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Volumn 5, Issue 2, 2008, Pages 147-157

The catalytic core of γ-secretase: Presenilin revisited

Author keywords

secretase; Alzheimer's disease; Amyloid peptide; Presenilin

Indexed keywords

AMINO ACID; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; GAMMA SECRETASE; NOTCH RECEPTOR; PRESENILIN; PRESENILIN 1; PRESENILIN 2; PROTEINASE;

EID: 42149182981     PISSN: 15672050     EISSN: None     Source Type: Journal    
DOI: 10.2174/156720508783954677     Document Type: Review
Times cited : (34)

References (167)
  • 1
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • Haass C and Selkoe DJ. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide. Nat Rev Mol Cell Biol 8: 101-112 (2007).
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 2
    • 1442264828 scopus 로고    scopus 로고
    • Take five - BACE and the γ-secretase quartet conduct Alzheimer's amyloid β-peptide generation
    • Haass C. Take five - BACE and the γ-secretase quartet conduct Alzheimer's amyloid β-peptide generation. EMBO J 23: 483-488 (2004).
    • (2004) EMBO J , vol.23 , pp. 483-488
    • Haass, C.1
  • 3
    • 28644437291 scopus 로고    scopus 로고
    • The amyloid-β precursor protein: Integrating structure with biological function
    • Reinhard C, Hebert SS and De Strooper B. The amyloid-β precursor protein: integrating structure with biological function. EMBO J 24: 3996-4006 (2005).
    • (2005) EMBO J , vol.24 , pp. 3996-4006
    • Reinhard, C.1    Hebert, S.S.2    De Strooper, B.3
  • 4
    • 0028169925 scopus 로고
    • Visualization of Aβ42(43) and Aβ40 in senile plaques with endspecific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43)
    • Iwatsubo T, Odaka A, Suzuki N, Mizusawa H, Nukina N and Ihara Y. Visualization of Aβ42(43) and Aβ40 in senile plaques with endspecific Aβ monoclonals: evidence that an initially deposited species is Aβ42(43). Neuron 13: 45-53 (1994).
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 5
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-β in Alzheimer's disease
    • Laferla FM, Green KN and Oddo S. Intracellular amyloid-β in Alzheimer's disease. Nat Rev Neurosci 8: 499-509 (2007).
    • (2007) Nat Rev Neurosci , vol.8 , pp. 499-509
    • Laferla, F.M.1    Green, K.N.2    Oddo, S.3
  • 6
    • 0036727463 scopus 로고    scopus 로고
    • Presenilins are not required for Aβ42 production in the early secretory pathway
    • Wilson CA, Doms RW, Zheng H and Lee VM. Presenilins are not required for Aβ42 production in the early secretory pathway. Nat Neurosci 5: 849-855 (2002).
    • (2002) Nat Neurosci , vol.5 , pp. 849-855
    • Wilson, C.A.1    Doms, R.W.2    Zheng, H.3    Lee, V.M.4
  • 8
    • 0028322017 scopus 로고
    • An increased percentage of long amyloid β-protein secreted by familial amyloid β-protein precursor (βAPP717) mutants
    • Suzuki N, Cheung TT, Cai XD, Odaka A, Otvos L Jr., Eckman C, et al. An increased percentage of long amyloid β-protein secreted by familial amyloid β-protein precursor (βAPP717) mutants. Science 264: 1336-1340 (1994).
    • (1994) Science , vol.264 , pp. 1336-1340
    • Suzuki, N.1    Cheung, T.T.2    Cai, X.D.3    Odaka, A.4    Otvos Jr., L.5    Eckman, C.6
  • 9
    • 0033616590 scopus 로고    scopus 로고
    • Ancolio K, Dumanchin C, Barelli H, Warter JM, Brice A, Campion D, et al. Unusual phenotypic alteration of β amyloid precursor protein (βAPP) maturation by a new Val-715 - > Met βAPP-770 mutation responsible for probable early-onset Alzheimer's disease. Proc Natl Acad Sci USA 96: 4119-4124. (1999).
    • Ancolio K, Dumanchin C, Barelli H, Warter JM, Brice A, Campion D, et al. Unusual phenotypic alteration of β amyloid precursor protein (βAPP) maturation by a new Val-715 - > Met βAPP-770 mutation responsible for probable early-onset Alzheimer's disease. Proc Natl Acad Sci USA 96: 4119-4124. (1999).
  • 10
    • 0026745610 scopus 로고
    • Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production
    • Citron M, Oltersdorf T, Haass C, McConlogue L, Hung AY, Seubert P, et al. Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production. Nature 360: 672-674 (1992).
    • (1992) Nature , vol.360 , pp. 672-674
    • Citron, M.1    Oltersdorf, T.2    Haass, C.3    McConlogue, L.4    Hung, A.Y.5    Seubert, P.6
  • 11
    • 0033595706 scopus 로고    scopus 로고
    • β-Secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • Vassar R, Bennett BD, Babu-Khan S, Kahn S, Mendiaz EA, Denis P, et al. β-Secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 286: 735-741 (1999).
    • (1999) Science , vol.286 , pp. 735-741
    • Vassar, R.1    Bennett, B.D.2    Babu-Khan, S.3    Kahn, S.4    Mendiaz, E.A.5    Denis, P.6
  • 12
    • 0035112647 scopus 로고    scopus 로고
    • BACE1 is the major β-secretase for generation of Aβ peptides by neurons
    • Cai H, Wang Y, McCarthy D, Wen H, Borchelt DR, Price DL, et al. BACE1 is the major β-secretase for generation of Aβ peptides by neurons. Nat Neurosci 4: 233-234 (2001).
    • (2001) Nat Neurosci , vol.4 , pp. 233-234
    • Cai, H.1    Wang, Y.2    McCarthy, D.3    Wen, H.4    Borchelt, D.R.5    Price, D.L.6
  • 13
    • 0035116273 scopus 로고    scopus 로고
    • Mice deficient in BACE1, the Alzheimer's β-secretase, have normal phenotype and abolished β-amyloid generation
    • Luo Y, Bolon B, Kahn S, Bennett BD, Babu-Khan S, Denis P, et al. Mice deficient in BACE1, the Alzheimer's β-secretase, have normal phenotype and abolished β-amyloid generation. Nat Neurosci 4: 231-232 (2001).
    • (2001) Nat Neurosci , vol.4 , pp. 231-232
    • Luo, Y.1    Bolon, B.2    Kahn, S.3    Bennett, B.D.4    Babu-Khan, S.5    Denis, P.6
  • 15
    • 33845236399 scopus 로고    scopus 로고
    • Bace1 modulates myelination in the central and peripheral nervous system
    • Hu X, Hicks CW, He W, Wong P, Macklin WB, Trapp BD, et al. Bace1 modulates myelination in the central and peripheral nervous system. Nat Neurosci 9: 1520-1525 (2006).
    • (2006) Nat Neurosci , vol.9 , pp. 1520-1525
    • Hu, X.1    Hicks, C.W.2    He, W.3    Wong, P.4    Macklin, W.B.5    Trapp, B.D.6
  • 19
    • 5144224126 scopus 로고    scopus 로고
    • Coordinated and widespread expression of γ-secretase in vivo: Evidence for size and molecular heterogeneity
    • Hebert SS, Serneels L, Dejaegere T, Horre K, Dabrowski M, Baert V, et al. Coordinated and widespread expression of γ-secretase in vivo: evidence for size and molecular heterogeneity. Neurobiol Dis 17: 260-272 (2004).
    • (2004) Neurobiol Dis , vol.17 , pp. 260-272
    • Hebert, S.S.1    Serneels, L.2    Dejaegere, T.3    Horre, K.4    Dabrowski, M.5    Baert, V.6
  • 20
    • 4744375540 scopus 로고    scopus 로고
    • Identification of distinct γ-secretase complexes with different APH-1 variants
    • Shirotani K, Edbauer D, Prokop S, Haass C and Steiner H. Identification of distinct γ-secretase complexes with different APH-1 variants. J Biol Chem 279: 41340-41345 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 41340-41345
    • Shirotani, K.1    Edbauer, D.2    Prokop, S.3    Haass, C.4    Steiner, H.5
  • 22
    • 33847021476 scopus 로고    scopus 로고
    • Presenilin diversifies its portfolio
    • Parks AL and Curtis D. Presenilin diversifies its portfolio. Trends Genet 23: 140-150 (2007).
    • (2007) Trends Genet , vol.23 , pp. 140-150
    • Parks, A.L.1    Curtis, D.2
  • 23
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
    • Sherrington R, Rogaev EI, Liang Y, Rogaeva EA, Levesque G, Ikeda M, et al. Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature 375: 754-760 (1995).
    • (1995) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1    Rogaev, E.I.2    Liang, Y.3    Rogaeva, E.A.4    Levesque, G.5    Ikeda, M.6
  • 24
    • 0029101491 scopus 로고
    • Familial Alzheimer's disease in kindreds with mis sense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene
    • Rogaev EI, Sherrington R, Rogaeva EA, Levesque G, Ikeda M, Liang Y, et al. Familial Alzheimer's disease in kindreds with mis sense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene. Nature 376: 775-778. (1995).
    • (1995) Nature , vol.376 , pp. 775-778
    • Rogaev, E.I.1    Sherrington, R.2    Rogaeva, E.A.3    Levesque, G.4    Ikeda, M.5    Liang, Y.6
  • 26
    • 23944511109 scopus 로고    scopus 로고
    • Evidence that the COOH terminus of human presenilin 1 is located in extracytoplasmic space
    • Oh YS and Turner RJ. Evidence that the COOH terminus of human presenilin 1 is located in extracytoplasmic space. Am J Physiol Cell Physiol 289: C576-581 (2005).
    • (2005) Am J Physiol Cell Physiol , vol.289
    • Oh, Y.S.1    Turner, R.J.2
  • 27
    • 20444481683 scopus 로고    scopus 로고
    • A novel transmembrane topology of presenilin based on reconciling experimental and computational evidence
    • Henricson A, Kall L and Sonnhammer EL. A novel transmembrane topology of presenilin based on reconciling experimental and computational evidence. FEBS J 272: 2727-2733 (2005).
    • (2005) FEBS J , vol.272 , pp. 2727-2733
    • Henricson, A.1    Kall, L.2    Sonnhammer, E.L.3
  • 29
    • 33748746861 scopus 로고    scopus 로고
    • Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway
    • Spasic D, Tolia A, Dillen K, Baert V, De Strooper B, Vrijens S, et al. Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway. J Biol Chem 281: 26569-26577 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 26569-26577
    • Spasic, D.1    Tolia, A.2    Dillen, K.3    Baert, V.4    De Strooper, B.5    Vrijens, S.6
  • 30
    • 15844425969 scopus 로고    scopus 로고
    • Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo
    • Thinakaran G, Borchelt DR, Lee MK, Slunt HH, Spitzer L, Kim G, et al. Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo. Neuron 17: 181-190 (1996).
    • (1996) Neuron , vol.17 , pp. 181-190
    • Thinakaran, G.1    Borchelt, D.R.2    Lee, M.K.3    Slunt, H.H.4    Spitzer, L.5    Kim, G.6
  • 31
    • 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 linked to familial Alzheimer's disease
    • Scheuner D, Eckman C, Jensen M, Song X, Citron M, Suzuki N, et al. 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 linked to familial Alzheimer's disease. Nat Med 2: 864-870 (1996).
    • (1996) Nat Med , vol.2 , pp. 864-870
    • Scheuner, D.1    Eckman, C.2    Jensen, M.3    Song, X.4    Citron, M.5    Suzuki, N.6
  • 32
    • 18444391830 scopus 로고    scopus 로고
    • Presenilin-1 mutations of leucine 166 equally affect the generation of the Notch and APP intracellular domains independent of their effect on Aβ42 production
    • Moehlmann T, Winkler E, Xia X, Edbauer D, Murrell J, Capell A, et al. Presenilin-1 mutations of leucine 166 equally affect the generation of the Notch and APP intracellular domains independent of their effect on Aβ42 production. Proc Natl Acad Sci USA 99: 8025-8030 (2002).
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8025-8030
    • Moehlmann, T.1    Winkler, E.2    Xia, X.3    Edbauer, D.4    Murrell, J.5    Capell, A.6
  • 33
    • 33645105621 scopus 로고    scopus 로고
    • Presenilin clinical mutations can affect γ-secretase activity by different mechanisms
    • Bentahir M, Nyabi O, Verhamme J, Tolia A, Horre K, Wiltfang J, et al. Presenilin clinical mutations can affect γ-secretase activity by different mechanisms. J Neurochem 96: 732-742 (2006).
    • (2006) J Neurochem , vol.96 , pp. 732-742
    • Bentahir, M.1    Nyabi, O.2    Verhamme, J.3    Tolia, A.4    Horre, K.5    Wiltfang, J.6
  • 34
    • 33745700370 scopus 로고    scopus 로고
    • Mean age-of-onset of familial Alzheimer disease caused by presenilin mutations correlates with both increased Aβ42 and decreased Aβ40
    • Kumar-Singh S, Theuns J, Van Broeck B, Pirici D, Vennekens K, Corsmit E, et al. Mean age-of-onset of familial Alzheimer disease caused by presenilin mutations correlates with both increased Aβ42 and decreased Aβ40. Hum Mutat 27: 686-695 (2006).
    • (2006) Hum Mutat , vol.27 , pp. 686-695
    • Kumar-Singh, S.1    Theuns, J.2    Van Broeck, B.3    Pirici, D.4    Vennekens, K.5    Corsmit, E.6
  • 35
    • 13844275951 scopus 로고    scopus 로고
    • Mean age of onset in familial Alzheimer's disease is determined by amyloid β 42
    • Duering M, Grimm MO, Grimm HS, Schroder J and Hartmann T. Mean age of onset in familial Alzheimer's disease is determined by amyloid β 42. Neurobiol Aging 26: 785-788 (2005).
    • (2005) Neurobiol Aging , vol.26 , pp. 785-788
    • Duering, M.1    Grimm, M.O.2    Grimm, H.S.3    Schroder, J.4    Hartmann, T.5
  • 36
    • 13244299288 scopus 로고    scopus 로고
    • Presenilin 2 familial Alzheimer's disease mutations result in partial loss of function and dramatic changes in Aβ42/40 ratios
    • Walker ES, Martinez M, Brunkan AL and Goate A. Presenilin 2 familial Alzheimer's disease mutations result in partial loss of function and dramatic changes in Aβ42/40 ratios. J Neurochem 92: 294-301 (2005).
    • (2005) J Neurochem , vol.92 , pp. 294-301
    • Walker, E.S.1    Martinez, M.2    Brunkan, A.L.3    Goate, A.4
  • 37
    • 10544229795 scopus 로고    scopus 로고
    • Expression of presenilin 1 and 2 (PS1 and PS2) in human and murine tissues
    • Lee MK, Slunt HH, Martin LJ, Thinakaran G, Kim G, Gandy SE, et al. Expression of presenilin 1 and 2 (PS1 and PS2) in human and murine tissues. J Neurosci 16: 7513-7525 (1996).
    • (1996) J Neurosci , vol.16 , pp. 7513-7525
    • Lee, M.K.1    Slunt, H.H.2    Martin, L.J.3    Thinakaran, G.4    Kim, G.5    Gandy, S.E.6
  • 38
    • 0037590902 scopus 로고    scopus 로고
    • Presenilin-1 and presenilin-2 exhibit distinct yet overlapping γ-secretase activities
    • Lai MT, Chen E, Crouthamel MC, DiMuzio-Mower J, Xu M, Huang Q, et al. Presenilin-1 and presenilin-2 exhibit distinct yet overlapping γ-secretase activities. J Biol Chem 278: 22475-22481 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 22475-22481
    • Lai, M.T.1    Chen, E.2    Crouthamel, M.C.3    DiMuzio-Mower, J.4    Xu, M.5    Huang, Q.6
  • 39
    • 0029116848 scopus 로고
    • Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene
    • Levitan D and Greenwald I. Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene. Nature 377: 351-354 (1995).
    • (1995) Nature , vol.377 , pp. 351-354
    • Levitan, D.1    Greenwald, I.2
  • 44
    • 0032574993 scopus 로고    scopus 로고
    • Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain
    • Schroeter EH, Kisslinger JA and Kopan R. Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain. Nature 393: 382-386 (1998).
    • (1998) Nature , vol.393 , pp. 382-386
    • Schroeter, E.H.1    Kisslinger, J.A.2    Kopan, R.3
  • 45
    • 0033868818 scopus 로고    scopus 로고
    • A novel proteolytic cleavage involved in Notch signaling: The role of the disintegrin-metalloprotease TACE
    • Brou C, Logeat F, Gupta N, Bessia C, LeBail O, Doedens JR, et al. A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE. Mol Cell 5: 207-216 (2000).
    • (2000) Mol Cell , vol.5 , pp. 207-216
    • Brou, C.1    Logeat, F.2    Gupta, N.3    Bessia, C.4    LeBail, O.5    Doedens, J.R.6
  • 46
    • 0033867521 scopus 로고    scopus 로고
    • A ligand-induced extracellular cleavage regulates γ-secretase-like proteolytic activation of Notch1
    • Mumm JS, Schroeter EH, Saxena MT, Griesemer A, Tian X, Pan DJ, et al. A ligand-induced extracellular cleavage regulates γ-secretase-like proteolytic activation of Notch1. Mol Cell 5: 197-206 (2000).
    • (2000) Mol Cell , vol.5 , pp. 197-206
    • Mumm, J.S.1    Schroeter, E.H.2    Saxena, M.T.3    Griesemer, A.4    Tian, X.5    Pan, D.J.6
  • 47
    • 0032524325 scopus 로고    scopus 로고
    • Nuclear access and action of Notch in vivo
    • Struhl G and Adachi A. Nuclear access and action of Notch in vivo. Cell 93: 649-660 (1998).
    • (1998) Cell , vol.93 , pp. 649-660
    • Struhl, G.1    Adachi, A.2
  • 48
    • 0033535508 scopus 로고    scopus 로고
    • Presenilin is required for activity and nuclear access of Notch in Drosophila
    • Struhl G and Greenwald I. Presenilin is required for activity and nuclear access of Notch in Drosophila. Nature 398: 522-525 (1999).
    • (1999) Nature , vol.398 , pp. 522-525
    • Struhl, G.1    Greenwald, I.2
  • 49
    • 0033535504 scopus 로고    scopus 로고
    • A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain
    • De Strooper B, Annaert W, Cupers P, Saftig P, Craessaerts K, Mumm JS, et al. A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain. Nature 398: 518-522 (1999).
    • (1999) Nature , vol.398 , pp. 518-522
    • De Strooper, B.1    Annaert, W.2    Cupers, P.3    Saftig, P.4    Craessaerts, K.5    Mumm, J.S.6
  • 51
    • 0033779635 scopus 로고    scopus 로고
    • Presenilins are required for γ-secretase cleavage of βAPP and transmembrane cleavage of Notch-1
    • Zhang Z, Nadeau P, Song W, Donoviel D, Yuan M, Bernstein A, et al. Presenilins are required for γ-secretase cleavage of βAPP and transmembrane cleavage of Notch-1. Nat Cell Biol 2: 463-465 (2000).
    • (2000) Nat Cell Biol , vol.2 , pp. 463-465
    • Zhang, Z.1    Nadeau, P.2    Song, W.3    Donoviel, D.4    Yuan, M.5    Bernstein, A.6
  • 52
    • 0033597105 scopus 로고    scopus 로고
    • γ-Secretase, evidence for multiple proteolytic activities and influence of membrane positioning of substrate on generation of amyloid β peptides of varying length
    • Murphy MP, Hickman LJ, Eckman CB, Uljon SN, Wang R and Golde TE. γ-Secretase, evidence for multiple proteolytic activities and influence of membrane positioning of substrate on generation of amyloid β peptides of varying length. J Biol Chem 274: 11914-11923 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 11914-11923
    • Murphy, M.P.1    Hickman, L.J.2    Eckman, C.B.3    Uljon, S.N.4    Wang, R.5    Golde, T.E.6
  • 53
    • 0031915681 scopus 로고    scopus 로고
    • A substrate-based difluoro ketone selectively inhibits Alzheimer's γ-secretase activity
    • Wolfe MS, Citron M, Diehl TS, Xia W, Donkor IO and Selkoe DJ. A substrate-based difluoro ketone selectively inhibits Alzheimer's γ-secretase activity. J Med Chem 41: 6-9 (1998).
    • (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
  • 54
    • 0033551099 scopus 로고    scopus 로고
    • Peptidomimetic probes and molecular modeling suggest that Alzheimer's γ-secretase is an intramembrane-cleaving aspartyl protease
    • Wolfe MS, Xia W, Moore CL, Leatherwood DD, Ostaszewski B, Rahmati T, et al. Peptidomimetic probes and molecular modeling suggest that Alzheimer's γ-secretase is an intramembrane-cleaving aspartyl protease. Biochemistry 38: 4720-4727 (1999).
    • (1999) Biochemistry , vol.38 , pp. 4720-4727
    • Wolfe, M.S.1    Xia, W.2    Moore, C.L.3    Leatherwood, D.D.4    Ostaszewski, B.5    Rahmati, T.6
  • 55
    • 0034254585 scopus 로고    scopus 로고
    • L-685,458, an aspartyl protease transition state mimic, is a potent inhibitor of amyloid β-protein precursor γ-secretase activity
    • Shearman MS, Beher D, Clarke EE, Lewis HD, Harrison T, Hunt P, et al. L-685,458, an aspartyl protease transition state mimic, is a potent inhibitor of amyloid β-protein precursor γ-secretase activity. Biochemistry 39: 8698-8704 (2000).
    • (2000) Biochemistry , vol.39 , pp. 8698-8704
    • Shearman, M.S.1    Beher, D.2    Clarke, E.E.3    Lewis, H.D.4    Harrison, T.5    Hunt, P.6
  • 57
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity
    • Wolfe MS, Xia W, Ostaszewski BL, Diehl TS, Kimberly WT and Selkoe DJ. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity. Nature 398: 513-517 (1999).
    • (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
  • 58
    • 0033214070 scopus 로고    scopus 로고
    • A loss of function mutation of presenilin-2 interferes with amyloid β-peptide production and Notch signaling
    • Steiner H, Duff K, Capell A, Romig H, Grim MG, Lincoln S, et al. A loss of function mutation of presenilin-2 interferes with amyloid β-peptide production and Notch signaling. J Biol Chem 274: 28669-28673 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 28669-28673
    • Steiner, H.1    Duff, K.2    Capell, A.3    Romig, H.4    Grim, M.G.5    Lincoln, S.6
  • 59
    • 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 WT, Xia W, Rahmati T, Wolfe MS and Selkoe DJ. The transmembrane aspartates in presenilin 1 and 2 are obligatory for γ-secretase activity and amyloid β-protein generation. J Biol Chem 275: 3173-3178 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 3173-3178
    • Kimberly, W.T.1    Xia, W.2    Rahmati, T.3    Wolfe, M.S.4    Selkoe, D.J.5
  • 60
    • 0033550061 scopus 로고    scopus 로고
    • Zebrafish (Danio rerio) presenilin promotes aberrant amyloid β-peptide production and requires a critical aspartate residue for its function in amyloidogenesis
    • Leimer U, Lun K, Romig H, Walter J, Grünberg J, Brand M, et al. Zebrafish (Danio rerio) presenilin promotes aberrant amyloid β-peptide production and requires a critical aspartate residue for its function in amyloidogenesis. Biochemistry 38: 13602-13609 (1999).
    • (1999) Biochemistry , vol.38 , pp. 13602-13609
    • Leimer, U.1    Lun, K.2    Romig, H.3    Walter, J.4    Grünberg, J.5    Brand, M.6
  • 62
    • 0034621824 scopus 로고    scopus 로고
    • Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1
    • Li YM, Xu M, Lai MT, Huang Q, Castro JL, DiMuzio-Mower J, et al. Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1. Nature 405: 689-694 (2000).
    • (2000) Nature , vol.405 , pp. 689-694
    • Li, Y.M.1    Xu, M.2    Lai, M.T.3    Huang, Q.4    Castro, J.L.5    DiMuzio-Mower, J.6
  • 64
    • 0035159756 scopus 로고    scopus 로고
    • The β-secretase, BACE. A prime target for Alzheimer's disease
    • Vassar R. The β-secretase, BACE. A prime target for Alzheimer's disease. J Mol Neurosci 17: 157-170 (2001).
    • (2001) J Mol Neurosci , vol.17 , pp. 157-170
    • Vassar, R.1
  • 65
    • 0033778262 scopus 로고    scopus 로고
    • Glycine 384 is required for presenilin-1 function and is conserved in polytopic bacterial aspartyl proteases
    • Steiner H, Kostka M, Romig H, Basset G, Pesold B, Hardy J, et al. Glycine 384 is required for presenilin-1 function and is conserved in polytopic bacterial aspartyl proteases. Nat Cell Biol 2: 848-851 (2000).
    • (2000) Nat Cell Biol , vol.2 , pp. 848-851
    • Steiner, H.1    Kostka, M.2    Romig, H.3    Basset, G.4    Pesold, B.5    Hardy, J.6
  • 66
    • 0033978638 scopus 로고    scopus 로고
    • The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases
    • LaPointe CF and Taylor RK. The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases. J Biol Chem 275: 1502-1510 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 1502-1510
    • LaPointe, C.F.1    Taylor, R.K.2
  • 67
    • 0037150672 scopus 로고    scopus 로고
    • Identification of signal peptide peptidase, a presenilin-type aspartic protease
    • Weihofen A, Binns K, Lemberg MK, Ashman K and Martoglio B. Identification of signal peptide peptidase, a presenilin-type aspartic protease. Science 296: 2215-2218 (2002).
    • (2002) Science , vol.296 , pp. 2215-2218
    • Weihofen, A.1    Binns, K.2    Lemberg, M.K.3    Ashman, K.4    Martoglio, B.5
  • 68
    • 33746618450 scopus 로고    scopus 로고
    • SPPL2a and SPPL2b promote intramembrane proteolysis of TNFα in activated dendritic cells to trigger IL-12 production
    • Friedmann E, Hauben E, Maylandt K, Schleeger S, Vreugde S, Lichtenthaler SF, et al. SPPL2a and SPPL2b promote intramembrane proteolysis of TNFα in activated dendritic cells to trigger IL-12 production. Nat Cell Biol 8: 843-848 (2006).
    • (2006) Nat Cell Biol , vol.8 , pp. 843-848
    • Friedmann, E.1    Hauben, E.2    Maylandt, K.3    Schleeger, S.4    Vreugde, S.5    Lichtenthaler, S.F.6
  • 69
    • 33746608185 scopus 로고    scopus 로고
    • A γ-secretase-like intramembrane cleavage of TNFα by the GxGD aspartyl protease SPPL2b
    • Fluhrer R, Grammer G, Israel L, Condron MM, Haffner C, Friedmann E, et al. A γ-secretase-like intramembrane cleavage of TNFα by the GxGD aspartyl protease SPPL2b. Nat Cell Biol 8: 894-896 (2006).
    • (2006) Nat Cell Biol , vol.8 , pp. 894-896
    • Fluhrer, R.1    Grammer, G.2    Israel, L.3    Condron, M.M.4    Haffner, C.5    Friedmann, E.6
  • 71
    • 0036628917 scopus 로고    scopus 로고
    • Novel class of polytopic proteins with domains associated with putative protease activity
    • Grigorenko AP, Moliaka YK, Korovaitseva GI and Rogaev EI. Novel class of polytopic proteins with domains associated with putative protease activity. Biochemistry (Mosc) 67: 826-835 (2002).
    • (2002) Biochemistry (Mosc) , vol.67 , pp. 826-835
    • Grigorenko, A.P.1    Moliaka, Y.K.2    Korovaitseva, G.I.3    Rogaev, E.I.4
  • 72
    • 10944270703 scopus 로고    scopus 로고
    • Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins
    • Friedmann E, Lemberg MK, Weihofen A, Dev KK, Dengler U, Rovelli G, et al. Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins. J Biol Chem 279: 50790-50798 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 50790-50798
    • Friedmann, E.1    Lemberg, M.K.2    Weihofen, A.3    Dev, K.K.4    Dengler, U.5    Rovelli, G.6
  • 73
    • 4143084775 scopus 로고    scopus 로고
    • Intramembrane proteolysis: Theme and variations
    • Wolfe MS and Kopan R. Intramembrane proteolysis: theme and variations. Science 305: 1119-1123 (2004).
    • (2004) Science , vol.305 , pp. 1119-1123
    • Wolfe, M.S.1    Kopan, R.2
  • 74
    • 0033783140 scopus 로고    scopus 로고
    • Presenilin-1 differentially facilitates endoproteolysis of the β-amyloid precursor protein and Notch
    • Capell A, Steiner H, Romig H, Keck S, Baader M, Grim MG, et al. Presenilin-1 differentially facilitates endoproteolysis of the β-amyloid precursor protein and Notch. Nat Cell Biol 2: 205-211 (2000).
    • (2000) Nat Cell Biol , vol.2 , pp. 205-211
    • Capell, A.1    Steiner, H.2    Romig, H.3    Keck, S.4    Baader, M.5    Grim, M.G.6
  • 75
    • 0034727882 scopus 로고    scopus 로고
    • Absence of endoproteolysis but no effects on amyloid β production by alternative splicing forms of presenilin-1, which lack exon 8 and replace D257A
    • Morihara T, Katayama T, Sato N, Yoneda T, Manabe T, Hitomi J, et al. Absence of endoproteolysis but no effects on amyloid β production by alternative splicing forms of presenilin-1, which lack exon 8 and replace D257A. Brain Res Mol Brain Res 85: 85-90. (2000).
    • (2000) Brain Res Mol Brain Res , vol.85 , pp. 85-90
    • Morihara, T.1    Katayama, T.2    Sato, N.3    Yoneda, T.4    Manabe, T.5    Hitomi, J.6
  • 76
    • 0035900686 scopus 로고    scopus 로고
    • Multiple effects of aspartate mutant presenilin 1 on the processing and trafficking of amyloid precursor protein
    • Kim SH, Leem JY, Lah JJ, Slunt HH, Levey AI, Thinakaran G, et al. Multiple effects of aspartate mutant presenilin 1 on the processing and trafficking of amyloid precursor protein. J Biol Chem 276: 43343-43350. (2001).
    • (2001) J Biol Chem , vol.276 , pp. 43343-43350
    • Kim, S.H.1    Leem, J.Y.2    Lah, J.J.3    Slunt, H.H.4    Levey, A.I.5    Thinakaran, G.6
  • 77
    • 0242321947 scopus 로고    scopus 로고
    • Presenilins mutated at Asp257 or Asp385 restore Pen-2 expression and Nicastrin glycosylation but remain catalytically inactive in the absence of wild type Presenilin
    • Nyabi O, Bentahir M, Horre K, Herreman A, Gottardi-Littell N, Van Broeckhoven C, et al. Presenilins mutated at Asp257 or Asp385 restore Pen-2 expression and Nicastrin glycosylation but remain catalytically inactive in the absence of wild type Presenilin. J Biol Chem 278: 43430-43436 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 43430-43436
    • Nyabi, O.1    Bentahir, M.2    Horre, K.3    Herreman, A.4    Gottardi-Littell, N.5    Van Broeckhoven, C.6
  • 78
    • 0037176727 scopus 로고    scopus 로고
    • A novel ε-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing
    • Weidemann A, Eggert S, Reinhard FB, Vogel M, Paliga K, Baier G, et al. A novel ε-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing. Biochemistry 41: 2825-2835 (2002).
    • (2002) Biochemistry , vol.41 , pp. 2825-2835
    • Weidemann, A.1    Eggert, S.2    Reinhard, F.B.3    Vogel, M.4    Paliga, K.5    Baier, G.6
  • 79
    • 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, Capell A, Multhaup G, Condron MM, et al. Presenilin-dependent γ-secretase processing of β-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch. EMBO Rep 2: 835-841 (2001).
    • (2001) EMBO Rep , vol.2 , pp. 835-841
    • Sastre, M.1    Steiner, H.2    Fuchs, K.3    Capell, A.4    Multhaup, G.5    Condron, M.M.6
  • 80
    • 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 276: 35235-35238. (2001).
    • (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
  • 81
    • 0035941278 scopus 로고    scopus 로고
    • Characterization of a presenilin-mediated APP carboxyl terminal fragment γ: Evidence for distinct mechanisms involved in γ-secretase processing of the APP and Notch1 transmembrane domains
    • Yu C, Kim SH, Ikeuchi T, Xu H, Gasparini L, Wang R, et al. Characterization of a presenilin-mediated APP carboxyl terminal fragment γ: evidence for distinct mechanisms involved in γ-secretase processing of the APP and Notch1 transmembrane domains. J Biol Chem 276: 43756-43760 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 43756-43760
    • Yu, C.1    Kim, S.H.2    Ikeuchi, T.3    Xu, H.4    Gasparini, L.5    Wang, R.6
  • 82
    • 18644367748 scopus 로고    scopus 로고
    • Presenilins mediate a dual intramembraneous γ-secretase cleavage of Notch-1
    • Okochi M, Steiner H, Fukumori A, Tanii H, Tomita T, Tanaka T, et al. Presenilins mediate a dual intramembraneous γ-secretase cleavage of Notch-1. EMBO J 21: 5408-5416 (2002).
    • (2002) EMBO J , vol.21 , pp. 5408-5416
    • Okochi, M.1    Steiner, H.2    Fukumori, A.3    Tanii, H.4    Tomita, T.5    Tanaka, T.6
  • 83
    • 0033944273 scopus 로고    scopus 로고
    • Aspartate mutations in presenilin and γ-secretase inhibitors both impair notch1 proteolysis and nuclear translocation with relative preservation of notch1 signaling
    • Berezovska O, Jack C, McLean P, Aster JC, Hicks C, Xia W, et al. Aspartate mutations in presenilin and γ-secretase inhibitors both impair notch1 proteolysis and nuclear translocation with relative preservation of notch1 signaling. J Neurochem 75: 583-593. (2000).
    • (2000) J Neurochem , vol.75 , pp. 583-593
    • Berezovska, O.1    Jack, C.2    McLean, P.3    Aster, J.C.4    Hicks, C.5    Xia, W.6
  • 85
    • 0036023971 scopus 로고    scopus 로고
    • A γ-secretase inhibitor blocks Notch signaling in vivo and causes a severe neurogenic phenotype in zebrafish
    • Geling A, Steiner H, Willem M and Bally-Cuif L, Haass C. A γ-secretase inhibitor blocks Notch signaling in vivo and causes a severe neurogenic phenotype in zebrafish. EMBO Rep 3: 688-694 (2002).
    • (2002) EMBO Rep , vol.3 , pp. 688-694
    • Geling, A.1    Steiner, H.2    Willem, M.3    Bally-Cuif, L.4    Haass, C.5
  • 86
    • 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 CL, Ratovitski T, Davenport F, Slunt HH, Price DL, et al. Evidence that levels of presenilins (PS1 and PS2) are coordinately regulated by competition for limiting cellular factors. J Biol Chem 272: 28415-28422 (1997).
    • (1997) J Biol Chem , vol.272 , pp. 28415-28422
    • Thinakaran, G.1    Harris, C.L.2    Ratovitski, T.3    Davenport, F.4    Slunt, H.H.5    Price, D.L.6
  • 88
    • 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, Grünberg J, Pesold B, Diehlmann A, Citron M, Nixon R, 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 273: 3205-3211 (1998).
    • (1998) J Biol Chem , vol.273 , pp. 3205-3211
    • Capell, A.1    Grünberg, J.2    Pesold, B.3    Diehlmann, A.4    Citron, M.5    Nixon, R.6
  • 90
    • 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, Nishimura M, Zhang DM, Levesque L, et al. The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains β-catenin. J Biol Chem 273: 16470-16475 (1998).
    • (1998) J Biol Chem , vol.273 , pp. 16470-16475
    • Yu, G.1    Chen, F.2    Levesque, G.3    Nishimura, M.4    Zhang, D.M.5    Levesque, L.6
  • 91
    • 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, Carlson G, Diehl T, Levesque G, 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 3: 67-72 (1997).
    • (1997) Nat Med , vol.3 , pp. 67-72
    • Citron, M.1    Westaway, D.2    Xia, W.3    Carlson, G.4    Diehl, T.5    Levesque, G.6
  • 92
    • 24144441879 scopus 로고    scopus 로고
    • Uncovering γ-secretase
    • Steiner H. Uncovering γ-secretase. Curr Alzheimer Res 1: 175-181 (2004).
    • (2004) Curr Alzheimer Res , vol.1 , pp. 175-181
    • Steiner, H.1
  • 93
    • 2942604376 scopus 로고    scopus 로고
    • The γ-secretase complex: Machinery for intramembrane proteolysis
    • Iwatsubo T. The γ-secretase complex: machinery for intramembrane proteolysis. Curr Opin Neurobiol 14: 379-383 (2004).
    • (2004) Curr Opin Neurobiol , vol.14 , pp. 379-383
    • Iwatsubo, T.1
  • 94
    • 2542454942 scopus 로고    scopus 로고
    • Requirement of PEN-2 for stabilization of the presenilin NTF/CTF heterodimer within the γ-secretase complex
    • Prokop S, Shirotani K, Edbauer D, Haass C and Steiner H. Requirement of PEN-2 for stabilization of the presenilin NTF/CTF heterodimer within the γ-secretase complex. J Biol Chem 279: 23255-23261 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 23255-23261
    • Prokop, S.1    Shirotani, K.2    Edbauer, D.3    Haass, C.4    Steiner, H.5
  • 95
    • 23744491374 scopus 로고    scopus 로고
    • Nicastrin functions as a γ-secretase-substrate receptor
    • Shah S, Lee SF, Tabuchi K, Hao YH, Yu C, LaPlant Q, et al. Nicastrin functions as a γ-secretase-substrate receptor. Cell 122: 435-447 (2005).
    • (2005) Cell , vol.122 , pp. 435-447
    • Shah, S.1    Lee, S.F.2    Tabuchi, K.3    Hao, Y.H.4    Yu, C.5    LaPlant, Q.6
  • 96
    • 0036327098 scopus 로고    scopus 로고
    • A presenilin-1/nicastrin complex is targeted to the plasma membrane and affects trafficking and processing of the β-amyloid precursor protein
    • Kaether C, Lammich S, Edbauer D, Ertl M, Rietdorf J, Capell A, et al. A presenilin-1/nicastrin complex is targeted to the plasma membrane and affects trafficking and processing of the β-amyloid precursor protein. J Cell Biol 158: 551-561 (2002).
    • (2002) J Cell Biol , vol.158 , pp. 551-561
    • Kaether, C.1    Lammich, S.2    Edbauer, D.3    Ertl, M.4    Rietdorf, J.5    Capell, A.6
  • 98
    • 14244268498 scopus 로고    scopus 로고
    • γ-Secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage
    • Chyung JH, Raper DM and Selkoe DJ. γ-Secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage. J Biol Chem 280: 4383-4392 (2005).
    • (2005) J Biol Chem , vol.280 , pp. 4383-4392
    • Chyung, J.H.1    Raper, D.M.2    Selkoe, D.J.3
  • 99
    • 14844326290 scopus 로고    scopus 로고
    • Aph-1 interacts at the cell surface with proteins in the active γ-secretase complex and membrane-tethered Notch
    • Hansson EM, Stromberg K, Bergstedt S, Yu G, Naslund J, Lundkvist J, et al. Aph-1 interacts at the cell surface with proteins in the active γ-secretase complex and membrane-tethered Notch. J Neurochem 92: 1010-1020 (2005).
    • (2005) J Neurochem , vol.92 , pp. 1010-1020
    • Hansson, E.M.1    Stromberg, K.2    Bergstedt, S.3    Yu, G.4    Naslund, J.5    Lundkvist, J.6
  • 100
    • 33644862462 scopus 로고    scopus 로고
    • Amyloid precursor protein and Notch intracellular domains are generated after transport of their precursors to the cell surface
    • Kaether C, Schmitt S, Willem M and Haass C. Amyloid precursor protein and Notch intracellular domains are generated after transport of their precursors to the cell surface. Traffic 7: 408-415 (2006).
    • (2006) Traffic , vol.7 , pp. 408-415
    • Kaether, C.1    Schmitt, S.2    Willem, M.3    Haass, C.4
  • 101
    • 0032720496 scopus 로고    scopus 로고
    • Presenilin 1 controls γ-secretase processing of amyloid precursor protein in pre-golgi compartments of hippocampal neurons
    • Annaert WG, Levesque L, Craessaerts K, Dierinck I, Snellings G, Westaway D, et al. Presenilin 1 controls γ-secretase processing of amyloid precursor protein in pre-golgi compartments of hippocampal neurons. J Cell Biol 147: 277-294 (1999).
    • (1999) J Cell Biol , vol.147 , pp. 277-294
    • Annaert, W.G.1    Levesque, L.2    Craessaerts, K.3    Dierinck, I.4    Snellings, G.5    Westaway, D.6
  • 102
    • 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, Orlans I, Vanderstichele H, Saftig P, et al. The discrepancy between presenilin subcellular localization and γ-secretase processing of amyloid precursor protein. J Cell Biol 154: 731-740 (2001).
    • (2001) J Cell Biol , vol.154 , pp. 731-740
    • Cupers, P.1    Bentahir, M.2    Craessaerts, K.3    Orlans, I.4    Vanderstichele, H.5    Saftig, P.6
  • 103
    • 0033583047 scopus 로고    scopus 로고
    • The biological and pathological function of the presenilin-1 Δexon 9 mutation is independent of its defect to undergo proteolytic processing
    • Steiner H, Romig H, Grim MG, Philipp U, Pesold B, Citron M, et al. The biological and pathological function of the presenilin-1 Δexon 9 mutation is independent of its defect to undergo proteolytic processing. J Biol Chem 274: 7615-7618 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 7615-7618
    • Steiner, H.1    Romig, H.2    Grim, M.G.3    Philipp, U.4    Pesold, B.5    Citron, M.6
  • 104
    • 0030889220 scopus 로고    scopus 로고
    • Presenilin proteins undergo heterogeneous endoproteolysis between Thr291 and Ala299 and occur as stable N- and C-terminal fragments in normal and Alzheimer brain tissue
    • Podlisny MB, Citron M, Amarante P, Sherrington R, Xia W, Zhang J, et al. Presenilin proteins undergo heterogeneous endoproteolysis between Thr291 and Ala299 and occur as stable N- and C-terminal fragments in normal and Alzheimer brain tissue. Neurobiol Dis 3: 325-337 (1997).
    • (1997) Neurobiol Dis , vol.3 , pp. 325-337
    • Podlisny, M.B.1    Citron, M.2    Amarante, P.3    Sherrington, R.4    Xia, W.5    Zhang, J.6
  • 105
    • 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, Philipp U, Baader M, Citron M, et al. Amyloidogenic function of the Alzheimer's disease-associated presenilin 1 in the absence of endoproteolysis. Biochemistry 38: 14600-14605 (1999).
    • (1999) Biochemistry , vol.38 , pp. 14600-14605
    • Steiner, H.1    Romig, H.2    Pesold, B.3    Philipp, U.4    Baader, M.5    Citron, M.6
  • 106
    • 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, Bur D, Kocyba C, Kurt H, et al. The influence of endoproteolytic processing of familial Alzheimer's disease presenilin 2 on Aβ42 amyloid peptide formation. J Biol Chem 274: 35233-35239 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 35233-35239
    • Jacobsen, H.1    Reinhardt, D.2    Brockhaus, M.3    Bur, D.4    Kocyba, C.5    Kurt, H.6
  • 107
    • 0034602957 scopus 로고    scopus 로고
    • Mutational analysis of intrinsic regions of presenilin 2 that determine its endoproteolytic cleavage and pathological function
    • Shirotani K, Takahashi K, Araki W, Maruyama K and Tabira T. Mutational analysis of intrinsic regions of presenilin 2 that determine its endoproteolytic cleavage and pathological function. J Biol Chem 275: 3681-3686 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 3681-3686
    • Shirotani, K.1    Takahashi, K.2    Araki, W.3    Maruyama, K.4    Tabira, T.5
  • 108
    • 2642513216 scopus 로고    scopus 로고
    • Functional domains in presenilin 1: The Tyr-288 residue controls γ-secretase activity and endoproteolysis
    • Laudon H, Karlstrom H, Mathews PM, Farmery MR, Gandy SE, Lundkvist J, et al. Functional domains in presenilin 1: the Tyr-288 residue controls γ-secretase activity and endoproteolysis. J Biol Chem 279: 23925-23932 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 23925-23932
    • Laudon, H.1    Karlstrom, H.2    Mathews, P.M.3    Farmery, M.R.4    Gandy, S.E.5    Lundkvist, J.6
  • 109
    • 1842523970 scopus 로고    scopus 로고
    • Conserved "PAL" sequence in presenilins is essential for γ-secretase activity, but not required for formation or stabilization of γ-secretase complexes
    • Wang J, Brunkan AL, Hecimovic S, Walker E and Goate A. Conserved "PAL" sequence in presenilins is essential for γ-secretase activity, but not required for formation or stabilization of γ-secretase complexes. Neurobiol Dis 15: 654-666 (2004).
    • (2004) Neurobiol Dis , vol.15 , pp. 654-666
    • Wang, J.1    Brunkan, A.L.2    Hecimovic, S.3    Walker, E.4    Goate, A.5
  • 110
    • 21444450394 scopus 로고    scopus 로고
    • Random mutagenesis of presenilin-1 identifies novel mutants exclusively generating long amyloid β-peptides
    • Nakaya Y, Yamane T, Shiraishi H, Wang HQ, Matsubara E, Sato T, et al. Random mutagenesis of presenilin-1 identifies novel mutants exclusively generating long amyloid β-peptides. J Biol Chem 280: 19070-19077 (2005).
    • (2005) J Biol Chem , vol.280 , pp. 19070-19077
    • Nakaya, Y.1    Yamane, T.2    Shiraishi, H.3    Wang, H.Q.4    Matsubara, E.5    Sato, T.6
  • 112
    • 0035977071 scopus 로고    scopus 로고
    • Pharmacological knock-down of the presenilin 1 heterodimer by a novel γ-secretase inhibitor: Implications for presenilin biology
    • Beher D, Wrigley JD, Nadin A, Evin G, Masters CL, Harrison T, et al. Pharmacological knock-down of the presenilin 1 heterodimer by a novel γ-secretase inhibitor: implications for presenilin biology. J Biol Chem 276: 45394-45402 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 45394-45402
    • Beher, D.1    Wrigley, J.D.2    Nadin, A.3    Evin, G.4    Masters, C.L.5    Harrison, T.6
  • 113
    • 0037066084 scopus 로고    scopus 로고
    • Endoproteolysis of presenilin in vitro: Inhibition by γ-secretase inhibitors
    • Campbell WA, Iskandar MK, Reed ML and Xia W. Endoproteolysis of presenilin in vitro: inhibition by γ-secretase inhibitors. Biochemistry 41: 3372-3379 (2002).
    • (2002) Biochemistry , vol.41 , pp. 3372-3379
    • Campbell, W.A.1    Iskandar, M.K.2    Reed, M.L.3    Xia, W.4
  • 114
    • 0037795653 scopus 로고    scopus 로고
    • Presenilin endoproteolysis mediated by an aspartyl protease activity pharmacologically distinct from γ-secretase
    • Campbell WA, Reed ML, Strahle J, Wolfe MS and Xia W. Presenilin endoproteolysis mediated by an aspartyl protease activity pharmacologically distinct from γ-secretase. J Neurochem 85: 1563-1574 (2003).
    • (2003) J Neurochem , vol.85 , pp. 1563-1574
    • Campbell, W.A.1    Reed, M.L.2    Strahle, J.3    Wolfe, M.S.4    Xia, W.5
  • 115
    • 33748743559 scopus 로고    scopus 로고
    • Contribution of presenilin transmembrane domains 6 and 7 to a water-containing cavity in the γ-secretase complex
    • Tolia A, Chavez-Gutierrez L and De Strooper B. Contribution of presenilin transmembrane domains 6 and 7 to a water-containing cavity in the γ-secretase complex. J Biol Chem 281: 27633-27642 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 27633-27642
    • Tolia, A.1    Chavez-Gutierrez, L.2    De Strooper, B.3
  • 116
    • 33751087756 scopus 로고    scopus 로고
    • Structure of the catalytic pore of γ-secretase probed by the accessibility of substituted cysteines
    • Sato C, Morohashi Y, Tomita T and Iwatsubo T. Structure of the catalytic pore of γ-secretase probed by the accessibility of substituted cysteines. J Neurosci 26: 12081-12088 (2006).
    • (2006) J Neurosci , vol.26 , pp. 12081-12088
    • Sato, C.1    Morohashi, Y.2    Tomita, T.3    Iwatsubo, T.4
  • 117
    • 4544229745 scopus 로고    scopus 로고
    • Conserved residues within the putative active site of γ-secretase differentially influence enzyme activity and inhibitor binding
    • Wrigley JD, Nunn EJ, Nyabi O, Clarke EE, Hunt P, Nadin A, et al. Conserved residues within the putative active site of γ-secretase differentially influence enzyme activity and inhibitor binding. J Neurochem 90: 1312-1320 (2004).
    • (2004) J Neurochem , vol.90 , pp. 1312-1320
    • Wrigley, J.D.1    Nunn, E.J.2    Nyabi, O.3    Clarke, E.E.4    Hunt, P.5    Nadin, A.6
  • 118
    • 33644839624 scopus 로고    scopus 로고
    • C-terminal PAL motif of presenilin and presenilin homologues required for normal active site conformation
    • Wang J, Beher D, Nyborg AC, Shearman MS, Golde TE and Goate A. C-terminal PAL motif of presenilin and presenilin homologues required for normal active site conformation. J Neurochem 96: 218-227 (2006).
    • (2006) J Neurochem , vol.96 , pp. 218-227
    • Wang, J.1    Beher, D.2    Nyborg, A.C.3    Shearman, M.S.4    Golde, T.E.5    Goate, A.6
  • 120
    • 33646483640 scopus 로고    scopus 로고
    • Electron microscopic structure of purified, active γ-secretase reveals an aqueous intramembrane chamber and two pores
    • Lazarov VK, Fraering PC, Ye W, Wolfe MS, Selkoe DJ and Li H. Electron microscopic structure of purified, active γ-secretase reveals an aqueous intramembrane chamber and two pores. Proc Natl Acad Sci USA 103: 6889-6894 (2006).
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 6889-6894
    • Lazarov, V.K.1    Fraering, P.C.2    Ye, W.3    Wolfe, M.S.4    Selkoe, D.J.5    Li, H.6
  • 121
    • 0037067655 scopus 로고    scopus 로고
    • Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-κB and β-amyloid precursor protein
    • Baek SH, Ohgi KA, Rose DW, Koo EH, Glass CK and Rosenfeld MG. Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-κB and β-amyloid precursor protein. Cell 110: 55-67 (2002).
    • (2002) Cell , vol.110 , pp. 55-67
    • Baek, S.H.1    Ohgi, K.A.2    Rose, D.W.3    Koo, E.H.4    Glass, C.K.5    Rosenfeld, M.G.6
  • 122
    • 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, Petit A, Kawarai T, Sunyach C, Alves da Costa C, Vincent B, et al. Presenilin-dependent transcriptional control of the Aβ-degrading enzyme neprilysin by intracellular domains of βAPP and APLP. Neuron 46: 541-554 (2005).
    • (2005) Neuron , vol.46 , pp. 541-554
    • Pardossi-Piquard, R.1    Petit, A.2    Kawarai, T.3    Sunyach, C.4    Alves da Costa, C.5    Vincent, B.6
  • 123
    • 5444275067 scopus 로고    scopus 로고
    • The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor
    • Von Rotz RC, Kohli BM, Bosset J, Meier M, Suzuki T, Nitsch RM, et al. The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor. J Cell Sci 117: 4435-4448 (2004).
    • (2004) J Cell Sci , vol.117 , pp. 4435-4448
    • Von Rotz, R.C.1    Kohli, B.M.2    Bosset, J.3    Meier, M.4    Suzuki, T.5    Nitsch, R.M.6
  • 124
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao X and Südhof TC. A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 293: 115-120. (2001).
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Südhof, T.C.2
  • 125
    • 33745584643 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis of amyloid precursor protein and regulation of expression of putative target genes
    • Hebert SS, Serneels L, Tolia A, Craessaerts K, Derks C, Filippov MA, et al. Regulated intramembrane proteolysis of amyloid precursor protein and regulation of expression of putative target genes. EMBO Rep 7: 739-745 (2006).
    • (2006) EMBO Rep , vol.7 , pp. 739-745
    • Hebert, S.S.1    Serneels, L.2    Tolia, A.3    Craessaerts, K.4    Derks, C.5    Filippov, M.A.6
  • 126
    • 34547539177 scopus 로고    scopus 로고
    • Presenilin/γ- secretase-dependent processing of β-amyloid precursor protein regulates EGF receptor expression
    • Zhang YW, Wang R, Liu Q, Zhang H, Liao FF and Xu H. Presenilin/γ- secretase-dependent processing of β-amyloid precursor protein regulates EGF receptor expression. Proc Natl Acad Sci USA 104: 10613-10618 (2007).
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 10613-10618
    • Zhang, Y.W.1    Wang, R.2    Liu, Q.3    Zhang, H.4    Liao, F.F.5    Xu, H.6
  • 127
    • 2942557122 scopus 로고    scopus 로고
    • γ-Secretase: Proteasome of the membrane?
    • Kopan R and Ilagan MX. γ-Secretase: proteasome of the membrane? Nat Rev Mol Cell Biol 5: 499-504 (2004).
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 499-504
    • Kopan, R.1    Ilagan, M.X.2
  • 128
    • 12144250683 scopus 로고    scopus 로고
    • APH-1a is the principal mammalian APH-1 isoform present in γ-secretase complexes during embryonic development
    • Ma G, Li T, Price DL and Wong PC. APH-1a is the principal mammalian APH-1 isoform present in γ-secretase complexes during embryonic development. J Neurosci 25: 192-198 (2005).
    • (2005) J Neurosci , vol.25 , pp. 192-198
    • Ma, G.1    Li, T.2    Price, D.L.3    Wong, P.C.4
  • 130
    • 30744465376 scopus 로고    scopus 로고
    • Reduced Aph-1b expression causes tissueand substrate-specific changes in γ-secretase activity in rats with a complex phenotype
    • Coolen MW, Van Loo KM, van Bakel NN, Ellenbroek BA, Cools AR and Martens GJ. Reduced Aph-1b expression causes tissueand substrate-specific changes in γ-secretase activity in rats with a complex phenotype. FASEB J 20: 175-177 (2006).
    • (2006) FASEB J , vol.20 , pp. 175-177
    • Coolen, M.W.1    Van Loo, K.M.2    van Bakel, N.N.3    Ellenbroek, B.A.4    Cools, A.R.5    Martens, G.J.6
  • 131
    • 34250328818 scopus 로고    scopus 로고
    • Pathological activity of familial Alzheimer's disease-associated mutant presenilin can be executed by six different γ-secretase complexes
    • Shirotani K, Tomioka M, Kremmer E, Haass C and Steiner H. Pathological activity of familial Alzheimer's disease-associated mutant presenilin can be executed by six different γ-secretase complexes. Neurobiol Dis 27: 102-107 (2007).
    • (2007) Neurobiol Dis , vol.27 , pp. 102-107
    • Shirotani, K.1    Tomioka, M.2    Kremmer, E.3    Haass, C.4    Steiner, H.5
  • 132
    • 21144447065 scopus 로고    scopus 로고
    • Dissociated phenotypes in presenilin transgenic mice define functionally distinct γ-secretases
    • Mastrangelo P, Mathews PM, Chishti MA, Schmidt SD, Gu Y, Yang J, et al. Dissociated phenotypes in presenilin transgenic mice define functionally distinct γ-secretases. Proc Natl Acad Sci USA 102: 8972-8977 (2005).
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8972-8977
    • Mastrangelo, P.1    Mathews, P.M.2    Chishti, M.A.3    Schmidt, S.D.4    Gu, Y.5    Yang, J.6
  • 133
    • 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: 625-636 (2000).
    • (2000) Mol Cell , vol.6 , pp. 625-636
    • Struhl, G.1    Adachi, A.2
  • 134
    • 0037022644 scopus 로고    scopus 로고
    • Activity-dependent isolation of the presenilin-γ-secretase complex reveals nicastrin and a γ substrate
    • Esler WP, Kimberly WT, Ostaszewski BL, Ye W, Diehl TS, Selkoe DJ, et al. Activity-dependent isolation of the presenilin-γ-secretase complex reveals nicastrin and a γ substrate. Proc Natl Acad Sci USA 99: 2720-2725. (2002).
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2720-2725
    • Esler, W.P.1    Kimberly, W.T.2    Ostaszewski, B.L.3    Ye, W.4    Diehl, T.S.5    Selkoe, D.J.6
  • 135
    • 0037200036 scopus 로고    scopus 로고
    • Linear non-competitive inhibition of solubilized human γ-secretase by pepstatin A methylester, L685458, sulfonamides, and benzodiazepines
    • Tian G, Sobotka-Briner CD, Zysk J, Liu X, Birr C, Sylvester MA, et al. Linear non-competitive inhibition of solubilized human γ-secretase by pepstatin A methylester, L685458, sulfonamides, and benzodiazepines. J Biol Chem 277: 31499-31505 (2002).
    • (2002) J Biol Chem , vol.277 , pp. 31499-31505
    • Tian, G.1    Sobotka-Briner, C.D.2    Zysk, J.3    Liu, X.4    Birr, C.5    Sylvester, M.A.6
  • 136
    • 0042206671 scopus 로고    scopus 로고
    • The mechanism of γ-secretase: Multiple inhibitor binding sites for transition state analogs and small molecule inhibitors
    • Tian G, Ghanekar SV, Aharony D, Shenvi AB, Jacobs RT, Liu X, et al. The mechanism of γ-secretase: multiple inhibitor binding sites for transition state analogs and small molecule inhibitors. J Biol Chem 278: 28968-28975 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 28968-28975
    • Tian, G.1    Ghanekar, S.V.2    Aharony, D.3    Shenvi, A.B.4    Jacobs, R.T.5    Liu, X.6
  • 137
    • 0038607066 scopus 로고    scopus 로고
    • Differential effects of inhibitors on the γ-secretase complex. Mechanistic implications
    • Kornilova AY, Das C and Wolfe MS. Differential effects of inhibitors on the γ-secretase complex. Mechanistic implications. J Biol Chem 278: 16470-16473 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 16470-16473
    • Kornilova, A.Y.1    Das, C.2    Wolfe, M.S.3
  • 138
    • 14744267675 scopus 로고    scopus 로고
    • The initial substrate-binding site of γ-secretase is located on presenilin near the active site
    • Kornilova AY, Bihel F, Das C and Wolfe MS. The initial substrate-binding site of γ-secretase is located on presenilin near the active site. Proc Natl Acad Sci USA 102: 3230-3235 (2005).
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3230-3235
    • Kornilova, A.Y.1    Bihel, F.2    Das, C.3    Wolfe, M.S.4
  • 139
    • 33645559774 scopus 로고    scopus 로고
    • The GxGD motif of presenilin contributes to catalytic function and substrate identification of γ-secretase
    • Yamasaki A, Eimer S, Okochi M, Smialowska A, Kaether C, Baumeister R, et al. The GxGD motif of presenilin contributes to catalytic function and substrate identification of γ-secretase. J Neurosci 26: 3821-3828 (2006).
    • (2006) J Neurosci , vol.26 , pp. 3821-3828
    • Yamasaki, A.1    Eimer, S.2    Okochi, M.3    Smialowska, A.4    Kaether, C.5    Baumeister, R.6
  • 140
    • 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, Okochi M, Takeda M, Kaether C, Capell A, Zimmer AK, 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: 44754-44759 (2002).
    • (2002) J Biol Chem , vol.277 , pp. 44754-44759
    • Lammich, S.1    Okochi, M.2    Takeda, M.3    Kaether, C.4    Capell, A.5    Zimmer, A.K.6
  • 141
    • 10944259134 scopus 로고    scopus 로고
    • Identification of a new presenilin-dependent ζ-cleavage site within the transmembrane domain of amyloid precursor protein
    • Zhao G, Mao G, Tan J, Dong Y, Cui MZ, Kim SH, et al. Identification of a new presenilin-dependent ζ-cleavage site within the transmembrane domain of amyloid precursor protein. J Biol Chem 279: 50647-50650 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 50647-50650
    • Zhao, G.1    Mao, G.2    Tan, J.3    Dong, Y.4    Cui, M.Z.5    Kim, S.H.6
  • 142
    • 19944430034 scopus 로고    scopus 로고
    • Longer forms of amyloid β protein: Implications for the mechanism of intramembrane cleavage by γ-secretase
    • Qi-Takahara Y, Morishima-Kawashima M, Tanimura Y, Dolios G, Hirotani N, Horikoshi Y, et al. Longer forms of amyloid β protein: implications for the mechanism of intramembrane cleavage by γ-secretase. J Neurosci 25: 436-445 (2005).
    • (2005) J Neurosci , vol.25 , pp. 436-445
    • Qi-Takahara, Y.1    Morishima-Kawashima, M.2    Tanimura, Y.3    Dolios, G.4    Hirotani, N.5    Horikoshi, Y.6
  • 143
    • 33644837810 scopus 로고    scopus 로고
    • Analysis of transmembrane domain mutants is consistent with sequential cleavage of Notch by γ-secretase
    • Chandu D, Huppert SS and Kopan R. Analysis of transmembrane domain mutants is consistent with sequential cleavage of Notch by γ-secretase. J Neurochem 96: 228-235 (2006).
    • (2006) J Neurochem , vol.96 , pp. 228-235
    • Chandu, D.1    Huppert, S.S.2    Kopan, R.3
  • 144
    • 33749072714 scopus 로고    scopus 로고
    • Presenilindependent ErbB4 nuclear signaling regulates the timing of astrogenesis in the developing brain
    • Sardi SP, Murtie J, Koirala S, Patten BA and Corfas G. Presenilindependent ErbB4 nuclear signaling regulates the timing of astrogenesis in the developing brain. Cell 127: 185-197 (2006).
    • (2006) Cell , vol.127 , pp. 185-197
    • Sardi, S.P.1    Murtie, J.2    Koirala, S.3    Patten, B.A.4    Corfas, G.5
  • 145
    • 33947597857 scopus 로고    scopus 로고
    • GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Aβ42
    • Munter LM, Voigt P, Harmeier A, Kaden D, Gottschalk KE, Weise C, et al. GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Aβ42. EMBO J 26: 1702-1712 (2007).
    • (2007) EMBO J , vol.26 , pp. 1702-1712
    • Munter, L.M.1    Voigt, P.2    Harmeier, A.3    Kaden, D.4    Gottschalk, K.E.5    Weise, C.6
  • 146
    • 0035823039 scopus 로고    scopus 로고
    • Homodimerization of presenilin N-terminal fragments is affected by mutations linked to Alzheimer's disease
    • Cervantes S, Gonzalez-Duarte R and Marfany G. Homodimerization of presenilin N-terminal fragments is affected by mutations linked to Alzheimer's disease. FEBS Lett 505: 81-86 (2001).
    • (2001) FEBS Lett , vol.505 , pp. 81-86
    • Cervantes, S.1    Gonzalez-Duarte, R.2    Marfany, G.3
  • 147
    • 4344632844 scopus 로고    scopus 로고
    • Functional implications of the presenilin dimerization: Reconstitution of γ-secretase activity by assembly of a catalytic site at the dimer interface of two catalytically inactive presenilins
    • Cervantes S, Saura CA, Pomares E, Gonzalez-Duarte R and Marfany G. Functional implications of the presenilin dimerization: reconstitution of γ-secretase activity by assembly of a catalytic site at the dimer interface of two catalytically inactive presenilins. J Biol Chem 279: 36519-36529 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 36519-36529
    • Cervantes, S.1    Saura, C.A.2    Pomares, E.3    Gonzalez-Duarte, R.4    Marfany, G.5
  • 148
    • 0242331600 scopus 로고    scopus 로고
    • A presenilin dimer at the core of the γ-secretase enzyme: Insights from parallel analysis of Notch 1 and APP proteolysis
    • Schroeter EH, Ilagan MX, Brunkan AL, Hecimovic S, Li YM, Xu M, et al. A presenilin dimer at the core of the γ-secretase enzyme: insights from parallel analysis of Notch 1 and APP proteolysis. Proc Natl Acad Sci USA 100: 13075-13080 (2003).
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13075-13080
    • Schroeter, E.H.1    Ilagan, M.X.2    Brunkan, A.L.3    Hecimovic, S.4    Li, Y.M.5    Xu, M.6
  • 149
    • 33845975652 scopus 로고    scopus 로고
    • Intra- or intercomplex binding to the γ-secretase enzyme. A model to differentiate inhibitor classes
    • Clarke EE, Churcher I, Ellis S, Wrigley JD, Lewis HD, Harrison T, et al. Intra- or intercomplex binding to the γ-secretase enzyme. A model to differentiate inhibitor classes. J Biol Chem 281: 31279-31289 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 31279-31289
    • Clarke, E.E.1    Churcher, I.2    Ellis, S.3    Wrigley, J.D.4    Lewis, H.D.5    Harrison, T.6
  • 150
    • 33947201115 scopus 로고    scopus 로고
    • Loss-of-function presenilin mutations in Alzheimer disease. Talking Point on the role of presenilin mutations in Alzheimer disease
    • De Strooper B. Loss-of-function presenilin mutations in Alzheimer disease. Talking Point on the role of presenilin mutations in Alzheimer disease. EMBO Rep 8: 141-146 (2007).
    • (2007) EMBO Rep , vol.8 , pp. 141-146
    • De Strooper, B.1
  • 151
    • 33947242870 scopus 로고    scopus 로고
    • When loss is gain: Reduced presenilin proteolytic function leads to increased Aβ42/Aβ40. Talking Point on the role of presenilin mutations in Alzheimer disease
    • Wolfe MS. When loss is gain: reduced presenilin proteolytic function leads to increased Aβ42/Aβ40. Talking Point on the role of presenilin mutations in Alzheimer disease. EMBO Rep 8: 136-140 (2007).
    • (2007) EMBO Rep , vol.8 , pp. 136-140
    • Wolfe, M.S.1
  • 152
    • 0031108103 scopus 로고    scopus 로고
    • Human presenilin-1, but not familial Alzheimer's disease (FAD) mutants, facilitate Caenorhabditis elegans Notch signalling independently of proteolytic processing
    • Baumeister R, Leimer U, Zweckbronner I, Jakubek C, Grünberg J and Haass C. Human presenilin-1, but not familial Alzheimer's disease (FAD) mutants, facilitate Caenorhabditis elegans Notch signalling independently of proteolytic processing. Genes Funct 1: 149-159 (1997).
    • (1997) Genes Funct , vol.1 , pp. 149-159
    • Baumeister, R.1    Leimer, U.2    Zweckbronner, I.3    Jakubek, C.4    Grünberg, J.5    Haass, C.6
  • 154
    • 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
    • Song W, Nadeau P, Yuan M, Yang X, Shen J and Yankner BA. 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: 6959-6963 (1999).
    • (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
  • 155
    • 0037184062 scopus 로고    scopus 로고
    • Presenilin 1 mutations activate γ42-secretase but reciprocally inhibit ε-secretase cleavage of amyloid precursor protein (APP) and S3-cleavage of notch
    • Chen F, Gu Y, Hasegawa H, Ruan X, Arawaka S, Fraser P, et al. Presenilin 1 mutations activate γ42-secretase but reciprocally inhibit ε-secretase cleavage of amyloid precursor protein (APP) and S3-cleavage of notch. J Biol Chem 277: 36521-36526 (2002).
    • (2002) J Biol Chem , vol.277 , pp. 36521-36526
    • Chen, F.1    Gu, Y.2    Hasegawa, H.3    Ruan, X.4    Arawaka, S.5    Fraser, P.6
  • 156
    • 24144451760 scopus 로고    scopus 로고
    • Familial Alzheimer's disease mutations inhibit γ-secretase-mediated liberation of β-amyloid precursor protein carboxy-terminal fragment
    • Wiley JC, Hudson M, Kanning KC, Schecterson LC and Bothwell M. Familial Alzheimer's disease mutations inhibit γ-secretase-mediated liberation of β-amyloid precursor protein carboxy-terminal fragment. J Neurochem 94: 1189-1201 (2005).
    • (2005) J Neurochem , vol.94 , pp. 1189-1201
    • Wiley, J.C.1    Hudson, M.2    Kanning, K.C.3    Schecterson, L.C.4    Bothwell, M.5
  • 157
    • 0034705196 scopus 로고    scopus 로고
    • Separation of presenilin function in amyloid β-peptide generation and endoproteolysis of Notch
    • Kulic L, Walter J, Multhaup G, Teplow DB, Baumeister R, Romig H, et al. Separation of presenilin function in amyloid β-peptide generation and endoproteolysis of Notch. Proc Natl Acad Sci USA 97: 5913-5918. (2000).
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5913-5918
    • Kulic, L.1    Walter, J.2    Multhaup, G.3    Teplow, D.B.4    Baumeister, R.5    Romig, H.6
  • 158
    • 0032032847 scopus 로고    scopus 로고
    • Mutant human presenilin 1 protects presenilin 1 null mouse against embryonic lethality and elevates Aβ1-42/43 expression
    • Qian S, Jiang P, Guan XM, Singh G, Trumbauer ME, Yu H, et al. Mutant human presenilin 1 protects presenilin 1 null mouse against embryonic lethality and elevates Aβ1-42/43 expression. Neuron 20: 611-617 (1998).
    • (1998) Neuron , vol.20 , pp. 611-617
    • Qian, S.1    Jiang, P.2    Guan, X.M.3    Singh, G.4    Trumbauer, M.E.5    Yu, H.6
  • 159
    • 0032032019 scopus 로고    scopus 로고
    • An Alzheimer's disease-linked PS1 variant rescues the developmental abnormalities of PS1-deficient embryos
    • Davis JA, Naruse S, Chen H, Eckman C, Younkin S, Price DL, et al. An Alzheimer's disease-linked PS1 variant rescues the developmental abnormalities of PS1-deficient embryos. Neuron 20: 603-609 (1998).
    • (1998) Neuron , vol.20 , pp. 603-609
    • Davis, J.A.1    Naruse, S.2    Chen, H.3    Eckman, C.4    Younkin, S.5    Price, D.L.6
  • 160
    • 0035829592 scopus 로고    scopus 로고
    • A subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activity
    • Weggen S, Eriksen JL, Das P, Sagi SA, Wang R, Pietrzik CU, et al. A subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activity. Nature 414: 212-216 (2001).
    • (2001) Nature , vol.414 , pp. 212-216
    • Weggen, S.1    Eriksen, J.L.2    Das, P.3    Sagi, S.A.4    Wang, R.5    Pietrzik, C.U.6
  • 161
    • 0038719688 scopus 로고    scopus 로고
    • Sulindac sulfide is a noncompetitive γ-secretase inhibitor that preferentially reduces Aβ42 generation
    • Takahashi Y, Hayashi I, Tominari Y, Rikimaru K, Morohashi Y, Kan T, et al. Sulindac sulfide is a noncompetitive γ-secretase inhibitor that preferentially reduces Aβ42 generation. J Biol Chem 278: 18664-18670 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 18664-18670
    • Takahashi, Y.1    Hayashi, I.2    Tominari, Y.3    Rikimaru, K.4    Morohashi, Y.5    Kan, T.6
  • 162
    • 6344233805 scopus 로고    scopus 로고
    • Selected non-steroidal anti-inflammatory drugs and their derivatives target γ-secretase at a novel site. Evidence for an allosteric mechanism
    • Beher D, Clarke EE, Wrigley JD, Martin AC, Nadin A, Churcher I, et al. Selected non-steroidal anti-inflammatory drugs and their derivatives target γ-secretase at a novel site. Evidence for an allosteric mechanism. J Biol Chem 279: 43419-43426 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 43419-43426
    • Beher, D.1    Clarke, E.E.2    Wrigley, J.D.3    Martin, A.C.4    Nadin, A.5    Churcher, I.6
  • 163
    • 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 99: 8666-8671 (2002).
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8666-8671
    • Edbauer, D.1    Winkler, E.2    Haass, C.3    Steiner, H.4
  • 165
    • 19644389648 scopus 로고    scopus 로고
    • Zhou S, Zhou H, Walian PJ and Jap BK. CD147 is a regulatory subunit of the γ-secretase complex in Alzheimer's disease amyloid β-peptide production. Proc Natl Acad Sci USA 102: 7499-7504 (2005).
    • Zhou S, Zhou H, Walian PJ and Jap BK. CD147 is a regulatory subunit of the γ-secretase complex in Alzheimer's disease amyloid β-peptide production. Proc Natl Acad Sci USA 102: 7499-7504 (2005).
  • 166
    • 33646369950 scopus 로고    scopus 로고
    • TMP21 is a presenilin complex component that modulates γ-secretase but not ε-secretase activity
    • Chen F, Hasegawa H, Schmitt-Ulms G, Kawarai T, Bohm C, Katayama T, et al. TMP21 is a presenilin complex component that modulates γ-secretase but not ε-secretase activity. Nature 440: 1208-1212 (2006).
    • (2006) Nature , vol.440 , pp. 1208-1212
    • Chen, F.1    Hasegawa, H.2    Schmitt-Ulms, G.3    Kawarai, T.4    Bohm, C.5    Katayama, T.6
  • 167
    • 34247887500 scopus 로고    scopus 로고
    • Dual roles of the transmembrane protein p23/TMP21 in the modulation of amyloid precursor protein metabolism
    • Vetrivel KS, Gong P, Bowen JW, Cheng H, Chen Y, Carter M, et al. Dual roles of the transmembrane protein p23/TMP21 in the modulation of amyloid precursor protein metabolism. Mol Neurodegener 2: 4 (2007).
    • (2007) Mol Neurodegener , vol.2 , pp. 4
    • Vetrivel, K.S.1    Gong, P.2    Bowen, J.W.3    Cheng, H.4    Chen, Y.5    Carter, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.