메뉴 건너뛰기




Volumn 5, Issue 3, 2010, Pages

γ-Secretase dependent production of intracellular domains is reduced in adult compared to embryonic rat brain membranes

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; CADHERIN; EPHRIN B1; NERVE GROWTH FACTOR RECEPTOR; SECRETASE; TNFRSF16 PROTEIN, RAT;

EID: 78650887258     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0009772     Document Type: Article
Times cited : (12)

References (60)
  • 1
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297: 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 3
    • 44549087765 scopus 로고    scopus 로고
    • Soluble oligomers of the amyloid beta-protein impair synaptic plasticity and behavior
    • Selkoe DJ (2008) Soluble oligomers of the amyloid beta-protein impair synaptic plasticity and behavior. Behav Brain Res 192: 106-113.
    • (2008) Behav Brain Res , vol.192 , pp. 106-113
    • Selkoe, D.J.1
  • 4
    • 34248190279 scopus 로고    scopus 로고
    • A beta oligomers-a decade of discovery
    • Walsh DM, Selkoe DJ (2007) A beta oligomers-a decade of discovery. J Neurochem 101: 1172-1184.
    • (2007) J Neurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 5
    • 0033595706 scopus 로고    scopus 로고
    • Betasecretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • Vassar R, Bennett BD, Babu-Khan S, Kahn S, Mendiaz EA, et al. (1999) Betasecretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 286: 735-741.
    • (1999) Science , vol.286 , pp. 735-741
    • Vassar, R.1    Bennett, B.D.2    Babu-Khan, S.3    Kahn, S.4    Mendiaz, E.A.5
  • 7
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe DJ (2001) Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 81: 741-766.
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 8
    • 0037176727 scopus 로고    scopus 로고
    • A novel epsilon-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing
    • Weidemann A, Eggert S, Reinhard FB, Vogel M, Paliga K, et al. (2002) A novel epsilon-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing. Biochemistry 41: 2825-2835.
    • (2002) Biochemistry , vol.41 , pp. 2825-2835
    • Weidemann, A.1    Eggert, S.2    Reinhard, F.B.3    Vogel, M.4    Paliga, K.5
  • 9
    • 0034774969 scopus 로고    scopus 로고
    • Presenilindependent gamma-secretase processing of beta-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch
    • Sastre M, Steiner H, Fuchs K, Capell A, Multhaup G, et al. (2001) Presenilindependent gamma-secretase processing of beta-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch. EMBO Rep 2: 835-841.
    • (2001) EMBO Rep , vol.2 , pp. 835-841
    • Sastre, M.1    Steiner, H.2    Fuchs, K.3    Capell, A.4    Multhaup, G.5
  • 10
    • 0038652102 scopus 로고    scopus 로고
    • Gamma-secretase is a membrane protein complex comprised of presenilin, nicastrin, Aph-1, and Pen-2
    • Kimberly WT, LaVoie MJ, Ostaszewski BL, Ye W, Wolfe MS, et al. (2003) Gamma-secretase is a membrane protein complex comprised of presenilin, nicastrin, Aph-1, and Pen-2. Proc Natl Acad Sci U S A 100: 6382-6387.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 6382-6387
    • Kimberly, W.T.1    LaVoie, M.J.2    Ostaszewski, B.L.3    Ye, W.4    Wolfe, M.S.5
  • 12
    • 36349024875 scopus 로고    scopus 로고
    • Active gamma-secretase complexes contain only one of each component
    • Sato T, Diehl TS, Narayanan S, Funamoto S, Ihara Y, et al. (2007) Active gamma-secretase complexes contain only one of each component. J Biol Chem 282: 33985-33993.
    • (2007) J Biol Chem , vol.282 , pp. 33985-33993
    • Sato, T.1    Diehl, T.S.2    Narayanan, S.3    Funamoto, S.4    Ihara, Y.5
  • 13
    • 15844425969 scopus 로고    scopus 로고
    • Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo
    • Thinakaran G, Borchelt DR, Lee MK, Slunt HH, Spitzer L, et al. (1996) Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo. Neuron 17: 181-190.
    • (1996) Neuron , vol.17 , pp. 181-190
    • Thinakaran, G.1    Borchelt, D.R.2    Lee, M.K.3    Slunt, H.H.4    Spitzer, L.5
  • 14
    • 5144224126 scopus 로고    scopus 로고
    • Coordinated and widespread expression of gamma-secretase in vivo: Evidence for size and molecular heterogeneity
    • Hebert SS, Serneels L, Dejaegere T, Horre K, Dabrowski M, et al. (2004) Coordinated and widespread expression of gamma-secretase in vivo: evidence for size and molecular heterogeneity. Neurobiol Dis 17: 260-272.
    • (2004) Neurobiol Dis , vol.17 , pp. 260-272
    • Hebert, S.S.1    Serneels, L.2    Dejaegere, T.3    Horre, K.4    Dabrowski, M.5
  • 15
    • 0033553564 scopus 로고    scopus 로고
    • Evidence that intramolecular associations between presenilin domains are obligatory for endoproteolytic processing
    • Saura CA, Tomita T, Davenport F, Harris CL, Iwatsubo T, et al. (1999) Evidence that intramolecular associations between presenilin domains are obligatory for endoproteolytic processing. J Biol Chem 274: 13818-13823.
    • (1999) J Biol Chem , vol.274 , pp. 13818-13823
    • Saura, C.A.1    Tomita, T.2    Davenport, F.3    Harris, C.L.4    Iwatsubo, T.5
  • 16
  • 17
    • 4744375540 scopus 로고    scopus 로고
    • Identification of distinct gamma-secretase complexes with different APH-1 variants
    • Shirotani K, Edbauer D, Prokop S, Haass C, Steiner H (2004) Identification of distinct gamma-secretase complexes with different APH-1 variants. J Biol Chem 279: 41340-41345.
    • (2004) J Biol Chem , vol.279 , pp. 41340-41345
    • Shirotani, K.1    Edbauer, D.2    Prokop, S.3    Haass, C.4    Steiner, H.5
  • 18
    • 43049163813 scopus 로고    scopus 로고
    • Substrate specificity of gamma-secretase and other intramembrane proteases
    • Beel AJ, Sanders CR (2008) Substrate specificity of gamma-secretase and other intramembrane proteases. Cell Mol Life Sci 65: 1311-1334.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1311-1334
    • Beel, A.J.1    Sanders, C.R.2
  • 19
    • 64249172203 scopus 로고    scopus 로고
    • The canonical Notch signaling pathway: Unfolding the activation mechanism
    • Kopan R, Ilagan MX (2009) The canonical Notch signaling pathway: unfolding the activation mechanism. Cell 137: 216-233.
    • (2009) Cell , vol.137 , pp. 216-233
    • Kopan, R.1    Ilagan, M.X.2
  • 20
    • 0032524325 scopus 로고    scopus 로고
    • Nuclear access and action of notch in vivo
    • Struhl G, Adachi A (1998) Nuclear access and action of notch in vivo. Cell 93: 649-660.
    • (1998) Cell , vol.93 , pp. 649-660
    • Struhl, G.1    Adachi, A.2
  • 21
    • 0033535504 scopus 로고    scopus 로고
    • A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain
    • De Strooper B, Annaert W, Cupers P, Saftig P, Craessaerts K, et al. (1999) A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain. Nature 398: 518-522.
    • (1999) Nature , vol.398 , pp. 518-522
    • de Strooper, B.1    Annaert, W.2    Cupers, P.3    Saftig, P.4    Craessaerts, K.5
  • 22
    • 0032574993 scopus 로고    scopus 로고
    • Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain
    • Schroeter EH, Kisslinger JA, Kopan R (1998) Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain. Nature 393: 382-386.
    • (1998) Nature , vol.393 , pp. 382-386
    • Schroeter, E.H.1    Kisslinger, J.A.2    Kopan, R.3
  • 23
    • 33747623018 scopus 로고    scopus 로고
    • Notch signalling: A simple pathway becomes complex
    • Bray SJ (2006) Notch signalling: a simple pathway becomes complex. Nat Rev Mol Cell Biol 7: 678-689.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 678-689
    • Bray, S.J.1
  • 24
    • 56749163716 scopus 로고    scopus 로고
    • Notch: From neural development to neurological disorders
    • Lathia JD, Mattson MP, Cheng A (2008) Notch: from neural development to neurological disorders. J Neurochem 107: 1471-1481.
    • (2008) J Neurochem , vol.107 , pp. 1471-1481
    • Lathia, J.D.1    Mattson, M.P.2    Cheng, A.3
  • 26
    • 0034702303 scopus 로고    scopus 로고
    • Embryonic lethality in mice homozygous for a processing-deficient allele of Notch1
    • Huppert SS, Le A, Schroeter EH, Mumm JS, Saxena MT, et al. (2000) Embryonic lethality in mice homozygous for a processing-deficient allele of Notch1. Nature 405: 966-970.
    • (2000) Nature , vol.405 , pp. 966-970
    • Huppert, S.S.1    Le, A.2    Schroeter, E.H.3    Mumm, J.S.4    Saxena, M.T.5
  • 27
    • 0142242199 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis of the p75 neurotrophin receptor modulates its association with the TrkA receptor
    • Jung KM, Tan S, Landman N, Petrova K, Murray S, et al. (2003) Regulated intramembrane proteolysis of the p75 neurotrophin receptor modulates its association with the TrkA receptor. J Biol Chem 278: 42161-42169.
    • (2003) J Biol Chem , vol.278 , pp. 42161-42169
    • Jung, K.M.1    Tan, S.2    Landman, N.3    Petrova, K.4    Murray, S.5
  • 28
    • 0038045714 scopus 로고    scopus 로고
    • Proteolytic processing of the p75 neurotrophin receptor and two homologs generates C-terminal fragments with signaling capability
    • Kanning KC, Hudson M, Amieux PS, Wiley JC, Bothwell M, et al. (2003) Proteolytic processing of the p75 neurotrophin receptor and two homologs generates C-terminal fragments with signaling capability. J Neurosci 23: 5425-5436.
    • (2003) J Neurosci , vol.23 , pp. 5425-5436
    • Kanning, K.C.1    Hudson, M.2    Amieux, P.S.3    Wiley, J.C.4    Bothwell, M.5
  • 29
    • 0141429160 scopus 로고    scopus 로고
    • A CBP binding transcriptional repressor produced by the PS1/epsilon-cleavage of Ncadherin is inhibited by PS1 FAD mutations
    • Marambaud P, Wen PH, Dutt A, Shioi J, Takashima A, et al. (2003) A CBP binding transcriptional repressor produced by the PS1/epsilon-cleavage of Ncadherin is inhibited by PS1 FAD mutations. Cell 114: 635-645.
    • (2003) Cell , vol.114 , pp. 635-645
    • Marambaud, P.1    Wen, P.H.2    Dutt, A.3    Shioi, J.4    Takashima, A.5
  • 30
    • 33645277094 scopus 로고    scopus 로고
    • Metalloproteinase/Presenilin1 processing of ephrinB regulates EphB-induced Src phosphorylation and signaling
    • Georgakopoulos A, Litterst C, Ghersi E, Baki L, Xu C, et al. (2006) Metalloproteinase/Presenilin1 processing of ephrinB regulates EphB-induced Src phosphorylation and signaling. Embo J 25: 1242-1252.
    • (2006) Embo J , vol.25 , pp. 1242-1252
    • Georgakopoulos, A.1    Litterst, C.2    Ghersi, E.3    Baki, L.4    Xu, C.5
  • 32
    • 33847021476 scopus 로고    scopus 로고
    • Presenilin diversifies its portfolio
    • Parks AL, Curtis D (2007) Presenilin diversifies its portfolio. Trends Genet 23: 140-150.
    • (2007) Trends Genet , vol.23 , pp. 140-150
    • Parks, A.L.1    Curtis, D.2
  • 33
    • 33745632662 scopus 로고    scopus 로고
    • Presenilin-dependent gamma-secretase-mediated control of p53-associated cell death in Alzheimer's disease
    • Alves da Costa C, Sunyach C, Pardossi-Piquard R, Sevalle J, Vincent B, et al. (2006) Presenilin-dependent gamma-secretase-mediated control of p53-associated cell death in Alzheimer's disease. J Neurosci 26: 6377-6385.
    • (2006) J Neurosci , vol.26 , pp. 6377-6385
    • Alves da Costa, C.1    Sunyach, C.2    Pardossi-Piquard, R.3    Sevalle, J.4    Vincent, B.5
  • 34
    • 2942557122 scopus 로고    scopus 로고
    • Gamma-secretase: Proteasome of the membrane?
    • Kopan R, Ilagan MX (2004) Gamma-secretase: proteasome of the membrane? Nat Rev Mol Cell Biol 5: 499-504.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 499-504
    • Kopan, R.1    Ilagan, M.X.2
  • 35
    • 0037590902 scopus 로고    scopus 로고
    • Presenilin-1 and presenilin-2 exhibit distinct yet overlapping gamma-secretase activities
    • Lai MT, Chen E, Crouthamel MC, DiMuzio-Mower J, Xu M, et al. (2003) Presenilin-1 and presenilin-2 exhibit distinct yet overlapping gamma-secretase activities. J Biol Chem 278: 22475-22481.
    • (2003) J Biol Chem , vol.278 , pp. 22475-22481
    • Lai, M.T.1    Chen, E.2    Crouthamel, M.C.3    DiMuzio-Mower, J.4    Xu, M.5
  • 36
    • 0032556859 scopus 로고    scopus 로고
    • Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
    • De Strooper B, Saftig P, Craessaerts K, Vanderstichele H, Guhde G, et al. (1998) Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature 391: 387-390.
    • (1998) Nature , vol.391 , pp. 387-390
    • de Strooper, B.1    Saftig, P.2    Craessaerts, K.3    Vanderstichele, H.4    Guhde, G.5
  • 37
    • 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
    • Herreman A, Hartmann D, Annaert W, Saftig P, Craessaerts K, et al. (1999) 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 U S A 96: 11872-11877.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 11872-11877
    • Herreman, A.1    Hartmann, D.2    Annaert, W.3    Saftig, P.4    Craessaerts, K.5
  • 38
    • 0030779784 scopus 로고    scopus 로고
    • Skeletal and CNS defects in Presenilin-1-deficient mice
    • Shen J, Bronson RT, Chen DF, Xia W, Selkoe DJ, et al. (1997) Skeletal and CNS defects in Presenilin-1-deficient mice. Cell 89: 629-639.
    • (1997) Cell , vol.89 , pp. 629-639
    • Shen, J.1    Bronson, R.T.2    Chen, D.F.3    Xia, W.4    Selkoe, D.J.5
  • 39
    • 12144250683 scopus 로고    scopus 로고
    • APH-1a is the principal mammalian APH-1 isoform present in gamma-secretase complexes during embryonic development
    • Ma G, Li T, Price DL, Wong PC (2005) APH-1a is the principal mammalian APH-1 isoform present in gamma-secretase complexes during embryonic development. J Neurosci 25: 192-198.
    • (2005) J Neurosci , vol.25 , pp. 192-198
    • Ma, G.1    Li, T.2    Price, D.L.3    Wong, P.C.4
  • 40
    • 47749095968 scopus 로고    scopus 로고
    • Deficiency of Aph1B/C-gamma-secretase disturbs Nrg1 cleavage and sensorimotor gating that can be reversed with antipsychotic treatment
    • Dejaegere T, Serneels L, Schafer MK, Van Biervliet J, Horre K, et al. (2008) Deficiency of Aph1B/C-gamma-secretase disturbs Nrg1 cleavage and sensorimotor gating that can be reversed with antipsychotic treatment. Proc Natl Acad Sci U S A 105: 9775-9780.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 9775-9780
    • Dejaegere, T.1    Serneels, L.2    Schafer, M.K.3    van Biervliet, J.4    Horre, K.5
  • 41
    • 1642585717 scopus 로고    scopus 로고
    • Binding sites of gamma-secretase inhibitors in rodent brain: Distribution, postnatal development, and effect of deafferentation
    • Yan XX, Li T, Rominger CM, Prakash SR, Wong PC, et al. (2004) Binding sites of gamma-secretase inhibitors in rodent brain: distribution, postnatal development, and effect of deafferentation. J Neurosci 24: 2942-2952.
    • (2004) J Neurosci , vol.24 , pp. 2942-2952
    • Yan, X.X.1    Li, T.2    Rominger, C.M.3    Prakash, S.R.4    Wong, P.C.5
  • 42
    • 21844448354 scopus 로고    scopus 로고
    • Spatial segregation of gamma-secretase and substrates in distinct membrane domains
    • Vetrivel KS, Cheng H, Kim SH, Chen Y, Barnes NY, et al. (2005) Spatial segregation of gamma-secretase and substrates in distinct membrane domains. J Biol Chem 280: 25892-25900.
    • (2005) J Biol Chem , vol.280 , pp. 25892-25900
    • Vetrivel, K.S.1    Cheng, H.2    Kim, S.H.3    Chen, Y.4    Barnes, N.Y.5
  • 43
    • 40349102241 scopus 로고    scopus 로고
    • Active gamma-secretase is localized to detergent-resistant membranes in human brain
    • Hur JY, Welander H, Behbahani H, Aoki M, Franberg J, et al. (2008) Active gamma-secretase is localized to detergent-resistant membranes in human brain. Febs J 275: 1174-1187.
    • (2008) Febs J , vol.275 , pp. 1174-1187
    • Hur, J.Y.1    Welander, H.2    Behbahani, H.3    Aoki, M.4    Franberg, J.5
  • 44
    • 0036180950 scopus 로고    scopus 로고
    • Cholesteroldependent gamma-secretase activity in buoyant cholesterol-rich membrane microdomains
    • Wahrle S, Das P, Nyborg AC, McLendon C, Shoji M, et al. (2002) Cholesteroldependent gamma-secretase activity in buoyant cholesterol-rich membrane microdomains. Neurobiol Dis 9: 11-23.
    • (2002) Neurobiol Dis , vol.9 , pp. 11-23
    • Wahrle, S.1    Das, P.2    Nyborg, A.C.3    McLendon, C.4    Shoji, M.5
  • 45
    • 0035808416 scopus 로고    scopus 로고
    • A novel gamma-secretase assay based on detection of the putative C-terminal fragmentgamma of amyloid beta protein precursor
    • Pinnix I, Musunuru U, Tun H, Sridharan A, Golde T, et al. (2001) A novel gamma-secretase assay based on detection of the putative C-terminal fragmentgamma of amyloid beta protein precursor. J Biol Chem 276: 481-487.
    • (2001) J Biol Chem , vol.276 , pp. 481-487
    • Pinnix, I.1    Musunuru, U.2    Tun, H.3    Sridharan, A.4    Golde, T.5
  • 46
    • 0037134505 scopus 로고    scopus 로고
    • Insulindegrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD)
    • Edbauer D, Willem M, Lammich S, Steiner H, Haass C (2002) Insulindegrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD). J Biol Chem 277: 13389-13393.
    • (2002) J Biol Chem , vol.277 , pp. 13389-13393
    • Edbauer, D.1    Willem, M.2    Lammich, S.3    Steiner, H.4    Haass, C.5
  • 47
    • 0034457993 scopus 로고    scopus 로고
    • Requirement for presenilin 1 in facilitating lagged 2-mediated endoproteolysis and signaling of notch 1
    • Martys-Zage JL, Kim SH, Berechid B, Bingham SJ, Chu S, et al. (2000) Requirement for presenilin 1 in facilitating lagged 2-mediated endoproteolysis and signaling of notch 1. J Mol Neurosci 15: 189-204.
    • (2000) J Mol Neurosci , vol.15 , pp. 189-204
    • Martys-Zage, J.L.1    Kim, S.H.2    Berechid, B.3    Bingham, S.J.4    Chu, S.5
  • 49
    • 0028641294 scopus 로고
    • Reciprocal changes in expression of the receptor lin-12 and its ligand lag-2 prior to commitment in a C. elegans cell fate decision
    • Wilkinson HA, Fitzgerald K, Greenwald I (1994) Reciprocal changes in expression of the receptor lin-12 and its ligand lag-2 prior to commitment in a C. elegans cell fate decision. Cell 79: 1187-1198.
    • (1994) Cell , vol.79 , pp. 1187-1198
    • Wilkinson, H.A.1    Fitzgerald, K.2    Greenwald, I.3
  • 50
    • 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
  • 51
    • 0034530036 scopus 로고    scopus 로고
    • Biochemical identification of the neutral endopeptidase family member responsible for the catabolism of amyloid beta peptide in the brain
    • Takaki Y, Iwata N, Tsubuki S, Taniguchi S, Toyoshima S, et al. (2000) Biochemical identification of the neutral endopeptidase family member responsible for the catabolism of amyloid beta peptide in the brain. J Biochem 128: 897-902.
    • (2000) J Biochem , vol.128 , pp. 897-902
    • Takaki, Y.1    Iwata, N.2    Tsubuki, S.3    Taniguchi, S.4    Toyoshima, S.5
  • 52
    • 77749319891 scopus 로고    scopus 로고
    • Affinity pulldown of gamma-secretase and associated proteins from human and rat brain
    • Epub ahead of print
    • Teranishi Y, Hur JY, Welander H, Franberg J, Aoki M, et al. (2009) Affinity pulldown of gamma-secretase and associated proteins from human and rat brain. J Cell Mol Med. Epub ahead of print.
    • (2009) J Cell Mol Med.
    • Teranishi, Y.1    Hur, J.Y.2    Welander, H.3    Franberg, J.4    Aoki, M.5
  • 53
    • 34250831492 scopus 로고    scopus 로고
    • Rat brain gamma-secretase activity is highly influenced by detergents
    • Franberg J, Welander H, Aoki M, Winblad B, Tjernberg LO, et al. (2007) Rat brain gamma-secretase activity is highly influenced by detergents. Biochemistry 46: 7647-7654.
    • (2007) Biochemistry , vol.46 , pp. 7647-7654
    • Franberg, J.1    Welander, H.2    Aoki, M.3    Winblad, B.4    Tjernberg, L.O.5
  • 54
    • 33645013015 scopus 로고    scopus 로고
    • Effects of a gamma-secretase inhibitor in a randomized study of patients with Alzheimer disease
    • Siemers ER, Quinn JF, Kaye J, Farlow MR, Porsteinsson A, et al. (2006) Effects of a gamma-secretase inhibitor in a randomized study of patients with Alzheimer disease. Neurology 66: 602-604.
    • (2006) Neurology , vol.66 , pp. 602-604
    • Siemers, E.R.1    Quinn, J.F.2    Kaye, J.3    Farlow, M.R.4    Porsteinsson, A.5
  • 55
    • 0242412482 scopus 로고    scopus 로고
    • Adipsin, a biomarker of gastrointestinal toxicity mediated by a functional gamma-secretase inhibitor
    • Searfoss GH, Jordan WH, Calligaro DO, Galbreath EJ, Schirtzinger LM, et al. (2003) Adipsin, a biomarker of gastrointestinal toxicity mediated by a functional gamma-secretase inhibitor. J Biol Chem 278: 46107-46116.
    • (2003) J Biol Chem , vol.278 , pp. 46107-46116
    • Searfoss, G.H.1    Jordan, W.H.2    Calligaro, D.O.3    Galbreath, E.J.4    Schirtzinger, L.M.5
  • 56
    • 11144355129 scopus 로고    scopus 로고
    • Chronic treatment with the gamma-secretase inhibitor LY-411,575 inhibits beta-amyloid peptide production and alters lymphopoiesis and intestinal cell differentiation
    • Wong GT, Manfra D, Poulet FM, Zhang Q, Josien H, et al. (2004) Chronic treatment with the gamma-secretase inhibitor LY-411,575 inhibits beta-amyloid peptide production and alters lymphopoiesis and intestinal cell differentiation. J Biol Chem 279: 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
  • 58
    • 59149088690 scopus 로고    scopus 로고
    • Pen2 and presenilin-1 modulate the dynamic equilibrium of presenilin-1 and presenilin-2 gamma-secretase complexes
    • Placanica L, Tarassishin L, Yang G, Peethumnongsin E, Kim SH, et al. (2009) Pen2 and presenilin-1 modulate the dynamic equilibrium of presenilin-1 and presenilin-2 gamma-secretase complexes. J Biol Chem 284: 2967-2977.
    • (2009) J Biol Chem , vol.284 , pp. 2967-2977
    • Placanica, L.1    Tarassishin, L.2    Yang, G.3    Peethumnongsin, E.4    Kim, S.H.5
  • 59
    • 64549113016 scopus 로고    scopus 로고
    • Gender-and age-dependent gamma-secretase activity in mouse brain and its implication in sporadic Alzheimer disease
    • Placanica L, Zhu L, Li YM (2009) Gender-and age-dependent gamma-secretase activity in mouse brain and its implication in sporadic Alzheimer disease. PLoS One 4: e5088.
    • (2009) PLoS One , vol.4
    • Placanica, L.1    Zhu, L.2    Li, Y.M.3
  • 60
    • 0032728957 scopus 로고    scopus 로고
    • Mice lacking both presenilin genes exhibit early embryonic patterning defects
    • Donoviel DB, Hadjantonakis AK, Ikeda M, Zheng H, Hyslop PS, et al. (1999) Mice lacking both presenilin genes exhibit early embryonic patterning defects. Genes Dev 13: 2801-2810.
    • (1999) Genes Dev , vol.13 , pp. 2801-2810
    • Donoviel, D.B.1    Hadjantonakis, A.K.2    Ikeda, M.3    Zheng, H.4    Hyslop, P.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.