메뉴 건너뛰기




Volumn 14, Issue 5, 2004, Pages 582-588

Amyloid-beta precursor protein processing in neurodegeneration

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; PEPTIDE;

EID: 5344240284     PISSN: 09594388     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.conb.2004.08.001     Document Type: Review
Times cited : (217)

References (58)
  • 1
    • 0036861112 scopus 로고    scopus 로고
    • Testing times for the 'amyloid cascade hypothesis'
    • author reply 1101-1075.
    • Hardy J: Testing times for the 'amyloid cascade hypothesis'. Neurobiol Aging 2002. 23:1073-1074; author reply 1101-1075.
    • (2002) Neurobiol Aging , vol.23 , pp. 1073-1074
    • Hardy, J.1
  • 2
    • 0038204547 scopus 로고    scopus 로고
    • Dutch, Flemish, Italian, and Arctic mutations of APP and resistance of Aβ to physiologically relevant proteolytic degradation
    • S. Tsubuki, Y. Takaki, and T.C. Saido Dutch, Flemish, Italian, and Arctic mutations of APP and resistance of Aβ to physiologically relevant proteolytic degradation Lancet 361 2003 1957 1958 This study shows that some of the missense mutations in the amyloid sequence associated with familial AD make the peptide more resistant to degradation by neprilysin.
    • (2003) Lancet , vol.361 , pp. 1957-1958
    • Tsubuki, S.1    Takaki, Y.2    Saido, T.C.3
  • 3
    • 0034049944 scopus 로고    scopus 로고
    • Proteolytic processing and cell biological functions of the amyloid precursor protein
    • B. De Strooper, and W. Annaert Proteolytic processing and cell biological functions of the amyloid precursor protein J Cell Sci 113 2000 1857 1870
    • (2000) J Cell Sci , vol.113 , pp. 1857-1870
    • De Strooper, B.1    Annaert, W.2
  • 4
    • 0345743462 scopus 로고    scopus 로고
    • Adaptor protein interactions: Modulators of amyloid precursor protein metabolism and Alzheimer's disease risk?
    • G.D. King, and R. Scott Turner Adaptor protein interactions: modulators of amyloid precursor protein metabolism and Alzheimer's disease risk? Exp Neurol 185 2004 208 219
    • (2004) Exp Neurol , vol.185 , pp. 208-219
    • King, G.D.1    Scott Turner, R.2
  • 5
    • 1442306058 scopus 로고    scopus 로고
    • Binding of F-spondin to amyloid-β precursor protein: A candidate amyloid-β precursor protein ligand that modulates amyloid-β precursor protein cleavage
    • A. Ho, and T.C. Sudhof Binding of F-spondin to amyloid-β precursor protein: a candidate amyloid-β precursor protein ligand that modulates amyloid-β precursor protein cleavage Proc Natl Acad Sci USA 101 2004 2548 2553 This study identifies a first candidate ligand for APP.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2548-2553
    • Ho, A.1    Sudhof, T.C.2
  • 6
    • 0035818998 scopus 로고    scopus 로고
    • Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP
    • A. Kamal, A. Almenar-Queralt, J.F. LeBlanc, E.A. Roberts, and L.S. Goldstein Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP Nature 414 2001 643 648
    • (2001) Nature , vol.414 , pp. 643-648
    • Kamal, A.1    Almenar-Queralt, A.2    Leblanc, J.F.3    Roberts, E.A.4    Goldstein, L.S.5
  • 7
    • 2442498577 scopus 로고    scopus 로고
    • FE65 constitutes the functional link between the low-density lipoprotein receptor-related protein and the amyloid precursor protein
    • C.U. Pietrzik, I.S. Yoon, S. Jaeger, T. Busse, S. Weggen, and E.H. Koo FE65 constitutes the functional link between the low-density lipoprotein receptor-related protein and the amyloid precursor protein J Neurosci 24 2004 4259 4265
    • (2004) J Neurosci , vol.24 , pp. 4259-4265
    • Pietrzik, C.U.1    Yoon, I.S.2    Jaeger, S.3    Busse, T.4    Weggen, S.5    Koo, E.H.6
  • 8
    • 0142103374 scopus 로고    scopus 로고
    • The intracellular domain of the low density lipoprotein receptor-related protein modulates transactivation mediated by amyloid precursor protein and Fe65
    • A. Kinoshita, T. Shah, M.M. Tangredi, D.K. Strickland, and B.T. Hyman The intracellular domain of the low density lipoprotein receptor-related protein modulates transactivation mediated by amyloid precursor protein and Fe65 J Biol Chem 278 2003 41182 41188
    • (2003) J Biol Chem , vol.278 , pp. 41182-41188
    • Kinoshita, A.1    Shah, T.2    Tangredi, M.M.3    Strickland, D.K.4    Hyman, B.T.5
  • 9
    • 0027221517 scopus 로고
    • Amino acid sequence RERMS represents the active domain of amyloid β/A4 protein precursor that promotes fibroblast growth
    • H. Ninomiya, J.M. Roch, M.P. Sundsmo, D.A. Otero, and T. Saitoh Amino acid sequence RERMS represents the active domain of amyloid β/A4 protein precursor that promotes fibroblast growth J Cell Biol 121 1993 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
  • 10
    • 2542519087 scopus 로고    scopus 로고
    • Soluble form of amyloid precursor protein regulates proliferation of progenitors in the adult subventricular zone
    • I.I. Caille, B. Allinquant, E. Dupont, C. Bouillot, A. Langer, U. Muller, and A. Prochiantz Soluble form of amyloid precursor protein regulates proliferation of progenitors in the adult subventricular zone Development 131 2004 2173 2181 This study provides good evidence for a growth promoting function of APP in the subventricular zone.
    • (2004) Development , vol.131 , pp. 2173-2181
    • Caille, I.I.1    Allinquant, B.2    Dupont, E.3    Bouillot, C.4    Langer, A.5    Muller, U.6    Prochiantz, A.7
  • 11
    • 0345602771 scopus 로고    scopus 로고
    • Amyloid β protein toxicity mediated by the formation of amyloid-β protein precursor complexes
    • D.C. Lu, G.M. Shaked, E. Masliah, D.E. Bredesen, and E.H. Koo Amyloid β protein toxicity mediated by the formation of amyloid-β protein precursor complexes Ann Neurol 54 2003 781 789
    • (2003) Ann Neurol , vol.54 , pp. 781-789
    • Lu, D.C.1    Shaked, G.M.2    Masliah, E.3    Bredesen, D.E.4    Koo, E.H.5
  • 12
    • 0035433962 scopus 로고    scopus 로고
    • Alzheimer's disease and Aβ toxicity: From top to bottom
    • D.H. Small, S.S. Mok, and J.C. Bornstein Alzheimer's disease and Aβ toxicity: from top to bottom Nat Rev Neurosci 2 2001 595 598
    • (2001) Nat Rev Neurosci , vol.2 , pp. 595-598
    • Small, D.H.1    Mok, S.S.2    Bornstein, J.C.3
  • 13
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • D.M. Walsh, I. Klyubin, J.V. Fadeeva, W.K. Cullen, R. Anwyl, M.S. Wolfe, M.J. Rowan, and D.J. Selkoe Naturally secreted oligomers of 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.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 14
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small Aβ oligomers: The solution to an Alzheimer's disease conundrum?
    • W.L. Klein, G.A. Krafft, and C.E. Finch Targeting small Aβ oligomers: the solution to an Alzheimer's disease conundrum? Trends Neurosci 24 2001 219 224
    • (2001) Trends Neurosci , vol.24 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 15
    • 0038045587 scopus 로고    scopus 로고
    • The production of amyloid β peptide is a critical requirement for the viability of central neurons
    • L.D. Plant, J.P. Boyle, I.F. Smith, C. Peers, and H.A. Pearson The production of amyloid β peptide is a critical requirement for the viability of central neurons J Neurosci 23 2003 5531 5535
    • (2003) J Neurosci , vol.23 , pp. 5531-5535
    • Plant, L.D.1    Boyle, J.P.2    Smith, I.F.3    Peers, C.4    Pearson, H.A.5
  • 17
    • 13044278313 scopus 로고    scopus 로고
    • Presenilin 2 deficiency causes a mild pulmonary phenotype and no changes in amyloid precursor protein processing but enhances the embryonic lethal phenotype of presenilin 1 deficiency
    • A. Herreman, D. Hartmann, W. Annaert, P. Saftig, K. Craessaerts, L. Serneels, L. Umans, V. Schrijvers, F. Checler, and H. Vanderstichele Presenilin 2 deficiency causes a mild pulmonary phenotype and no changes in amyloid precursor protein processing but enhances the embryonic lethal phenotype of presenilin 1 deficiency Proc Natl Acad Sci USA 96 1999 11872 11877
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11872-11877
    • Herreman, A.1    Hartmann, D.2    Annaert, W.3    Saftig, P.4    Craessaerts, K.5    Serneels, L.6    Umans, L.7    Schrijvers, V.8    Checler, F.9    Vanderstichele, H.10
  • 18
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60
    • X. Cao, and T.C. Sudhof A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60 Science 293 2001 115 120
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 19
    • 2642582435 scopus 로고    scopus 로고
    • Dissection of APP-dependent transcriptional transactivation
    • X. Cao, and T.C. Sudhof Dissection of APP-dependent transcriptional transactivation J Biol Chem 279 2004 24601 24611
    • (2004) J Biol Chem , vol.279 , pp. 24601-24611
    • Cao, X.1    Sudhof, T.C.2
  • 20
    • 0035794182 scopus 로고    scopus 로고
    • The β-amyloid precursor protein functions as a cytosolic anchoring site that prevents Fe65 nuclear translocation
    • G. Minopoli, P. de Candia, A. Bonetti, R. Faraonio, N. Zambrano, and T. Russo The β-amyloid precursor protein functions as a cytosolic anchoring site that prevents Fe65 nuclear translocation J Biol Chem 276 2001 6545 6550
    • (2001) J Biol Chem , vol.276 , pp. 6545-6550
    • Minopoli, G.1    De Candia, P.2    Bonetti, A.3    Faraonio, R.4    Zambrano, N.5    Russo, T.6
  • 21
    • 0037067655 scopus 로고    scopus 로고
    • Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kappaB and β-amyloid precursor protein
    • S.H. Baek, K.A. Ohgi, D.W. Rose, E.H. Koo, C.K. Glass, and M.G. Rosenfeld Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kappaB and β-amyloid precursor protein Cell 110 2002 55 67
    • (2002) Cell , vol.110 , pp. 55-67
    • Baek, S.H.1    Ohgi, K.A.2    Rose, D.W.3    Koo, E.H.4    Glass, C.K.5    Rosenfeld, M.G.6
  • 22
    • 0042887148 scopus 로고    scopus 로고
    • Demonstration by FRET of BACE interaction with the amyloid precursor protein at the cell surface and in early endosomes
    • A. Kinoshita, H. Fukumoto, T. Shah, C.M. Whelan, M.C. Irizarry, and B.T. Hyman Demonstration by FRET of BACE interaction with the amyloid precursor protein at the cell surface and in early endosomes J Cell Sci 116 2003 3339 3346
    • (2003) J Cell Sci , vol.116 , pp. 3339-3346
    • Kinoshita, A.1    Fukumoto, H.2    Shah, T.3    Whelan, C.M.4    Irizarry, M.C.5    Hyman, B.T.6
  • 23
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid β-protein involves the endocytic pathway
    • E.H. Koo, and S.L. Squazzo Evidence that production and release of amyloid β-protein involves the endocytic pathway J Biol Chem 269 1994 17386 17389
    • (1994) J Biol Chem , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 24
    • 0345803941 scopus 로고    scopus 로고
    • Inhibition of receptor-mediated endocytosis demonstrates generation of amyloid β-protein at the cell surface
    • J.H. Chyung, and D.J. Selkoe Inhibition of receptor-mediated endocytosis demonstrates generation of amyloid β-protein at the cell surface J Biol Chem 278 2003 51035 51043
    • (2003) J Biol Chem , vol.278 , pp. 51035-51043
    • Chyung, J.H.1    Selkoe, D.J.2
  • 25
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts
    • R. Ehehalt, P. Keller, C. Haass, C. Thiele, and K. Simons Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts J Cell Biol 160 2003 113 123 This study suggests a role for lipid rafts in the β-secretase cleavage of APP.
    • (2003) J Cell Biol , vol.160 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 26
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • K. Simons, and E. Ikonen Functional rafts in cell membranes Nature 387 1997 569 572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 27
    • 0035928732 scopus 로고    scopus 로고
    • Compartmentalization of β-secretase (Asp2) into low-buoyant density, noncaveolar lipid rafts
    • D.R. Riddell, G. Christie, I. Hussain, and C. Dingwall Compartmentalization of β-secretase (Asp2) into low-buoyant density, noncaveolar lipid rafts Curr Biol 11 2001 1288 1293
    • (2001) Curr Biol , vol.11 , pp. 1288-1293
    • Riddell, D.R.1    Christie, G.2    Hussain, I.3    Dingwall, C.4
  • 28
    • 0141482022 scopus 로고    scopus 로고
    • Exclusively targeting β-secretase to lipid rafts by GPI-anchor addition up-regulates β-site processing of the amyloid precursor protein
    • J.M. Cordy, I. Hussain, C. Dingwall, N.M. Hooper, and A.J. Turner Exclusively targeting β-secretase to lipid rafts by GPI-anchor addition up-regulates β-site processing of the amyloid precursor protein Proc Natl Acad Sci USA 100 2003 11735 11740
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11735-11740
    • Cordy, J.M.1    Hussain, I.2    Dingwall, C.3    Hooper, N.M.4    Turner, A.J.5
  • 29
    • 0347318065 scopus 로고    scopus 로고
    • Cholesterol and the biology of Alzheimer's disease
    • B. Wolozin Cholesterol and the biology of Alzheimer's disease Neuron 41 2004 7 10
    • (2004) Neuron , vol.41 , pp. 7-10
    • Wolozin, B.1
  • 30
    • 0142059961 scopus 로고    scopus 로고
    • Heparan sulfate regulates amyloid precursor protein processing by BACE1, the Alzheimer's β-secretase
    • Z. Scholefield, E.A. Yates, G. Wayne, A. Amour, W. McDowell, and J.E. Turnbull Heparan sulfate regulates amyloid precursor protein processing by BACE1, the Alzheimer's β-secretase J Cell Biol 163 2003 97 107 This study provides good evidence for a role of proteoglycans in the regulation of β-secretase cleavage of APP.
    • (2003) J Cell Biol , vol.163 , pp. 97-107
    • Scholefield, Z.1    Yates, E.A.2    Wayne, G.3    Amour, A.4    McDowell, W.5    Turnbull, J.E.6
  • 31
    • 0038722283 scopus 로고    scopus 로고
    • The amyloid precursor protein and its regulatory protein, FE65, in growth cones and synapses in vitro and in vivo
    • S.L. Sabo, A.F. Ikin, J.D. Buxbaum, and P. Greengard The amyloid precursor protein and its regulatory protein, FE65, in growth cones and synapses in vitro and in vivo J Neurosci 23 2003 5407 5415
    • (2003) J Neurosci , vol.23 , pp. 5407-5415
    • Sabo, S.L.1    Ikin, A.F.2    Buxbaum, J.D.3    Greengard, P.4
  • 35
    • 0037431082 scopus 로고    scopus 로고
    • Aph-1, Pen-2, and nicastrin with presenilin generate an active γ-secretase complex
    • B. De Strooper Aph-1, Pen-2, and nicastrin with presenilin generate an active γ-secretase complex Neuron 38 2003 9 12
    • (2003) Neuron , vol.38 , pp. 9-12
    • De Strooper, B.1
  • 36
    • 11144355129 scopus 로고    scopus 로고
    • Chronic treatment with the γ-secretase inhibitor LY-411,575 inhibits β-amyloid peptide production and alters lymphopoiesis and intestinal cell differentiation
    • G.T. Wong, D. Manfra, F.M. Poulet, Q. Zhang, H. Josien, T. Bara, L. Engstrom, M. Pinzon-Ortiz, J.S. Fine, and H.J. Lee Chronic treatment with the γ-secretase inhibitor LY-411,575 inhibits β-amyloid peptide production and alters lymphopoiesis and intestinal cell differentiation J Biol Chem 279 2004 12876 12882
    • (2004) J Biol Chem , vol.279 , pp. 12876-12882
    • Wong, G.T.1    Manfra, D.2    Poulet, F.M.3    Zhang, Q.4    Josien, H.5    Bara, T.6    Engstrom, L.7    Pinzon-Ortiz, M.8    Fine, J.S.9    Lee, H.J.10
  • 37
    • 3242713169 scopus 로고    scopus 로고
    • Partial loss of presenilins causes seborrheic keratosis and autoimmune disease in mice
    • J. Tournoy, X. Bossuyt, A. Snellinx, M. Regent, M. Garmyn, L. Serneels, P. Saftig, K. Craessaerts, B. De Strooper, and D. Hartmann Partial loss of presenilins causes seborrheic keratosis and autoimmune disease in mice Hum Mol Genet 13 2004 1321 1331 The authors describe an autoimmune phenotype in transgenic mice with partial inactivation of γ-secretase activity, providing in vivo evidence for a role of presenilin in the control of the adult immune system.
    • (2004) Hum Mol Genet , vol.13 , pp. 1321-1331
    • Tournoy, J.1    Bossuyt, X.2    Snellinx, A.3    Regent, M.4    Garmyn, M.5    Serneels, L.6    Saftig, P.7    Craessaerts, K.8    De Strooper, B.9    Hartmann, D.10
  • 39
    • 0348111479 scopus 로고    scopus 로고
    • Notch1 competes with the amyloid precursor protein for γ-secretase and down-regulates presenilin-1 gene expression
    • A. Lleo, O. Berezovska, P. Ramdya, H. Fukumoto, S. Raju, T. Shah, and B.T. Hyman Notch1 competes with the amyloid precursor protein for γ-secretase and down-regulates presenilin-1 gene expression J Biol Chem 278 2003 47370 47375
    • (2003) J Biol Chem , vol.278 , pp. 47370-47375
    • Lleo, A.1    Berezovska, O.2    Ramdya, P.3    Fukumoto, H.4    Raju, S.5    Shah, T.6    Hyman, B.T.7
  • 40
    • 0037184062 scopus 로고    scopus 로고
    • Presenilin 1 mutations activate γ 42-secretase but reciprocally inhibit epsilon-secretase cleavage of amyloid precursor protein (APP) and S3-cleavage of notch
    • F. Chen, Y. Gu, H. Hasegawa, X. Ruan, S. Arawaka, P. Fraser, D. Westaway, H. Mount, and P. St George-Hyslop Presenilin 1 mutations activate γ 42-secretase but reciprocally inhibit epsilon-secretase cleavage of amyloid precursor protein (APP) and S3-cleavage of notch J Biol Chem 277 2002 36521 36526
    • (2002) J Biol Chem , vol.277 , pp. 36521-36526
    • Chen, F.1    Gu, Y.2    Hasegawa, H.3    Ruan, X.4    Arawaka, S.5    Fraser, P.6    Westaway, D.7    Mount, H.8    St George-Hyslop, P.9
  • 41
    • 0036290522 scopus 로고    scopus 로고
    • γ-Secretase-like cleavages of Notch and β APP are mutually exclusive in human cells
    • A. Petit, P. St George-Hyslop, P. Fraser, and F. Checler γ-Secretase-like cleavages of Notch and β APP are mutually exclusive in human cells Biochem Biophys Res Commun 290 2002 1408 1410
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 1408-1410
    • Petit, A.1    St George-Hyslop, P.2    Fraser, P.3    Checler, F.4
  • 44
    • 2442543552 scopus 로고    scopus 로고
    • Cell-type-specific processing of the amyloid precursor protein by Presenilin during Drosophila development
    • A. Loewer, P. Soba, K. Beyreuther, R. Paro, and G. Merdes Cell-type-specific processing of the amyloid precursor protein by Presenilin during Drosophila development EMBO Rep 5 2004 405 411 This study investigates the γ-secretase processing of APP and Notch in an in vivo setting and demonstrates that additional unknown but tissue-specific factors are involved in the regulation of the cleavage of these substrates.
    • (2004) EMBO Rep , vol.5 , pp. 405-411
    • Loewer, A.1    Soba, P.2    Beyreuther, K.3    Paro, R.4    Merdes, G.5
  • 46
    • 0036327098 scopus 로고    scopus 로고
    • Presenilin-1 affects trafficking and processing of βaPP and is targeted in a complex with nicastrin to the plasma membrane
    • C. Kaether, S. Lammich, D. Edbauer, M. Ertl, J. Rietdorf, A. Capell, H. Steiner, and C. Haass Presenilin-1 affects trafficking and processing of βAPP and is targeted in a complex with nicastrin to the plasma membrane J Cell Biol 158 2002 551 561
    • (2002) J Cell Biol , vol.158 , pp. 551-561
    • Kaether, C.1    Lammich, S.2    Edbauer, D.3    Ertl, M.4    Rietdorf, J.5    Capell, A.6    Steiner, H.7    Haass, C.8
  • 47
    • 0037659067 scopus 로고    scopus 로고
    • Nicastrin is required for assembly of presenilin/γ-secretase complexes to mediate Notch signaling and for processing and trafficking of β-amyloid precursor protein in mammals
    • T. Li, G. Ma, H. Cai, D.L. Price, and P.C. Wong Nicastrin is required for assembly of presenilin/γ-secretase complexes to mediate Notch signaling and for processing and trafficking of β-amyloid precursor protein in mammals J Neurosci 23 2003 3272 3277
    • (2003) J Neurosci , vol.23 , pp. 3272-3277
    • Li, T.1    Ma, G.2    Cai, H.3    Price, D.L.4    Wong, P.C.5
  • 49
  • 50
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils
    • J. Gotz, F. Chen, J. van Dorpe, and R.M. Nitsch Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils Science 293 2001 1491 1495
    • (2001) Science , vol.293 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    Van Dorpe, J.3    Nitsch, R.M.4
  • 52
    • 0042697305 scopus 로고    scopus 로고
    • Triple-transgenic model of Alzheimer's disease with plaques and tangles: Intracellular Aβ and synaptic dysfunction
    • S. Oddo, A. Caccamo, J.D. Shepherd, M.P. Murphy, T.E. Golde, R. Kayed, R. Metherate, M.P. Mattson, Y. Akbari, and F.M. LaFerla Triple-transgenic model of Alzheimer's disease with plaques and tangles: intracellular Aβ and synaptic dysfunction Neuron 39 2003 409 421 This study presents the most complete mouse model for AD available currently.
    • (2003) Neuron , vol.39 , pp. 409-421
    • Oddo, S.1    Caccamo, A.2    Shepherd, J.D.3    Murphy, M.P.4    Golde, T.E.5    Kayed, R.6    Metherate, R.7    Mattson, M.P.8    Akbari, Y.9    Laferla, F.M.10
  • 54
    • 0346055155 scopus 로고    scopus 로고
    • BACE1 deficiency rescues memory deficits and cholinergic dysfunction in a mouse model of Alzheimer's disease
    • M. Ohno, E.A. Sametsky, L.H. Younkin, H. Oakley, S.G. Younkin, M. Citron, R. Vassar, and J.F. Disterhoft BACE1 deficiency rescues memory deficits and cholinergic dysfunction in a mouse model of Alzheimer's disease Neuron 41 2004 27 33 The authors provide good evidence that the amyloid-β peptide itself plays a major part in determining the pathological phenotype in a mouse model for AD.
    • (2004) Neuron , vol.41 , pp. 27-33
    • Ohno, M.1    Sametsky, E.A.2    Younkin, L.H.3    Oakley, H.4    Younkin, S.G.5    Citron, M.6    Vassar, R.7    Disterhoft, J.F.8
  • 55
    • 0035950225 scopus 로고    scopus 로고
    • Clearing the brain's amyloid cobwebs
    • D.J. Selkoe Clearing the brain's amyloid cobwebs Neuron 32 2001 177 180
    • (2001) Neuron , vol.32 , pp. 177-180
    • Selkoe, D.J.1
  • 57
    • 1642290835 scopus 로고    scopus 로고
    • Partial loss-of-function mutations in insulin-degrading enzyme that induce diabetes also impair degradation of amyloid β-protein
    • W. Farris, S. Mansourian, M.A. Leissring, E.A. Eckman, L. Bertram, C.B. Eckman, R.E. Tanzi, and D.J. Selkoe Partial loss-of-function mutations in insulin-degrading enzyme that induce diabetes also impair degradation of amyloid β-protein Am J Pathol 164 2004 1425 1434
    • (2004) Am J Pathol , vol.164 , pp. 1425-1434
    • Farris, W.1    Mansourian, S.2    Leissring, M.A.3    Eckman, E.A.4    Bertram, L.5    Eckman, C.B.6    Tanzi, R.E.7    Selkoe, D.J.8
  • 58
    • 0346101885 scopus 로고    scopus 로고
    • Enhanced proteolysis of β-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death
    • M.A. Leissring, W. Farris, A.Y. Chang, D.M. Walsh, X. Wu, X. Sun, M.P. Frosch, and D.J. Selkoe Enhanced proteolysis of β-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death Neuron 40 2003 1087 1093 This study provides in vivo evidence that neprilysin and insulin-degrading enzyme can contribute to amyloid-β peptide turnover in the brain.
    • (2003) Neuron , vol.40 , pp. 1087-1093
    • Leissring, M.A.1    Farris, W.2    Chang, A.Y.3    Walsh, D.M.4    Wu, X.5    Sun, X.6    Frosch, M.P.7    Selkoe, D.J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.