메뉴 건너뛰기




Volumn 391, Issue 8, 2010, Pages 839-847

Structure, mechanism and inhibition of γ-secretase and presenilin-like proteases

Author keywords

Amyloid; Notch receptor; Peptidomimetics; Signal peptide peptidase; Substrate analogs; Substrate recognition

Indexed keywords

AMYLOID PRECURSOR PROTEIN; GAMMA SECRETASE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; NOTCH RECEPTOR; PRESENILIN; PROTEINASE; SIGNAL PEPTIDE PEPTIDASE; UNCLASSIFIED DRUG;

EID: 77955944764     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2010.086     Document Type: Conference Paper
Times cited : (38)

References (96)
  • 1
    • 43049163813 scopus 로고    scopus 로고
    • Substrate specificity of γ-secretase and other intramembrane proteases
    • Beel, A.J. and Sanders, C.R. (2008). Substrate specificity of γ-secretase and other intramembrane proteases. Cell. Mol. Life Sci. 65, 1311-1334.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 1311-1334
    • Beel, A.J.1    Sanders, C.R.2
  • 2
    • 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, E.E., Wrigley, J.D., Martin, A.C., Nadin, A., Churcher, I., and Shearman, M.S. (2004). 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) 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    Shearman, M.S.7
  • 3
    • 33846275257 scopus 로고    scopus 로고
    • Structural basis for intramembrane proteolysis by rhomboid serine proteases
    • Ben-Shem, A., Fass, D., and Bibi, E. (2007). Structural basis for intramembrane proteolysis by rhomboid serine proteases. Proc. Natl. Acad. Sci. USA 104, 462-466.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 462-466
    • Ben-Shem, A.1    Fass, D.2    Bibi, E.3
  • 5
    • 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., Diehlmann, A., Citron, M., Nixon, R., Beyreuther, K., Selkoe, D.J., and Haass, C. (1998). 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) J. Biol. Chem. , vol.273 , pp. 3205-3211
    • Capell, A.1    Grunberg, J.2    Pesold, B.3    Diehlmann, A.4    Citron, M.5    Nixon, R.6    Beyreuther, K.7    Selkoe, D.J.8    Haass, C.9
  • 6
    • 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, C.A., Pomares, E., Gonzalez-Duarte, R., and Marfany, G. (2004). 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) 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
  • 7
    • 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., Johnson-Wood, K., Lee, M., Seubert, P., Davis, A., et al. (1997). 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) 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    Johnson-Wood, K.7    Lee, M.8    Seubert, P.9    Davis, A.10
  • 9
    • 57649217285 scopus 로고    scopus 로고
    • The role of APP processing by BACE1, the β-secretase, in Alzheimer's disease pathophysiology
    • Cole, S.L. and Vassar, R. (2008). The role of APP processing by BACE1, the β-secretase, in Alzheimer's disease pathophysiology. J. Biol. Chem. 283, 29621-29625.
    • (2008) J. Biol. Chem. , vol.283 , pp. 29621-29625
    • Cole, S.L.1    Vassar, R.2
  • 11
    • 0037431082 scopus 로고    scopus 로고
    • Aph-1, Pen-2, and nicastrin with presenilin generate an active γ-secretase complex
    • De Strooper, B. (2003). Aph-1, Pen-2, and nicastrin with presenilin generate an active γ-secretase complex. Neuron 38, 9-12.
    • (2003) Neuron , vol.38 , pp. 9-12
    • De Strooper, B.1
  • 15
    • 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. (2002). Presenilin and nicastrin regulate each other and determine amyloid β-peptide production via complex formation. Proc. Natl. Acad. Sci. USA 99, 8666-8671.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8666-8671
    • Edbauer, D.1    Winkler, E.2    Haass, C.3    Steiner, H.4
  • 19
    • 15544380450 scopus 로고    scopus 로고
    • Transition-state analogue γ-secretase inhibitors stabilize a 900 kDa presenilin/nicastrin complex
    • DOI 10.1021/bi0481702
    • Evin, G., Canterford, L.D., Hoke, D.E., Sharples, R.A., Culvenor, J.G., and Masters, C.L. (2005). Transition-state analogue γ-secretase inhibitors stabilize a 900 kDa presenilin/nicastrin complex. Biochemistry 44, 4332-4341. (Pubitemid 40403974)
    • (2005) Biochemistry , vol.44 , Issue.11 , pp. 4332-4341
    • Evin, G.1    Canterford, L.D.2    Hoke, D.E.3    Sharples, R.A.4    Culvenor, J.G.5    Masters, C.L.6
  • 20
    • 36849037428 scopus 로고    scopus 로고
    • Structure of a site-2 protease family intramembrane metalloprotease
    • DOI 10.1126/science.1150755
    • Feng, L., Yan, H., Wu, Z., Yan, N., Wang, Z., Jeffrey, P.D., and Shi, Y. (2007). Structure of a site-2 protease family intramembrane metalloprotease. Science 318, 1608-1612. (Pubitemid 350233656)
    • (2007) Science , vol.318 , Issue.5856 , pp. 1608-1612
    • Feng, L.1    Yan, H.2    Wu, Z.3    Yan, N.4    Wang, Z.5    Jeffrey, P.D.6    Shi, Y.7
  • 22
    • 67649794833 scopus 로고    scopus 로고
    • Intramembrane proteolysis by signal peptide peptidases: A comparative discussion of GXGD-type aspartyl proteases
    • Fluhrer, R., Steiner, H., and Haass, C. (2009). Intramembrane proteolysis by signal peptide peptidases: a comparative discussion of GXGD-type aspartyl proteases. J. Biol. Chem. 284, 13975-13979.
    • (2009) J. Biol. Chem. , vol.284 , pp. 13975-13979
    • Fluhrer, R.1    Steiner, H.2    Haass, C.3
  • 24
    • 29644431788 scopus 로고    scopus 로고
    • γ-Secretase substrate selectivity can be modulated directly via interaction with a nucleotide binding site
    • Fraering, P.C., Ye, W., Lavoie, M.J., Ostaszewski, B.L., Selkoe, D.J., and Wolfe, M.S. (2005). γ-Secretase substrate selectivity can be modulated directly via interaction with a nucleotide binding site. J. Biol. Chem. 280, 41987-41996.
    • (2005) J. Biol. Chem. , vol.280 , pp. 41987-41996
    • Fraering, P.C.1    Ye, W.2    Lavoie, M.J.3    Ostaszewski, B.L.4    Selkoe, D.J.5    Wolfe, M.S.6
  • 25
    • 18444417998 scopus 로고    scopus 로고
    • aph-1 and pen-2 are required for Notch pathway signaling, γ-secretase cleavage of betaAPP, and presenilin protein accumulation
    • Francis, R., McGrath, G., Zhang, J., Ruddy, D.A., Sym, M., Apfeld, J., Nicoll, M., Maxwell, M., Hai, B., Ellis, M.C., et al. (2002). aph-1 and pen-2 are required for Notch pathway signaling, γ-secretase cleavage of betaAPP, and presenilin protein accumulation. Dev. Cell 3, 85-97.
    • (2002) Dev. Cell , vol.3 , pp. 85-97
    • Francis, R.1    McGrath, G.2    Zhang, J.3    Ruddy, D.A.4    Sym, M.5    Apfeld, J.6    Nicoll, M.7    Maxwell, M.8    Hai, B.9    Ellis, M.C.10
  • 26
    • 0034080403 scopus 로고    scopus 로고
    • Aph-2 encodes a novel extracellular protein required for GLP-1-mediated signaling
    • Goutte, C., Hepler, W., Mickey, K.M., and Priess, J.R. (2000). aph-2 encodes a novel extracellular protein required for GLP-1-mediated signaling. Development 127, 2481-2492. (Pubitemid 30386585)
    • (2000) Development , vol.127 , Issue.11 , pp. 2481-2492
    • Goutte, C.1    Hepler, W.2    Mickey, K.M.3    Priess, J.R.4
  • 27
    • 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. (2002). APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos. Proc. Natl. Acad. Sci. USA 99, 775-779.
    • (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
  • 28
    • 72549105935 scopus 로고    scopus 로고
    • Effect of tarenflurbil on cognitive decline and activities of daily living in patients with mild Alzheimer disease: A randomized controlled trial
    • Green, R.C., Schneider, L.S., Amato, D.A., Beelen, A.P., Wilcock, G., Swabb, E.A., and Zavitz, K.H. (2009). Effect of tarenflurbil on cognitive decline and activities of daily living in patients with mild Alzheimer disease: a randomized controlled trial. J. Am. Med. Assoc. 302, 2557-2564.
    • (2009) J. Am. Med. Assoc. , vol.302 , pp. 2557-2564
    • Green, R.C.1    Schneider, L.S.2    Amato, D.A.3    Beelen, A.P.4    Wilcock, G.5    Swabb, E.A.6    Zavitz, K.H.7
  • 29
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy, J. and Selkoe, D.J. (2002). The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356. (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 32
    • 2942557122 scopus 로고    scopus 로고
    • γ-Secretase: Proteasome of the membrane?
    • Kopan, R. and Ilagan, M.X. (2004). γ-Secretase: proteasome of the membrane? Nat. Rev. Mol. Cell Biol. 5, 499-504.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 499-504
    • Kopan, R.1    Ilagan, M.X.2
  • 33
    • 0038607066 scopus 로고    scopus 로고
    • Differential effects of inhibitors on the γ-secretase complex. Mechanistic implications
    • Kornilova, A.Y., Das, C., and Wolfe, M.S. (2003). Differential effects of inhibitors on the γ-secretase complex. Mechanistic implications. J. Biol. Chem. 278, 16470-16473.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16470-16473
    • Kornilova, A.Y.1    Das, C.2    Wolfe, M.S.3
  • 34
    • 14744267675 scopus 로고    scopus 로고
    • The initial substrate-binding site of γ-secretase is located on presenilin near the active site
    • Kornilova, A.Y., Bihel, F., Das, C., and Wolfe, M.S. (2005). 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) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3230-3235
    • Kornilova, A.Y.1    Bihel, F.2    Das, C.3    Wolfe, M.S.4
  • 35
    • 33745152311 scopus 로고    scopus 로고
    • Deducing the transmembrane domain organization of presenilin-1 in γ-secretase by cysteine disulfide cross-linking
    • DOI 10.1021/bi060107k
    • Kornilova, A.Y., Kim, J., Laudon, H., and Wolfe, M.S. (2006). Deducing the transmembrane domain organization of presenilin-1 in γ-secretase by cysteine disulfide cross-linking. Biochemistry 45, 7598-7604. (Pubitemid 43894951)
    • (2006) Biochemistry , vol.45 , Issue.24 , pp. 7598-7604
    • Kornilova, A.Y.1    Kim, J.2    Laudon, H.3    Wolfe, M.S.4
  • 38
    • 33646483640 scopus 로고    scopus 로고
    • Electron microscopic structure of purified, active γ-secretase reveals an aqueous intramembrane chamber and two pores
    • Lazarov, V.K., Fraering, P.C., Ye, W., Wolfe, M.S., Selkoe, D.J., and Li, H. (2006). 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) 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
  • 39
    • 0035576260 scopus 로고    scopus 로고
    • Intramembrane proteolysis of signal peptides: An essential step in the generation of HLA-E epitopes
    • Lemberg, M.K., Bland, F.A., Weihofen, A., Braud, V.M., and Martoglio, B. (2001). Intramembrane proteolysis of signal peptides: an essential step in the generation of HLA-E epitopes. J. Immunol. 167, 6441-6446. (Pubitemid 33081577)
    • (2001) Journal of Immunology , vol.167 , Issue.11 , pp. 6441-6446
    • Lemberg, M.K.1    Bland, F.A.2    Weihofen, A.3    Braud, V.M.4    Martoglio, B.5
  • 41
    • 33846543356 scopus 로고    scopus 로고
    • The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis
    • Lemieux, M.J., Fischer, S.J., Cherney, M.M., Bateman, K.S., and James, M.N. (2007). The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis. Proc. Natl. Acad. Sci. USA 104, 750-754.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 750-754
    • Lemieux, M.J.1    Fischer, S.J.2    Cherney, M.M.3    Bateman, K.S.4    James, M.N.5
  • 42
    • 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. (1995). Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene. Nature 377, 351-354.
    • (1995) Nature , vol.377 , pp. 351-354
    • Levitan, D.1    Greenwald, I.2
  • 47
    • 38349144907 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b
    • Martin, L., Fluhrer, R., Reiss, K., Kremmer, E., Saftig, P., and Haass, C. (2008). Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b. J. Biol. Chem. 283, 1644-1652.
    • (2008) J. Biol. Chem. , vol.283 , pp. 1644-1652
    • Martin, L.1    Fluhrer, R.2    Reiss, K.3    Kremmer, E.4    Saftig, P.5    Haass, C.6
  • 48
    • 0036683052 scopus 로고    scopus 로고
    • Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets
    • DOI 10.1093/emboj/cdf414
    • McLauchlan, J., Lemberg, M.K., Hope, G., and Martoglio, B. (2002). Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets. EMBO J. 21, 3980-3988. (Pubitemid 34857431)
    • (2002) EMBO Journal , vol.21 , Issue.15 , pp. 3980-3988
    • McLauchlan, J.1    Lemberg, M.K.2    Hope, G.3    Martoglio, B.4
  • 49
    • 0033867521 scopus 로고    scopus 로고
    • A ligand-induced extracellular cleavage regulates γ-secretase-like proteolytic activation of Notch1
    • Mumm, J.S., Schroeter, E.H., Saxena, M.T., Griesemer, A., Tian, X., Pan, D.J., Ray, W.J., and Kopan, R. (2000). A ligand-induced extracellular cleavage regulates γ-secretase-like proteolytic activation of Notch1. Mol. Cell 5, 197-206. (Pubitemid 30628079)
    • (2000) Molecular Cell , vol.5 , Issue.2 , 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    Ray, W.J.7    Kopan, R.8
  • 50
    • 34547094392 scopus 로고    scopus 로고
    • A C-terminal region of signal peptide peptidase defines a functional domain for intramembrane aspartic protease catalysis
    • Narayanan, S., Sato, T., and Wolfe, M.S. (2007). A C-terminal region of signal peptide peptidase defines a functional domain for intramembrane aspartic protease catalysis. J. Biol. Chem. 282, 20172-20179.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20172-20179
    • Narayanan, S.1    Sato, T.2    Wolfe, M.S.3
  • 52
    • 33749327877 scopus 로고    scopus 로고
    • Intramembrane proteolytic cleavage by human signal peptide peptidase like 3 and malaria signal peptide peptidase
    • DOI 10.1096/fj.06-5762com
    • Nyborg, A.C., Ladd, T.B., Jansen, K., Kukar, T., and Golde, T.E. (2006). Intramembrane proteolytic cleavage by human signal peptide peptidase like 3 and malaria signal peptide peptidase. FASEB J. 20, 1671-1679. (Pubitemid 44943804)
    • (2006) FASEB Journal , vol.20 , Issue.10 , pp. 1671-1679
    • Nyborg, A.C.1    Ladd, T.B.2    Jansen, K.3    Kukar, T.4    Golde, T.E.5
  • 55
    • 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, M.B., Citron, M., Amarante, P., Sherrington, R., Xia, W., Zhang, J., Diehl, T., Levesque, G., Fraser, P., Haass, C., et al. (1997). 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) 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    Diehl, T.7    Levesque, G.8    Fraser, P.9    Haass, C.10
  • 58
    • 0029101491 scopus 로고
    • Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene
    • Rogaev, E.I., Sherrington, R., Rogaeva, E.A., Levesque, G., Ikeda, M., Liang, Y., Chi, H., Lin, C., Holman, K., Tsuda, T., et al. (1995). Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene. Nature 376, 775-778.
    • (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    Chi, H.7    Lin, C.8    Holman, K.9    Tsuda, T.10
  • 59
    • 33751087756 scopus 로고    scopus 로고
    • Structure of the catalytic pore of γ-secretase probed by the accessibility of substituted cysteines
    • DOI 10.1523/JNEUROSCI.3614-06.2006
    • Sato, C., Morohashi, Y., Tomita, T., and Iwatsubo, T. (2006a). Structure of the catalytic pore of γ-secretase probed by the accessibility of substituted cysteines. J. Neurosci. 26, 12081-12088. (Pubitemid 44772118)
    • (2006) Journal of Neuroscience , vol.26 , Issue.46 , pp. 12081-12088
    • Sato, C.1    Morohashi, Y.2    Tomita, T.3    Iwatsubo, T.4
  • 60
    • 33745586176 scopus 로고    scopus 로고
    • Signal peptide peptidase: Biochemical properties and modulation by nonsteroidal antiinflanimatory drugs
    • DOI 10.1021/bi060597g
    • Sato, T., Nyborg, A.C., Iwata, N., Diehl, T.S., Saido, T.C., Golde, T.E., and Wolfe, M.S. (2006b). Signal peptide peptidase: biochemical properties and modulation by nonsteroidal antiinflammatory drugs. Biochemistry 45, 8649-8656. (Pubitemid 44078885)
    • (2006) Biochemistry , vol.45 , Issue.28 , pp. 8649-8656
    • Sato, T.1    Nyborg, A.C.2    Iwata, N.3    Diehl, T.S.4    Saido, T.C.5    Golde, T.E.6    Wolfe, M.S.7
  • 62
    • 46749127360 scopus 로고    scopus 로고
    • The C-terminal PAL motif and transmembrane domain 9 of presenilin 1 are involved in the formation of the catalytic pore of the γ-secretase
    • Sato, C., Takagi, S., Tomita, T., and Iwatsubo, T. (2008). The C-terminal PAL motif and transmembrane domain 9 of presenilin 1 are involved in the formation of the catalytic pore of the γ-secretase. J. Neurosci. 28, 6264-6271.
    • (2008) J. Neurosci. , vol.28 , pp. 6264-6271
    • Sato, C.1    Takagi, S.2    Tomita, T.3    Iwatsubo, T.4
  • 63
    • 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., Bird, T.D., Hardy, J., Hutton, M., Kukull, W., et al. (1996). 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) 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    Bird, T.D.7    Hardy, J.8    Hutton, M.9    Kukull, W.10
  • 64
    • 0032574993 scopus 로고    scopus 로고
    • Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain
    • Schroeter, E.H., Kisslinger, J.A., and Kopan, R. (1998). Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain. Nature 393, 382-386.
    • (1998) Nature , vol.393 , pp. 382-386
    • Schroeter, E.H.1    Kisslinger, J.A.2    Kopan, R.3
  • 67
    • 0041355557 scopus 로고    scopus 로고
    • Notch and Presenilin: Regulated intramembrane proteolysis links development and degeneration
    • Selkoe, D. and Kopan, R. (2003). Notch and Presenilin: regulated intramembrane proteolysis links development and degeneration. Annu. Rev. Neurosci. 26, 565-597.
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 565-597
    • Selkoe, D.1    Kopan, R.2
  • 68
    • 35348860241 scopus 로고    scopus 로고
    • Presenilin: Running with scissors in the membrane
    • Selkoe, D.J. and Wolfe, M.S. (2007). Presenilin: running with scissors in the membrane. Cell 131, 215-221.
    • (2007) Cell , vol.131 , pp. 215-221
    • Selkoe, D.J.1    Wolfe, M.S.2
  • 75
    • 13944276825 scopus 로고    scopus 로고
    • Twenty years of the Alzheimer's disease amyloid hypothesis: A genetic perspective
    • Tanzi, R.E. and Bertram, L. (2005). Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective. Cell 120, 545-555.
    • (2005) Cell , vol.120 , pp. 545-555
    • Tanzi, R.E.1    Bertram, L.2
  • 76
  • 77
    • 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. (2006). 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) J. Biol. Chem. , vol.281 , pp. 27633-27642
    • Tolia, A.1    Chavez-Gutierrez, L.2    De Strooper, B.3
  • 78
    • 50349097998 scopus 로고    scopus 로고
    • Transmembrane domain 9 of presenilin determines the dynamic conformation of the catalytic site of γ-secretase
    • Tolia, A., Horré, K., and De Strooper, B. (2008). Transmembrane domain 9 of presenilin determines the dynamic conformation of the catalytic site of γ-secretase. J. Biol. Chem. 283, 19793-19803.
    • (2008) J. Biol. Chem. , vol.283 , pp. 19793-19803
    • Tolia, A.1    Horré, K.2    De Strooper, B.3
  • 79
    • 33847793631 scopus 로고    scopus 로고
    • Open-cap conformation of intramembrane protease GlpG
    • Wang, Y. and Ha, Y. (2007). Open-cap conformation of intramembrane protease GlpG. Proc. Natl. Acad. Sci. USA 104, 2098-2102.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2098-2102
    • Wang, Y.1    Ha, Y.2
  • 80
    • 33750886311 scopus 로고    scopus 로고
    • Crystal structure of a rhomboid family intramembrane protease
    • Wang, Y., Zhang, Y., and Ha, Y. (2006). Crystal structure of a rhomboid family intramembrane protease. Nature 444, 179-180.
    • (2006) Nature , vol.444 , pp. 179-180
    • Wang, Y.1    Zhang, Y.2    Ha, Y.3
  • 82
    • 0041876229 scopus 로고    scopus 로고
    • Evidence that nonsteroidal anti-inflammatory drugs decrease amyloid β42 production by direct modulation of γ-secretase activity
    • Weggen, S., Eriksen, J.L., Sagi, S.A., Pietrzik, C.U., Ozols, V., Fauq, A., Golde, T.E., and Koo, E.H. (2003). Evidence that nonsteroidal anti-inflammatory drugs decrease amyloid β42 production by direct modulation of γ-secretase activity. J. Biol. Chem. 278, 31831-31837.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31831-31837
    • Weggen, S.1    Eriksen, J.L.2    Sagi, S.A.3    Pietrzik, C.U.4    Ozols, V.5    Fauq, A.6    Golde, T.E.7    Koo, E.H.8
  • 83
    • 0037176727 scopus 로고    scopus 로고
    • A novel ε-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with notch processing
    • DOI 10.1021/bi015794o
    • Weidemann, A., Eggert, S., Reinhard, F.B., Vogel, M., Paliga, K., Baier, G., Masters, C.L., Beyreuther, K., and Evin, G. (2002). A novel var ε-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with notch processing. Biochemistry 41, 2825-2835. (Pubitemid 34168952)
    • (2002) Biochemistry , vol.41 , Issue.8 , pp. 2825-2835
    • Weidemann, A.1    Eggert, S.2    Reinhard, F.B.M.3    Vogel, M.4    Paliga, K.5    Baier, G.6    Masters, C.L.7    Beyreuther, K.8    Evin, G.9
  • 84
    • 0037150672 scopus 로고    scopus 로고
    • Identification of signal peptide peptidase, a presenilin-type aspartic protease
    • DOI 10.1126/science.1070925
    • Weihofen, A., Binns, K., Lemberg, M.K., Ashman, K., and Martoglio, B. (2002). Identification of signal peptide peptidase, a presenilin-type aspartic protease. Science 296, 2215-2218. (Pubitemid 34680305)
    • (2002) Science , vol.296 , Issue.5576 , pp. 2215-2218
    • Weihofen, A.1    Binns, K.2    Lemberg, M.K.3    Ashman, K.4    Martoglio, B.5
  • 86
    • 40349114687 scopus 로고    scopus 로고
    • γ-Secretase: Structure, function, and modulation for Alzheimer's disease
    • Wolfe, M.S. (2008). γ-Secretase: structure, function, and modulation for Alzheimer's disease. Curr. Top. Med. Chem. 8, 2-8.
    • (2008) Curr. Top. Med. Chem. , vol.8 , pp. 2-8
    • Wolfe, M.S.1
  • 87
    • 67649827390 scopus 로고    scopus 로고
    • Intramembrane-cleaving proteases
    • Wolfe, M.S. (2009). Intramembrane-cleaving proteases. J. Biol. Chem. 284, 13969-13973.
    • (2009) J. Biol. Chem. , vol.284 , pp. 13969-13973
    • Wolfe, M.S.1
  • 88
    • 0033621152 scopus 로고    scopus 로고
    • Are presenilins intramembrane-cleaving proteases? Implications for the molecular mechanism of Alzheimer's disease
    • DOI 10.1021/bi991080q
    • Wolfe, M.S., De Los Angeles, J., Miller, D.D., Xia, W., and Selkoe, D.J. (1999a). Are presenilins intramembrane-cleaving proteases? Implications for the molecular mechanism of Alzheimer's disease. Biochemistry 38, 11223-11230. (Pubitemid 29420941)
    • (1999) Biochemistry , vol.38 , Issue.35 , pp. 11223-11230
    • Wolfe, M.S.1    De Los Angeles, J.2    Miller, D.D.3    Xia, W.4    Selkoe, D.J.5
  • 89
    • 0033551099 scopus 로고    scopus 로고
    • Peptidomimetic probes and molecular modeling suggest that Alzheimer's γ-secretase is an intramembrane-cleaving aspartyl protease
    • Wolfe, M.S., Xia, W., Moore, C.L., Leatherwood, D.D., Ostaszewski, B., Donkor, I.O., and Selkoe, D.J. (1999b). Peptidomimetic probes and molecular modeling suggest Alzheimer's γ-secretases are intramembrane-cleaving aspartyl proteases. Biochemistry 38, 4720-4727. (Pubitemid 129514811)
    • (1999) Biochemistry , vol.38 , Issue.15 , pp. 4720-4727
    • Wolfe, M.S.1    Xia, W.2    Moore, C.L.3    Leatherwood, D.D.4    Ostaszewski, B.5    Rahmati, T.6    Donkor, I.O.7    Selkoe, D.J.8
  • 90
    • 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. (1999c). Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity. Nature 398, 513-517. (Pubitemid 129523589)
    • (1999) Nature , vol.398 , Issue.6727 , 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
  • 91
    • 11144355129 scopus 로고    scopus 로고
    • Chronic treatment with the γ-secretase inhibitor LY-411,575 inhibits β-amyloid peptide production and alters lymphopoiesis and intestinal cell differentiation
    • Wong, G.T., Manfra, D., Poulet, F.M., Zhang, Q., Josien, H., Bara, T., Engstrom, L., Pinzon-Ortiz, M., Fine, J.S., Lee, H.J., et al. (2004). Chronic treatment with the γ-secretase inhibitor LY-411,575 inhibits β-amyloid peptide production and alters lymphopoiesis and intestinal cell differentiation. J. Biol. Chem. 279, 12876-12882.
    • (2004) J. Biol. Chem. , vol.279 , pp. 12876-12882
    • Wong, G.T.1    Manfra, D.2    Poulet, F.M.3    Zhang, Q.4    Josien, H.5    Bara, T.6    Engstrom, L.7    Pinzon-Ortiz, M.8    Fine, J.S.9    Lee, H.J.10
  • 93
    • 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, D.M., Levesque, L., Rogaeva, E., Xu, D., Liang, Y., Duthie, M., et al. (1998). 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) 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    Rogaeva, E.7    Xu, D.8    Liang, Y.9    Duthie, M.10
  • 95
    • 0032524865 scopus 로고    scopus 로고
    • Subcellular distribution and turnover of presenilins in transfected cells
    • Zhang, J., Kang, D.E., Xia, W., Okochi, M., Mori, H., Selkoe, D.J., and Koo, E.H. (1998). Subcellular distribution and turnover of presenilins in transfected cells. J. Biol. Chem. 273, 12436-12442.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12436-12442
    • Zhang, J.1    Kang, D.E.2    Xia, W.3    Okochi, M.4    Mori, H.5    Selkoe, D.J.6    Koo, E.H.7
  • 96
    • 0033779635 scopus 로고    scopus 로고
    • Presenilins are required for γ-secretase cleavage of β-APP and transmembrane cleavage of Notch-1
    • Zhang, Z., Nadeau, P., Song, W., Donoviel, D., Yuan, M., Bernstein, A., and Yankner, B.A. (2000). Presenilins are required for γ-secretase cleavage of β-APP and transmembrane cleavage of Notch-1. Nat. Cell Biol. 2, 463-465.
    • (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    Yankner, B.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.