메뉴 건너뛰기




Volumn 3, Issue 1, 2010, Pages

Rapid and Direct Transport of Cell Surface APP to the Lysosome defines a novel selective pathway

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN;

EID: 77952530222     PISSN: None     EISSN: 17566606     Source Type: Journal    
DOI: 10.1186/1756-6606-3-11     Document Type: Article
Times cited : (58)

References (57)
  • 2
    • 0034647752 scopus 로고    scopus 로고
    • Characterization of Alzheimer's beta -secretase protein BACE. A pepsin family member with unusual properties
    • 10.1074/jbc.M002095200. 10887202
    • Characterization of Alzheimer's beta -secretase protein BACE. A pepsin family member with unusual properties. M Haniu P Denis Y Young EA Mendiaz J Fuller JO Hui BD Bennett S Kahn S Ross T Burgess, et al. J Biol Chem 2000 275 21099 21106 10.1074/jbc.M002095200 10887202
    • (2000) J Biol Chem , vol.275 , pp. 21099-21106
    • Haniu, M.1    Denis, P.2    Young, Y.3    Mendiaz, E.A.4    Fuller, J.5    Hui, J.O.6    Bennett, B.D.7    Kahn, S.8    Ross, S.9    Burgess, T.10
  • 3
    • 0000792598 scopus 로고    scopus 로고
    • The transmembrane aspartates in presenilin 1 and 2 are obligatory for gamma-secretase activity and amyloid beta-protein generation
    • 10.1074/jbc.275.5.3173. 10652302
    • The transmembrane aspartates in presenilin 1 and 2 are obligatory for gamma-secretase activity and amyloid beta-protein generation. WT Kimberly W Xia T Rahmati MS Wolfe DJ Selkoe, J Biol Chem 2000 275 3173 3178 10.1074/jbc.275.5.3173 10652302
    • (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
  • 5
    • 0029950149 scopus 로고    scopus 로고
    • Trafficking of cell-surface amyloid beta-protein precursor. I. Secretion, endocytosis and recycling as detected by labeled monoclonal antibody
    • 8743946
    • Trafficking of cell-surface amyloid beta-protein precursor. I. Secretion, endocytosis and recycling as detected by labeled monoclonal antibody. EH Koo SL Squazzo DJ Selkoe CH Koo, J Cell Sci 1996 109 991 998 8743946
    • (1996) J Cell Sci , vol.109 , pp. 991-998
    • Koo, E.H.1    Squazzo, S.L.2    Selkoe, D.J.3    Koo, C.H.4
  • 6
    • 0028966092 scopus 로고
    • Characterization of sorting signals in the beta-amyloid precursor protein cytoplasmic domain
    • 10.1074/jbc.270.8.3565. 7876092
    • Characterization of sorting signals in the beta-amyloid precursor protein cytoplasmic domain. A Lai SS Sisodia IS Trowbridge, J Biol Chem 1995 270 3565 3573 10.1074/jbc.270.8.3565 7876092
    • (1995) J Biol Chem , vol.270 , pp. 3565-3573
    • Lai, A.1    Sisodia, S.S.2    Trowbridge, I.S.3
  • 7
    • 0029934134 scopus 로고    scopus 로고
    • Trafficking of cell-surface amyloid beta-protein precursor. II. Endocytosis, recycling and lysosomal targeting detected by immunolocalization
    • 8743947
    • Trafficking of cell-surface amyloid beta-protein precursor. II. Endocytosis, recycling and lysosomal targeting detected by immunolocalization. T Yamazaki EH Koo DJ Selkoe, J Cell Sci 1996 109 999 1008 8743947
    • (1996) J Cell Sci , vol.109 , pp. 999-1008
    • Yamazaki, T.1    Koo, E.H.2    Selkoe, D.J.3
  • 8
    • 0027250352 scopus 로고
    • Processing of the beta-amyloid precursor. Multiple proteases generate and degrade potentially amyloidogenic fragments
    • 8344942
    • Processing of the beta-amyloid precursor. Multiple proteases generate and degrade potentially amyloidogenic fragments. R Siman S Mistretta JT Durkin MJ Savage T Loh S Trusko RW Scott, J Biol Chem 1993 268 16602 16609 8344942
    • (1993) J Biol Chem , vol.268 , pp. 16602-16609
    • Siman, R.1    Mistretta, S.2    Durkin, J.T.3    Savage, M.J.4    Loh, T.5    Trusko, S.6    Scott, R.W.7
  • 9
    • 0031031006 scopus 로고    scopus 로고
    • Trafficking of cell-surface beta-amyloid precursor protein: Evidence that a sorting intermediate participates in synaptic vesicle recycling
    • 8987743
    • Trafficking of cell-surface beta-amyloid precursor protein: evidence that a sorting intermediate participates in synaptic vesicle recycling. NR Marquez-Sterling AC Lo SS Sisodia EH Koo, J Neurosci 1997 17 140 151 8987743
    • (1997) J Neurosci , vol.17 , pp. 140-151
    • Marquez-Sterling, N.R.1    Lo, A.C.2    Sisodia, S.S.3    Koo, E.H.4
  • 10
    • 0026735070 scopus 로고
    • Targeting of cell-surface beta-amyloid precursor protein to lysosomes: Alternative processing into amyloid-bearing fragments
    • 10.1038/357500a0. 1608449
    • Targeting of cell-surface beta-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments. C Haass EH Koo A Mellon AY Hung DJ Selkoe, Nature 1992 357 500 503 10.1038/357500a0 1608449
    • (1992) Nature , vol.357 , pp. 500-503
    • Haass, C.1    Koo, E.H.2    Mellon, A.3    Hung, A.Y.4    Selkoe, D.J.5
  • 11
    • 1842532328 scopus 로고    scopus 로고
    • The role of the endosomal/lysosomal system in amyloid-beta production and the pathophysiology of Alzheimer's disease: Reexamining the spatial paradox from a lysosomal perspective
    • 15004328
    • The role of the endosomal/lysosomal system in amyloid-beta production and the pathophysiology of Alzheimer's disease: reexamining the spatial paradox from a lysosomal perspective. SH Pasternak JW Callahan DJ Mahuran, J Alzheimers Dis 2004 6 53 65 15004328
    • (2004) J Alzheimers Dis , vol.6 , pp. 53-65
    • Pasternak, S.H.1    Callahan, J.W.2    Mahuran, D.J.3
  • 12
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid beta-protein involves the endocytic pathway
    • 8021238
    • Evidence that production and release of amyloid beta-protein involves the endocytic pathway. EH Koo SL Squazzo, J Biol Chem 1994 269 17386 17389 8021238
    • (1994) J Biol Chem , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 14
    • 0029972129 scopus 로고    scopus 로고
    • Effect of alkalizing agents on the processing of the beta-amyloid precursor protein
    • 10.1016/0006-8993(96)00002-9. 8738224
    • Effect of alkalizing agents on the processing of the beta-amyloid precursor protein. G Schrader-Fischer PA Paganetti, Brain Res 1996 716 91 100 10.1016/0006-8993(96)00002-9 8738224
    • (1996) Brain Res , vol.716 , pp. 91-100
    • Schrader-Fischer, G.1    Paganetti, P.A.2
  • 16
    • 0028987849 scopus 로고
    • Inhibition of beta-amyloid formation identifies proteolytic precursors and subcellular site of catabolism
    • 10.1016/0896-6273(95)90322-4. 7695912
    • Inhibition of beta-amyloid formation identifies proteolytic precursors and subcellular site of catabolism. J Higaki D Quon Z Zhong B Cordell, Neuron 1995 14 651 659 10.1016/0896-6273(95)90322-4 7695912
    • (1995) Neuron , vol.14 , pp. 651-659
    • Higaki, J.1    Quon, D.2    Zhong, Z.3    Cordell, B.4
  • 17
    • 0026539090 scopus 로고
    • Processing of the amyloid protein precursor to potentially amyloidogenic derivatives
    • 10.1126/science.1738847. 1738847
    • Processing of the amyloid protein precursor to potentially amyloidogenic derivatives. TE Golde S Estus LH Younkin DJ Selkoe SG Younkin, Science 1992 255 728 730 10.1126/science.1738847 1738847
    • (1992) Science , vol.255 , pp. 728-730
    • Golde, T.E.1    Estus, S.2    Younkin, L.H.3    Selkoe, D.J.4    Younkin, S.G.5
  • 18
    • 0034711207 scopus 로고    scopus 로고
    • Carboxyl-terminal fragments of Alzheimer beta-amyloid precursor protein accumulate in restricted and unpredicted intracellular compartments in presenilin 1-deficient cells
    • 10.1074/jbc.M006986200. 10962005
    • Carboxyl-terminal fragments of Alzheimer beta-amyloid precursor protein accumulate in restricted and unpredicted intracellular compartments in presenilin 1-deficient cells. F Chen DS Yang S Petanceska A Yang A Tandon G Yu R Rozmahel J Ghiso M Nishimura DM Zhang, et al. J Biol Chem 2000 275 36794 36802 10.1074/jbc.M006986200 10962005
    • (2000) J Biol Chem , vol.275 , pp. 36794-36802
    • Chen, F.1    Yang, D.S.2    Petanceska, S.3    Yang, A.4    Tandon, A.5    Yu, G.6    Rozmahel, R.7    Ghiso, J.8    Nishimura, M.9    Zhang, D.M.10
  • 21
    • 0035921427 scopus 로고    scopus 로고
    • The discrepancy between presenilin subcellular localization and gamma- secretase processing of amyloid precursor protein
    • 10.1083/jcb.200104045. 11502763
    • The discrepancy between presenilin subcellular localization and gamma- secretase processing of amyloid precursor protein. P Cupers M Bentahir K Craessaerts I Orlans H Vanderstichele P Saftig B De Strooper W Annaert, J Cell Biol 2001 154 731 740 10.1083/jcb.200104045 11502763
    • (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    De Strooper, B.7    Annaert, W.8
  • 22
    • 0033613129 scopus 로고    scopus 로고
    • Cellular mechanisms of beta-amyloid production and secretion
    • 10.1073/pnas.96.20.11049. 10500121
    • Cellular mechanisms of beta-amyloid production and secretion. S Sinha I Lieberburg, Proc Natl Acad Sci USA 1999 96 11049 11053 10.1073/pnas.96.20.11049 10500121
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11049-11053
    • Sinha, S.1    Lieberburg, I.2
  • 23
    • 0028906488 scopus 로고
    • Basolateral secretion of amyloid precursor protein in Madin-Darby canine kidney cells is disturbed by alterations of intracellular pH and by introducing a mutation associated with familial Alzheimer's disease
    • 10.1074/jbc.270.8.4058. 7876155
    • Basolateral secretion of amyloid precursor protein in Madin-Darby canine kidney cells is disturbed by alterations of intracellular pH and by introducing a mutation associated with familial Alzheimer's disease. B De Strooper K Craessaerts I Dewachter D Moechars B Greenberg F Van Leuven H Van den Berghe, J Biol Chem 1995 270 4058 4065 10.1074/jbc.270.8.4058 7876155
    • (1995) J Biol Chem , vol.270 , pp. 4058-4065
    • De Strooper, B.1    Craessaerts, K.2    Dewachter, I.3    Moechars, D.4    Greenberg, B.5    Van Leuven, F.6    Van Den Berghe, H.7
  • 24
    • 0029942495 scopus 로고    scopus 로고
    • Metabolism of the "swedish" amyloid precursor protein variant in neuro2a (N2a) cells. Evidence that cleavage at the "beta-secretase" site occurs in the golgi apparatus
    • 10.1074/jbc.271.16.9390. 8621605
    • Metabolism of the "Swedish" amyloid precursor protein variant in neuro2a (N2a) cells. Evidence that cleavage at the "beta-secretase" site occurs in the golgi apparatus. G Thinakaran DB Teplow R Siman B Greenberg SS Sisodia, J Biol Chem 1996 271 9390 9397 10.1074/jbc.271.16.9390 8621605
    • (1996) J Biol Chem , vol.271 , pp. 9390-9397
    • Thinakaran, G.1    Teplow, D.B.2    Siman, R.3    Greenberg, B.4    Sisodia, S.S.5
  • 25
    • 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. C Haass CA Lemere A Capell M Citron P Seubert D Schenk L Lannfelt DJ Selkoe, 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
  • 26
    • 0031715512 scopus 로고    scopus 로고
    • Monogenetic determinants of Alzheimer's disease: APP mutations
    • 10.1007/s000180050218. 9791531
    • Monogenetic determinants of Alzheimer's disease: APP mutations. AM Goate, Cell Mol Life Sci 1998 54 897 901 10.1007/s000180050218 9791531
    • (1998) Cell Mol Life Sci , vol.54 , pp. 897-901
    • Goate, A.M.1
  • 28
    • 0037698096 scopus 로고    scopus 로고
    • Presenilin-1, nicastrin, amyloid precursor protein, and gamma-secretase activity are co-localized in the lysosomal membrane
    • 10.1074/jbc.M304009200. 12736250
    • Presenilin-1, nicastrin, amyloid precursor protein, and gamma-secretase activity are co-localized in the lysosomal membrane. SH Pasternak RD Bagshaw M Guiral S Zhang CA Ackerley BJ Pak JW Callahan DJ Mahuran, J Biol Chem 2003 278 26687 26694 10.1074/jbc.M304009200 12736250
    • (2003) J Biol Chem , vol.278 , pp. 26687-26694
    • Pasternak, S.H.1    Bagshaw, R.D.2    Guiral, M.3    Zhang, S.4    Ackerley, C.A.5    Pak, B.J.6    Callahan, J.W.7    Mahuran, D.J.8
  • 30
    • 0029795254 scopus 로고    scopus 로고
    • Amyloid beta-protein reduces acetylcholine synthesis in a cell line derived from cholinergic neurons of the basal forebrain
    • 10.1073/pnas.93.15.8068. 8755604
    • Amyloid beta-protein reduces acetylcholine synthesis in a cell line derived from cholinergic neurons of the basal forebrain. WA Pedersen MA Kloczewiak JK Blusztajn, Proc Natl Acad Sci USA 1996 93 8068 8071 10.1073/pnas.93.15.8068 8755604
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8068-8071
    • Pedersen, W.A.1    Kloczewiak, M.A.2    Blusztajn, J.K.3
  • 31
    • 0022850323 scopus 로고
    • Neuronal properties of clonal hybrid cell lines derived from central cholinergic neurons
    • 10.1126/science.3775382. 3775382
    • Neuronal properties of clonal hybrid cell lines derived from central cholinergic neurons. DN Hammond BH Wainer JH Tonsgard A Heller, Science 1986 234 1237 1240 10.1126/science.3775382 3775382
    • (1986) Science , vol.234 , pp. 1237-1240
    • Hammond, D.N.1    Wainer, B.H.2    Tonsgard, J.H.3    Heller, A.4
  • 32
    • 1842404212 scopus 로고    scopus 로고
    • Beta-amyloid-induced neurotoxicity of a hybrid septal cell line associated with increased tau phosphorylation and expression of beta-amyloid precursor protein
    • 9282919
    • Beta-amyloid-induced neurotoxicity of a hybrid septal cell line associated with increased tau phosphorylation and expression of beta-amyloid precursor protein. WD Le WJ Xie R Kong SH Appel, J Neurochem 1997 69 978 985 9282919
    • (1997) J Neurochem , vol.69 , pp. 978-985
    • Le, W.D.1    Xie, W.J.2    Kong, R.3    Appel, S.H.4
  • 33
    • 0033995111 scopus 로고    scopus 로고
    • Digital analysis of light microscope immunofluorescence: High-resolution co-localization of synaptic proteins in cultured neurons
    • 10.1016/S0165-0270(99)00148-X. 10704665
    • Digital analysis of light microscope immunofluorescence: high-resolution co-localization of synaptic proteins in cultured neurons. B Hutcheon LA Brown MO Poulter, J Neurosci Methods 2000 96 1 9 10.1016/S0165-0270(99)00148-X 10704665
    • (2000) J Neurosci Methods , vol.96 , pp. 1-9
    • Hutcheon, B.1    Brown, L.A.2    Poulter, M.O.3
  • 34
    • 33645105247 scopus 로고    scopus 로고
    • Differential regulation of corticotropin releasing factor 1alpha receptor endocytosis and trafficking by beta-arrestins and Rab GTPases
    • 10.1111/j.1471-4159.2005.03603.x. 16412099
    • Differential regulation of corticotropin releasing factor 1alpha receptor endocytosis and trafficking by beta-arrestins and Rab GTPases. KD Holmes AV Babwah LB Dale MO Poulter SS Ferguson, J Neurochem 2006 96 934 949 10.1111/j.1471-4159.2005.03603.x 16412099
    • (2006) J Neurochem , vol.96 , pp. 934-949
    • Holmes, K.D.1    Babwah, A.V.2    Dale, L.B.3    Poulter, M.O.4    Ferguson, S.S.5
  • 35
    • 2442615053 scopus 로고    scopus 로고
    • Organization of GABA receptor alpha-subunit clustering in the developing rat neocortex and hippocampus
    • 10.1111/j.0953-816X.2004.03349.x. 15128401
    • Organization of GABA receptor alpha-subunit clustering in the developing rat neocortex and hippocampus. B Hutcheon JM Fritschy MO Poulter, Eur J Neurosci 2004 19 2475 2487 10.1111/j.0953-816X.2004.03349.x 15128401
    • (2004) Eur J Neurosci , vol.19 , pp. 2475-2487
    • Hutcheon, B.1    Fritschy, J.M.2    Poulter, M.O.3
  • 37
    • 0024815331 scopus 로고
    • The amyloid precursor protein is concentrated in neuronal lysosomes in normal and Alzheimer disease subjects
    • 10.1016/0014-4886(89)90156-8. 2591522
    • The amyloid precursor protein is concentrated in neuronal lysosomes in normal and Alzheimer disease subjects. LI Benowitz W Rodriguez P Paskevich EJ Mufson D Schenk RL Neve, Exp Neurol 1989 106 237 250 10.1016/0014-4886(89)90156- 8 2591522
    • (1989) Exp Neurol , vol.106 , pp. 237-250
    • Benowitz, L.I.1    Rodriguez, W.2    Paskevich, P.3    Mufson, E.J.4    Schenk, D.5    Neve, R.L.6
  • 39
    • 0026555037 scopus 로고
    • Proteases and proteolysis in the lysosome
    • 10.1007/BF01923508. 1740187
    • Proteases and proteolysis in the lysosome. P Bohley PO Seglen, Experientia 1992 48 151 157 10.1007/BF01923508 1740187
    • (1992) Experientia , vol.48 , pp. 151-157
    • Bohley, P.1    Seglen, P.O.2
  • 40
    • 19444374721 scopus 로고    scopus 로고
    • Uptake and neuritic transport of scrapie prion protein coincident with infection of neuronal cells
    • 10.1523/JNEUROSCI.0653-05.2005. 15917460
    • Uptake and neuritic transport of scrapie prion protein coincident with infection of neuronal cells. AC Magalhaes GS Baron KS Lee O Steele-Mortimer D Dorward MA Prado B Caughey, J Neurosci 2005 25 5207 5216 10.1523/JNEUROSCI.0653- 05.2005 15917460
    • (2005) J Neurosci , vol.25 , pp. 5207-5216
    • Magalhaes, A.C.1    Baron, G.S.2    Lee, K.S.3    Steele-Mortimer, O.4    Dorward, D.5    Prado, M.A.6    Caughey, B.7
  • 44
    • 33748535402 scopus 로고    scopus 로고
    • Distinct clathrin-coated pits sort different G protein-coupled receptor cargo
    • 10.1111/j.1600-0854.2006.00469.x. 16899088
    • Distinct clathrin-coated pits sort different G protein-coupled receptor cargo. SJ Mundell J Luo JL Benovic PB Conley AW Poole, Traffic 2006 7 1420 1431 10.1111/j.1600-0854.2006.00469.x 16899088
    • (2006) Traffic , vol.7 , pp. 1420-1431
    • Mundell, S.J.1    Luo, J.2    Benovic, J.L.3    Conley, P.B.4    Poole, A.W.5
  • 45
    • 33749079184 scopus 로고    scopus 로고
    • Cargo regulates clathrin-coated pit dynamics
    • 10.1016/j.cell.2006.08.035. 17018281
    • Cargo regulates clathrin-coated pit dynamics. MA Puthenveedu M von Zastrow, Cell 2006 127 113 124 10.1016/j.cell.2006.08.035 17018281
    • (2006) Cell , vol.127 , pp. 113-124
    • Puthenveedu, M.A.1    Von Zastrow, M.2
  • 46
    • 33644764063 scopus 로고    scopus 로고
    • Ligands for clathrin-mediated endocytosis are differentially sorted into distinct populations of early endosomes
    • 10.1016/j.cell.2005.12.038. 16530046
    • Ligands for clathrin-mediated endocytosis are differentially sorted into distinct populations of early endosomes. M Lakadamyali MJ Rust X Zhuang, Cell 2006 124 997 1009 10.1016/j.cell.2005.12.038 16530046
    • (2006) Cell , vol.124 , pp. 997-1009
    • Lakadamyali, M.1    Rust, M.J.2    Zhuang, X.3
  • 47
    • 34248172449 scopus 로고    scopus 로고
    • Structure and functions of the human amyloid precursor protein: The whole is more than the sum of its parts
    • 10.1016/j.pneurobio.2007.02.001. 17428603
    • Structure and functions of the human amyloid precursor protein: the whole is more than the sum of its parts. M Gralle ST Ferreira, Prog Neurobiol 2007 82 11 32 10.1016/j.pneurobio.2007.02.001 17428603
    • (2007) Prog Neurobiol , vol.82 , pp. 11-32
    • Gralle, M.1    Ferreira, S.T.2
  • 48
    • 0028985176 scopus 로고
    • Polarized sorting of beta-amyloid precursor protein and its proteolytic products in MDCK cells is regulated by two independent signals
    • 10.1083/jcb.128.4.537. 7860629
    • Polarized sorting of beta-amyloid precursor protein and its proteolytic products in MDCK cells is regulated by two independent signals. C Haass EH Koo A Capell DB Teplow DJ Selkoe, J Cell Biol 1995 128 537 547 10.1083/jcb.128.4.537 7860629
    • (1995) J Cell Biol , vol.128 , pp. 537-547
    • Haass, C.1    Koo, E.H.2    Capell, A.3    Teplow, D.B.4    Selkoe, D.J.5
  • 49
    • 0030966774 scopus 로고    scopus 로고
    • Intracellular and secreted Alzheimer beta-amyloid species are generated by distinct mechanisms in cultured hippocampal neurons
    • 10.1073/pnas.94.8.4125. 9108116
    • Intracellular and secreted Alzheimer beta-amyloid species are generated by distinct mechanisms in cultured hippocampal neurons. PJ Tienari N Ida E Ikonen M Simons A Weidemann G Multhaup CL Masters CG Dotti K Beyreuther, Proc Natl Acad Sci USA 1997 94 4125 4130 10.1073/pnas.94.8.4125 9108116
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4125-4130
    • Tienari, P.J.1    Ida, N.2    Ikonen, E.3    Simons, M.4    Weidemann, A.5    Multhaup, G.6    Masters, C.L.7    Dotti, C.G.8    Beyreuther, K.9
  • 51
    • 0033639117 scopus 로고    scopus 로고
    • Requirements for presenilin-dependent cleavage of notch and other transmembrane proteins
    • 10.1016/S1097-2765(00)00061-7. 11030342
    • Requirements for presenilin-dependent cleavage of notch and other transmembrane proteins. G Struhl A Adachi, Mol Cell 2000 6 625 636 10.1016/S1097-2765(00)00061-7 11030342
    • (2000) Mol Cell , vol.6 , pp. 625-636
    • Struhl, G.1    Adachi, A.2
  • 52
    • 0036327098 scopus 로고    scopus 로고
    • Presenilin-1 affects trafficking and processing of {beta}APP and is targeted in a complex with nicastrin to the plasma membrane
    • 10.1083/jcb.200201123. 12147673
    • Presenilin-1 affects trafficking and processing of {beta}APP and is targeted in a complex with nicastrin to the plasma membrane. C Kaether S Lammich D Edbauer M Ertl J Rietdorf A Capell H Steiner C Haass, J Cell Biol 2002 158 551 561 10.1083/jcb.200201123 12147673
    • (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    Steiner, H.7    Haass, C.8
  • 53
    • 0035847186 scopus 로고    scopus 로고
    • Alpha-synuclein-positive structures in cases with sporadic Alzheimer's disease: Morphology and its relationship to tau aggregation
    • 10.1016/S0006-8993(00)03082-1. 11150486
    • Alpha-synuclein-positive structures in cases with sporadic Alzheimer's disease: morphology and its relationship to tau aggregation. Y Arai M Yamazaki O Mori H Muramatsu G Asano Y Katayama, Brain Res 2001 888 287 296 10.1016/S0006-8993(00)03082-1 11150486
    • (2001) Brain Res , vol.888 , pp. 287-296
    • Arai, Y.1    Yamazaki, M.2    Mori, O.3    Muramatsu, H.4    Asano, G.5    Katayama, Y.6
  • 54
    • 0035823518 scopus 로고    scopus 로고
    • Cellular membrane composition defines A beta-lipid interactions
    • 10.1074/jbc.M103598200. 11438533
    • Cellular membrane composition defines A beta-lipid interactions. SA Waschuk EA Elton AA Darabie PE Fraser JA McLaurin, J Biol Chem 2001 276 33561 33568 10.1074/jbc.M103598200 11438533
    • (2001) J Biol Chem , vol.276 , pp. 33561-33568
    • Waschuk, S.A.1    Elton, E.A.2    Darabie, A.A.3    Fraser, P.E.4    McLaurin, J.A.5
  • 55
    • 0032792982 scopus 로고    scopus 로고
    • A novel substrate for analyzing Alzheimer's disease gamma-secretase
    • 10.1016/S0014-5793(99)00730-9. 10405162
    • A novel substrate for analyzing Alzheimer's disease gamma-secretase. SF Lichtenthaler G Multhaup CL Masters K Beyreuther, FEBS Lett 1999 453 288 292 10.1016/S0014-5793(99)00730-9 10405162
    • (1999) FEBS Lett , vol.453 , pp. 288-292
    • Lichtenthaler, S.F.1    Multhaup, G.2    Masters, C.L.3    Beyreuther, K.4
  • 56
    • 45549093275 scopus 로고    scopus 로고
    • Independent inhibition of Alzheimer disease beta- and gamma-secretase cleavage by lowered cholesterol levels
    • 10.1074/jbc.M801520200. 18308724
    • Independent inhibition of Alzheimer disease beta- and gamma-secretase cleavage by lowered cholesterol levels. MO Grimm HS Grimm I Tomic K Beyreuther T Hartmann C Bergmann, J Biol Chem 2008 283 11302 11311 10.1074/jbc.M801520200 18308724
    • (2008) J Biol Chem , vol.283 , pp. 11302-11311
    • Grimm, M.O.1    Grimm, H.S.2    Tomic, I.3    Beyreuther, K.4    Hartmann, T.5    Bergmann, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.