메뉴 건너뛰기




Volumn 16, Issue 2, 2003, Pages 69-74

Relationship between presenilinase and γ-secretase

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; ANTERIOR PHARYNX DEFECTIVE 1 PROTEIN; ASPARTIC ACID; ASPARTIC PROTEINASE; GAMMA SECRETASE; MEMBRANE PROTEIN; NICASTRIN; PRESENILIN 1; PRESENILIN 2; PRESENILINASE; PROTEIN PEN 2; UNCLASSIFIED DRUG;

EID: 0037933495     PISSN: 02140934     EISSN: None     Source Type: Journal    
DOI: 10.1358/dnp.2003.16.2.740248     Document Type: Review
Times cited : (13)

References (82)
  • 1
    • 0033600274 scopus 로고    scopus 로고
    • Translating Cell biology into therapeutic advances in Alzheimer's disease
    • Selkoe, D.J. Translating Cell biology into therapeutic advances in Alzheimer's disease. Nature 1999, 399(Suppl): A23-1.
    • (1999) Nature , vol.399 , Issue.SUPPL.
    • Selkoe, D.J.1
  • 2
    • 16044366039 scopus 로고    scopus 로고
    • Increased amyloid-β2(43) in brains of mice expressing mutant presenilin 1
    • Duff, K., Eckman, C., Zehr, C. et al. Increased amyloid-β2(43) in brains of mice expressing mutant presenilin 1. Nature 1996, 383: 710-3.
    • (1996) Nature , vol.383 , pp. 710-713
    • Duff, K.1    Eckman, C.2    Zehr, C.3
  • 3
    • 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
    • Citron, M., Westaway, D., Xia, W. et al. Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice. Nat Med 1997, 3: 67-72.
    • (1997) Nat Med , vol.3 , pp. 67-72
    • Citron, M.1    Westaway, D.2    Xia, W.3
  • 4
    • 16044365171 scopus 로고    scopus 로고
    • The E280A presenilin 1 Alsheimer mutation produces increased Aβ42 deposition and severe cerebellar pathology
    • Lemere, C.A., Lopera, F., Kosik, K.S. et al. The E280A presenilin 1 Alsheimer mutation produces increased Aβ42 deposition and severe cerebellar pathology. Nat Med 1996, 2: 1146-50.
    • (1996) Nat Med , vol.2 , pp. 1146-1150
    • Lemere, C.A.1    Lopera, F.2    Kosik, K.S.3
  • 5
    • 16944365745 scopus 로고    scopus 로고
    • Enhanced production and oligomerization of the 42-residue amyloid β-protein by Chinese hamster ovary cells stably expressing mutant presenilins
    • Xia, W., Zhang, J., Kholodenko, D. et al. Enhanced production and oligomerization of the 42-residue amyloid β-protein by Chinese hamster ovary cells stably expressing mutant presenilins. J Biol Chem 1997, 272: 7977-82.
    • (1997) J Biol Chem , vol.272 , pp. 7977-7982
    • Xia, W.1    Zhang, J.2    Kholodenko, D.3
  • 6
    • 0034100349 scopus 로고    scopus 로고
    • Mutant presenilin 1 increases the levels of Alsheimer amyloid β-peptide Aβ42 in late compartments of the constitutive secretory pathway
    • Petanceska, S.S., Seeger, M., Checler, F. and Gandy, S. Mutant presenilin 1 increases the levels of Alsheimer amyloid β-peptide Aβ42 in late compartments of the constitutive secretory pathway. J Neurochem 2000, 74: 1878-84.
    • (2000) J Neurochem , vol.74 , pp. 1878-1884
    • Petanceska, S.S.1    Seeger, M.2    Checler, F.3    Gandy, S.4
  • 7
    • 0030293854 scopus 로고    scopus 로고
    • Protein topology of presenilin 1
    • Doan, A., Thinakaran, G., Borchelt, D.R. et al. Protein topology of presenilin 1. Neuron 1996, 17: 1023-30.
    • (1996) Neuron , vol.17 , pp. 1023-1030
    • Doan, A.1    Thinakaran, G.2    Borchelt, D.R.3
  • 8
    • 15844425969 scopus 로고    scopus 로고
    • Endoprotreolysis of presenilin 1 and accumulation of processed derivatives in vivo
    • Thinakaran, G., Borchelt, D.R., Lee, M.K. et al. Endoprotreolysis of presenilin 1 and accumulation of processed derivatives in vivo. Neuron 1996, 17: 181-90.
    • (1996) Neuron , vol.17 , pp. 181-190
    • Thinakaran, G.1    Borchelt, D.R.2    Lee, M.K.3
  • 9
    • 0030667426 scopus 로고    scopus 로고
    • Evidence that levels of presenilins (PS1 and PS2) are coordinately regulated by competition for limiting cellular factors
    • Thinakaran, G., Harris, C.L., Ratovitski, T. et al. Evidence that levels of presenilins (PS1 and PS2) are coordinately regulated by competition for limiting cellular factors. J Biol Chem 1997, 272: 28415-22.
    • (1997) J Biol Chem , vol.272 , pp. 28415-28422
    • Thinakaran, G.1    Harris, C.L.2    Ratovitski, T.3
  • 11
    • 0032524865 scopus 로고    scopus 로고
    • Subcellular distribution and turnover of presenilins in transfected cells
    • Zhang, J., Kang, D.E., Xia, W. et al. Subcellular distribution and turnover of presenilins in transfected cells. J Biol Chem 1998, 273: 12436-42.
    • (1998) J Biol Chem , vol.273 , pp. 12436-12442
    • Zhang, J.1    Kang, D.E.2    Xia, W.3
  • 12
    • 0030293676 scopus 로고    scopus 로고
    • Familial Alzheimer's disease-linked presenilin 1 variants elevate Aβ1-42/I-40 ratio in vitro and in vivo
    • Borchelt, D.R., Thinakaran, G., Eckman, C.B. et al. Familial Alzheimer's disease-linked presenilin 1 variants elevate Aβ1-42/I-40 ratio in vitro and in vivo. Neuron 1996, 17: 1005-13.
    • (1996) Neuron , vol.17 , pp. 1005-1013
    • Borchelt, D.R.1    Thinakaran, G.2    Eckman, C.B.3
  • 13
    • 0030868903 scopus 로고    scopus 로고
    • Alternative cleavage of Alzheimer-associated pesenilins during apoptosis by a caspase-3 family protease
    • Kim, T.W., Pettingell, W.H., Jung, Y.K., Kovacs, D.M. and Tanzi, R.E. Alternative cleavage of Alzheimer-associated pesenilins during apoptosis by a caspase-3 family protease. Science 1997, 277: 373-6.
    • (1997) Science , vol.277 , pp. 373-376
    • Kim, T.W.1    Pettingell, W.H.2    Jung, Y.K.3    Kovacs, D.M.4    Tanzi, R.E.5
  • 14
    • 0030873546 scopus 로고    scopus 로고
    • Presenilins are processed by caspase-type proteases
    • Loetscher, H., Deuschle, U., Brockhaus, M. et al. Presenilins are processed by caspase-type proteases. J Biol Chem 1997, 272: 20655-9.
    • (1997) J Biol Chem , vol.272 , pp. 20655-20659
    • Loetscher, H.1    Deuschle, U.2    Brockhaus, M.3
  • 15
    • 0032720496 scopus 로고    scopus 로고
    • Presenilin 1 controls γ-secretase processing of amyloid precursor protein in preGolgi compartments of hippocampal neurons
    • Annaert, W.G., Levesque, L., Craessaerts, K. et al. Presenilin 1 controls γ-secretase processing of amyloid precursor protein in preGolgi compartments of hippocampal neurons. J Cell Biol 1999, 147: 277-94.
    • (1999) J Cell Biol , vol.147 , pp. 277-294
    • Annaert, W.G.1    Levesque, L.2    Craessaerts, K.3
  • 16
    • 8044231311 scopus 로고    scopus 로고
    • The Alzheimer's disease associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum
    • Walter, J., Capell, A., Grunberg, J. et al. The Alzheimer's disease associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum. Molec Med 1996, 2: 673-91.
    • (1996) Molec Med , vol.2 , pp. 673-691
    • Walter, J.1    Capell, A.2    Grunberg, J.3
  • 17
    • 0032564388 scopus 로고    scopus 로고
    • Presenilin I regulates the processing APP C-terminal fragments and the generation of amyloid β-protein in ER and Golgi
    • Xia, W., Zhang, J., Ostaszewski, B.L. et al. Presenilin I regulates the processing APP C-terminal fragments and the generation of amyloid β-protein in ER and Golgi. Biochem 1998, 37: 16465-71.
    • (1998) Biochem , vol.37 , pp. 16465-16471
    • Xia, W.1    Zhang, J.2    Ostaszewski, B.L.3
  • 18
    • 0035921427 scopus 로고    scopus 로고
    • The discrepancy between presenilin subcellular localization and γ-secretase processing of amyloid precursor protein
    • Cupers, P., Bentahir, M., Craessaerts, K. et al. The discrepancy between presenilin subcellular localization and γ-secretase processing of amyloid precursor protein. J Cell Biol 2001, 154: 731-40.
    • (2001) J Cell Biol , vol.154 , pp. 731-740
    • Cupers, P.1    Bentahir, M.2    Craessaerts, K.3
  • 19
    • 0033845327 scopus 로고    scopus 로고
    • Endogenous presenilin-1 targets to endocytic rather than biosynthetic compartments
    • Lah, J.J. and Levey, A.I. Endogenous presenilin-1 targets to endocytic rather than biosynthetic compartments. Mol Cell Neurosci 2000, 16: 111-26.
    • (2000) Mol Cell Neurosci , vol.16 , pp. 111-126
    • Lah, J.J.1    Levey, A.I.2
  • 20
    • 0033579505 scopus 로고    scopus 로고
    • Cell surface presenilin-1 participates in the γ-secretase-like proteolysis of notch
    • Ray, W.J., Yao, M., Mumm, J. et al. Cell surface presenilin-1 participates in the γ-secretase-like proteolysis of notch. J Biol Chem 1999, 274: 36801-7.
    • (1999) J Biol Chem , vol.274 , pp. 36801-36807
    • Ray, W.J.1    Yao, M.2    Mumm, J.3
  • 21
    • 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
    • Georgakopoulos, A., Marambaud, P., Efthimiopoulos, S. et al. Presenilin-1 forms complexes with the cadherin/catenin cell-cell adhesion system and is recruited to intercellular and synaptic contacts. Mol Cell 1999, 4: 893-902.
    • (1999) Mol Cell , vol.4 , pp. 893-902
    • Georgakopoulos, A.1    Marambaud, P.2    Efthimiopoulos, S.3
  • 22
    • 0036327098 scopus 로고    scopus 로고
    • Presenilin-1 affects trafficking and processing of βAPP and is targeted in a complex with to the plasma membrane
    • Kaether, C., Lammich, S., Edbauer, D. et al. Presenilin-1 affects trafficking and processing of βAPP and is targeted in a complex with to the plasma membrane. J Cell Biol 2002, 158: 551-61.
    • (2002) J Cell Biol , vol.158 , pp. 551-561
    • Kaether, C.1    Lammich, S.2    Edbauer, D.3
  • 23
    • 0034645063 scopus 로고    scopus 로고
    • Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation
    • Mah, A., Perry, G., Smith, M. and Monteiro, M. Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation. J Cell Biol 2000, 151: 847-62.
    • (2000) J Cell Biol , vol.151 , pp. 847-862
    • Mah, A.1    Perry, G.2    Smith, M.3    Monteiro, M.4
  • 24
    • 0035903090 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 regulates presenilin 1 C-terminal fragment levels
    • Kirschenbaum, F., Hsu, S.-C., Cordell, B. and McCarthy, J. Glycogen synthase kinase-3 regulates presenilin 1 C-terminal fragment levels. J Biol Chem 2001, 276: 30701-7.
    • (2001) J Biol Chem , vol.276 , pp. 30701-30707
    • Kirschenbaum, F.1    Hsu, S.-C.2    Cordell, B.3    McCarthy, J.4
  • 25
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity
    • Wolfe, M.S., Xia, W., Ostaszewski, B.L., Diehl, T.S., Kimberly, W.T. and Selkoe, D.J. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity. Nature 1999, 398: 513-7.
    • (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
  • 26
    • 0032556859 scopus 로고    scopus 로고
    • Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
    • De Strooper, B., Saftig, P., Craessaerts, K. et al. Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature 1998, 391: 387-90.
    • (1998) Nature , vol.391 , pp. 387-390
    • De Strooper, B.1    Saftig, P.2    Craessaerts, K.3
  • 28
    • 17944376442 scopus 로고    scopus 로고
    • APP processing and synaptic plasticity in presenilin-1 conditional knockout mice
    • Yu, H., Saura, C., Choi, S. et al. APP processing and synaptic plasticity in presenilin-1 conditional knockout mice. Neuron 2001, 31: 713-26.
    • (2001) Neuron , vol.31 , pp. 713-726
    • Yu, H.1    Saura, C.2    Choi, S.3
  • 29
    • 0033214070 scopus 로고    scopus 로고
    • A loss of function mutation of presenilin-2 interferes with amyloid α-peptide production and Notch signaling
    • Steiner, H., Duff, K., Capell, A. et al. A loss of function mutation of presenilin-2 interferes with amyloid α-peptide production and Notch signaling. J Biol Chem 1999, 274: 28669-73.
    • (1999) J Biol Chem , vol.274 , pp. 28669-28673
    • Steiner, H.1    Duff, K.2    Capell, A.3
  • 30
    • 0000792598 scopus 로고    scopus 로고
    • The transmembrane aspartates in presenilin 1 and 2 are obligatory for γ-secretase activity and amyloid β-protein generation
    • Kimberly, W.T., Xia, W., Rahmati, R., Wolfe, M.S. and Selkoe, D.J. The transmembrane aspartates in presenilin 1 and 2 are obligatory for γ-secretase activity and amyloid β-protein generation. J Biol Chem 2000, 275:3173-8.
    • (2000) J Biol Chem , vol.275 , pp. 3173-3178
    • Kimberly, W.T.1    Xia, W.2    Rahmati, R.3    Wolfe, M.S.4    Selkoe, D.J.5
  • 31
    • 0034255029 scopus 로고    scopus 로고
    • Presenilin complexes with the C-terminal fragments of amyloid precursor protein at the sites of amyloid β-protein generation
    • Xia, W., Ray, W.J., Ostaszewski, B.L. et al. Presenilin complexes with the C-terminal fragments of amyloid precursor protein at the sites of amyloid β-protein generation. Proc Natl Acad Sci USA 2000, 97: 9299-304.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9299-9304
    • Xia, W.1    Ray, W.J.2    Ostaszewski, B.L.3
  • 32
    • 0034523058 scopus 로고    scopus 로고
    • FAD mutations in presenilin-1 or amyloid precursor protein decrease the efficacy of a γ-secretase inhibitor: A direct involvement of PS1 in the γ-secretase cleavage complex
    • Xia, W., Ostaszewski, B.L., Kimberly, W.T. et al. FAD mutations in presenilin-1 or amyloid precursor protein decrease the efficacy of a γ-secretase inhibitor: A direct involvement of PS1 in the γ-secretase cleavage complex. Neurobiol Dis 2000, 7: 673-81.
    • (2000) Neurobiol Dis , vol.7 , pp. 673-681
    • Xia, W.1    Ostaszewski, B.L.2    Kimberly, W.T.3
  • 33
    • 0033780472 scopus 로고    scopus 로고
    • Transition-state analog inhibitors of γ-secretase bind directly to presenilin-1
    • Esler, W.P., Kimberly, W.T., Ostaszewski, B.L. et al. Transition-state analog inhibitors of γ-secretase bind directly to presenilin-1. Nat Cell Biol 2000, 2: 428-34.
    • (2000) Nat Cell Biol , vol.2 , pp. 428-434
    • Esler, W.P.1    Kimberly, W.T.2    Ostaszewski, B.L.3
  • 34
    • 0034621824 scopus 로고    scopus 로고
    • Photo-activated γ-secretase inhibitors directed to the active site covalently label presenilin 1
    • Li, Y.-M., Xu, M., Lai, M.-T. et al. Photo-activated γ-secretase inhibitors directed to the active site covalently label presenilin 1. Nature 2000, 405: 689-94.
    • (2000) Nature , vol.405 , pp. 689-694
    • Li, Y.-M.1    Xu, M.2    Lai, M.-T.3
  • 35
    • 0034602419 scopus 로고    scopus 로고
    • Presenilin-1 and -2 are molecular targets for γ-secretase inhibitors
    • Seiffert, D., Bradley, J.D., Rominger, C.M. et al. Presenilin-1 and -2 are molecular targets for γ-secretase inhibitors. J Biol Chem 2000, 275: 34086-91.
    • (2000) J Biol Chem , vol.275 , pp. 34086-34091
    • Seiffert, D.1    Bradley, J.D.2    Rominger, C.M.3
  • 36
    • 0033778262 scopus 로고    scopus 로고
    • Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases
    • Steiner, H., Kostka, M., Romig, H. et al. Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases. Nat Cell Biol 2000, 2: 848-51.
    • (2000) Nat Cell Biol , vol.2 , pp. 848-851
    • Steiner, H.1    Kostka, M.2    Romig, H.3
  • 38
    • 0037150672 scopus 로고    scopus 로고
    • Identification of signal peptide peptidase, a presenilin-type aspartic protease
    • Weihofen, A., Binns, K., Lemberg, M.K., Ashman, K. and Martoglio, B. Identification of signal peptide peptidase, a presenilin-type aspartic protease. Science 2002, 296: 2215-8.
    • (2002) Science , vol.296 , pp. 2215-2218
    • Weihofen, A.1    Binns, K.2    Lemberg, M.K.3    Ashman, K.4    Martoglio, B.5
  • 39
    • 12644264304 scopus 로고    scopus 로고
    • Proteolytic processing of the Alzheimer diseas-associated presenilin-1 generates an in vivo substrate for protein kinase C
    • Walter, J., Grunberg, J., Capell, A. et al. Proteolytic processing of the Alzheimer diseas-associated presenilin-1 generates an in vivo substrate for protein kinase C. Proc Natl Acad Sci USA 1997, 94: 5349-54.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5349-5354
    • Walter, J.1    Grunberg, J.2    Capell, A.3
  • 40
    • 12644290265 scopus 로고    scopus 로고
    • Evidence for phosphorylation and oligomeric assembly of presenilin 1
    • Seeger, M., Nordsted, C., Petanceska, S. et al. Evidence for phosphorylation and oligomeric assembly of presenilin 1. Proc Natl Acad Sci USA 1997, 94: 5090-4.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5090-5094
    • Seeger, M.1    Nordsted, C.2    Petanceska, S.3
  • 41
    • 0032488995 scopus 로고    scopus 로고
    • The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass complex
    • Capell, A., Grunberg, J., Pesold, B. et al. The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass complex. J Biol Chem 1998, 273: 3205-11.
    • (1998) J Biol Chem , vol.273 , pp. 3205-3211
    • Capell, A.1    Grunberg, J.2    Pesold, B.3
  • 42
    • 0032568821 scopus 로고    scopus 로고
    • The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains β-catenin
    • Yu, G., Chen, F., Levesque, G. et al. The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains β-catenin. J Biol Chem 1998, 273: 16470-5.
    • (1998) J Biol Chem , vol.273 , pp. 16470-16475
    • Yu, G.1    Chen, F.2    Levesque, G.3
  • 43
    • 0035980073 scopus 로고    scopus 로고
    • The first proline of PALP motif at the C terminus of presenilins is obligatory for stabilization, complex formation and γ-secretase activities of presenilins
    • Tomita, T., Watabiki, T., Takikawa, R. et al. The first proline of PALP motif at the C terminus of presenilins is obligatory for stabilization, complex formation and γ-secretase activities of presenilins. J Biol Chem 2001, 276: 33273-81.
    • (2001) J Biol Chem , vol.276 , pp. 33273-33281
    • Tomita, T.1    Watabiki, T.2    Takikawa, R.3
  • 44
    • 0034282749 scopus 로고    scopus 로고
    • Mutation of conserved aspartates affects maturation of both aspartate mutant and endogenous presenilin 1 and presenilin 2 complexes
    • Yu, G., Chen, F., Nishimura, M. et al. Mutation of conserved aspartates affects maturation of both aspartate mutant and endogenous presenilin 1 and presenilin 2 complexes. J Biol Chem 2000, 275: 27348-53.
    • (2000) J Biol Chem , vol.275 , pp. 27348-27353
    • Yu, G.1    Chen, F.2    Nishimura, M.3
  • 45
    • 0037022644 scopus 로고    scopus 로고
    • Activity dependent isolation of the presenilin-γ-secretase complex reveals nicastrin and a g substrate
    • Esler, W.P., Kimberly, W., Ostaszewski, B. et al. Activity dependent isolation of the presenilin-γ-secretase complex reveals nicastrin and a g substrate. Proc Natl Acad Sci USA 2002, 99: 2720-5.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2720-2725
    • Esler, W.P.1    Kimberly, W.2    Ostaszewski, B.3
  • 46
    • 0034618715 scopus 로고    scopus 로고
    • Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing
    • Yu, G., Nishimura, M., Arawaka, S. et al. Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing. Nature 2000, 407: 48-54.
    • (2000) Nature , vol.407 , pp. 48-54
    • Yu, G.1    Nishimura, M.2    Arawaka, S.3
  • 47
    • 0035204206 scopus 로고    scopus 로고
    • Nicastrin is required for presenilin mediated transmembrane cleavage in Drosophila
    • Chung, H.-M. and Struhl, G. Nicastrin is required for Presenilin mediated transmembrane cleavage in Drosophila. Nat Cell Biol 2001, 3: 1129-32.
    • (2001) Nat Cell Biol , vol.3 , pp. 1129-1132
    • Chung, H.-M.1    Struhl, G.2
  • 48
    • 0036007117 scopus 로고    scopus 로고
    • Nicastrin is required for γ-secretase cleavage of the Drosophila Notch receptor
    • Hu, Y., Ye, Y. and Fortini, M. Nicastrin is required for γ-secretase cleavage of the Drosophila Notch receptor. Dev Cell 2002, 2: 69-78.
    • (2002) Dev Cell , vol.2 , pp. 69-78
    • Hu, Y.1    Ye, Y.2    Fortini, M.3
  • 49
    • 0037173115 scopus 로고    scopus 로고
    • Presenilin and nicastrin regulate each other and determine amyloid β-peptide production via complex formation
    • Edbauer, D., Winkler, E., Haass, C. and Steiner, H. Presenilin and nicastrin regulate each other and determine amyloid β-peptide production via complex formation. Proc Natl Acad Sci USA 2002, 99: 8666-71.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8666-8671
    • Edbauer, D.1    Winkler, E.2    Haass, C.3    Steiner, H.4
  • 50
    • 0037024364 scopus 로고    scopus 로고
    • Complex N-glycosylated form of nicastrin is stabilized and selectively bound to presenilin fragments
    • Tomita, T., Katayama, R., Takikawa, R. and Iwatsubo, T. Complex N-glycosylated form of nicastrin is stabilized and selectively bound to presenilin fragments. FEBS Lett 2002, 520: 117-21.
    • (2002) FEBS Lett , vol.520 , pp. 117-121
    • Tomita, T.1    Katayama, R.2    Takikawa, R.3    Iwatsubo, T.4
  • 51
    • 0037008723 scopus 로고    scopus 로고
    • Mature glycosylation and trafficking of nicastrin modulate its binding to presenilins
    • Yang, D.-S., Tandon, A., Chen, F. et al. Mature glycosylation and trafficking of nicastrin modulate its binding to presenilins. J Biol Chem 2002, 277: 28135-42.
    • (2002) J Biol Chem , vol.277 , pp. 28135-28142
    • Yang, D.-S.1    Tandon, A.2    Chen, F.3
  • 52
    • 0037166349 scopus 로고    scopus 로고
    • Presenilin 1 is required for maturation and cell surface accumulation of nicastrin
    • Leem, J.Y., Vijayan, S., Han, P. et al. Presenilin 1 is required for maturation and cell surface accumulation of nicastrin. J Biol Chem 2002, 277: 19236-40.
    • (2002) J Biol Chem , vol.277 , pp. 19236-19240
    • Leem, J.Y.1    Vijayan, S.2    Han, P.3
  • 53
    • 0037154158 scopus 로고    scopus 로고
    • APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos
    • Goutte, C., Tsunozaki, M., Hale, V.A. and Priess, J.R. APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos. Proc Natl Acad Sci USA 2002, 99: 775-9.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 775-779
    • Goutte, C.1    Tsunozaki, M.2    Hale, V.A.3    Priess, J.R.4
  • 54
    • 18444417998 scopus 로고    scopus 로고
    • aph-1 and pen-2 are required for Notch pathway signaling, γ-secretase cleavage of bAPP and presenilin protein accumulation
    • Francis, R., McGrath, G., Zhang, J. et al. aph-1 and pen-2 are required for Notch pathway signaling, γ-secretase cleavage of bAPP and presenilin protein accumulation. Dev Cell 2002, 3: 85-97.
    • (2002) Dev Cell , vol.3 , pp. 85-97
    • Francis, R.1    McGrath, G.2    Zhang, J.3
  • 55
    • 0037131218 scopus 로고    scopus 로고
    • PEN-2 is an integral component of the γ-secretase complex required for coordinated expression of presenilin and nicastrin
    • Steiner, H., Winkler, E., Edbauer, D. et al. PEN-2 is an integral component of the γ-secretase complex required for coordinated expression of presenilin and nicastrin. J Biol Chem 2002, 277: 39062-5.
    • (2002) J Biol Chem , vol.277 , pp. 39062-39065
    • Steiner, H.1    Winkler, E.2    Edbauer, D.3
  • 56
    • 0037160063 scopus 로고    scopus 로고
    • Mammalian APH-1 interacts with presenilin and nicastrin, and is required for intramembrane proteolysis of APP and notch
    • Lee, S., Shah, S., Li, H., Yu, C., Han, W. and Yu, G. Mammalian APH-1 interacts with presenilin and nicastrin, and is required for intramembrane proteolysis of APP and notch. J Biol Chem 2002, 277: 45013-9.
    • (2002) J Biol Chem , vol.277 , pp. 45013-45019
    • Lee, S.1    Shah, S.2    Li, H.3    Yu, C.4    Han, W.5    Yu, G.6
  • 57
    • 0034774969 scopus 로고    scopus 로고
    • Presenilin-dependent γ-secretase processing of β-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch
    • Sastre, M., Steiner, H., Fuchs, K. et al. Presenilin-dependent γ-secretase processing of β-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch. EMBO Rep 2001, 2: 835-41.
    • (2001) EMBO Rep , vol.2 , pp. 835-841
    • Sastre, M.1    Steiner, H.2    Fuchs, K.3
  • 58
    • 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, F. et al. A novel epsilon-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing. Biochem 2002, 41: 2825-35.
    • (2002) Biochem , vol.41 , pp. 2825-2835
    • Weidemann, A.1    Eggert, S.2    Reinhard, F.3
  • 59
    • 0030889220 scopus 로고    scopus 로고
    • 299 and occur as stable N- and C-terminal fragments in normal and Alzheimer brain tissue
    • 299 and occur as stable N- and C-terminal fragments in normal and Alzheimer brain tissue. Neurobiol Dis 1997, 3: 325-37.
    • (1997) Neurobiol Dis , vol.3 , pp. 325-337
    • Podlisny, M.B.1    Citron, M.2    Amarante, P.3
  • 60
    • 0033517844 scopus 로고    scopus 로고
    • Amyloidogenic function of the Alzheimer's disease-associated presenilin 1 in the absence of endoproteolysis
    • Steiner, H., Romig, H., Pesold, B. et al. Amyloidogenic function of the Alzheimer's disease-associated presenilin 1 in the absence of endoproteolysis. Biochem 1999, 38: 14600-5.
    • (1999) Biochem , vol.38 , pp. 14600-14605
    • Steiner, H.1    Romig, H.2    Pesold, B.3
  • 61
    • 0035929554 scopus 로고    scopus 로고
    • Distinct intramembrane cleavage of the β-amyloid precursor protein family resembling γ-secretase-like cleavage of Notch
    • Gu, Y., Misonou, H., Sato, T., Dohmae, N., Takio, K. and Ihara, Y. Distinct intramembrane cleavage of the β-amyloid precursor protein family resembling γ-secretase-like cleavage of Notch. J Biol Chem 2001, 276: 35235-8.
    • (2001) J Biol Chem , vol.276 , pp. 35235-35238
    • Gu, Y.1    Misonou, H.2    Sato, T.3    Dohmae, N.4    Takio, K.5    Ihara, Y.6
  • 62
    • 0035941278 scopus 로고    scopus 로고
    • Characterization of a presenilin-mediated amyloid precursor protein carboxyl-terminal fragment gamma. Evidence for distinct mechanisms involved in γ-secretase processing of the APP and Notch1 transmembrane domains
    • Yu, C., Kim, S.H., Ikeuchi, T. et al. Characterization of a presenilin-mediated amyloid precursor protein carboxyl-terminal fragment gamma. Evidence for distinct mechanisms involved in γ-secretase processing of the APP and Notch1 transmembrane domains. J Biol Chem 2001, 276: 43756-60.
    • (2001) J Biol Chem , vol.276 , pp. 43756-43760
    • Yu, C.1    Kim, S.H.2    Ikeuchi, T.3
  • 63
    • 0037066084 scopus 로고    scopus 로고
    • Endoproteolysis of presenilin in vitro: Inhibition by γ-secretase inhibitors
    • Campbell, W., Iskandar, M.-K., Reed, M. and Xia, W. Endoproteolysis of presenilin in vitro: Inhibition by γ-secretase inhibitors. Biochem 2002, 41: 3372-9.
    • (2002) Biochem , vol.41 , pp. 3372-3379
    • Campbell, W.1    Iskandar, M.-K.2    Reed, M.3    Xia, W.4
  • 64
    • 0035977071 scopus 로고    scopus 로고
    • Pharmacological knock-down of the presenilin I heterodimer by a novel γ-secretase inhibitor: Implications for presenilin biology
    • Beher, D., Wrigley, J.D., Nadin, A. et al. Pharmacological knock-down of the presenilin I heterodimer by a novel γ-secretase inhibitor: Implications for presenilin biology. J Biol Chem 2001, 276: 45394-402.
    • (2001) J Biol Chem , vol.276 , pp. 45394-45402
    • Beher, D.1    Wrigley, J.D.2    Nadin, A.3
  • 65
    • 0031968723 scopus 로고    scopus 로고
    • Presenilin 1 is actively degraded by the 26S proteasome
    • Fraser, P.E., Levesque, G., Yu, G. et al. Presenilin 1 is actively degraded by the 26S proteasome. Neurobiol Aging 1998, 19: S19-21.
    • (1998) Neurobiol Aging , vol.19
    • Fraser, P.E.1    Levesque, G.2    Yu, G.3
  • 66
    • 0033610863 scopus 로고    scopus 로고
    • Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation
    • Steiner, H., Capell, A., Pesold, B. et al. Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation. J Biol Chem 1998, 273: 32322-31.
    • (1998) J Biol Chem , vol.273 , pp. 32322-32331
    • Steiner, H.1    Capell, A.2    Pesold, B.3
  • 67
    • 0033605588 scopus 로고    scopus 로고
    • Calpain inhibitor 1 increases β-amyloid peptide production by inhibiting the degradation of the substrate of γ-secretase. Evidence that substrate availability limits β-amyloid peptide production
    • Zhang, L., Song, L. and Parker, E.M. Calpain inhibitor 1 increases β-amyloid peptide production by inhibiting the degradation of the substrate of γ-secretase. Evidence that substrate availability limits β-amyloid peptide production. J Biol Chem 1999, 274: 8966-72.
    • (1999) J Biol Chem , vol.274 , pp. 8966-8972
    • Zhang, L.1    Song, L.2    Parker, E.M.3
  • 68
    • 0034142022 scopus 로고    scopus 로고
    • A distinct ER/IC γ-secretase competes with the proteasome for cleavage of APP
    • Skovronsky, D.M., Pijak, D.S., Doms, R.W., and Lee, V.M. A distinct ER/IC γ-secretase competes with the proteasome for cleavage of APP. Biochem 2000, 39: 810-7.
    • (2000) Biochem , vol.39 , pp. 810-817
    • Skovronsky, D.M.1    Pijak, D.S.2    Doms, R.W.3    Lee, V.M.4
  • 69
    • 0034797234 scopus 로고    scopus 로고
    • The C-terminal fragment of the Alzheimer's disease amyloid protein precursor is degraded by a proteasome-dependent mechanism distinct from γ-secretase
    • Nunan, J., Shearman, M.S., Checler, F. et al. The C-terminal fragment of the Alzheimer's disease amyloid protein precursor is degraded by a proteasome-dependent mechanism distinct from γ-secretase. Eur J Biochem 2001, 268: 5329-36.
    • (2001) Eur J Biochem , vol.268 , pp. 5329-5336
    • Nunan, J.1    Shearman, M.S.2    Checler, F.3
  • 70
    • 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 2001, 293: 115-20.
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 71
    • 0035909901 scopus 로고    scopus 로고
    • The γ-secretase cleaved C-terminal fragment of amyloid precursor protein mediates signaling to the nucleus
    • Gao, Y. and Pimplikar, S.W. The γ-secretase cleaved C-terminal fragment of amyloid precursor protein mediates signaling to the nucleus. Proc Natl Acad Sci USA 2001, 98: 14979-84.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14979-14984
    • Gao, Y.1    Pimplikar, S.W.2
  • 72
    • 0035955693 scopus 로고    scopus 로고
    • The intracellular domain of the β-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a Notch-like manner
    • Kimberly, W.T., Zheng, J.B., Guenette, S.Y. and Selkoe, D.J. The intracellular domain of the β-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a Notch-like manner. J Biol Chem 2001, 276: 40288-92.
    • (2001) J Biol Chem , vol.276 , pp. 40288-40292
    • Kimberly, W.T.1    Zheng, J.B.2    Guenette, S.Y.3    Selkoe, D.J.4
  • 73
    • 0037076398 scopus 로고    scopus 로고
    • The γ-secretase generated intracellular domain of amyloid precursor protein binds Numb and inhibits Notch signaling
    • Roncarati, R., Sestan, N., Scheinfeld, M. et al. The γ-secretase generated intracellular domain of amyloid precursor protein binds Numb and inhibits Notch signaling. Proc Natl Acad Sci USA 2002, 99: 7102-7.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 7102-7107
    • Roncarati, R.1    Sestan, N.2    Scheinfeld, M.3
  • 74
    • 0033573477 scopus 로고    scopus 로고
    • C terminus of presenilin is required for overproduction of amyloidogenic Aβ42 through stabilization and endoproteolysis of presenilin
    • Tomita, T., Takikawa, R., Koyama, A. et al. C terminus of presenilin is required for overproduction of amyloidogenic Aβ42 through stabilization and endoproteolysis of presenilin. J Neurosci 1999, 19: 10627-34.
    • (1999) J Neurosci , vol.19 , pp. 10627-10634
    • Tomita, T.1    Takikawa, R.2    Koyama, A.3
  • 75
    • 0033551099 scopus 로고    scopus 로고
    • Peptidomimetic probes and molecular modeling suggest Alzheimer's γ-secretase is an intramembrane-cleaving aspartyl protease
    • Wolfe, M.S., Xia, W., Moore, C.L. et al. Peptidomimetic probes and molecular modeling suggest Alzheimer's γ-secretase is an intramembrane-cleaving aspartyl protease. Biochem 1999, 38: 4720-7.
    • (1999) Biochem , vol.38 , pp. 4720-4727
    • Wolfe, M.S.1    Xia, W.2    Moore, C.L.3
  • 76
    • 0037493896 scopus 로고    scopus 로고
    • Beynon, R. and Salvesen, G. (Beynon, R., and Bond, J., eds). Oxford University Press, New York 1996, 241-9
    • Beynon, R. and Salvesen, G. (Beynon, R., and Bond, J., eds). Oxford University Press, New York 1996, 241-9.
    • Beynon, R.1    Salvesen, G.2
  • 77
    • 0034528028 scopus 로고    scopus 로고
    • Toward the characterization and identification of γ-secretases using transition-state analog inhibitors
    • Moore, C., Diehl, T., Selkoe, D. and Wolfe, M. Toward the characterization and identification of γ-secretases using transition-state analog inhibitors. Ann NY Acad Sci 2000, 920: 197-205.
    • (2000) Ann NY Acad Sci , vol.920 , pp. 197-205
    • Moore, C.1    Diehl, T.2    Selkoe, D.3    Wolfe, M.4
  • 78
    • 0031915681 scopus 로고    scopus 로고
    • A substrate-based difluoro ketone selectively inhibits Alzheimer's γ-secretase activity
    • Wolfe, M.S., Citron, M., Diehl, T.S., Xia, W., Donkor, I.O. and Selkoe, D.J. A substrate-based difluoro ketone selectively inhibits Alzheimer's γ-secretase activity. J Med Chem 1998, 41: 6-9.
    • (1998) J Med Chem , vol.41 , pp. 6-9
    • Wolfe, M.S.1    Citron, M.2    Diehl, T.S.3    Xia, W.4    Donkor, I.O.5    Selkoe, D.J.6
  • 79
    • 0033521141 scopus 로고    scopus 로고
    • The influence of endoproteolytic processing of familial Alzheimer's disease presenilin 2 on Aβ42 amyloid peptide formation
    • Jacobsen, H., Reinhardt, D., Brockhaus, M. et al. The influence of endoproteolytic processing of familial Alzheimer's disease presenilin 2 on Aβ42 amyloid peptide formation. J Biol Chem 1999, 274: 35233-9.
    • (1999) J Biol Chem , vol.274 , pp. 35233-35239
    • Jacobsen, H.1    Reinhardt, D.2    Brockhaus, M.3
  • 80
    • 0035923750 scopus 로고    scopus 로고
    • Interaction with telencephalin and the amyloid precursor protein predicts a ring structure for presenilins
    • Annaert, W.G., Esselens, C., Baert, V. et al. Interaction with telencephalin and the amyloid precursor protein predicts a ring structure for presenilins. Neuron 2001, 32: 579-89.
    • (2001) Neuron , vol.32 , pp. 579-589
    • Annaert, W.G.1    Esselens, C.2    Baert, V.3
  • 81
    • 0037468759 scopus 로고    scopus 로고
    • The role of presenilin co-factors in the gamma-secretase complex
    • in press
    • Takasugi, N., Tomita, T., Hayashi, I. et al. The role of presenilin co-factors in the gamma-secretase complex. Nature 2003, in press.
    • (2003) Nature
    • Takasugi, N.1    Tomita, T.2    Hayashi, I.3
  • 82
    • 0038652102 scopus 로고    scopus 로고
    • Gamma-secretase is a member protein complex comprised of presenilin, nicastrin, aph-1 and pen-2
    • in press
    • Kimberly, W., LaVoie, M. Ostaszewski, B. et al. Gamma-secretase is a member protein complex comprised of presenilin, nicastrin, aph-1 and pen-2. Proc Natl Acad Sci USA 2003, in press
    • (2003) Proc Natl Acad Sci USA
    • Kimberly, W.1    LaVoie, M.2    Ostaszewski, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.