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Volumn 4, Issue 2, 2012, Pages

Molecular consequences of amyloid precursor protein and presenilin mutations causing autosomal-dominant Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; GAMMA SECRETASE; PRESENILIN;

EID: 84858720343     PISSN: None     EISSN: 17589193     Source Type: Journal    
DOI: 10.1186/alzrt107     Document Type: Review
Times cited : (131)

References (128)
  • 1
    • 79952730699 scopus 로고    scopus 로고
    • 2011 Alzheimer's disease facts and figures
    • Alzheimer Association 21414557
    • 2011 Alzheimer's disease facts and figures. Alzheimer Association, Alzheimers Dement 2011 7 208 244 21414557
    • (2011) Alzheimers Dement , vol.7 , pp. 208-244
  • 2
    • 78049374467 scopus 로고    scopus 로고
    • Novel research horizons for presenilins and gamma-secretases in cell biology and disease
    • 10.1146/annurev-cellbio-100109-104117 20604710
    • Novel research horizons for presenilins and gamma-secretases in cell biology and disease. De Strooper B, Annaert W, Annu Rev Cell Dev Biol 2010 26 235 260 10.1146/annurev-cellbio-100109-104117 20604710
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 235-260
    • De Strooper, B.1    Annaert, W.2
  • 3
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Alzheimer's disease: genes, proteins, and therapy. Selkoe DJ, Physiol Rev 2001 81 741 766 11274343 (Pubitemid 32267077)
    • (2001) Physiological Reviews , vol.81 , Issue.2 , pp. 741-766
    • Selkoe, D.J.1
  • 5
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Glenner GG, Wong CW, Biochem Biophys Res Commun 1984 120 885 890 10.1016/S0006-291X(84)80190-4 6375662 (Pubitemid 14104991)
    • (1984) Biochemical and Biophysical Research Communications , vol.120 , Issue.3 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 6
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • DOI 10.1038/325733a0
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Kang J, Lemaire HG, Unterbeck A, Salbaum JM, Masters CL, Grzeschik KH, Multhaup G, Beyreuther K, Muller-Hill B, Nature 1987 325 733 736 10.1038/325733a0 2881207 (Pubitemid 17054046)
    • (1987) Nature , vol.325 , Issue.6106 , pp. 733-736
    • Kang, J.1    Lemaire, H.-G.2    Unterbeck, A.3
  • 8
    • 0023103748 scopus 로고
    • The genetic defect causing familial Alzheimer's disease maps on chromosome 21
    • The genetic defect causing familial Alzheimer's disease maps on chromosome 21. St George-Hyslop PH, Tanzi RE, Polinsky RJ, Haines JL, Nee L, Watkins PC, Myers RH, Feldman RG, Pollen D, Drachman D, Science 1987 235 885 890 10.1126/science.2880399 2880399 (Pubitemid 17019126)
    • (1987) Science , vol.235 , Issue.4791 , pp. 885-890
    • St George-Hyslop, P.H.1    Tanzi, R.E.2    Polinsky, R.J.3
  • 9
    • 0023109592 scopus 로고
    • Amyloid beta protein gene: cDNA, mRNA distribution, and genetic linkage near the Alzheimer locus
    • Amyloid beta protein gene: cDNA, mRNA distribution, and genetic linkage near the Alzheimer locus. Tanzi RE, Gusella JF, Watkins PC, Bruns GA, St George-Hyslop P, Van Keuren ML, Patterson D, Pagan S, Kurnit DM, Neve RL, Science 1987 235 880 884 10.1126/science.2949367 2949367 (Pubitemid 17019125)
    • (1987) Science , vol.235 , Issue.4791 , pp. 880-884
    • Tanzi, R.E.1    Gusella, J.F.2    Watkins, P.C.3
  • 12
    • 0025950987 scopus 로고
    • A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease
    • A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease. Murrell J, Farlow M, Ghetti B, Benson MD, Science 1991 254 97 99 10.1126/science.1925564 1925564 (Pubitemid 21917324)
    • (1991) Science , vol.254 , Issue.5028 , pp. 97-99
    • Murrell, J.1    Farlow, M.2    Ghetti, B.3    Benson, M.D.4
  • 15
    • 43149083897 scopus 로고    scopus 로고
    • Role of the familial Dutch mutation E22Q in the folding and aggregation of the 15-28 fragment of the Alzheimer amyloid-beta protein
    • DOI 10.1073/pnas.0708193105
    • Role of the familial Dutch mutation E22Q in the folding and aggregation of the 15-28 fragment of the Alzheimer amyloid-beta protein. Baumketner A, Krone MG, Shea JE, Proc Natl Acad Sci USA 2008 105 6027 6032 10.1073/pnas.0708193105 18408165 (Pubitemid 351758393)
    • (2008) Proceedings of the National Academy of Sciences of the United States of America , vol.105 , Issue.16 , pp. 6027-6032
    • Baumketner, A.1    Krone, M.G.2    Shea, J.-E.3
  • 16
    • 0034282630 scopus 로고    scopus 로고
    • Substitutions at codon 22 of Alzheimer's abeta peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells
    • 10821838
    • Substitutions at codon 22 of Alzheimer's abeta peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells. Miravalle L, Tokuda T, Chiarle R, Giaccone G, Bugiani O, Tagliavini F, Frangione B, Ghiso J, J Biol Chem 2000 275 27110 27116 10821838
    • (2000) J Biol Chem , vol.275 , pp. 27110-27116
    • Miravalle, L.1    Tokuda, T.2    Chiarle, R.3    Giaccone, G.4    Bugiani, O.5    Tagliavini, F.6    Frangione, B.7    Ghiso, J.8
  • 18
    • 22444449900 scopus 로고    scopus 로고
    • On the nucleation of amyloid beta-protein monomer folding
    • DOI 10.1110/ps.041292205
    • On the nucleation of amyloid beta-protein monomer folding. Lazo ND, Grant MA, Condron MC, Rigby AC, Teplow DB, Protein Sci 2005 14 1581 1596 15930005 (Pubitemid 41007920)
    • (2005) Protein Science , vol.14 , Issue.6 , pp. 1581-1596
    • Lazo, N.D.1    Grant, M.A.2    Condron, M.C.3    Rigby, A.C.4    Teplow, D.B.5
  • 20
    • 0242580170 scopus 로고    scopus 로고
    • Neurotoxicity and physicochemical properties of Abeta mutant peptides from cerebral amyloid angiopathy: Implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer's disease
    • DOI 10.1074/jbc.M301874200
    • Neurotoxicity and physicochemical properties of Abeta mutant peptides from cerebral amyloid angiopathy: implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer's disease. Murakami K, Irie K, Morimoto A, Ohigashi H, Shindo M, Nagao M, Shimizu T, Shirasawa T, J Biol Chem 2003 278 46179 46187 10.1074/jbc.M301874200 12944403 (Pubitemid 37432769)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.46 , pp. 46179-46187
    • Murakami, K.1    Irie, K.2    Morimoto, A.3    Ohigashi, H.4    Shindo, M.5    Nagao, M.6    Shimizu, T.7    Shirasawa, T.8
  • 21
    • 0037931536 scopus 로고    scopus 로고
    • Differential degradation of amyloid beta genetic variants associated with hereditary dementia or stroke by insulin-degrading enzyme
    • DOI 10.1074/jbc.M300276200
    • Differential degradation of amyloid beta genetic variants associated with hereditary dementia or stroke by insulin-degrading enzyme. Morelli L, Llovera R, Gonzalez SA, Affranchino JL, Prelli F, Frangione B, Ghiso J, Castano EM, J Biol Chem 2003 278 23221 23226 10.1074/jbc.M300276200 12695513 (Pubitemid 36830134)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.26 , pp. 23221-23226
    • Morelli, L.1    Llovera, R.2    Gonzalez, S.A.3    Affranchino, J.L.4    Prelli, F.5    Frangione, B.6    Ghiso, J.7    Castano, E.M.8
  • 22
    • 62549156196 scopus 로고    scopus 로고
    • E22Q-mutant Abeta peptide (AbetaDutch) increases vascular but reduces parenchymal Abeta deposition
    • 10.2353/ajpath.2009.080790 19218342
    • E22Q-mutant Abeta peptide (AbetaDutch) increases vascular but reduces parenchymal Abeta deposition. Herzig MC, Eisele YS, Staufenbiel M, Jucker M, Am J Pathol 2009 174 722 726 10.2353/ajpath.2009.080790 19218342
    • (2009) Am J Pathol , vol.174 , pp. 722-726
    • Herzig, M.C.1    Eisele, Y.S.2    Staufenbiel, M.3    Jucker, M.4
  • 24
    • 0028246308 scopus 로고
    • Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid beta-protein precursor
    • 8021287
    • Mutations associated with a locus for familial Alzheimer's disease result in alternative processing of amyloid beta-protein precursor. Haass C, Hung AY, Selkoe DJ, Teplow DB, J Biol Chem 1994 269 17741 17748 8021287
    • (1994) J Biol Chem , vol.269 , pp. 17741-17748
    • Haass, C.1    Hung, A.Y.2    Selkoe, D.J.3    Teplow, D.B.4
  • 25
    • 76249118271 scopus 로고    scopus 로고
    • An APP inhibitory domain containing the Flemish mutation residue modulates gamma-secretase activity for Abeta production
    • 10.1038/nsmb.1743 20062056
    • An APP inhibitory domain containing the Flemish mutation residue modulates gamma-secretase activity for Abeta production. Tian Y, Bassit B, Chau D, Li YM, Nat Struct Mol Biol 2010 17 151 158 10.1038/nsmb.1743 20062056
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 151-158
    • Tian, Y.1    Bassit, B.2    Chau, D.3    Li, Y.M.4
  • 31
    • 80052205634 scopus 로고    scopus 로고
    • Structural dynamics of the DeltaE22 (Osaka) familial Alzheimer's disease-linked amyloid beta-protein
    • 21838450
    • Structural dynamics of the DeltaE22 (Osaka) familial Alzheimer's disease-linked amyloid beta-protein. Inayathullah M, Teplow DB, Amyloid 2011 18 98 107 21838450
    • (2011) Amyloid , vol.18 , pp. 98-107
    • Inayathullah, M.1    Teplow, D.B.2
  • 32
    • 79955038897 scopus 로고    scopus 로고
    • The Osaka FAD mutation E22Delta leads to the formation of a previously unknown type of amyloid beta fibrils and modulates Abeta neurotoxicity
    • 10.1016/j.jmb.2011.02.049 21402079
    • The Osaka FAD mutation E22Delta leads to the formation of a previously unknown type of amyloid beta fibrils and modulates Abeta neurotoxicity. Ovchinnikova OY, Finder VH, Vodopivec I, Nitsch RM, Glockshuber R, J Mol Biol 2011 408 780 791 10.1016/j.jmb.2011.02.049 21402079
    • (2011) J Mol Biol , vol.408 , pp. 780-791
    • Ovchinnikova, O.Y.1    Finder, V.H.2    Vodopivec, I.3    Nitsch, R.M.4    Glockshuber, R.5
  • 33
    • 79952938717 scopus 로고    scopus 로고
    • The Japanese mutant Abeta (DeltaE22-Abeta(1-39)) forms fibrils instantaneously, with low-thioflavin T fluorescence: Seeding of wild-type Abeta(1-40) into atypical fibrils by DeltaE22-Abeta(1-39)
    • 10.1021/bi1016217 21291268
    • The Japanese mutant Abeta (DeltaE22-Abeta(1-39)) forms fibrils instantaneously, with low-thioflavin T fluorescence: seeding of wild-type Abeta(1-40) into atypical fibrils by DeltaE22-Abeta(1-39). Cloe AL, Orgel JP, Sachleben JR, Tycko R, Meredith SC, Biochemistry 2011 50 2026 2039 10.1021/bi1016217 21291268
    • (2011) Biochemistry , vol.50 , pp. 2026-2039
    • Cloe, A.L.1    Orgel, J.P.2    Sachleben, J.R.3    Tycko, R.4    Meredith, S.C.5
  • 34
    • 0031983456 scopus 로고    scopus 로고
    • Pathologic amyloid beta-protein cell surface fibril assembly on cultured human cerebrovascular smooth muscle cells
    • Pathologic amyloid beta-protein cell surface fibril assembly on cultured human cerebrovascular smooth muscle cells. Van Nostrand WE, Melchor JP, Ruffini L, J Neurochem 1998 70 216 223 9422365 (Pubitemid 28020846)
    • (1998) Journal of Neurochemistry , vol.70 , Issue.1 , pp. 216-223
    • Van Nostrand, W.E.1    Melchor, J.P.2    Ruffini, L.3
  • 35
    • 0027526419 scopus 로고
    • Release of excess amyloid beta protein from a mutant amyloid beta protein precursor
    • Release of excess amyloid beta protein from a mutant amyloid beta protein precursor. Cai XD, Golde TE, Younkin SG, Science 1993 259 514 516 10.1126/science.8424174 8424174 (Pubitemid 23058708)
    • (1993) Science , vol.259 , Issue.5094 , pp. 514-516
    • Cai, X.-D.1    Golde, T.E.2    Younkin, S.G.3
  • 36
    • 0026745610 scopus 로고
    • Mutation of the beta-amyloid precursor protein in familial Alzheimer's disease increases beta-protein production
    • DOI 10.1038/360672a0
    • Mutation of the beta-amyloid precursor protein in familial Alzheimer's disease increases beta-protein production. Citron M, Oltersdorf T, Haass C, McConlogue L, Hung AY, Seubert P, Vigo-Pelfrey C, Lieberburg I, Selkoe DJ, Nature 1992 360 672 674 10.1038/360672a0 1465129 (Pubitemid 23007680)
    • (1992) Nature , vol.360 , Issue.6405 , pp. 672-674
    • Citron, M.1    Oltersdorf, T.2    Haass, C.3    McConlogue, L.4    Hung, A.Y.5    Seubert, P.6    Vigo-Pelfrey, C.7    Lieberburg, I.8    Selkoe, D.J.9
  • 38
    • 0026907151 scopus 로고
    • A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of beta-amyloid
    • 10.1038/ng0892-345 1302033
    • A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of beta-amyloid. Mullan M, Crawford F, Axelman K, Houlden H, Lilius L, Winblad B, Lannfelt L, Nat Genet 1992 1 345 347 10.1038/ng0892-345 1302033
    • (1992) Nat Genet , vol.1 , pp. 345-347
    • Mullan, M.1    Crawford, F.2    Axelman, K.3    Houlden, H.4    Lilius, L.5    Winblad, B.6    Lannfelt, L.7
  • 41
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid beta-protein involves the endocytic pathway
    • Evidence that production and release of amyloid beta-protein involves the endocytic pathway. Koo EH, Squazzo SL, J Biol Chem 1994 269 17386 17389 8021238 (Pubitemid 24218009)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.26 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 42
    • 0028866435 scopus 로고
    • The Swedish mutation causes early-onset Alzheimer's disease by beta-secretase cleavage within the secretory pathway
    • 10.1038/nm1295-1291 7489411
    • The Swedish mutation causes early-onset Alzheimer's disease by beta-secretase cleavage within the secretory pathway. Haass C, Lemere CA, Capell A, Citron M, Seubert P, Schenk D, Lannfelt L, Selkoe DJ, Nat Med 1995 1 1291 1296 10.1038/nm1295-1291 7489411
    • (1995) Nat Med , vol.1 , pp. 1291-1296
    • Haass, C.1    Lemere, C.A.2    Capell, A.3    Citron, M.4    Seubert, P.5    Schenk, D.6    Lannfelt, L.7    Selkoe, D.J.8
  • 45
    • 0037530133 scopus 로고    scopus 로고
    • APP intracellular domain formation and unaltered signaling in the presence of familial Alzheimer's disease mutations
    • DOI 10.1016/S0014-4827(03)00117-4
    • APP intracellular domain formation and unaltered signaling in the presence of familial Alzheimer's disease mutations. Bergman A, Religa D, Karlstrom H, Laudon H, Winblad B, Lannfelt L, Lundkvist J, Naslund J, Exp Cell Res 2003 287 1 9 10.1016/S0014-4827(03)00117-4 12799176 (Pubitemid 36683195)
    • (2003) Experimental Cell Research , vol.287 , Issue.1 , pp. 1-9
    • Bergman, A.1    Religa, D.2    Karlstrom, H.3    Laudon, H.4    Winblad, B.5    Lannfelt, L.6    Lundkvist, J.7    Naslund, J.8
  • 46
    • 5144230066 scopus 로고    scopus 로고
    • Mutations in APP have independent effects on Abeta and CTFgamma generation
    • DOI 10.1016/j.nbd.2004.04.018, PII S0969996104001561
    • Mutations in APP have independent effects on Abeta and CTFgamma generation. Hecimovic S, Wang J, Dolios G, Martinez M, Wang R, Goate AM, Neurobiol Dis 2004 17 205 218 10.1016/j.nbd.2004.04.018 15474359 (Pubitemid 39345777)
    • (2004) Neurobiology of Disease , vol.17 , Issue.2 , pp. 205-218
    • Hecimovic, S.1    Wang, J.2    Dolios, G.3    Martinez, M.4    Wang, R.5    Goate, A.M.6
  • 47
    • 0028322017 scopus 로고
    • An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants
    • 10.1126/science.8191290 8191290
    • An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants. Suzuki N, Cheung TT, Cai XD, Odaka A, Otvos L Jr, Eckman C, Golde TE, Younkin SG, Science 1994 264 1336 1340 10.1126/science.8191290 8191290
    • (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    Golde, T.E.7    Younkin, S.G.8
  • 49
    • 0035929554 scopus 로고    scopus 로고
    • Distinct intramembrane cleavage of the beta-amyloid precursor protein family resembling gamma-secretase-like cleavage of Notch
    • 10.1074/jbc.C100357200 11483588
    • Distinct intramembrane cleavage of the beta-amyloid precursor protein family resembling gamma-secretase-like cleavage of Notch. Gu Y, Misonou H, Sato T, Dohmae N, Takio K, Ihara Y, J Biol Chem 2001 276 35235 35238 10.1074/jbc.C100357200 11483588
    • (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
  • 50
    • 70350451482 scopus 로고    scopus 로고
    • {gamma}-Secretase: Successive tripeptide and tetrapeptide release from the transmembrane domain of {beta}-carboxyl terminal fragment
    • 10.1523/JNEUROSCI.2362-09.2009 19828817
    • {gamma}-Secretase: successive tripeptide and tetrapeptide release from the transmembrane domain of {beta}-carboxyl terminal fragment. Takami M, Nagashima Y, Sano Y, Ishihara S, Morishima-Kawashima M, Funamoto S, Ihara Y, J Neurosci 2009 29 13042 13052 10.1523/JNEUROSCI.2362-09.2009 19828817
    • (2009) J Neurosci , vol.29 , pp. 13042-13052
    • Takami, M.1    Nagashima, Y.2    Sano, Y.3    Ishihara, S.4    Morishima-Kawashima, M.5    Funamoto, S.6    Ihara, Y.7
  • 51
    • 0032981558 scopus 로고    scopus 로고
    • Mechanism of the cleavage specificity of Alzheimer's disease gamma- secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein
    • DOI 10.1073/pnas.96.6.3053
    • Mechanism of the cleavage specificity of Alzheimer's disease gamma-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein. Lichtenthaler SF, Wang R, Grimm H, Uljon SN, Masters CL, Beyreuther K, Proc Natl Acad Sci USA 1999 96 3053 3058 10.1073/pnas.96.6.3053 10077635 (Pubitemid 29148842)
    • (1999) Proceedings of the National Academy of Sciences of the United States of America , vol.96 , Issue.6 , pp. 3053-3058
    • Lichtenthaler, S.F.1    Wang, R.2    Grimm, H.3    Uljon, S.N.4    Masters, C.L.5    Beyreuther, K.6
  • 54
    • 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
    • 10.1038/376775a0 7651536
    • 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 EI, Sherrington R, Rogaeva EA, Levesque G, Ikeda M, Liang Y, Chi H, Lin C, Holman K, Tsuda T, et al. Nature 1995 376 775 778 10.1038/376775a0 7651536
    • (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
  • 58
    • 33749072714 scopus 로고    scopus 로고
    • Presenilin-Dependent ErbB4 Nuclear Signaling Regulates the Timing of Astrogenesis in the Developing Brain
    • DOI 10.1016/j.cell.2006.07.037, PII S0092867406012074
    • Presenilin-dependent ErbB4 nuclear signaling regulates the timing of astrogenesis in the developing brain. Sardi SP, Murtie J, Koirala S, Patten BA, Corfas G, Cell 2006 127 185 197 10.1016/j.cell.2006.07.037 17018285 (Pubitemid 44466644)
    • (2006) Cell , vol.127 , Issue.1 , pp. 185-197
    • Sardi, S.P.1    Murtie, J.2    Koirala, S.3    Patten, B.A.4    Corfas, G.5
  • 61
    • 77953634580 scopus 로고    scopus 로고
    • ER calcium and Alzheimer's disease: In a state of flux
    • 10.1126/scisignal.3114pe10 20332425
    • ER calcium and Alzheimer's disease: in a state of flux. Mattson MP, Sci Signal 2010 3 e10 10.1126/scisignal.3114pe10 20332425
    • (2010) Sci Signal , vol.3
    • Mattson, M.P.1
  • 62
    • 33847021476 scopus 로고    scopus 로고
    • Presenilin diversifies its portfolio
    • DOI 10.1016/j.tig.2007.01.008, PII S0168952507000352
    • Presenilin diversifies its portfolio. Parks AL, Curtis D, Trends Genet 2007 23 140 150 10.1016/j.tig.2007.01.008 17280736 (Pubitemid 46275145)
    • (2007) Trends in Genetics , vol.23 , Issue.3 , pp. 140-150
    • Parks, A.L.1    Curtis, D.2
  • 64
    • 33645105621 scopus 로고    scopus 로고
    • Presenilin clinical mutations can affect gamma-secretase activity by different mechanisms
    • 10.1111/j.1471-4159.2005.03578.x 16405513
    • Presenilin clinical mutations can affect gamma-secretase activity by different mechanisms. Bentahir M, Nyabi O, Verhamme J, Tolia A, Horre K, Wiltfang J, Esselmann H, De Strooper B, J Neurochem 2006 96 732 742 10.1111/j.1471-4159.2005.03578.x 16405513
    • (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    Esselmann, H.7    De Strooper, B.8
  • 65
    • 13244299288 scopus 로고    scopus 로고
    • Presenilin 2 familial Alzheimer's disease mutations result in partial loss of function and dramatic changes in Abeta 42/40 ratios
    • DOI 10.1111/j.1471-4159.2004.02858.x
    • Presenilin 2 familial Alzheimer's disease mutations result in partial loss of function and dramatic changes in Abeta 42/40 ratios. Walker ES, Martinez M, Brunkan AL, Goate A, J Neurochem 2005 92 294 301 10.1111/j.1471-4159.2004. 02858.x 15663477 (Pubitemid 40194020)
    • (2005) Journal of Neurochemistry , vol.92 , Issue.2 , pp. 294-301
    • Walker, E.S.1    Martinez, M.2    Brunkan, A.L.3    Goate, A.4
  • 69
    • 33744952846 scopus 로고    scopus 로고
    • Wild-type presenilin 1 protects against Alzheimer disease mutation-induced amyloid pathology
    • DOI 10.1074/jbc.M512574200
    • Wild-type presenilin 1 protects against Alzheimer disease mutation-induced amyloid pathology. Wang R, Wang B, He W, Zheng H, J Biol Chem 2006 281 15330 15336 10.1074/jbc.M512574200 16574645 (Pubitemid 43855123)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.22 , pp. 15330-15336
    • Wang, R.1    Wang, B.2    He, W.3    Zheng, H.4
  • 71
    • 33947201115 scopus 로고    scopus 로고
    • Loss-of-function presenilin mutations in Alzheimer disease. Talking Point on the role of presenilin mutations in Alzheimer disease
    • DOI 10.1038/sj.embor.7400897, PII 7400897
    • Loss-of-function presenilin mutations in Alzheimer disease. Talking Point on the role of presenilin mutations in Alzheimer disease. De Strooper B, EMBO Rep 2007 8 141 146 10.1038/sj.embor.7400897 17268505 (Pubitemid 46420841)
    • (2007) EMBO Reports , vol.8 , Issue.2 , pp. 141-146
    • De Strooper, B.1
  • 73
    • 33947242870 scopus 로고    scopus 로고
    • When loss is gain: Reduced presenilin proteolytic function leads to increased Abeta42/Abeta40. Talking Point on the role of presenilin mutations in Alzheimer disease
    • DOI 10.1038/sj.embor.7400896, PII 7400896
    • When loss is gain: reduced presenilin proteolytic function leads to increased Abeta42/Abeta40. Talking Point on the role of presenilin mutations in Alzheimer disease. Wolfe MS, EMBO Rep 2007 8 136 140 10.1038/sj.embor.7400896 17268504 (Pubitemid 46420840)
    • (2007) EMBO Reports , vol.8 , Issue.2 , pp. 136-140
    • Wolfe, M.S.1
  • 76
    • 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
    • 10.1046/j.1365-4624.1997.00012.x 9680315
    • 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, Grunberg J, Haass C, Genes Funct 1997 1 149 159 10.1046/j.1365-4624.1997.00012.x 9680315
    • (1997) Genes Funct , vol.1 , pp. 149-159
    • Baumeister, R.1    Leimer, U.2    Zweckbronner, I.3    Jakubek, C.4    Grunberg, J.5    Haass, C.6
  • 78
    • 0037184062 scopus 로고    scopus 로고
    • Presenilin 1 mutations activate gamma 42-secretase but reciprocally inhibit epsilon-secretase cleavage of amyloid precursor protein (APP) and S3-cleavage of notch
    • 10.1074/jbc.M205093200 12119298
    • Presenilin 1 mutations activate gamma 42-secretase but reciprocally inhibit epsilon-secretase cleavage of amyloid precursor protein (APP) and S3-cleavage of notch. Chen F, Gu Y, Hasegawa H, Ruan X, Arawaka S, Fraser P, Westaway D, Mount H, St George-Hyslop P, J Biol Chem 2002 277 36521 36526 10.1074/jbc.M205093200 12119298
    • (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    Westaway, D.7    Mount, H.8    St George-Hyslop, P.9
  • 79
    • 0141429160 scopus 로고    scopus 로고
    • A CBP binding transcriptional repressor produced by the PS1/ cleavage of N-Cadherin is inhibited by PS1 FAD mutations
    • DOI 10.1016/j.cell.2003.08.008
    • A CBP binding transcriptional repressor produced by the PS1/epsilon-cleavage of N-cadherin is inhibited by PS1 FAD mutations. Marambaud P, Wen PH, Dutt A, Shioi J, Takashima A, Siman R, Robakis NK, Cell 2003 114 635 645 10.1016/j.cell.2003.08.008 13678586 (Pubitemid 37159259)
    • (2003) Cell , vol.114 , Issue.5 , pp. 635-645
    • Marambaud, P.1    Wen, P.H.2    Dutt, A.3    Shioi, J.4    Takashima, A.5    Siman, R.6    Robakis, N.K.7
  • 81
    • 0034667650 scopus 로고    scopus 로고
    • Notch-1 activation by familial Alzheimer's disease (FAD)-linked mutant forms of presenilin-1
    • 10.1002/1097-4547(20001015)62:2<311: AID-JNR16>3.0.CO;2-G 11020224
    • Notch-1 activation by familial Alzheimer's disease (FAD)-linked mutant forms of presenilin-1. Nakajima M, Shimizu T, Shirasawa T, J Neurosci Res 2000 62 311 317 10.1002/1097-4547(20001015)62:2<311::AID-JNR16>3.0.CO;2-G 11020224
    • (2000) J Neurosci Res , vol.62 , pp. 311-317
    • Nakajima, M.1    Shimizu, T.2    Shirasawa, T.3
  • 83
    • 0037417750 scopus 로고    scopus 로고
    • Distinct mechanisms by mutant presenilin 1 and 2 leading to increased intracellular levels of amyloid beta-protein 42 in Chinese hamster ovary cells
    • DOI 10.1021/bi0267590
    • Distinct mechanisms by mutant presenilin 1 and 2 leading to increased intracellular levels of amyloid beta-protein 42 in Chinese hamster ovary cells. Qi Y, Morishima-Kawashima M, Sato T, Mitsumori R, Ihara Y, Biochemistry 2003 42 1042 1052 10.1021/bi0267590 12549925 (Pubitemid 36159538)
    • (2003) Biochemistry , vol.42 , Issue.4 , pp. 1042-1052
    • Qi, Y.1    Morishima-Kawashima, M.2    Sato, T.3    Mitsumori, R.4    Ihara, Y.5
  • 84
    • 47749093936 scopus 로고    scopus 로고
    • Enzymatic characteristics of I213T mutant presenilin-1/gamma-secretase in cell models and knock-in mouse brains: Familial Alzheimer disease-linked mutation impairs gamma-site cleavage of amyloid precursor protein C-terminal fragment beta
    • 10.1074/jbc.M801279200 18430735
    • Enzymatic characteristics of I213T mutant presenilin-1/gamma-secretase in cell models and knock-in mouse brains: familial Alzheimer disease-linked mutation impairs gamma-site cleavage of amyloid precursor protein C-terminal fragment beta. Shimojo M, Sahara N, Mizoroki T, Funamoto S, Morishima-Kawashima M, Kudo T, Takeda M, Ihara Y, Ichinose H, Takashima A, J Biol Chem 2008 283 16488 16496 10.1074/jbc.M801279200 18430735
    • (2008) J Biol Chem , vol.283 , pp. 16488-16496
    • Shimojo, M.1    Sahara, N.2    Mizoroki, T.3    Funamoto, S.4    Morishima-Kawashima, M.5    Kudo, T.6    Takeda, M.7    Ihara, Y.8    Ichinose, H.9    Takashima, A.10
  • 85
    • 0032032019 scopus 로고    scopus 로고
    • An Alzheimer's disease-linked PS1 variant rescues the developmental abnormalities of PS1-deficient embryos
    • DOI 10.1016/S0896-6273(00)80998-8
    • 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, Borchelt DR, Sisodia SS, Wong PC, Neuron 1998 20 603 609 10.1016/S0896-6273(00)80998-8 9539132 (Pubitemid 28153088)
    • (1998) Neuron , vol.20 , Issue.3 , pp. 603-609
    • Davis, J.A.1    Naruse, S.2    Chen, H.3    Eckman, C.4    Younkin, S.5    Price, D.L.6    Borchelt, D.R.7    Sisodia, S.S.8    Wong, P.C.9
  • 86
    • 0032032847 scopus 로고    scopus 로고
    • Mutant human presenilin 1 protects presenilin 1 null mouse against embryonic lethality and elevates Abeta1-42/43 expression
    • DOI 10.1016/S0896-6273(00)80999-X
    • Mutant human presenilin 1 protects presenilin 1 null mouse against embryonic lethality and elevates Abeta1-42/43 expression. Qian S, Jiang P, Guan XM, Singh G, Trumbauer ME, Yu H, Chen HY, Van de Ploeg LH, Zheng H, Neuron 1998 20 611 617 10.1016/S0896-6273(00)80999-X 9539133 (Pubitemid 28153089)
    • (1998) Neuron , vol.20 , Issue.3 , pp. 611-617
    • Qian, S.1    Jiang, P.2    Guan, X.-M.3    Singh, G.4    Trumbauer, M.E.5    Yu, H.6    Chen, H.Y.7    Van Der Ploeg, L.H.T.8    Zheng, H.9
  • 91
    • 38349014705 scopus 로고    scopus 로고
    • Wild-type but not FAD mutant presenilin-1 prevents neuronal degeneration by promoting phosphatidylinositol 3-kinase neuroprotective signaling
    • 10.1523/JNEUROSCI.4067-07.2008
    • Wild-type but not FAD mutant presenilin-1 prevents neuronal degeneration by promoting phosphatidylinositol 3-kinase neuroprotective signaling. Baki L, Neve RL, Shao Z, Shioi J, Georgakopoulos A, Robakis NK, Neurosci 2008 28 483 490 10.1523/JNEUROSCI.4067-07.2008
    • (2008) Neurosci , vol.28 , pp. 483-490
    • Baki, L.1    Neve, R.L.2    Shao, Z.3    Shioi, J.4    Georgakopoulos, A.5    Robakis, N.K.6
  • 92
    • 24744459453 scopus 로고    scopus 로고
    • Presenilins mediate phosphatidylinositol 3-kinase/AKT and ERK activation via select signaling receptors: Selectivity of PS2 in platelet-derived growth factor signaling
    • DOI 10.1074/jbc.M500833200
    • Presenilins mediate phosphatidylinositol 3-kinase/AKT and ERK activation via select signaling receptors. Selectivity of PS2 in platelet-derived growth factor signaling. Kang DE, Yoon IS, Repetto E, Busse T, Yermian N, Ie L, Koo EH, J Biol Chem 2005 280 31537 31547 10.1074/jbc.M500833200 16014629 (Pubitemid 41291897)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.36 , pp. 31537-31547
    • Kang, D.E.1    Yoon, I.S.2    Repetto, E.3    Busse, T.4    Yermian, N.5    Ie, L.6    Koo, E.H.7
  • 94
    • 34548317423 scopus 로고    scopus 로고
    • Insensitivity to Abeta42-lowering nonsteroidal anti-inflammatory drugs and gamma-secretase inhibitors is common among aggressive presenilin-1 mutations
    • DOI 10.1074/jbc.M700618200
    • Insensitivity to Abeta 42-lowering non-steroidal anti-inflammatory drugs (NSAIDs) and gamma-secretase inhibitors is common among aggressive presenilin-1 mutations. Czirr E, Leuchtenberger S, Dorner-Ciossek C, Schneider A, Jucker M, Koo EH, Pietrzik CU, Baumann K, Weggen S, J Biol Chem 2007 282 24504 24513 10.1074/jbc.M700618200 17573346 (Pubitemid 47347550)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.34 , pp. 24504-24513
    • Czirr, E.1    Leuchtenberger, S.2    Dorner-Ciossek, C.3    Schneider, A.4    Jucker, M.5    Koo, E.H.6    Pietrzik, C.U.7    Baumann, K.8    Weggen, S.9
  • 95
    • 0037470192 scopus 로고    scopus 로고
    • Familial Alzheimer disease-linked presenilin 1 variants enhance production of both Abeta1-40 and Abeta1-42 peptides that are only partially sensitive to a potent aspartyl protease transition state inhibitor of "gamma-secretase"
    • DOI 10.1074/jbc.M209252200
    • Familial Alzheimer disease-linked presenilin 1 variants enhance production of both Abeta 1-40 and Abeta 1-42 peptides that are only partially sensitive to a potent aspartyl protease transition state inhibitor of "gamma-secretase". Ikeuchi T, Dolios G, Kim SH, Wang R, Sisodia SS, J Biol Chem 2003 278 7010 7018 10.1074/jbc.M209252200 12493731 (Pubitemid 36800696)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.9 , pp. 7010-7018
    • Ikeuchi, T.1    Dolios, G.2    Kim, S.-H.3    Wang, R.4    Sisodia, S.S.5
  • 96
    • 0034523058 scopus 로고    scopus 로고
    • FAD mutations in presenilin-1 or amyloid precursor protein decrease the efficacy of a gamma-secretase inhibitor: Evidence for direct involvement of PS1 in the gamma-secretase cleavage complex
    • DOI 10.1006/nbdi.2000.0322
    • FAD mutations in presenilin-1 or amyloid precursor protein decrease the efficacy of a gamma-secretase inhibitor: evidence for direct involvement of PS1 in the gamma-secretase cleavage complex. Xia W, Ostaszewski BL, Kimberly WT, Rahmati T, Moore CL, Wolfe MS, Selkoe DJ, Neurobiol Dis 2000 7 673 681 10.1006/nbdi.2000.0322 11114265 (Pubitemid 32044291)
    • (2000) Neurobiology of Disease , vol.7 , Issue.6 , pp. 673-681
    • Xia, W.1    Ostaszewski, B.L.2    Taylor Kimberly, W.3    Rahmati, T.4    Moore, C.L.5    Wolfe, M.S.6    Selkoe, D.J.7
  • 97
    • 78651316278 scopus 로고    scopus 로고
    • Presenilin-1 but not amyloid precursor protein mutations present in mouse models of Alzheimer's disease attenuate the response of cultured cells to gamma-secretase modulators regardless of their potency and structure
    • 10.1111/j.1471-4159.2010.07118.x 21091478
    • Presenilin-1 but not amyloid precursor protein mutations present in mouse models of Alzheimer's disease attenuate the response of cultured cells to gamma-secretase modulators regardless of their potency and structure. Hahn S, Bruning T, Ness J, Czirr E, Baches S, Gijsen H, Korth C, Pietrzik CU, Bulic B, Weggen S, J Neurochem 2011 116 385 395 10.1111/j.1471-4159.2010.07118.x 21091478
    • (2011) J Neurochem , vol.116 , pp. 385-395
    • Hahn, S.1    Bruning, T.2    Ness, J.3    Czirr, E.4    Baches, S.5    Gijsen, H.6    Korth, C.7    Pietrzik, C.U.8    Bulic, B.9    Weggen, S.10
  • 98
    • 38149013121 scopus 로고    scopus 로고
    • Generation of Abeta 38 and Abeta 42 is independently and differentially affected by FAD-associated presenilin 1 mutations and gamma -secretase modulation
    • 10.1074/jbc.M708754200 17962197
    • Generation of Abeta 38 and Abeta 42 is independently and differentially affected by FAD-associated presenilin 1 mutations and gamma -secretase modulation. Page RM, Baumann K, Tomioka M, Perez-Revuelta BI, Fukumori A, Jacobsen H, Flohr A, Luebbers T, Ozmen L, Steiner H, Haass C, J Biol Chem 2008 283 677 683 10.1074/jbc.M708754200 17962197
    • (2008) J Biol Chem , vol.283 , pp. 677-683
    • Page, R.M.1    Baumann, K.2    Tomioka, M.3    Perez-Revuelta, B.I.4    Fukumori, A.5    Jacobsen, H.6    Flohr, A.7    Luebbers, T.8    Ozmen, L.9    Steiner, H.10    Haass, C.11
  • 99
    • 77952947184 scopus 로고    scopus 로고
    • APP mutants respond to {gamma}-secretase modulators
    • 10.1074/jbc.M110.103283 20348104
    • APP mutants respond to {gamma}-secretase modulators. Page RM, Gutsmiedl A, Fukumori A, Winkler E, Haass C, Steiner H, J Biol Chem 2010 285 17798 17810 10.1074/jbc.M110.103283 20348104
    • (2010) J Biol Chem , vol.285 , pp. 17798-17810
    • Page, R.M.1    Gutsmiedl, A.2    Fukumori, A.3    Winkler, E.4    Haass, C.5    Steiner, H.6
  • 100
    • 0041876229 scopus 로고    scopus 로고
    • Evidence that nonsteroidal anti-inflammatory drugs decrease amyloid beta42 production by direct modulation of gamma-secretase activity
    • DOI 10.1074/jbc.M303592200
    • Evidence that nonsteroidal anti-inflammatory drugs decrease amyloid beta 42 production by direct modulation of gamma-secretase activity. Weggen S, Eriksen JL, Sagi SA, Pietrzik CU, Ozols V, Fauq A, Golde TE, Koo EH, J Biol Chem 2003 278 31831 31837 10.1074/jbc.M303592200 12805356 (Pubitemid 37048365)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.34 , 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
  • 101
    • 79955426777 scopus 로고    scopus 로고
    • Attenuated A{beta}42 responses to low potency {gamma}-secretase modulators can be overcome for many pathogenic presenilin mutants by second-generation compounds
    • 10.1074/jbc.M110.213587 21357415
    • Attenuated A{beta}42 responses to low potency {gamma}-secretase modulators can be overcome for many pathogenic presenilin mutants by second-generation compounds. Kretner B, Fukumori A, Gutsmiedl A, Page RM, Luebbers T, Galley G, Baumann K, Haass C, Steiner H, J Biol Chem 2011 286 15240 15251 10.1074/jbc.M110.213587 21357415
    • (2011) J Biol Chem , vol.286 , pp. 15240-15251
    • Kretner, B.1    Fukumori, A.2    Gutsmiedl, A.3    Page, R.M.4    Luebbers, T.5    Galley, G.6    Baumann, K.7    Haass, C.8    Steiner, H.9
  • 102
    • 79958260092 scopus 로고    scopus 로고
    • The human brain in a dish: The promise of iPSC-derived neurons
    • 10.1016/j.cell.2011.05.034 21663789
    • The human brain in a dish: the promise of iPSC-derived neurons. Dolmetsch R, Geschwind DH, Cell 2011 145 831 834 10.1016/j.cell.2011.05.034 21663789
    • (2011) Cell , vol.145 , pp. 831-834
    • Dolmetsch, R.1    Geschwind, D.H.2
  • 104
    • 79952310557 scopus 로고    scopus 로고
    • Recombinase-mediated cassette exchange (RMCE): Traditional concepts and current challenges
    • 10.1016/j.jmb.2011.01.004 21241707
    • Recombinase-mediated cassette exchange (RMCE): traditional concepts and current challenges. Turan S, Galla M, Ernst E, Qiao J, Voelkel C, Schiedlmeier B, Zehe C, Bode J, J Mol Biol 2011 407 193 221 10.1016/j.jmb.2011.01.004 21241707
    • (2011) J Mol Biol , vol.407 , pp. 193-221
    • Turan, S.1    Galla, M.2    Ernst, E.3    Qiao, J.4    Voelkel, C.5    Schiedlmeier, B.6    Zehe, C.7    Bode, J.8
  • 110
    • 0034982951 scopus 로고    scopus 로고
    • Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy
    • DOI 10.1002/ana.1009
    • Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy. Grabowski TJ, Cho HS, Vonsattel JP, Rebeck GW, Greenberg SM, Ann Neurol 2001 49 697 705 10.1002/ana.1009 11409420 (Pubitemid 32530235)
    • (2001) Annals of Neurology , vol.49 , Issue.6 , pp. 697-705
    • Grabowski, T.J.1    Cho, H.S.2    Vonsattel, J.P.G.3    William Rebeck, G.4    Greenberg, S.M.5
  • 112
    • 0034327364 scopus 로고    scopus 로고
    • Nonfibrillar diffuse amyloid deposition due to a gamma(42)-secretase site mutation points to an essential role for N-truncated A beta(42) in Alzheimer's disease
    • 10.1093/hmg/9.18.2589 11063718
    • Nonfibrillar diffuse amyloid deposition due to a gamma(42)-secretase site mutation points to an essential role for N-truncated A beta(42) in Alzheimer's disease. Kumar-Singh S, De Jonghe C, Cruts M, Kleinert R, Wang R, Mercken M, De Strooper B, Vanderstichele H, Löfgren A, Vanderhoeven I, Backhovens H, Vanmechelen E, Kroisel PM, Van Broeckhoven C, Hum Mol Genet 2000 9 2589 2598 10.1093/hmg/9.18.2589 11063718
    • (2000) Hum Mol Genet , vol.9 , pp. 2589-2598
    • Kumar-Singh, S.1    De Jonghe, C.2    Cruts, M.3    Kleinert, R.4    Wang, R.5    Mercken, M.6    De7
  • 118
    • 0034094214 scopus 로고    scopus 로고
    • Early-onset Alzheimer disease caused by a new mutation (V717L) in the amyloid precursor protein gene
    • Early-onset Alzheimer disease caused by a new mutation (V717L) in the amyloid precursor protein gene. Murrell JR, Hake AM, Quaid KA, Farlow MR, Ghetti B, Arch Neurol 2000 57 885 887 10.1001/archneur.57.6.885 10867787 (Pubitemid 30397192)
    • (2000) Archives of Neurology , vol.57 , Issue.6 , pp. 885-887
    • Murrell, J.R.1    Hake, A.M.2    Quaid, K.A.3    Farlow, M.R.4    Ghetti, B.5
  • 120
    • 0033966705 scopus 로고    scopus 로고
    • Novel Leu723Pro amyloid precursor protein mutation increases amyloid beta42(43) peptide levels and induces apoptosis
    • DOI 10.1002/1531-8249(200002)47:2<249::AID-ANA18>3.0.CO;2-8
    • Novel Leu723Pro amyloid precursor protein mutation increases amyloid beta42(43) peptide levels and induces apoptosis. Kwok JB, Li QX, Hallupp M, Whyte S, Ames D, Beyreuther K, Masters CL, Schofi eld PR, Ann Neurol 2000 47 249 253 10.1002/1531-8249(200002)47:2<249::AID-ANA18>3.0.CO;2-8 10665499 (Pubitemid 30078575)
    • (2000) Annals of Neurology , vol.47 , Issue.2 , pp. 249-253
    • Kwok, J.B.J.1    Li, Q.-X.2    Hallupp, M.3    Whyte, S.4    Ames, D.5    Beyreuther, K.6    Masters, C.L.7    Schofield, P.R.8
  • 122
    • 26844552573 scopus 로고    scopus 로고
    • APP substitutions V715F and L720P alter PS1 conformation and differentially affect Abeta and AICD generation
    • DOI 10.1111/j.1471-4159.2005.03381.x
    • APP substitutions V715F and L720P alter PS1 conformation and differentially affect Abeta and AICD generation. Tesco G, Ginestroni A, Hiltunen M, Kim M, Dolios G, Hyman BT, Wang R, Berezovska O, Tanzi RE, J Neurochem 2005 95 446 456 10.1111/j.1471-4159.2005.03381.x 16086682 (Pubitemid 41457513)
    • (2005) Journal of Neurochemistry , vol.95 , Issue.2 , pp. 446-456
    • Tesco, G.1    Ginestroni, A.2    Hiltunen, M.3    Kim, M.4    Dolios, G.5    Hyman, B.T.6    Wang, R.7    Berezovska, O.8    Tanzi, R.E.9
  • 123
    • 33847169885 scopus 로고    scopus 로고
    • Decreased Abeta secretion by cells expressing familial Alzheimer's disease-linked mutant presenilin 1
    • DOI 10.1016/j.neures.2006.12.005, PII S0168010206003245
    • Decreased Abeta secretion by cells expressing familial Alzheimer's disease-linked mutant presenilin 1. Shimojo M, Sahara N, Murayama M, Ichinose H, Takashima A, Neurosci Res 2007 57 446 453 10.1016/j.neures.2006.12.005 17210196 (Pubitemid 46283080)
    • (2007) Neuroscience Research , vol.57 , Issue.3 , pp. 446-453
    • Shimojo, M.1    Sahara, N.2    Murayama, M.3    Ichinose, H.4    Takashima, A.5
  • 128
    • 0034623284 scopus 로고    scopus 로고
    • Mutant presenilin 2 transgenic mice. A large increase in the levels of Abeta 42 is presumably associated with the low density membrane domain that contains decreased levels of glycerophospholipids and sphingomyelin
    • 10846187
    • Mutant presenilin 2 transgenic mice. A large increase in the levels of Abeta 42 is presumably associated with the low density membrane domain that contains decreased levels of glycerophospholipids and sphingomyelin. Sawamura N, Morishima-Kawashima M, Waki H, Kobayashi K, Kuramochi T, Frosch MP, Ding K, Ito M, Kim TW, Tanzi RE, Oyama F, Tabira T, Ando S, Ihara Y, J Biol Chem 2000 275 27901 27908 10846187
    • (2000) J Biol Chem , vol.275 , pp. 27901-27908
    • Sawamura, N.1    Morishima-Kawashima, M.2    Waki, H.3    Kobayashi, K.4    Kuramochi, T.5    Frosch, M.P.6    Ding, K.7    Ito, M.8    Kim, T.W.9    Tanzi, R.E.10    Oyama, F.11    Tabira, T.12    Ando, S.13    Ihara, Y.14


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