.L.1
  • 20
    • 63949084694 scopus 로고    scopus 로고
    • Lipoprotein receptors and cholesterol in APP trafficking and proteolytic processing, implications for Alzheimer's disease
    • Marzolo MP, Bu G, (2009) Lipoprotein receptors and cholesterol in APP trafficking and proteolytic processing, implications for Alzheimer's disease. Semin Cell Dev Biol 20: 191-200.
    • (2009) Semin Cell Dev Biol , vol.20 , pp. 191-200
    • Marzolo, M.P.1    Bu, G.2
  • 21
    • 67649366042 scopus 로고    scopus 로고
    • Neuroprotective secreted amyloid precursor protein acts by disrupting amyloid precursor protein dimers
    • Gralle M, Botelho MG, Wouters FS, (2009) Neuroprotective secreted amyloid precursor protein acts by disrupting amyloid precursor protein dimers. J Biol Chem 284: 15016-15025.
    • (2009) J Biol Chem , vol.284 , pp. 15016-15025
    • Gralle, M.1    Botelho, M.G.2    Wouters, F.S.3
  • 22
    • 43149088724 scopus 로고    scopus 로고
    • Amyloidogenic processing but not amyloid precursor protein (APP) intracellular C-terminal domain production requires a precisely oriented APP dimer assembled by transmembrane GXXXG motifs
    • Kienlen-Campard P, Tasiaux B, Van Hees J, Li M, Huysseune S, et al. (2008) Amyloidogenic processing but not amyloid precursor protein (APP) intracellular C-terminal domain production requires a precisely oriented APP dimer assembled by transmembrane GXXXG motifs. J Biol Chem 283: 7733-7744.
    • (2008) J Biol Chem , vol.283 , pp. 7733-7744
    • Kienlen-Campard, P.1    Tasiaux, B.2    van Hees, J.3    Li, M.4    Huysseune, S.5
  • 23
    • 70350350069 scopus 로고    scopus 로고
    • Induced dimerization of the amyloid precursor protein leads to decreased amyloid-beta protein production
    • Eggert S, Midthune B, Cottrell B, Koo EH, (2009) Induced dimerization of the amyloid precursor protein leads to decreased amyloid-beta protein production. J Biol Chem 284: 28943-28952.
    • (2009) J Biol Chem , vol.284 , pp. 28943-28952
    • Eggert, S.1    Midthune, B.2    Cottrell, B.3    Koo, E.H.4
  • 24
    • 84857355873 scopus 로고    scopus 로고
    • The amyloid precursor protein and its homologues: Structural and functional aspects of native and pathogenic oligomerization
    • Kaden D, Munter LM, Reif B, Multhaup G, (2012) The amyloid precursor protein and its homologues: Structural and functional aspects of native and pathogenic oligomerization. Eur J Cell Biol 91: 234-239.
    • (2012) Eur J Cell Biol , vol.91 , pp. 234-239
    • Kaden, D.1    Munter, L.M.2    Reif, B.3    Multhaup, G.4
  • 25
    • 4143105782 scopus 로고    scopus 로고
    • The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain
    • Wang Y, Ha Y, (2004) The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain. Mol Cell 15: 343-353.
    • (2004) Mol Cell , vol.15 , pp. 343-353
    • Wang, Y.1    Ha, Y.2
  • 26
    • 43749112022 scopus 로고    scopus 로고
    • Homophilic interactions of the amyloid precursor protein (APP) ectodomain are regulated by the loop region and affect beta-secretase cleavage of APP
    • Kaden D, Munter LM, Joshi M, Treiber C, Weise C, et al. (2008) Homophilic interactions of the amyloid precursor protein (APP) ectodomain are regulated by the loop region and affect beta-secretase cleavage of APP. J Biol Chem 283: 7271-7279.
    • (2008) J Biol Chem , vol.283 , pp. 7271-7279
    • Kaden, D.1    Munter, L.M.2    Joshi, M.3    Treiber, C.4    Weise, C.5
  • 27
    • 77950385325 scopus 로고    scopus 로고
    • Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein
    • Dahms SO, Hoefgen S, Roeser D, Schlott B, Guhrs KH, et al. (2010) Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein. Proc Natl Acad Sci U S A 107: 5381-5386.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 5381-5386
    • Dahms, S.O.1    Hoefgen, S.2    Roeser, D.3    Schlott, B.4    Guhrs, K.H.5
  • 28
    • 33344458873 scopus 로고    scopus 로고
    • Solution conformation and heparin-induced dimerization of the full-length extracellular domain of the human amyloid precursor protein
    • Gralle M, Oliveira CL, Guerreiro LH, McKinstry WJ, Galatis D, et al. (2006) Solution conformation and heparin-induced dimerization of the full-length extracellular domain of the human amyloid precursor protein. J Mol Biol 357: 493-508.
    • (2006) J Mol Biol , vol.357 , pp. 493-508
    • Gralle, M.1    Oliveira, C.L.2    Guerreiro, L.H.3    McKinstry, W.J.4    Galatis, D.5
  • 29
    • 0027981759 scopus 로고
    • Identification and regulation of the high affinity binding site of the Alzheimer's disease amyloid protein precursor (APP) to glycosaminoglycans
    • Multhaup G, (1994) Identification and regulation of the high affinity binding site of the Alzheimer's disease amyloid protein precursor (APP) to glycosaminoglycans. Biochimie 76: 304-311.
    • (1994) Biochimie , vol.76 , pp. 304-311
    • Multhaup, G.1
  • 31
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun DI, (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J Appl Crystallogr 25: 495-503.
    • (1992) J Appl Crystallogr , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 34
    • 27144541627 scopus 로고    scopus 로고
    • Controlling {beta}-amyloid oligomerization by the use of naphthalene sulfonates: trapping low molecular weight oligomeric species
    • Ferrao-Gonzales AD, Robbs BK, Moreau VH, Ferreira A, Juliano L, et al. (2005) Controlling {beta}-amyloid oligomerization by the use of naphthalene sulfonates: trapping low molecular weight oligomeric species. J Biol Chem 280: 34747-34754.
    • (2005) J Biol Chem , vol.280 , pp. 34747-34754
    • Ferrao-Gonzales, A.D.1    Robbs, B.K.2    Moreau, V.H.3    Ferreira, A.4    Juliano, L.5
  • 35
    • 0013913906 scopus 로고
    • Cooperative effects in binding by bovine serum albumin. I. The binding of 1-anilino-8-naphthalenesulfonate. Fluorimetric titrations
    • Daniel E, Weber G, (1966) Cooperative effects in binding by bovine serum albumin. I. The binding of 1-anilino-8-naphthalenesulfonate. Fluorimetric titrations. Biochemistry (Mosc) 5: 1893-1900.
    • (1966) Biochemistry (Mosc) , vol.5 , pp. 1893-1900
    • Daniel, E.1    Weber, G.2
  • 36
    • 77956741418 scopus 로고
    • Ultraviolet Spectra of proteins and amino acids
    • Wetlaufer DB, (1962) Ultraviolet Spectra of proteins and amino acids. Adv Protein Chem 17: 303-390.
    • (1962) Adv Protein Chem , vol.17 , pp. 303-390
    • Wetlaufer, D.B.1
  • 37
    • 0031972919 scopus 로고    scopus 로고
    • 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation
    • Matulis D, Lovrien R, (1998) 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation. Biophys J 74: 422-429.
    • (1998) Biophys J , vol.74 , pp. 422-429
    • Matulis, D.1    Lovrien, R.2
  • 38
    • 0037422540 scopus 로고    scopus 로고
    • Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways
    • Bitan G, Kirkitadze MD, Lomakin A, Vollers SS, Benedek GB, et al. (2003) Amyloid beta-protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways. Proc Natl Acad Sci U S A 100: 330-335.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 330-335
    • Bitan, G.1    Kirkitadze, M.D.2    Lomakin, A.3    Vollers, S.S.4    Benedek, G.B.5
  • 39
    • 13244291632 scopus 로고    scopus 로고
    • Amyloid-beta protofibrils differ from amyloid-beta aggregates induced in dilute hexafluoroisopropanol in stability and morphology
    • Nichols MR, Moss MA, Reed DK, Cratic-McDaniel S, Hoh JH, et al. (2005) Amyloid-beta protofibrils differ from amyloid-beta aggregates induced in dilute hexafluoroisopropanol in stability and morphology. J Biol Chem 280: 2471-2480.
    • (2005) J Biol Chem , vol.280 , pp. 2471-2480
    • Nichols, M.R.1    Moss, M.A.2    Reed, D.K.3    Cratic-McDaniel, S.4    Hoh, J.H.5
  • 41
    • 0027221517 scopus 로고
    • Amino acid sequence RERMS represents the active domain of amyloid beta/A4 protein precursor that promotes fibroblast growth
    • Ninomiya H, Roch JM, Sundsmo MP, Otero DA, Saitoh T, (1993) Amino acid sequence RERMS represents the active domain of amyloid beta/A4 protein precursor that promotes fibroblast growth. J Cell Biol 121: 879-886.
    • (1993) J Cell Biol , vol.121 , pp. 879-886
    • Ninomiya, H.1    Roch, J.M.2    Sundsmo, M.P.3    Otero, D.A.4    Saitoh, T.5
  • 42
    • 0028136865 scopus 로고
    • Peptides containing the RERMS sequence of amyloid beta/A4 protein precursor bind cell surface and promote neurite extension
    • Jin LW, Ninomiya H, Roch JM, Schubert D, Masliah E, et al. (1994) Peptides containing the RERMS sequence of amyloid beta/A4 protein precursor bind cell surface and promote neurite extension. J Neurosci 14: 5461-5470.
    • (1994) J Neurosci , vol.14 , pp. 5461-5470
    • Jin, L.W.1    Ninomiya, H.2    Roch, J.M.3    Schubert, D.4    Masliah, E.5
  • 43
    • 77956392552 scopus 로고    scopus 로고
    • ADAM10 is the physiologically relevant, constitutive alpha-secretase of the amyloid precursor protein in primary neurons
    • Kuhn PH, Wang H, Dislich B, Colombo A, Zeitschel U, et al. (2010) ADAM10 is the physiologically relevant, constitutive alpha-secretase of the amyloid precursor protein in primary neurons. EMBO J 29: 3020-3032.
    • (2010) EMBO J , vol.29 , pp. 3020-3032
    • Kuhn, P.H.1    Wang, H.2    Dislich, B.3    Colombo, A.4    Zeitschel, U.5
  • 44
    • 77957096840 scopus 로고    scopus 로고
    • Amyloid beta 42 peptide (Abeta42)-lowering compounds directly bind to Abeta and interfere with amyloid precursor protein (APP) transmembrane dimerization
    • Richter L, Munter LM, Ness J, Hildebrand PW, Dasari M, et al. (2010) Amyloid beta 42 peptide (Abeta42)-lowering compounds directly bind to Abeta and interfere with amyloid precursor protein (APP) transmembrane dimerization. Proc Natl Acad Sci U S A 107: 14597-14602.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 14597-14602
    • Richter, L.1    Munter, L.M.2    Ness, J.3    Hildebrand, P.W.4    Dasari, M.5
  • 45
    • 0033609449 scopus 로고    scopus 로고
    • Cleavage of Alzheimer's amyloid precursor protein by alpha-secretase occurs at the surface of neuronal cells
    • Parvathy S, Hussain I, Karran EH, Turner AJ, Hooper NM, (1999) Cleavage of Alzheimer's amyloid precursor protein by alpha-secretase occurs at the surface of neuronal cells. Biochemistry 38: 9728-9734.
    • (1999) Biochemistry , vol.38 , pp. 9728-9734
    • Parvathy, S.1    Hussain, I.2    Karran, E.H.3    Turner, A.J.4    Hooper, N.M.5
  • 46
    • 33750159885 scopus 로고    scopus 로고
    • Amyloid precursor protein and BACE function as oligomers
    • Multhaup G, (2006) Amyloid precursor protein and BACE function as oligomers. Neurodegener Dis 3: 270-274.
    • (2006) Neurodegener Dis , vol.3 , pp. 270-274
    • Multhaup, G.1
  • 47
    • 65249105453 scopus 로고    scopus 로고
    • Selective vulnerability in Alzheimer's disease: amyloid precursor protein and p75(NTR) interaction
    • Fombonne J, Rabizadeh S, Banwait S, Mehlen P, Bredesen DE, (2009) Selective vulnerability in Alzheimer's disease: amyloid precursor protein and p75(NTR) interaction. Ann Neurol 65: 294-303.
    • (2009) Ann Neurol , vol.65 , pp. 294-303
    • Fombonne, J.1    Rabizadeh, S.2    Banwait, S.3    Mehlen, P.4    Bredesen, D.E.5
  • 48
    • 0030797917 scopus 로고    scopus 로고
    • Apolipoprotein E forms stable complexes with recombinant Alzheimer's disease beta-amyloid precursor protein
    • Haas C, Cazorla P, Miguel CD, Valdivieso F, Vazquez J, (1997) Apolipoprotein E forms stable complexes with recombinant Alzheimer's disease beta-amyloid precursor protein. Biochem J 325 (Pt 1): 169-175.
    • (1997) Biochem J , vol.325 , Issue.Pt 1 , pp. 169-175
    • Haas, C.1    Cazorla, P.2    Miguel, C.D.3    Valdivieso, F.4    Vazquez, J.5
  • 49
    • 0032577578 scopus 로고    scopus 로고
    • Physical interaction of ApoE with amyloid precursor protein independent of the amyloid Abeta region in vitro
    • Hass S, Fresser F, Kochl S, Beyreuther K, Utermann G, et al. (1998) Physical interaction of ApoE with amyloid precursor protein independent of the amyloid Abeta region in vitro. J Biol Chem 273: 13892-13897.
    • (1998) J Biol Chem , vol.273 , pp. 13892-13897
    • Hass, S.1    Fresser, F.2    Kochl, S.3    Beyreuther, K.4    Utermann, G.5
  • 50
    • 33644962142 scopus 로고    scopus 로고
    • Visualization of APP dimerization and APP-Notch2 heterodimerization in living cells using bimolecular fluorescence complementation
    • Chen CD, Oh SY, Hinman JD, Abraham CR, (2006) Visualization of APP dimerization and APP-Notch2 heterodimerization in living cells using bimolecular fluorescence complementation. J Neurochem 97: 30-43.
    • (2006) J Neurochem , vol.97 , pp. 30-43
    • Chen, C.D.1    Oh, S.Y.2    Hinman, J.D.3    Abraham, C.R.4
  • 52
    • 27144547977 scopus 로고    scopus 로고
    • Homo- and heterodimerization of APP family members promotes intercellular adhesion
    • Soba P, Eggert S, Wagner K, Zentgraf H, Siehl K, et al. (2005) Homo- and heterodimerization of APP family members promotes intercellular adhesion. Embo J 24: 3624-3634.
    • (2005) Embo J , vol.24 , pp. 3624-3634
    • Soba, P.1    Eggert, S.2    Wagner, K.3    Zentgraf, H.4    Siehl, K.5
  • 53
    • 23844491144 scopus 로고    scopus 로고
    • The familial dementia BRI2 gene binds the Alzheimer gene amyloid-beta precursor protein and inhibits amyloid-beta production
    • Matsuda S, Giliberto L, Matsuda Y, Davies P, McGowan E, et al. (2005) The familial dementia BRI2 gene binds the Alzheimer gene amyloid-beta precursor protein and inhibits amyloid-beta production. J Biol Chem 280: 28912-28916.
    • (2005) J Biol Chem , vol.280 , pp. 28912-28916
    • Matsuda, S.1    Giliberto, L.2    Matsuda, Y.3    Davies, P.4    McGowan, E.5
  • 54
    • 67650156458 scopus 로고    scopus 로고
    • BRI3 inhibits amyloid precursor protein processing in a mechanistically distinct manner from its homologue dementia gene BRI2
    • Matsuda S, Matsuda Y, D'Adamio L, (2009) BRI3 inhibits amyloid precursor protein processing in a mechanistically distinct manner from its homologue dementia gene BRI2. J Biol Chem 284: 15815-15825.
    • (2009) J Biol Chem , vol.284 , pp. 15815-15825
    • Matsuda, S.1    Matsuda, Y.2    D'Adamio, L.3
  • 55
    • 0013916007 scopus 로고
    • Cooperative effects in binding by bovine serum albumin. II. The binding of 1-anilino-8-naphthalenesulfonate. Polarization of the ligand fluorescence and quenching of the protein fluorescence
    • Weber G, Daniel E, (1966) Cooperative effects in binding by bovine serum albumin. II. The binding of 1-anilino-8-naphthalenesulfonate. Polarization of the ligand fluorescence and quenching of the protein fluorescence. Biochemistry (Mosc) 5: 1900-1907.
    • (1966) Biochemistry (Mosc) , vol.5 , pp. 1900-1907
    • Weber, G.1    Daniel, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.