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Volumn 23, Issue 3, 2007, Pages 140-150

Presenilin diversifies its portfolio

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; BETA CATENIN; BINDING PROTEIN; CALCIUM; CALSENILIN; CD147 ANTIGEN; EPIDERMAL GROWTH FACTOR RECEPTOR 4; FILAMIN; GAMMA SECRETASE; GLYCOGEN SYNTHASE KINASE 3BETA; NOTCH RECEPTOR; PRESENILIN 1; PROTEIN BCL 2; PROTEIN BCL XL; RYANODINE RECEPTOR; SMALL INTERFERING RNA; STAT5 PROTEIN; SYNTAXIN; TAU PROTEIN; UBIQUITIN; VOLTAGE GATED SODIUM CHANNEL; WNT PROTEIN;

EID: 33847021476     PISSN: 01689525     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tig.2007.01.008     Document Type: Review
Times cited : (136)

References (110)
  • 1
    • 0036727125 scopus 로고    scopus 로고
    • γ-Secretase-mediated proteolysis in cell-surface-receptor signaling
    • Fortini M.E. γ-Secretase-mediated proteolysis in cell-surface-receptor signaling. Nat. Rev. Mol. Cell Biol. 3 (2002) 673-684
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 673-684
    • Fortini, M.E.1
  • 2
    • 3142512452 scopus 로고    scopus 로고
    • Potential role of presenilin-regulated signaling pathways in sporadic neurodegeneration
    • Koo E.H., and Kopan R. Potential role of presenilin-regulated signaling pathways in sporadic neurodegeneration. Nat. Med. 10 (2004) S26-S33
    • (2004) Nat. Med. , vol.10
    • Koo, E.H.1    Kopan, R.2
  • 3
    • 33745614108 scopus 로고    scopus 로고
    • The γ-secretase complex: membrane-embedded proteolytic ensemble
    • Wolfe M.S. The γ-secretase complex: membrane-embedded proteolytic ensemble. Biochemistry 45 (2006) 7931-7939
    • (2006) Biochemistry , vol.45 , pp. 7931-7939
    • Wolfe, M.S.1
  • 4
    • 7944233158 scopus 로고    scopus 로고
    • Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases
    • Selkoe D.J. Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases. Nat. Cell Biol. 6 (2004) 1054-1061
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1054-1061
    • Selkoe, D.J.1
  • 5
    • 33747623018 scopus 로고    scopus 로고
    • Notch signalling: a simple pathway becomes complex
    • Bray S.J. Notch signalling: a simple pathway becomes complex. Nat. Rev. Mol. Cell Biol. 7 (2006) 678-689
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 678-689
    • Bray, S.J.1
  • 6
    • 0033639117 scopus 로고    scopus 로고
    • Requirements for Presenilin-dependent cleavage of Notch and other transmembrane proteins
    • Struhl G., and Adachi A. Requirements for Presenilin-dependent cleavage of Notch and other transmembrane proteins. Mol. Cell 6 (2000) 625-636
    • (2000) Mol. Cell , vol.6 , pp. 625-636
    • Struhl, G.1    Adachi, A.2
  • 7
    • 2942557122 scopus 로고    scopus 로고
    • γ-Secretase: proteasome of the membrane?
    • Kopan R., and Ilagan M.X. γ-Secretase: proteasome of the membrane?. Nat. Rev. Mol. Cell Biol. 5 (2004) 499-504
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 499-504
    • Kopan, R.1    Ilagan, M.X.2
  • 8
    • 13844299709 scopus 로고    scopus 로고
    • Presenilin attenuates receptor-mediated signaling and synaptic function
    • Parent A.T., et al. Presenilin attenuates receptor-mediated signaling and synaptic function. J. Neurosci. 25 (2005) 1540-1549
    • (2005) J. Neurosci. , vol.25 , pp. 1540-1549
    • Parent, A.T.1
  • 9
    • 33749072019 scopus 로고    scopus 로고
    • Nuclear signaling by receptor tyrosine kinases: the first robin of spring
    • Schlessinger J., and Lemmon M.A. Nuclear signaling by receptor tyrosine kinases: the first robin of spring. Cell 127 (2006) 45-48
    • (2006) Cell , vol.127 , pp. 45-48
    • Schlessinger, J.1    Lemmon, M.A.2
  • 10
    • 8444243682 scopus 로고    scopus 로고
    • The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone
    • Williams C.C., et al. The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone. J. Cell Biol. 167 (2004) 469-478
    • (2004) J. Cell Biol. , vol.167 , pp. 469-478
    • Williams, C.C.1
  • 11
    • 33748087796 scopus 로고    scopus 로고
    • Coregulation of estrogen receptor by ERBB4/HER4 establishes a growth-promoting autocrine signal in breast tumor cells
    • Zhu Y., et al. Coregulation of estrogen receptor by ERBB4/HER4 establishes a growth-promoting autocrine signal in breast tumor cells. Cancer Res. 66 (2006) 7991-7998
    • (2006) Cancer Res. , vol.66 , pp. 7991-7998
    • Zhu, Y.1
  • 12
    • 33745714207 scopus 로고    scopus 로고
    • The ERBB4/HER4 intracellular domain 4ICD is a BH3-only protein promoting apoptosis of breast cancer cells
    • Naresh A., et al. The ERBB4/HER4 intracellular domain 4ICD is a BH3-only protein promoting apoptosis of breast cancer cells. Cancer Res. 66 (2006) 6412-6420
    • (2006) Cancer Res. , vol.66 , pp. 6412-6420
    • Naresh, A.1
  • 13
    • 33749072714 scopus 로고    scopus 로고
    • Presenilin-dependent ErbB4 nuclear signaling regulates the timing of astrogenesis in the developing brain
    • Sardi S.P., et al. Presenilin-dependent ErbB4 nuclear signaling regulates the timing of astrogenesis in the developing brain. Cell 127 (2006) 185-197
    • (2006) Cell , vol.127 , pp. 185-197
    • Sardi, S.P.1
  • 14
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao X., and Sudhof T.C. A transcriptionally 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
  • 15
    • 20444398562 scopus 로고    scopus 로고
    • Presenilin-dependent transcriptional control of the Aβ-degrading enzyme neprilysin by intracellular domains of βAPP and APLP
    • Pardossi-Piquard R., et al. Presenilin-dependent transcriptional control of the Aβ-degrading enzyme neprilysin by intracellular domains of βAPP and APLP. Neuron 46 (2005) 541-554
    • (2005) Neuron , vol.46 , pp. 541-554
    • Pardossi-Piquard, R.1
  • 16
    • 2642582435 scopus 로고    scopus 로고
    • Dissection of amyloid-β precursor protein-dependent transcriptional transactivation
    • Cao X., and Sudhof T.C. Dissection of amyloid-β precursor protein-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
  • 17
    • 25144490620 scopus 로고    scopus 로고
    • Presenilins in the developing, adult, and aging cerebral cortex
    • Wines-Samuelson M., and Shen J. Presenilins in the developing, adult, and aging cerebral cortex. Neuroscientist 11 (2005) 441-451
    • (2005) Neuroscientist , vol.11 , pp. 441-451
    • Wines-Samuelson, M.1    Shen, J.2
  • 18
    • 33846403492 scopus 로고    scopus 로고
    • Pathological and physiological functions of presenilins
    • 10.1186/1750-1326-1-4
    • Vetrivel K.S., et al. Pathological and physiological functions of presenilins. Mol. Neurodegener. 1 (2006) 4. www.molecularneurodegeneration.com 10.1186/1750-1326-1-4
    • (2006) Mol. Neurodegener. , vol.1 , pp. 4
    • Vetrivel, K.S.1
  • 19
    • 30744465376 scopus 로고    scopus 로고
    • Reduced Aph-1b expression causes tissue- and substrate-specific changes in γ-secretase activity in rats with a complex phenotype
    • Coolen M.W., et al. Reduced Aph-1b expression causes tissue- and substrate-specific changes in γ-secretase activity in rats with a complex phenotype. FASEB J. 20 (2006) 175-177
    • (2006) FASEB J. , vol.20 , pp. 175-177
    • Coolen, M.W.1
  • 20
    • 4744375540 scopus 로고    scopus 로고
    • Identification of distinct γ-secretase complexes with different APH-1 variants
    • Shirotani K., et al. Identification of distinct γ-secretase complexes with different APH-1 variants. J. Biol. Chem. 279 (2004) 41340-41345
    • (2004) J. Biol. Chem. , vol.279 , pp. 41340-41345
    • Shirotani, K.1
  • 21
    • 21144447065 scopus 로고    scopus 로고
    • Dissociated phenotypes in presenilin transgenic mice define functionally distinct γ-secretases
    • Mastrangelo P., et al. Dissociated phenotypes in presenilin transgenic mice define functionally distinct γ-secretases. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 8972-8977
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 8972-8977
    • Mastrangelo, P.1
  • 22
    • 13444268952 scopus 로고    scopus 로고
    • Differential contribution of the three Aph1 genes to γ-secretase activity in vivo
    • Serneels L., et al. Differential contribution of the three Aph1 genes to γ-secretase activity in vivo. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 1719-1724
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 1719-1724
    • Serneels, L.1
  • 23
    • 21844448354 scopus 로고    scopus 로고
    • Spatial segregation of γ-secretase and substrates in distinct membrane domains
    • Vetrivel K.S., et al. Spatial segregation of γ-secretase and substrates in distinct membrane domains. J. Biol. Chem. 280 (2005) 25892-25900
    • (2005) J. Biol. Chem. , vol.280 , pp. 25892-25900
    • Vetrivel, K.S.1
  • 24
    • 33745853091 scopus 로고    scopus 로고
    • Presenilin-1 is an unprimed glycogen synthase kinase-3β substrate
    • Twomey C., and McCarthy J.V. Presenilin-1 is an unprimed glycogen synthase kinase-3β substrate. FEBS Lett. 580 (2006) 4015-4020
    • (2006) FEBS Lett. , vol.580 , pp. 4015-4020
    • Twomey, C.1    McCarthy, J.V.2
  • 25
    • 0035903090 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3β regulates presenilin 1 C-terminal fragment levels
    • Kirschenbaum F., et al. Glycogen synthase kinase-3β regulates presenilin 1 C-terminal fragment levels. J. Biol. Chem. 276 (2001) 30701-30707
    • (2001) J. Biol. Chem. , vol.276 , pp. 30701-30707
    • Kirschenbaum, F.1
  • 26
    • 0035831453 scopus 로고    scopus 로고
    • Substitution of a glycogen synthase kinase-3β phosphorylation site in presenilin 1 separates presenilin function from β-catenin signaling
    • Kirschenbaum F., et al. Substitution of a glycogen synthase kinase-3β phosphorylation site in presenilin 1 separates presenilin function from β-catenin signaling. J. Biol. Chem. 276 (2001) 7366-7375
    • (2001) J. Biol. Chem. , vol.276 , pp. 7366-7375
    • Kirschenbaum, F.1
  • 27
    • 0345826185 scopus 로고    scopus 로고
    • Phosphorylation of presenilin 1 at the caspase recognition site regulates its proteolytic processing and the progression of apoptosis
    • Fluhrer R., et al. Phosphorylation of presenilin 1 at the caspase recognition site regulates its proteolytic processing and the progression of apoptosis. J. Biol. Chem. 279 (2004) 1585-1593
    • (2004) J. Biol. Chem. , vol.279 , pp. 1585-1593
    • Fluhrer, R.1
  • 28
    • 33646177464 scopus 로고    scopus 로고
    • Presenilin-based genetic screens in Drosophila melanogaster identify novel Notch pathway modifiers
    • Mahoney M.B., et al. Presenilin-based genetic screens in Drosophila melanogaster identify novel Notch pathway modifiers. Genetics 172 (2006) 2309-2324
    • (2006) Genetics , vol.172 , pp. 2309-2324
    • Mahoney, M.B.1
  • 29
    • 14844302825 scopus 로고    scopus 로고
    • Overexpression of calsenilin enhances γ-secretase activity
    • Jo D.G., et al. Overexpression of calsenilin enhances γ-secretase activity. Neurosci. Lett. 378 (2005) 59-64
    • (2005) Neurosci. Lett. , vol.378 , pp. 59-64
    • Jo, D.G.1
  • 30
    • 0038265452 scopus 로고    scopus 로고
    • Microtubular interactions of presenilin direct kinesis of Aβ peptide and its precursors
    • Tezapsidis N., et al. Microtubular interactions of presenilin direct kinesis of Aβ peptide and its precursors. FASEB J. 17 (2003) 1322-1324
    • (2003) FASEB J. , vol.17 , pp. 1322-1324
    • Tezapsidis, N.1
  • 31
    • 33645777828 scopus 로고    scopus 로고
    • Self-refinement of Notch activity through the transmembrane protein Crumbs: modulation of γ-secretase activity
    • Herranz H., et al. Self-refinement of Notch activity through the transmembrane protein Crumbs: modulation of γ-secretase activity. EMBO Rep. 7 (2006) 297-302
    • (2006) EMBO Rep. , vol.7 , pp. 297-302
    • Herranz, H.1
  • 32
    • 33646369950 scopus 로고    scopus 로고
    • TMP21 is a presenilin complex component that modulates γ-secretase but not ε-secretase activity
    • Chen F., et al. TMP21 is a presenilin complex component that modulates γ-secretase but not ε-secretase activity. Nature 440 (2006) 1208-1212
    • (2006) Nature , vol.440 , pp. 1208-1212
    • Chen, F.1
  • 33
    • 19644389648 scopus 로고    scopus 로고
    • CD147 is a regulatory subunit of the γ-secretase complex in Alzheimer's disease amyloid β-peptide production
    • Zhou S., et al. CD147 is a regulatory subunit of the γ-secretase complex in Alzheimer's disease amyloid β-peptide production. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 7499-7504
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 7499-7504
    • Zhou, S.1
  • 34
    • 4644257963 scopus 로고    scopus 로고
    • Presenilin 1 mediates the turnover of telencephalin in hippocampal neurons via an autophagic degradative pathway
    • Esselens C., et al. Presenilin 1 mediates the turnover of telencephalin in hippocampal neurons via an autophagic degradative pathway. J. Cell Biol. 166 (2004) 1041-1054
    • (2004) J. Cell Biol. , vol.166 , pp. 1041-1054
    • Esselens, C.1
  • 35
    • 11144354609 scopus 로고    scopus 로고
    • Loss of presenilin function causes impairments of memory and synaptic plasticity followed by age-dependent neurodegeneration
    • Saura C.A., et al. 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
  • 36
  • 37
    • 0000138540 scopus 로고    scopus 로고
    • Effects of PS1 deficiency on membrane protein trafficking in neurons
    • Naruse S., et al. Effects of PS1 deficiency on membrane protein trafficking in neurons. Neuron 21 (1998) 1213-1221
    • (1998) Neuron , vol.21 , pp. 1213-1221
    • Naruse, S.1
  • 38
    • 0141816599 scopus 로고    scopus 로고
    • Presenilin 1 is involved in maturation and trafficking of N-cadherin to the plasma membrane
    • Uemura K., et al. Presenilin 1 is involved in maturation and trafficking of N-cadherin to the plasma membrane. J. Neurosci. Res. 74 (2003) 184-191
    • (2003) J. Neurosci. Res. , vol.74 , pp. 184-191
    • Uemura, K.1
  • 39
    • 25844499702 scopus 로고    scopus 로고
    • Interaction of presenilins with FKBP38 promotes apoptosis by reducing mitochondrial Bcl-2
    • Wang H.Q., et al. Interaction of presenilins with FKBP38 promotes apoptosis by reducing mitochondrial Bcl-2. Hum. Mol. Genet. 14 (2005) 1889-1902
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 1889-1902
    • Wang, H.Q.1
  • 40
    • 33845655221 scopus 로고    scopus 로고
    • Presenilin/γ-secretase activity regulates protein clearance from the endocytic recycling compartment
    • Zhang M., et al. Presenilin/γ-secretase activity regulates protein clearance from the endocytic recycling compartment. FASEB J. 20 (2006) 1176-1178
    • (2006) FASEB J. , vol.20 , pp. 1176-1178
    • Zhang, M.1
  • 41
    • 31044438340 scopus 로고    scopus 로고
    • Regulation of tyrosinase trafficking and processing by presenilins: partial loss of function by familial Alzheimer's disease mutation
    • Wang R., et al. Regulation of tyrosinase trafficking and processing by presenilins: partial loss of function by familial Alzheimer's disease mutation. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 353-358
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 353-358
    • Wang, R.1
  • 42
    • 0037146553 scopus 로고    scopus 로고
    • Nectin-1α, an immunoglobulin-like receptor involved in the formation of synapses, is a substrate for presenilin/γ-secretase-like cleavage
    • Kim D.Y., et al. Nectin-1α, an immunoglobulin-like receptor involved in the formation of synapses, is a substrate for presenilin/γ-secretase-like cleavage. J. Biol. Chem. 277 (2002) 49976-49981
    • (2002) J. Biol. Chem. , vol.277 , pp. 49976-49981
    • Kim, D.Y.1
  • 43
    • 20744458852 scopus 로고    scopus 로고
    • Presenilin/γ-secretase-mediated cleavage of the voltage-gated sodium channel β2-subunit regulates cell adhesion and migration
    • Kim D.Y., et al. Presenilin/γ-secretase-mediated cleavage of the voltage-gated sodium channel β2-subunit regulates cell adhesion and migration. J. Biol. Chem. 280 (2005) 23251-23261
    • (2005) J. Biol. Chem. , vol.280 , pp. 23251-23261
    • Kim, D.Y.1
  • 44
    • 15744388308 scopus 로고    scopus 로고
    • Presenilin-dependent processing and nuclear function of γ-protocadherins
    • Haas I.G., et al. Presenilin-dependent processing and nuclear function of γ-protocadherins. J. Biol. Chem. 280 (2005) 9313-9319
    • (2005) J. Biol. Chem. , vol.280 , pp. 9313-9319
    • Haas, I.G.1
  • 45
    • 18144427413 scopus 로고    scopus 로고
    • γ-Protocadherins, presenilin-mediated release of C-terminal fragment promotes locus expression
    • Hambsch B., et al. γ-Protocadherins, presenilin-mediated release of C-terminal fragment promotes locus expression. J. Biol. Chem. 280 (2005) 15888-15897
    • (2005) J. Biol. Chem. , vol.280 , pp. 15888-15897
    • Hambsch, B.1
  • 46
    • 18744410937 scopus 로고    scopus 로고
    • γ Protocadherins are required for survival of spinal interneurons
    • Wang X., et al. γ Protocadherins are required for survival of spinal interneurons. Neuron 36 (2002) 843-854
    • (2002) Neuron , vol.36 , pp. 843-854
    • Wang, X.1
  • 47
    • 11844301330 scopus 로고    scopus 로고
    • γ Protocadherins are required for synaptic development in the spinal cord
    • Weiner J.A., et al. γ Protocadherins are required for synaptic development in the spinal cord. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 8-14
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 8-14
    • Weiner, J.A.1
  • 48
    • 23644451506 scopus 로고    scopus 로고
    • Assembly of the N-cadherin complex during synapse formation involves uncoupling of p120-catenin and association with presenilin 1
    • Rubio M.E., et al. Assembly of the N-cadherin complex during synapse formation involves uncoupling of p120-catenin and association with presenilin 1. Mol. Cell. Neurosci. 30 (2005) 611-623
    • (2005) Mol. Cell. Neurosci. , vol.30 , pp. 611-623
    • Rubio, M.E.1
  • 49
    • 9244253754 scopus 로고    scopus 로고
    • Presenilin 1 and cadherins: stabilization of cell-cell adhesion and proteolysis-dependent regulation of transcription
    • Parisiadou L., et al. Presenilin 1 and cadherins: stabilization of cell-cell adhesion and proteolysis-dependent regulation of transcription. Neurodegener. Dis. 1 (2004) 184-191
    • (2004) Neurodegener. Dis. , vol.1 , pp. 184-191
    • Parisiadou, L.1
  • 50
    • 18344380083 scopus 로고    scopus 로고
    • A presenilin-1/γ-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions
    • Marambaud P., et al. A presenilin-1/γ-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions. EMBO J. 21 (2002) 1948-1956
    • (2002) EMBO J. , vol.21 , pp. 1948-1956
    • Marambaud, P.1
  • 51
    • 33645104764 scopus 로고    scopus 로고
    • The cytoplasmic sequence of E-cadherin promotes non-amyloidogenic degradation of Aβ precursors
    • Agiostratidou G., et al. The cytoplasmic sequence of E-cadherin promotes non-amyloidogenic degradation of Aβ precursors. J. Neurochem. 96 (2006) 1182-1188
    • (2006) J. Neurochem. , vol.96 , pp. 1182-1188
    • Agiostratidou, G.1
  • 52
    • 0141429160 scopus 로고    scopus 로고
    • A CBP binding transcriptional repressor produced by the PS1/ε-cleavage of N-cadherin is inhibited by PS1 FAD mutations
    • Marambaud P., et al. A CBP binding transcriptional repressor produced by the PS1/ε-cleavage of N-cadherin is inhibited by PS1 FAD mutations. Cell 114 (2003) 635-645
    • (2003) Cell , vol.114 , pp. 635-645
    • Marambaud, P.1
  • 53
    • 33646834890 scopus 로고    scopus 로고
    • Activity-dependent regulation of β-catenin via ε-cleavage of N-cadherin
    • Uemura K., et al. Activity-dependent regulation of β-catenin via ε-cleavage of N-cadherin. Biochem. Biophys. Res. Commun. 345 (2006) 951-958
    • (2006) Biochem. Biophys. Res. Commun. , vol.345 , pp. 951-958
    • Uemura, K.1
  • 54
    • 0037014456 scopus 로고    scopus 로고
    • Depolarization drives β-catenin into neuronal spines promoting changes in synaptic structure and function
    • Murase S., et al. Depolarization drives β-catenin into neuronal spines promoting changes in synaptic structure and function. Neuron 35 (2002) 91-105
    • (2002) Neuron , vol.35 , pp. 91-105
    • Murase, S.1
  • 55
    • 33644989671 scopus 로고    scopus 로고
    • Presenilin-1 interacts with plakoglobin and enhances plakoglobin-Tcf-4 association. Implications for the regulation of β-catenin/Tcf-4-dependent transcription
    • Raurell I., et al. Presenilin-1 interacts with plakoglobin and enhances plakoglobin-Tcf-4 association. Implications for the regulation of β-catenin/Tcf-4-dependent transcription. J. Biol. Chem. 281 (2006) 1401-1411
    • (2006) J. Biol. Chem. , vol.281 , pp. 1401-1411
    • Raurell, I.1
  • 56
    • 3343005434 scopus 로고    scopus 로고
    • PS1 activates PI3K thus inhibiting GSK-3 activity and tau overphosphorylation: effects of FAD mutations
    • Baki L., et al. PS1 activates PI3K thus inhibiting GSK-3 activity and tau overphosphorylation: effects of FAD mutations. EMBO J. 23 (2004) 2586-2596
    • (2004) EMBO J. , vol.23 , pp. 2586-2596
    • Baki, L.1
  • 57
    • 0036830947 scopus 로고    scopus 로고
    • Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease
    • LaFerla F.M. Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease. Nat. Rev. Neurosci. 3 (2002) 862-872
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 862-872
    • LaFerla, F.M.1
  • 58
    • 24644456470 scopus 로고    scopus 로고
    • Calcium dysregulation in Alzheimer's disease: recent advances gained from genetically modified animals
    • Smith I.F., et al. Calcium dysregulation in Alzheimer's disease: recent advances gained from genetically modified animals. Cell Calcium 38 (2005) 427-437
    • (2005) Cell Calcium , vol.38 , pp. 427-437
    • Smith, I.F.1
  • 59
    • 15244352734 scopus 로고    scopus 로고
    • Calcium dysregulation, IP3 signaling, and Alzheimer's disease
    • Stutzmann G.E. Calcium dysregulation, IP3 signaling, and Alzheimer's disease. Neuroscientist 11 (2005) 110-115
    • (2005) Neuroscientist , vol.11 , pp. 110-115
    • Stutzmann, G.E.1
  • 60
    • 33748140720 scopus 로고    scopus 로고
    • + leak channels, a function disrupted by familial Alzheimer's disease-linked mutations
    • + leak channels, a function disrupted by familial Alzheimer's disease-linked mutations. Cell 126 (2006) 981-993
    • (2006) Cell , vol.126 , pp. 981-993
    • Tu, H.1
  • 61
    • 33845217332 scopus 로고    scopus 로고
    • Mutations of presenilin genes in dilated cardiomyopathy and heart failure
    • Li D., et al. Mutations of presenilin genes in dilated cardiomyopathy and heart failure. Am. J. Hum. Genet. 79 (2006) 1030-1039
    • (2006) Am. J. Hum. Genet. , vol.79 , pp. 1030-1039
    • Li, D.1
  • 62
    • 27444441308 scopus 로고    scopus 로고
    • A nine-transmembrane domain topology for presenilin 1
    • Laudon H., et al. A nine-transmembrane domain topology for presenilin 1. J. Biol. Chem. 280 (2005) 35352-35360
    • (2005) J. Biol. Chem. , vol.280 , pp. 35352-35360
    • Laudon, H.1
  • 63
    • 33748746861 scopus 로고    scopus 로고
    • Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway
    • Spasic D., et al. Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway. J. Biol. Chem. 281 (2006) 26569-26577
    • (2006) J. Biol. Chem. , vol.281 , pp. 26569-26577
    • Spasic, D.1
  • 64
    • 33646483640 scopus 로고    scopus 로고
    • Electron microscopic structure of purified, active γ-secretase reveals an aqueous intramembrane chamber and two pores
    • Lazarov V.K., et al. Electron microscopic structure of purified, active γ-secretase reveals an aqueous intramembrane chamber and two pores. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 6889-6894
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 6889-6894
    • Lazarov, V.K.1
  • 65
    • 33645116480 scopus 로고    scopus 로고
    • Three-dimensional structure of the γ-secretase complex
    • Ogura T., et al. Three-dimensional structure of the γ-secretase complex. Biochem. Biophys. Res. Commun. 343 (2006) 525-534
    • (2006) Biochem. Biophys. Res. Commun. , vol.343 , pp. 525-534
    • Ogura, T.1
  • 66
    • 23744491374 scopus 로고    scopus 로고
    • Nicastrin functions as a γ-secretase-substrate receptor
    • Shah S., et al. Nicastrin functions as a γ-secretase-substrate receptor. Cell 122 (2005) 435-447
    • (2005) Cell , vol.122 , pp. 435-447
    • Shah, S.1
  • 67
    • 33644837810 scopus 로고    scopus 로고
    • Analysis of transmembrane domain mutants is consistent with sequential cleavage of Notch by γ-secretase
    • Chandu D., et al. Analysis of transmembrane domain mutants is consistent with sequential cleavage of Notch by γ-secretase. J. Neurochem. 96 (2006) 228-235
    • (2006) J. Neurochem. , vol.96 , pp. 228-235
    • Chandu, D.1
  • 68
    • 0346363758 scopus 로고    scopus 로고
    • Phorbol 12-myristate 13-acetate-induced release of the colony-stimulating factor 1 receptor cytoplasmic domain into the cytosol involves two separate cleavage events
    • Wilhelmsen K., and van der Geer P. Phorbol 12-myristate 13-acetate-induced release of the colony-stimulating factor 1 receptor cytoplasmic domain into the cytosol involves two separate cleavage events. Mol. Cell. Biol. 24 (2004) 454-464
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 454-464
    • Wilhelmsen, K.1    van der Geer, P.2
  • 69
    • 0034702303 scopus 로고    scopus 로고
    • Embryonic lethality in mice homozygous for a processing-deficient allele of Notch1
    • Huppert S.S., et al. Embryonic lethality in mice homozygous for a processing-deficient allele of Notch1. Nature 405 (2000) 966-970
    • (2000) Nature , vol.405 , pp. 966-970
    • Huppert, S.S.1
  • 70
    • 0032574993 scopus 로고    scopus 로고
    • Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain
    • Schroeter E.H., et al. Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain. Nature 393 (1998) 382-386
    • (1998) Nature , vol.393 , pp. 382-386
    • Schroeter, E.H.1
  • 71
    • 21244487829 scopus 로고    scopus 로고
    • Presenilin-dependent γ-secretase processing regulates multiple ERBB4/HER4 activities
    • Vidal G.A., et al. Presenilin-dependent γ-secretase processing regulates multiple ERBB4/HER4 activities. J. Biol. Chem. 280 (2005) 19777-19783
    • (2005) J. Biol. Chem. , vol.280 , pp. 19777-19783
    • Vidal, G.A.1
  • 72
    • 0038322593 scopus 로고    scopus 로고
    • γ-Secretase cleavage and binding to FE65 regulate the nuclear translocation of the intracellular C-terminal domain (ICD) of the APP family of proteins
    • Walsh D.M., et al. γ-Secretase cleavage and binding to FE65 regulate the nuclear translocation of the intracellular C-terminal domain (ICD) of the APP family of proteins. Biochemistry 42 (2003) 6664-6673
    • (2003) Biochemistry , vol.42 , pp. 6664-6673
    • Walsh, D.M.1
  • 73
    • 27144504391 scopus 로고    scopus 로고
    • F-spondin interaction with the apolipoprotein E receptor ApoEr2 affects processing of amyloid precursor protein
    • Hoe H.S., et al. F-spondin interaction with the apolipoprotein E receptor ApoEr2 affects processing of amyloid precursor protein. Mol. Cell. Biol. 25 (2005) 9259-9268
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 9259-9268
    • Hoe, H.S.1
  • 74
    • 0141733204 scopus 로고    scopus 로고
    • Differential glycosylation regulates processing of lipoprotein receptors by γ-secretase
    • May P., et al. Differential glycosylation regulates processing of lipoprotein receptors by γ-secretase. J. Biol. Chem. 278 (2003) 37386-37392
    • (2003) J. Biol. Chem. , vol.278 , pp. 37386-37392
    • May, P.1
  • 75
    • 0347785491 scopus 로고    scopus 로고
    • Presenilin-dependent intramembrane proteolysis of CD44 leads to the liberation of its intracellular domain and the secretion of an Aβ-like peptide
    • Lammich S., et al. Presenilin-dependent intramembrane proteolysis of CD44 leads to the liberation of its intracellular domain and the secretion of an Aβ-like peptide. J. Biol. Chem. 277 (2002) 44754-44759
    • (2002) J. Biol. Chem. , vol.277 , pp. 44754-44759
    • Lammich, S.1
  • 76
    • 0037435016 scopus 로고    scopus 로고
    • Presenilin-dependent γ-secretase activity mediates the intramembranous cleavage of CD44
    • Murakami D., et al. Presenilin-dependent γ-secretase activity mediates the intramembranous cleavage of CD44. Oncogene 22 (2003) 1511-1516
    • (2003) Oncogene , vol.22 , pp. 1511-1516
    • Murakami, D.1
  • 77
    • 30444441681 scopus 로고    scopus 로고
    • The intracellular domain of CD44 promotes the fusion of macrophages
    • Cui W., et al. The intracellular domain of CD44 promotes the fusion of macrophages. Blood 107 (2006) 796-805
    • (2006) Blood , vol.107 , pp. 796-805
    • Cui, W.1
  • 78
    • 0043235625 scopus 로고    scopus 로고
    • Presenilin-dependent 'γ-secretase' processing of deleted in colorectal cancer (DCC)
    • Taniguchi Y., et al. Presenilin-dependent 'γ-secretase' processing of deleted in colorectal cancer (DCC). J. Biol. Chem. 278 (2003) 30425-30428
    • (2003) J. Biol. Chem. , vol.278 , pp. 30425-30428
    • Taniguchi, Y.1
  • 79
    • 0141817915 scopus 로고    scopus 로고
    • The Notch ligands, Jagged and Delta, are sequentially processed by α-secretase and presenilin/γ-secretase and release signaling fragments
    • LaVoie M.J., and Selkoe D.J. The Notch ligands, Jagged and Delta, are sequentially processed by α-secretase and presenilin/γ-secretase and release signaling fragments. J. Biol. Chem. 278 (2003) 34427-34437
    • (2003) J. Biol. Chem. , vol.278 , pp. 34427-34437
    • LaVoie, M.J.1    Selkoe, D.J.2
  • 80
    • 0038610845 scopus 로고    scopus 로고
    • The Notch ligand Delta1 is sequentially cleaved by an ADAM protease and γ-secretase
    • Six E., et al. The Notch ligand Delta1 is sequentially cleaved by an ADAM protease and γ-secretase. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 7638-7643
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 7638-7643
    • Six, E.1
  • 81
    • 33847014741 scopus 로고    scopus 로고
    • Presenilin-dependent intramembrane cleavage of ephrin-B1
    • 10.1186/1750-1326-1-2
    • Tomita T., et al. Presenilin-dependent intramembrane cleavage of ephrin-B1. Mol. Neurodegener. 1 (2006) 2. www.molecularneurodegeneration.com 10.1186/1750-1326-1-2
    • (2006) Mol. Neurodegener. , vol.1 , pp. 2
    • Tomita, T.1
  • 82
    • 33645277094 scopus 로고    scopus 로고
    • Metalloproteinase/Presenilin1 processing of ephrinB regulates EphB-induced Src phosphorylation and signaling
    • Georgakopoulos A., et al. Metalloproteinase/Presenilin1 processing of ephrinB regulates EphB-induced Src phosphorylation and signaling. EMBO J. 25 (2006) 1242-1252
    • (2006) EMBO J. , vol.25 , pp. 1242-1252
    • Georgakopoulos, A.1
  • 83
    • 21444457762 scopus 로고    scopus 로고
    • Growth hormone receptor is a target for presenilin-dependent γ-secretase cleavage
    • Cowan J.W., et al. Growth hormone receptor is a target for presenilin-dependent γ-secretase cleavage. J. Biol. Chem. 280 (2005) 19331-19342
    • (2005) J. Biol. Chem. , vol.280 , pp. 19331-19342
    • Cowan, J.W.1
  • 84
    • 0037592332 scopus 로고    scopus 로고
    • Glutamate receptor subunit 3 is modified by site-specific limited proteolysis including cleavage by γ-secretase
    • Meyer E.L., et al. Glutamate receptor subunit 3 is modified by site-specific limited proteolysis including cleavage by γ-secretase. J. Biol. Chem. 278 (2003) 23786-23796
    • (2003) J. Biol. Chem. , vol.278 , pp. 23786-23796
    • Meyer, E.L.1
  • 85
    • 33846322244 scopus 로고    scopus 로고
    • Presenilin/γ-secretase and α-secretase-like peptidases cleave human MHC class I proteins
    • Carey B.W., et al. Presenilin/γ-secretase and α-secretase-like peptidases cleave human MHC class I proteins. Biochem. J. 401 (2007) 121-127
    • (2007) Biochem. J. , vol.401 , pp. 121-127
    • Carey, B.W.1
  • 86
    • 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
    • Kinoshita A., et al. 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
  • 87
    • 0037166319 scopus 로고    scopus 로고
    • Proteolytic processing of low density lipoprotein receptor-related protein mediates regulated release of its intracellular domain
    • May P., et al. Proteolytic processing of low density lipoprotein receptor-related protein mediates regulated release of its intracellular domain. J. Biol. Chem. 277 (2002) 18736-18743
    • (2002) J. Biol. Chem. , vol.277 , pp. 18736-18743
    • May, P.1
  • 88
    • 0038045714 scopus 로고    scopus 로고
    • Proteolytic processing of the p75 neurotrophin receptor and two homologs generates C-terminal fragments with signaling capability
    • Kanning K.C., et al. Proteolytic processing of the p75 neurotrophin receptor and two homologs generates C-terminal fragments with signaling capability. J. Neurosci. 23 (2003) 5425-5436
    • (2003) J. Neurosci. , vol.23 , pp. 5425-5436
    • Kanning, K.C.1
  • 89
    • 20444365447 scopus 로고    scopus 로고
    • MAG induces regulated intramembrane proteolysis of the p75 neurotrophin receptor to inhibit neurite outgrowth
    • Domeniconi M., et al. MAG induces regulated intramembrane proteolysis of the p75 neurotrophin receptor to inhibit neurite outgrowth. Neuron 46 (2005) 849-855
    • (2005) Neuron , vol.46 , pp. 849-855
    • Domeniconi, M.1
  • 90
    • 27744497085 scopus 로고    scopus 로고
    • p75 neurotrophin receptor regulates expression of neural cell adhesion molecule 1
    • Mirnics Z.K., et al. p75 neurotrophin receptor regulates expression of neural cell adhesion molecule 1. Neurobiol. Dis. 20 (2005) 969-985
    • (2005) Neurobiol. Dis. , vol.20 , pp. 969-985
    • Mirnics, Z.K.1
  • 91
    • 1542677095 scopus 로고    scopus 로고
    • Syndecan 3 intramembrane proteolysis is presenilin/γ-secretase-dependent and modulates cytosolic signaling
    • Schulz J.G., et al. Syndecan 3 intramembrane proteolysis is presenilin/γ-secretase-dependent and modulates cytosolic signaling. J. Biol. Chem. 278 (2003) 48651-48657
    • (2003) J. Biol. Chem. , vol.278 , pp. 48651-48657
    • Schulz, J.G.1
  • 92
    • 23844529915 scopus 로고    scopus 로고
    • Involvement of presenilins in cell-survival signalling pathways
    • McCarthy J.V. Involvement of presenilins in cell-survival signalling pathways. Biochem. Soc. Trans. 33 (2005) 568-572
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 568-572
    • McCarthy, J.V.1
  • 93
    • 0034669203 scopus 로고    scopus 로고
    • Presenilin affects arm/β-catenin localization and function in Drosophila
    • Noll E., et al. Presenilin affects arm/β-catenin localization and function in Drosophila. Dev. Biol. 227 (2000) 450-464
    • (2000) Dev. Biol. , vol.227 , pp. 450-464
    • Noll, E.1
  • 94
    • 29644434488 scopus 로고    scopus 로고
    • Ca2+-independent binding and cellular expression profiles question a significant role of calmyrin in transduction of Ca2+-signals to Alzheimer's disease-related presenilin 2 in forebrain
    • Blazejczyk M., et al. Ca2+-independent binding and cellular expression profiles question a significant role of calmyrin in transduction of Ca2+-signals to Alzheimer's disease-related presenilin 2 in forebrain. Biochim. Biophys. Acta 1762 (2006) 66-72
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 66-72
    • Blazejczyk, M.1
  • 95
    • 24144440041 scopus 로고    scopus 로고
    • In vivo evidence of CHIP up-regulation attenuating tau aggregation
    • Sahara N., et al. In vivo evidence of CHIP up-regulation attenuating tau aggregation. J. Neurochem. 94 (2005) 1254-1263
    • (2005) J. Neurochem. , vol.94 , pp. 1254-1263
    • Sahara, N.1
  • 96
    • 1542438695 scopus 로고    scopus 로고
    • Presenilin-interacting proteins
    • Chen Q., and Schubert D. Presenilin-interacting proteins. Expert Rev. Mol. Med. 2002 (2002) 1-18
    • (2002) Expert Rev. Mol. Med. , vol.2002 , pp. 1-18
    • Chen, Q.1    Schubert, D.2
  • 97
    • 24744459453 scopus 로고    scopus 로고
    • Presenilins mediate phosphatidylinositol 3-kinase/AKT and ERK activation via select signaling receptors. Selectivity of PS2 in platelet-derived growth factor signaling
    • Kang D.E., et al. Presenilins mediate phosphatidylinositol 3-kinase/AKT and ERK activation via select signaling receptors. Selectivity of PS2 in platelet-derived growth factor signaling. J. Biol. Chem. 280 (2005) 31537-31547
    • (2005) J. Biol. Chem. , vol.280 , pp. 31537-31547
    • Kang, D.E.1
  • 98
    • 0037119365 scopus 로고    scopus 로고
    • A new splice variant of glial fibrillary acidic protein, GFAPε, interacts with the presenilin proteins
    • Nielsen A.L., et al. A new splice variant of glial fibrillary acidic protein, GFAPε, interacts with the presenilin proteins. J. Biol. Chem. 277 (2002) 29983-29991
    • (2002) J. Biol. Chem. , vol.277 , pp. 29983-29991
    • Nielsen, A.L.1
  • 99
    • 0037145062 scopus 로고    scopus 로고
    • Presenilin couples the paired phosphorylation of β-catenin independent of axin: implications for β-catenin activation in tumorigenesis
    • Kang D.E., et al. Presenilin couples the paired phosphorylation of β-catenin independent of axin: implications for β-catenin activation in tumorigenesis. Cell 110 (2002) 751-762
    • (2002) Cell , vol.110 , pp. 751-762
    • Kang, D.E.1
  • 100
    • 0037043330 scopus 로고    scopus 로고
    • A novel mechanism for the regulation of amyloid precursor protein metabolism
    • Chen Q., et al. A novel mechanism for the regulation of amyloid precursor protein metabolism. J. Cell Biol. 158 (2002) 79-89
    • (2002) J. Cell Biol. , vol.158 , pp. 79-89
    • Chen, Q.1
  • 101
    • 8544245734 scopus 로고    scopus 로고
    • The C-terminal tail of presenilin regulates Omi/HtrA2 protease activity
    • Gupta S., et al. The C-terminal tail of presenilin regulates Omi/HtrA2 protease activity. J. Biol. Chem. 279 (2004) 45844-45854
    • (2004) J. Biol. Chem. , vol.279 , pp. 45844-45854
    • Gupta, S.1
  • 102
    • 32444434357 scopus 로고    scopus 로고
    • Presenilin-1 uses phospholipase D1 as a negative regulator of β-amyloid formation
    • Cai D., et al. Presenilin-1 uses phospholipase D1 as a negative regulator of β-amyloid formation. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 1941-1946
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 1941-1946
    • Cai, D.1
  • 103
    • 0037073733 scopus 로고    scopus 로고
    • The novel presenilin-1-associated protein is a proapoptotic mitochondrial protein
    • Xu X., et al. The novel presenilin-1-associated protein is a proapoptotic mitochondrial protein. J. Biol. Chem. 277 (2002) 48913-48922
    • (2002) J. Biol. Chem. , vol.277 , pp. 48913-48922
    • Xu, X.1
  • 104
    • 28744456107 scopus 로고    scopus 로고
    • 2+ signaling
    • 2+ signaling. FASEB J. 19 (2005) 2069-2071
    • (2005) FASEB J. , vol.19 , pp. 2069-2071
    • Takeda, T.1
  • 105
    • 0036736222 scopus 로고    scopus 로고
    • SEL-10 interacts with presenilin 1, facilitates its ubiquitination, and alters A-β peptide production
    • Li J., et al. SEL-10 interacts with presenilin 1, facilitates its ubiquitination, and alters A-β peptide production. J. Neurochem. 82 (2002) 1540-1548
    • (2002) J. Neurochem. , vol.82 , pp. 1540-1548
    • Li, J.1
  • 106
    • 22244454702 scopus 로고    scopus 로고
    • Syntaxin 5 interacts specifically with presenilin holoproteins and affects processing of βAPP in neuronal cells
    • Suga K., et al. Syntaxin 5 interacts specifically with presenilin holoproteins and affects processing of βAPP in neuronal cells. J. Neurochem. 94 (2005) 425-439
    • (2005) J. Neurochem. , vol.94 , pp. 425-439
    • Suga, K.1
  • 107
    • 4344594413 scopus 로고    scopus 로고
    • Syntaxin 5 interacts with presenilin holoproteins, but not with their N- or C-terminal fragments, and affects β-amyloid peptide production
    • Suga K., et al. Syntaxin 5 interacts with presenilin holoproteins, but not with their N- or C-terminal fragments, and affects β-amyloid peptide production. Biochem. J. 381 (2004) 619-628
    • (2004) Biochem. J. , vol.381 , pp. 619-628
    • Suga, K.1
  • 108
    • 33748746862 scopus 로고    scopus 로고
    • Interaction between presenilin 1 and ubiquilin 1 as detected by fluorescence lifetime imaging microscopy and a high-throughput fluorescent plate reader
    • Thomas A.V., et al. Interaction between presenilin 1 and ubiquilin 1 as detected by fluorescence lifetime imaging microscopy and a high-throughput fluorescent plate reader. J. Biol. Chem. 281 (2006) 26400-26407
    • (2006) J. Biol. Chem. , vol.281 , pp. 26400-26407
    • Thomas, A.V.1
  • 109
    • 27744468749 scopus 로고    scopus 로고
    • Ubiquilin regulates presenilin endoproteolysis and modulates γ-secretase components, Pen-2 and nicastrin
    • Massey L.K., et al. Ubiquilin regulates presenilin endoproteolysis and modulates γ-secretase components, Pen-2 and nicastrin. Biochem. J. 391 (2005) 513-525
    • (2005) Biochem. J. , vol.391 , pp. 513-525
    • Massey, L.K.1
  • 110
    • 0032972547 scopus 로고    scopus 로고
    • Presenilins interact with armadillo proteins including neural-specific plakophilin-related protein and β-catenin
    • Levesque G., et al. Presenilins interact with armadillo proteins including neural-specific plakophilin-related protein and β-catenin. J. Neurochem. 72 (1999) 999-1008
    • (1999) J. Neurochem. , vol.72 , pp. 999-1008
    • Levesque, G.1


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