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Volumn 27, Issue 1, 2006, Pages 88-97

Transient abundance of presenilin 1 fragments/nicastrin complex associated with synaptogenesis during development in rat cerebellum

Author keywords

Secretase; Alzheimer's disease; Nicastrin; Presenilins; Purkinje; Synapse

Indexed keywords

NICASTRIN; PRESENILIN 1;

EID: 27744481740     PISSN: 01974580     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neurobiolaging.2004.12.011     Document Type: Article
Times cited : (15)

References (61)
  • 1
    • 0026686751 scopus 로고
    • Biotin amplification of biotin and horseradish peroxidase signals in histochemical stains
    • J.C. Adams Biotin amplification of biotin and horseradish peroxidase signals in histochemical stains J Histochem Cytochem 40 1992 1457 1463
    • (1992) J Histochem Cytochem , vol.40 , pp. 1457-1463
    • Adams, J.C.1
  • 2
    • 0003799113 scopus 로고    scopus 로고
    • In: Relation to its evolution, structure, and functions
    • CRC Press Boca Raton
    • J. Altman, and S.A. Bayer In: relation to its evolution, structure, and functions Development of the Cerebellar System 1997 CRC Press Boca Raton
    • (1997) Development of the Cerebellar System
    • Altman, J.1    Bayer, S.A.2
  • 3
    • 0037385034 scopus 로고    scopus 로고
    • Increased expression of neuronal apolipoprotein e in human brain with cerebral infarction
    • K. Aoki, T. Uchihara, and N. Sanjo Increased expression of neuronal apolipoprotein E in human brain with cerebral infarction Stroke 34 2003 875 880
    • (2003) Stroke , vol.34 , pp. 875-880
    • Aoki, K.1    Uchihara, T.2    Sanjo, N.3
  • 4
    • 18744371544 scopus 로고    scopus 로고
    • The levels of mature glycosylated nicastrin are regulated and correlate with g-secretase processing of amyloid β-precursor protein
    • S. Arawaka, H. Hasegawa, and A. Tandon The levels of mature glycosylated nicastrin are regulated and correlate with g-secretase processing of amyloid β-precursor protein J Neurochem 83 2002 1065 1071
    • (2002) J Neurochem , vol.83 , pp. 1065-1071
    • Arawaka, S.1    Hasegawa, H.2    Tandon, A.3
  • 5
    • 0033026550 scopus 로고    scopus 로고
    • Proteolytic fragments of Alzheimer's disease-associated presenilin 1 are present in synaptic organelles and growth cone membranes of rat brain
    • D. Beher, C. Elle, and J. Underwood Proteolytic fragments of Alzheimer's disease-associated presenilin 1 are present in synaptic organelles and growth cone membranes of rat brain J Neurochem 72 1999 1564 1573
    • (1999) J Neurochem , vol.72 , pp. 1564-1573
    • Beher, D.1    Elle, C.2    Underwood, J.3
  • 7
    • 0037068824 scopus 로고    scopus 로고
    • Spine motility: Phenomenology, mechanisms, and function
    • T. Bonhoeffer, and R. Yuste Spine motility: phenomenology, mechanisms, and function Neuron 35 2002 1019 1027
    • (2002) Neuron , vol.35 , pp. 1019-1027
    • Bonhoeffer, T.1    Yuste, R.2
  • 8
    • 0030293676 scopus 로고    scopus 로고
    • Familial Alzheimer's disease-linked presenilin 1 variants elevate Aβ1-42/1-40 ratio in vitro and in vivo
    • D.R. Borchelt, G. Thinakaran, and C.B. Eckman Familial Alzheimer's disease-linked presenilin 1 variants elevate Aβ1-42/1-40 ratio in vitro and in vivo Neuron 17 1996 1005 1013
    • (1996) Neuron , vol.17 , pp. 1005-1013
    • Borchelt, D.R.1    Thinakaran, G.2    Eckman, C.B.3
  • 9
    • 0034663023 scopus 로고    scopus 로고
    • A novel SNAP25-caveolin complex correlates with the onset of persistent synaptic potentiation
    • J.E.A. Braun, and D.V. Madison A novel SNAP25-caveolin complex correlates with the onset of persistent synaptic potentiation J Neurosci 20 2000 5997 6006
    • (2000) J Neurosci , vol.20 , pp. 5997-6006
    • Braun, J.E.A.1    Madison, D.V.2
  • 10
    • 0030657665 scopus 로고    scopus 로고
    • Cellular expression and proteolytic processing of presenilin proteins is developmentally regulated during neuronal differentiation
    • A. Capell, R. Saffrich, and J.C. Olivo Cellular expression and proteolytic processing of presenilin proteins is developmentally regulated during neuronal differentiation J Neurochem 69 1997 2432 2440
    • (1997) J Neurochem , vol.69 , pp. 2432-2440
    • Capell, A.1    Saffrich, R.2    Olivo, J.C.3
  • 11
    • 16944362157 scopus 로고    scopus 로고
    • Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice
    • M. Citron, D. Westaway, and W. Xia Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice Nat Med 3 1997 67 72
    • (1997) Nat Med , vol.3 , pp. 67-72
    • Citron, M.1    Westaway, D.2    Xia, W.3
  • 12
    • 0033990169 scopus 로고    scopus 로고
    • Alzheimer's disease: Biological functions and pathogenic mechanisms
    • C. Czech, G. Tremp, L. Pradier, and Presenilins Alzheimer's disease: biological functions and pathogenic mechanisms Prog Neurobiol 60 2000 363 384
    • (2000) Prog Neurobiol , vol.60 , pp. 363-384
    • Czech, C.1    Tremp, G.2    Pradier, L.3    Presenilins4
  • 13
    • 0037431082 scopus 로고    scopus 로고
    • Aph-1, pen-2, and nicastrin with presenilin gnerate an active γ-secretase complex
    • B. De Strooper Aph-1, pen-2, and nicastrin with presenilin gnerate an active γ-secretase complex Neuron 38 2003 9 12
    • (2003) Neuron , vol.38 , pp. 9-12
    • De Strooper, B.1
  • 14
    • 0032728957 scopus 로고    scopus 로고
    • Mice lacking both presenilin genes exhibit early embryonic patterning defects
    • D.B. Donoviel, A.K. Hadjantonakis, and M. Ikeda Mice lacking both presenilin genes exhibit early embryonic patterning defects Genes Dev 13 1999 2801 2810
    • (1999) Genes Dev , vol.13 , pp. 2801-2810
    • Donoviel, D.B.1    Hadjantonakis, A.K.2    Ikeda, M.3
  • 15
    • 16044366039 scopus 로고    scopus 로고
    • Increased amyloid-β42(43) in brains of mice expressing mutant presenilin 1
    • K. Duff, C. Eckman, and C. Zehr Increased amyloid-β42(43) in brains of mice expressing mutant presenilin 1 Nature 383 1996 710 713
    • (1996) Nature , vol.383 , pp. 710-713
    • Duff, K.1    Eckman, C.2    Zehr, C.3
  • 16
    • 0037363099 scopus 로고    scopus 로고
    • Spine motility: A means towards an end?
    • A. Dunaevsky, and C.A. Mason Spine motility: a means towards an end? Trends Neurosci 26 2003 155 160
    • (2003) Trends Neurosci , vol.26 , pp. 155-160
    • Dunaevsky, A.1    Mason, C.A.2
  • 17
    • 0031795935 scopus 로고    scopus 로고
    • Enrichment of presenilin 1 peptides in neuronal large dense-core and somatodendritic clathrin-coated vesicles
    • S. Efthimiopoulos, E. Floor, and A. Georgakopoulos Enrichment of presenilin 1 peptides in neuronal large dense-core and somatodendritic clathrin-coated vesicles J Neurochem 1998 1998 2365 2371
    • (1998) J Neurochem , vol.1998 , pp. 2365-2371
    • Efthimiopoulos, S.1    Floor, E.2    Georgakopoulos, A.3
  • 18
    • 10144234151 scopus 로고    scopus 로고
    • Identification and neuron specific expression of the S182/presenilin 1 protein in human and rodent brains
    • G.A. Elder, N. Tezapsidis, and J. Carter Identification and neuron specific expression of the S182/presenilin 1 protein in human and rodent brains J Neurosci Res 45 1996 308 320
    • (1996) J Neurosci Res , vol.45 , pp. 308-320
    • Elder, G.A.1    Tezapsidis, N.2    Carter, J.3
  • 19
    • 0033990845 scopus 로고    scopus 로고
    • Expressions of amyloid precursor protein, synaptophysin and presenilin 1 in the different areas of the developing cerebellum of rat
    • I. Fakla, I. Kovacs, H. Yamaguchi, C. Geula, and P. Kasa Expressions of amyloid precursor protein, synaptophysin and presenilin 1 in the different areas of the developing cerebellum of rat Neurochem Int 36 2000 143 151
    • (2000) Neurochem Int , vol.36 , pp. 143-151
    • Fakla, I.1    Kovacs, I.2    Yamaguchi, H.3    Geula, C.4    Kasa, P.5
  • 20
    • 0345826185 scopus 로고    scopus 로고
    • Phosphorylation of presenilin 1 at the caspase recognition site regulates its proteolytic processing and the progression of apoptosis
    • R. Fluhrer, A. Friedlein, C. Haass, and J. Walter Phosphorylation of presenilin 1 at the caspase recognition site regulates its proteolytic processing and the progression of apoptosis J Biol Chem 279 2003 1585 1593
    • (2003) J Biol Chem , vol.279 , pp. 1585-1593
    • Fluhrer, R.1    Friedlein, A.2    Haass, C.3    Walter, J.4
  • 21
    • 0034718209 scopus 로고    scopus 로고
    • Presenilin structure, function and role in Alzheimer disease
    • P.E. Fraser, D.-S. Yang, and G. Yu Presenilin structure, function and role in Alzheimer disease Biochim Biophys Acta 1502 2000 1 15
    • (2000) Biochim Biophys Acta , vol.1502 , pp. 1-15
    • Fraser, P.E.1    Yang, D.-S.2    Yu, G.3
  • 22
    • 0033401526 scopus 로고    scopus 로고
    • Presenilin 1 forms complexes with the cadherin/catenin cell-cell adhesion system and is recruited to intercellular and synaptic contacts
    • A. Georgakopoulos, P. Marambaud, and S. Efthimiopoulos Presenilin 1 forms complexes with the cadherin/catenin cell-cell adhesion system and is recruited to intercellular and synaptic contacts Mol Cell 4 1999 893 902
    • (1999) Mol Cell , vol.4 , pp. 893-902
    • Georgakopoulos, A.1    Marambaud, P.2    Efthimiopoulos, S.3
  • 23
    • 0031004532 scopus 로고    scopus 로고
    • Developmental regulation of presenilin 1 processing in the brain suggests a role in neuronal differentiation
    • H. Hartmann, J. Busciglio, K.H. Baumann, M. Staufenbiel, and B.A. Yankner Developmental regulation of presenilin 1 processing in the brain suggests a role in neuronal differentiation J Biol Chem 272 1997 14505 14508
    • (1997) J Biol Chem , vol.272 , pp. 14505-14508
    • Hartmann, H.1    Busciglio, J.2    Baumann, K.H.3    Staufenbiel, M.4    Yankner, B.A.5
  • 24
    • 0036327098 scopus 로고    scopus 로고
    • Presenilin 1 affects trafficking and processing of betaAPP and is targeted in a complex with nicastrin to the plasma membrane
    • C. Kaether, S. Lammich, and D. Edbauer Presenilin 1 affects trafficking and processing of betaAPP 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
  • 25
    • 0035818998 scopus 로고    scopus 로고
    • Kinesin-mediated axonal transport of a membrane compartment containing β-secretase and presenilin 1 requires APP
    • A. Kamal, A. Almenar-Queralt, J.F. LeBlanc, E.A. Roberts, and L.S.B. Goldstein Kinesin-mediated axonal transport of a membrane compartment containing β-secretase and presenilin 1 requires APP Nature 146 2001 643 648
    • (2001) Nature , vol.146 , pp. 643-648
    • Kamal, A.1    Almenar-Queralt, A.2    Leblanc, J.F.3    Roberts, E.A.4    Goldstein, L.S.B.5
  • 26
    • 0037354556 scopus 로고    scopus 로고
    • Expression of presenilin 1 and synapse-related proteins during postnatal development is not different between accelerated senescence-prone and -resistant mice
    • H. Keino, M. Kishikawa, M. Satoh, and A. Shimada Expression of presenilin 1 and synapse-related proteins during postnatal development is not different between accelerated senescence-prone and -resistant mice Neuropathology 23 2003 16 24
    • (2003) Neuropathology , vol.23 , pp. 16-24
    • Keino, H.1    Kishikawa, M.2    Satoh, M.3    Shimada, A.4
  • 27
    • 0035804769 scopus 로고    scopus 로고
    • Expression of presenilin 1 and notch-1 receptor in human embryonic CNS
    • B. Kostyszyn, R.F. Cowbum, A. Seiger, A.A. Kj, and E. Sundstrom Expression of presenilin 1 and notch-1 receptor in human embryonic CNS Neuroscience 103 2001 885 898
    • (2001) Neuroscience , vol.103 , pp. 885-898
    • Kostyszyn, B.1    Cowbum, R.F.2    Seiger, A.3    Kj, A.A.4    Sundstrom, E.5
  • 28
    • 0031017795 scopus 로고    scopus 로고
    • Light and electron microscopic localization of presenilin 1 in primate brain
    • J.J. Lah, C.J. Meilman, and N.R. Nash Light and electron microscopic localization of presenilin 1 in primate brain J Neurosci 17 1997 1971 1980
    • (1997) J Neurosci , vol.17 , pp. 1971-1980
    • Lah, J.J.1    Meilman, C.J.2    Nash, N.R.3
  • 29
    • 10544229795 scopus 로고    scopus 로고
    • Expression of presenilin 1 and 2 (PS1 and PS2) in human and murine tissues
    • M.K. Lee, H.H. Slunt, and L.J. Martin Expression of presenilin 1 and 2 (PS1 and PS2) in human and murine tissues J Neurosci 16 1996 7513 7525
    • (1996) J Neurosci , vol.16 , pp. 7513-7525
    • Lee, M.K.1    Slunt, H.H.2    Martin, L.J.3
  • 30
    • 16044365171 scopus 로고    scopus 로고
    • The E280A presenilin 1 Alzheimer mutation produces increased Aβ42 deposition and severe cerebellar pathology
    • C.A. Lemere, F. Lopera, and K.S. Kosik The E280A presenilin 1 Alzheimer mutation produces increased Aβ42 deposition and severe cerebellar pathology Nat Med 2 1996 1146 1150
    • (1996) Nat Med , vol.2 , pp. 1146-1150
    • Lemere, C.A.1    Lopera, F.2    Kosik, K.S.3
  • 31
    • 0040510921 scopus 로고    scopus 로고
    • Developmental expression of wild- type and mutant presenilin 1 in hippocampal neurons from transgenic mice: Evidence for novel species-specific properties of human presenilin 1
    • L. Levesque, W. Annaert, and K. Craessaerts Developmental expression of wild- type and mutant presenilin 1 in hippocampal neurons from transgenic mice: evidence for novel species-specific properties of human presenilin 1 Mol Med 5 1999 542 544
    • (1999) Mol Med , vol.5 , pp. 542-544
    • Levesque, L.1    Annaert, W.2    Craessaerts, K.3
  • 32
    • 0041355299 scopus 로고    scopus 로고
    • Positive and negative regulation of the γ-secretase activity by nicastrin in a murine model
    • J. Li, G.J. Fici, and C.-A. Mao Positive and negative regulation of the γ-secretase activity by nicastrin in a murine model J Biol Chem 278 2003 33445 33449
    • (2003) J Biol Chem , vol.278 , pp. 33445-33449
    • Li, J.1    Fici, G.J.2    Mao, C.-A.3
  • 33
    • 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
  • 34
    • 0033538896 scopus 로고    scopus 로고
    • Expression of presenilin 1 in nervous system during rat development
    • M.T. Moreno-Flores, M. Medina, and F. Wandosell Expression of presenilin 1 in nervous system during rat development J Comp Neural 410 1999 556 570
    • (1999) J Comp Neural , vol.410 , pp. 556-570
    • Moreno-Flores, M.T.1    Medina, M.2    Wandosell, F.3
  • 35
    • 1542513309 scopus 로고    scopus 로고
    • Dual enhancement of triple immunofluorescence using two antibodies from the same species
    • A. Nakamura, and T. Uchihara Dual enhancement of triple immunofluorescence using two antibodies from the same species J Neurosci Methods 135 2004 67 70
    • (2004) J Neurosci Methods , vol.135 , pp. 67-70
    • Nakamura, A.1    Uchihara, T.2
  • 36
    • 0033579505 scopus 로고    scopus 로고
    • Cell surface presenilin 1 participates in the gamma-secretase-like proteolysis of notch
    • W.J. Ray, M. Yao, and J. Mumm Cell surface presenilin 1 participates in the gamma-secretase-like proteolysis of notch J Biol Chem 274 1999 36801 36807
    • (1999) J Biol Chem , vol.274 , pp. 36801-36807
    • Ray, W.J.1    Yao, M.2    Mumm, J.3
  • 37
    • 0141957935 scopus 로고    scopus 로고
    • Alzheimer's disease proteins in cerebellar and hippocampal synapses during postnatal development and aging of the rat
    • C. Ribaut-Barassin, J.L. Dupont, and A.M. Haeberle Alzheimer's disease proteins in cerebellar and hippocampal synapses during postnatal development and aging of the rat Neuroscience 120 2003 405 423
    • (2003) Neuroscience , vol.120 , pp. 405-423
    • Ribaut-Barassin, C.1    Dupont, J.L.2    Haeberle, A.M.3
  • 38
    • 11144354609 scopus 로고    scopus 로고
    • Loss of presenilin function causes impairments of memory and synaptic plasticity followed by age-dependent neurodegeneration
    • C.A. Saura, S.-Y. Choi, and V. Beglopoulos Loss of presenilin function causes impairments of memory and synaptic plasticity followed by age-dependent neurodegeneration Neuron 42 2004 23 36
    • (2004) Neuron , vol.42 , pp. 23-36
    • Saura, C.A.1    Choi, S.-Y.2    Beglopoulos, V.3
  • 39
    • 16044373524 scopus 로고    scopus 로고
    • Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations liked to familial Alzheimer's disease
    • D. Scheuner, C. Eckman, and M. Jensen Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations liked to familial Alzheimer's disease Nat Med 2 1996 864 870
    • (1996) Nat Med , vol.2 , pp. 864-870
    • Scheuner, D.1    Eckman, C.2    Jensen, M.3
  • 40
    • 12644290265 scopus 로고    scopus 로고
    • Evidence for phosphorylation and oligomeric assembly of presenilin 1
    • M. Seeger, C. Nordstedt, and S. Petanceska Evidence for phosphorylation and oligomeric assembly of presenilin 1 J Biol Chem 94 1997 5090 5094
    • (1997) J Biol Chem , vol.94 , pp. 5090-5094
    • Seeger, M.1    Nordstedt, C.2    Petanceska, S.3
  • 41
    • 0041355557 scopus 로고    scopus 로고
    • Notch and presenilin: Regulated intramembrane proteolysis links development and degeneration
    • D. Selkoe, and R. Kopan Notch and presenilin: regulated intramembrane proteolysis links development and degeneration Annu Rev Neurosci 26 2003 565 597
    • (2003) Annu Rev Neurosci , vol.26 , pp. 565-597
    • Selkoe, D.1    Kopan, R.2
  • 43
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
    • R. Sherrington, E.I. Rogaev, and Y. Liang Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease Nature 375 1995 754 760
    • (1995) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1    Rogaev, E.I.2    Liang, Y.3
  • 44
    • 0038607071 scopus 로고    scopus 로고
    • γ-secretase activity is associated with a conformational change of nicastrin
    • K. Shirotani, D. Edbauer, A. Capell, J. Schmitz, H. Steiner, and C. Haass γ-secretase activity is associated with a conformational change of nicastrin J Biol Chem 278 2003 16474 16477
    • (2003) J Biol Chem , vol.278 , pp. 16474-16477
    • Shirotani, K.1    Edbauer, D.2    Capell, A.3    Schmitz, J.4    Steiner, H.5    Haass, C.6
  • 45
    • 0036548070 scopus 로고    scopus 로고
    • γ-secretase, notch, Aβ and Alzheimer's disease: Where do the presenilins fit in?
    • S.S. Sisodia, and P.H. St. George-Hyslop γ-secretase, notch, Aβ and Alzheimer's disease: where do the presenilins fit in? Nat Rev Neurosci 3 2002 281 290
    • (2002) Nat Rev Neurosci , vol.3 , pp. 281-290
    • Sisodia, S.S.1    St. George-Hyslop, P.H.2
  • 46
    • 0033536072 scopus 로고    scopus 로고
    • Proteolytic release and nuclear translocation of notch-1 are induced by presenilin 1 and impaired by pathogenic presenilin 1 mutations
    • W. Song, P. Nadeau, M. Yuan, X. Yang, J. Shen, and B.A. Yankner Proteolytic release and nuclear translocation of notch-1 are induced by presenilin 1 and impaired by pathogenic presenilin 1 mutations Proc Natl Acad Sci USA 96 1999 6959 6963
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6959-6963
    • Song, W.1    Nadeau, P.2    Yuan, M.3    Yang, X.4    Shen, J.5    Yankner, B.A.6
  • 47
    • 0032125862 scopus 로고    scopus 로고
    • Differential regulation of exocytosis by calcium and CAPS in semi-intact synaptosomes
    • A. Tandon, S. Bannykh, J.A. Kowalchyk, A. Baneijee, T.F.J. Martin, and W.E. Balch Differential regulation of exocytosis by calcium and CAPS in semi-intact synaptosomes Neuron 21 1998 147 154
    • (1998) Neuron , vol.21 , pp. 147-154
    • Tandon, A.1    Bannykh, S.2    Kowalchyk, J.A.3    Baneijee, A.4    Martin, T.F.J.5    Balch, W.E.6
  • 48
  • 49
    • 15844425969 scopus 로고    scopus 로고
    • Endoproteolysis of presenilin 1 and accumulation fo processed derivatives in vivo
    • G. Thinakaran, D.R. Borchelt, and M.K. Lee Endoproteolysis of presenilin 1 and accumulation fo processed derivatives in vivo Neuron 17 1996 181 190
    • (1996) Neuron , vol.17 , pp. 181-190
    • Thinakaran, G.1    Borchelt, D.R.2    Lee, M.K.3
  • 50
    • 0029843172 scopus 로고    scopus 로고
    • Widespread immunoreactivity of presenilin in neurons of normal and Alzheimer disease brains: Double labelling immunohistochemical study
    • T. Uchihara, H.K. El Hachimi, and C. Duyckaerts Widespread immunoreactivity of presenilin in neurons of normal and Alzheimer disease brains: double labelling immunohistochemical study Acta Neuropathol 92 1996 325 330
    • (1996) Acta Neuropathol , vol.92 , pp. 325-330
    • Uchihara, T.1    El Hachimi, H.K.2    Duyckaerts, C.3
  • 51
    • 0034527417 scopus 로고    scopus 로고
    • Dual enhancement of double immunofluorescent signals by CARD: Participation of ubiquitin during formation of neurofibrillary tangles
    • T. Uchihara, A. Nakamura, U. Nagaoka, M. Yamazaki, and O. Mori Dual enhancement of double immunofluorescent signals by CARD: participation of ubiquitin during formation of neurofibrillary tangles Histochem Cell Biol 114 2000 447 451
    • (2000) Histochem Cell Biol , vol.114 , pp. 447-451
    • Uchihara, T.1    Nakamura, A.2    Nagaoka, U.3    Yamazaki, M.4    Mori, O.5
  • 52
    • 0041819808 scopus 로고    scopus 로고
    • Triple immunofluorolabeling with two rabbit polyclonal antibodies and a mouse monoclonal antibody allowing three-dimensional analysis of cotton wool plaques in Alzheimer disease
    • T. Uchihara, A. Nakamura, and H. Nakayama Triple immunofluorolabeling with two rabbit polyclonal antibodies and a mouse monoclonal antibody allowing three-dimensional analysis of cotton wool plaques in Alzheimer disease J Histochem Cytochem 51 2003 1201 1206
    • (2003) J Histochem Cytochem , vol.51 , pp. 1201-1206
    • Uchihara, T.1    Nakamura, A.2    Nakayama, H.3
  • 53
    • 12644264304 scopus 로고    scopus 로고
    • Proteolytic processing of the Alzheimer disease-associated presenilin 1 generates an in vivo substrate for protein kinase C
    • J. Walter, J. Grünberg, and A. Capell Proteolytic processing of the Alzheimer disease-associated presenilin 1 generates an in vivo substrate for protein kinase C Proc Natl Acad Sci USA 94 1997 5349 5354
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5349-5354
    • Walter, J.1    Grünberg, J.2    Capell, A.3
  • 54
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin 1 required for presenilin endoproteolysis and γ-secretase activity
    • M.S. Wolfe, W. Xia, B.L. Ostaszewski, T.S. Diehl, W.T. Kimberly, and D.J. Selkoe Two transmembrane aspartates in presenilin 1 required for presenilin endoproteolysis and γ-secretase activity Nature 398 1999 513 517
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.2    Ostaszewski, B.L.3    Diehl, T.S.4    Kimberly, W.T.5    Selkoe, D.J.6
  • 55
    • 17744401440 scopus 로고    scopus 로고
    • Presenilin 1 is required for notch-1 and DII1 expression in the paraxial mesoderm
    • P.C. Wong, H. Zheng, and H. Chen Presenilin 1 is required for notch-1 and DII1 expression in the paraxial mesoderm Nature 387 1997 288 292
    • (1997) Nature , vol.387 , pp. 288-292
    • Wong, P.C.1    Zheng, H.2    Chen, H.3
  • 56
    • 0035845481 scopus 로고    scopus 로고
    • Loss of presenilin 1 is associated with enhanced beta-catenin signaling and skin tumorigenesis
    • X. Xia, S. Qian, and S. Soriano Loss of presenilin 1 is associated with enhanced beta-catenin signaling and skin tumorigenesis Proc Natl Acad Sci USA 98 2001 10863 10868
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10863-10868
    • Xia, X.1    Qian, S.2    Soriano, S.3
  • 57
    • 1642585717 scopus 로고    scopus 로고
    • Biding sites of γ-secretase inhibitors in rodent brain: Distribution, postnatal development, and effect of deafferentation
    • X.-X. Yan, T. Li, and C.M. Rominger Biding sites of γ-secretase inhibitors in rodent brain: distribution, postnatal development, and effect of deafferentation J Neurosci 24 2004 2942 2952
    • (2004) J Neurosci , vol.24 , pp. 2942-2952
    • Yan, X.-X.1    Li, T.2    Rominger, C.M.3
  • 58
    • 0037008723 scopus 로고    scopus 로고
    • Mature Glycosylation and trafficking of nicastrin modulate its binding to presenilin
    • D.-S. Yang, F. Tandon, and F. Chen Mature Glycosylation and trafficking of nicastrin modulate its binding to presenilin J Biol Chem 277 2002 28135 28142
    • (2002) J Biol Chem , vol.277 , pp. 28135-28142
    • Yang, D.-S.1    Tandon, F.2    Chen, F.3
  • 59
    • 0034536722 scopus 로고    scopus 로고
    • Role of presenilin 1 in murine neural development
    • X. Yang, M. Handler, and J. Shen Role of presenilin 1 in murine neural development Ann N Y Acad Sci 920 2000 165 170
    • (2000) Ann N Y Acad Sci , vol.920 , pp. 165-170
    • Yang, X.1    Handler, M.2    Shen, J.3
  • 60
    • 0032568821 scopus 로고    scopus 로고
    • The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains beta-catenin
    • G. Yu, F. Chen, and G. Levesque The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains beta-catenin J Biol Chem 273 1998 16470 16475
    • (1998) J Biol Chem , vol.273 , pp. 16470-16475
    • Yu, G.1    Chen, F.2    Levesque, G.3
  • 61
    • 0034618715 scopus 로고    scopus 로고
    • Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βaPP processing
    • G. Yu, M. Nishimura, and S. Arawaka Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing Nature 407 2000 48 54
    • (2000) Nature , vol.407 , pp. 48-54
    • Yu, G.1    Nishimura, M.2    Arawaka, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.