메뉴 건너뛰기




Volumn 211, Issue 6, 2015, Pages 1157-1176

Physical and functional interaction between the α- and γ-secretases: A new model of regulated intramembrane proteolysis

Author keywords

[No Author keywords available]

Indexed keywords

ADAM10 ENDOPEPTIDASE; ALPHA SECRETASE; AMYLOID PRECURSOR PROTEIN; AVAGACESTAT; BEGACESTAT; BETA SECRETASE 1; GAMMA SECRETASE; SEMAGACESTAT; TETRASPANIN; SECRETASE;

EID: 84979996194     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201502001     Document Type: Article
Times cited : (46)

References (59)
  • 2
    • 84933573947 scopus 로고    scopus 로고
    • Oxidative stress and lipid peroxidation are upstream of amyloid pathology
    • Arimon, M., S. Takeda, K.L. Post, S. Svirsky, B.T. Hyman, and O. Berezovska. 2015. Oxidative stress and lipid peroxidation are upstream of amyloid pathology. Neurobiol. Dis. 84:109-119. http ://dx.doi.org/10.1016/j.nbd.2015.06.013
    • (2015) Neurobiol. Dis , vol.84 , pp. 109-119
    • Arimon, M.1    Takeda, S.2    Post, K.L.3    Svirsky, S.4    Hyman, B.T.5    Berezovska, O.6
  • 3
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans
    • Brown, M.S., J. Ye, R.B. Rawson, and J.L. Goldstein. 2000. Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell. 100:391-398. http ://dx.doi.org/10.1016/S0092-8674(00)80675-3
    • (2000) Cell , vol.100 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 4
    • 14444272986 scopus 로고    scopus 로고
    • Evidence that tumor necrosis factor a converting enzyme is involved in regulated α-secretase cleavage of the Alzheimer amyloid protein precursor
    • Buxbaum, J.D., K.N. Liu, Y. Luo, J.L. Slack, K.L. Stocking, J.J. Peschon, R.S. Johnson, B.J. Castner, D.P. Cerretti, and R.A. Black. 1998. Evidence that tumor necrosis factor a converting enzyme is involved in regulated α-secretase cleavage of the Alzheimer amyloid protein precursor. J. Biol. Chem. 273:27765-27767. http ://dx.doi.org/10.1074/jbc.273.43.27765
    • (1998) J. Biol. Chem , vol.273 , pp. 27765-27767
    • Buxbaum, J.D.1    Liu, K.N.2    Luo, Y.3    Slack, J.L.4    Stocking, K.L.5    Peschon, J.J.6    Johnson, R.S.7    Castner, B.J.8    Cerretti, D.P.9    Black, R.A.10
  • 6
    • 77951236521 scopus 로고    scopus 로고
    • Aph-1 associates directly with full-length and C-terminal fragments of γ-secretase substrates
    • Chen, A.C., L.Y. Guo, B.L. Ostaszewski, D.J. Selkoe, and M.J. LaVoie. 2010. Aph-1 associates directly with full-length and C-terminal fragments of γ-secretase substrates. J. Biol. Chem. 285:11378-11391. http ://dx.doi.org/10.1074/jbc.M109.088815
    • (2010) J. Biol. Chem , vol.285 , pp. 11378-11391
    • Chen, A.C.1    Guo, L.Y.2    Ostaszewski, B.L.3    Selkoe, D.J.4    LaVoie, M.J.5
  • 7
    • 14244268498 scopus 로고    scopus 로고
    • γ-secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage
    • Chyung, J.H., D.M. Raper, and D.J. Selkoe. 2005. γ-secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage. J. Biol. Chem. 280:4383-4392. http ://dx.doi.org/10.1074/jbc.M409272200
    • (2005) J. Biol. Chem , vol.280 , pp. 4383-4392
    • Chyung, J.H.1    Raper, D.M.2    Selkoe, D.J.3
  • 8
    • 16944362157 scopus 로고    scopus 로고
    • Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid betaprotein in both transfected cells and transgenic mice
    • Citron, M., D. Westaway, W. Xia, G. Carlson, T. Diehl, G. Levesque, K. Johnson-Wood, M. Lee, P. Seubert, A. Davis, et al. 1997. Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid betaprotein in both transfected cells and transgenic mice. Nat. Med. 3:67-72. http ://dx.doi.org/10.1038/nm0197-67
    • (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
    • 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. http ://dx.doi.org/10.1016/S0896-6273(03)00205-8
    • (2003) Neuron , vol.38 , pp. 9-12
    • De Strooper, B.1
  • 12
    • 84869121252 scopus 로고    scopus 로고
    • TspanC8 tetraspanins regulate ADAM10/Kuzbanian trafficking and promote Notch activation in flies and mammals
    • Dornier, E., F. Coumailleau, J.F. Ottavi, J. Moretti, C. Boucheix, P. Mauduit, F. Schweisguth, and E. Rubinstein. 2012. TspanC8 tetraspanins regulate ADAM10/Kuzbanian trafficking and promote Notch activation in flies and mammals. J. Cell Biol. 199:481-496. http ://dx.doi.org/10.1083/jcb.201201133
    • (2012) J. Cell Biol , vol.199 , pp. 481-496
    • Dornier, E.1    Coumailleau, F.2    Ottavi, J.F.3    Moretti, J.4    Boucheix, C.5    Mauduit, P.6    Schweisguth, F.7    Rubinstein, E.8
  • 13
    • 77950540047 scopus 로고    scopus 로고
    • A conserved tetraspanin subfamily promotes Notch signaling in Caenorhabditis elegans and in human cells
    • Dunn, C.D., M.L. Sulis, A.A. Ferrando, and I. Greenwald. 2010. A conserved tetraspanin subfamily promotes Notch signaling in Caenorhabditis elegans and in human cells. Proc. Natl. Acad. Sci. USA. 107:5907-5912. http ://dx.doi.org/10.1073/pnas.1001647107
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 5907-5912
    • Dunn, C.D.1    Sulis, M.L.2    Ferrando, A.A.3    Greenwald, I.4
  • 14
    • 0037173115 scopus 로고    scopus 로고
    • Presenilin and nicastrin regulate each other and determine amyloid β-peptide production via complex formation
    • Edbauer, D., E. Winkler, C. Haass, and H. Steiner. 2002. Presenilin and nicastrin regulate each other and determine amyloid β-peptide production via complex formation. Proc. Natl. Acad. Sci. USA. 99:8666-8671. http ://dx.doi.org/10.1073/pnas.132277899
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8666-8671
    • Edbauer, D.1    Winkler, E.2    Haass, C.3    Steiner, H.4
  • 15
    • 0037022644 scopus 로고    scopus 로고
    • Activity-dependent isolation of the presenilin-γ-secretase complex reveals nicastrin and a γ substrate
    • Esler, W.P., W.T. Kimberly, B.L. Ostaszewski, W. Ye, T.S. Diehl, D.J. Selkoe, and M.S. Wolfe. 2002. Activity-dependent isolation of the presenilin-γ-secretase complex reveals nicastrin and a γ substrate. Proc. Natl. Acad. Sci. USA. 99:2720-2725. http ://dx.doi.org/10.1073/pnas.052436599
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2720-2725
    • Esler, W.P.1    Kimberly, W.T.2    Ostaszewski, B.L.3    Ye, W.4    Diehl, T.S.5    Selkoe, D.J.6    Wolfe, M.S.7
  • 16
    • 84865498471 scopus 로고    scopus 로고
    • Peptides based on the presenilin-APP binding domain inhibit APP processing and Aβ production through interfering with the APP transmembrane domain
    • Esselens, C., R. Sannerud, R. Gallardo, V. Baert, D. Kaden, L. Serneels, B. De Strooper, F. Rousseau, G. Multhaup, J. Schymkowitz, et al. 2012. Peptides based on the presenilin-APP binding domain inhibit APP processing and Aβ production through interfering with the APP transmembrane domain. FAS EB J. 26:3765-3778. http ://dx.doi.org/10.1096/fj.11-201368
    • (2012) FAS EB J , vol.26 , pp. 3765-3778
    • Esselens, C.1    Sannerud, R.2    Gallardo, R.3    Baert, V.4    Kaden, D.5    Serneels, L.6    De Strooper, B.7    Rousseau, F.8    Multhaup, G.9    Schymkowitz, J.10
  • 17
    • 15544380450 scopus 로고    scopus 로고
    • Transition-state analogue γ-secretase inhibitors stabilize a 900 kDa presenilin/nicastrin complex
    • Evin, G., L.D. Canterford, D.E. Hoke, R.A. Sharples, J.G. Culvenor, and C.L. Masters. 2005. Transition-state analogue γ-secretase inhibitors stabilize a 900 kDa presenilin/nicastrin complex. Biochemistry. 44:4332-4341. http ://dx.doi.org/10.1021/bi0481702
    • (2005) Biochemistry , vol.44 , 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
  • 18
    • 84863858264 scopus 로고    scopus 로고
    • Notch and the awesome power of genetics
    • Greenwald, I. 2012. Notch and the awesome power of genetics. Genetics. 191:655-669. http ://dx.doi.org/10.1534/genetics.112.141812
    • (2012) Genetics , vol.191 , pp. 655-669
    • Greenwald, I.1
  • 21
    • 84869211737 scopus 로고    scopus 로고
    • The TspanC8 subgroup of tetraspanins interacts with A disintegrin and metalloprotease 10 (ADAM10) and regulates its maturation and cell surface expression
    • Haining, E.J., J. Yang, R.L. Bailey, K. Khan, R. Collier, S. Tsai, S.P. Watson, J. Frampton, P. Garcia, and M.G. Tomlinson. 2012. The TspanC8 subgroup of tetraspanins interacts with A disintegrin and metalloprotease 10 (ADAM10) and regulates its maturation and cell surface expression. J. Biol. Chem. 287:39753-39765. http ://dx.doi.org/10.1074/jbc.M112.416503
    • (2012) J. Biol. Chem , vol.287 , pp. 39753-39765
    • Haining, E.J.1    Yang, J.2    Bailey, R.L.3    Khan, K.4    Collier, R.5    Tsai, S.6    Watson, S.P.7    Frampton, J.8    Garcia, P.9    Tomlinson, M.G.10
  • 22
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy, J., and D.J. Selkoe. 2002. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science. 297:353-356. http ://dx.doi.org/10.1126/science.1072994
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 24
    • 54949110552 scopus 로고    scopus 로고
    • Proteomic profiling of γ-secretase substrates and mapping of substrate requirements
    • Hemming, M.L., J.E. Elias, S.P. Gygi, and D.J. Selkoe. 2008. Proteomic profiling of γ-secretase substrates and mapping of substrate requirements. PLoS Biol. 6:e257. http ://dx.doi.org/10.1371/journal.pbio.0060257
    • (2008) PLoS Biol , vol.6
    • Hemming, M.L.1    Elias, J.E.2    Gygi, S.P.3    Selkoe, D.J.4
  • 26
    • 80155148102 scopus 로고    scopus 로고
    • Dynamic analysis of amyloid β-protein in behaving mice reveals opposing changes in ISF versus parenchymal Aβ during age-related plaque formation
    • Hong, S., O. Quintero-Monzon, B.L. Ostaszewski, D.R. Podlisny, W.T. Cavanaugh, T. Yang, D.M. Holtzman, J.R. Cirrito, and D.J. Selkoe. 2011. Dynamic analysis of amyloid β-protein in behaving mice reveals opposing changes in ISF versus parenchymal Aβ during age-related plaque formation. J. Neurosci. 31:15861-15869. http ://dx.doi.org/10.1523/JNE UROSCI.3272-11.2011
    • (2011) J. Neurosci , vol.31 , pp. 15861-15869
    • Hong, S.1    Quintero-Monzon, O.2    Ostaszewski, B.L.3    Podlisny, D.R.4    Cavanaugh, W.T.5    Yang, T.6    Holtzman, D.M.7    Cirrito, J.R.8    Selkoe, D.J.9
  • 27
    • 84980048764 scopus 로고    scopus 로고
    • Structured illumination microscopy for the investigation of synaptic structure and function
    • J.M. Walker, editor. Springer-Verlag New York Inc., New York. In press
    • Hong, S., D. Wilton, B. Stevens, and D. Richardson. 2015. Structured illumination microscopy for the investigation of synaptic structure and function. In Methods in Molecular Biology. J.M. Walker, editor. Springer-Verlag New York Inc., New York. In press.
    • (2015) Methods in Molecular Biology
    • Hong, S.1    Wilton, D.2    Stevens, B.3    Richardson, D.4
  • 29
    • 84885088410 scopus 로고    scopus 로고
    • A fast growing spectrum of biological functions of γ-secretase in development and disease
    • Jurisch-Yaksi, N., R. Sannerud, and W. Annaert. 2013. A fast growing spectrum of biological functions of γ-secretase in development and disease. Biochim. Biophys. Acta. 1828:2815-2827. http ://dx.doi.org/10.1016/j.bbamem.2013.04.016
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 2815-2827
    • Jurisch-Yaksi, N.1    Sannerud, R.2    Annaert, W.3
  • 30
    • 0036327098 scopus 로고    scopus 로고
    • Presenilin-1 affects trafficking and processing of βAPP and is targeted in a complex with nicastrin to the plasma membrane
    • Kaether, C., S. Lammich, D. Edbauer, M. Ertl, J. Rietdorf, A. Capell, H. Steiner, and C. Haass. 2002. Presenilin-1 affects trafficking and processing of βAPP and is targeted in a complex with nicastrin to the plasma membrane. J. Cell Biol. 158:551-561. http ://dx.doi.org/10.1083/jcb.200201123
    • (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
  • 31
    • 0038652102 scopus 로고    scopus 로고
    • γ-Secretase is a membrane protein complex comprised of presenilin, nicastrin, Aph-1, and Pen-2
    • Kimberly, W.T., M.J. LaVoie, B.L. Ostaszewski, W. Ye, M.S. Wolfe, and D.J. Selkoe. 2003. γ-Secretase is a membrane protein complex comprised of presenilin, nicastrin, Aph-1, and Pen-2. Proc. Natl. Acad. Sci. USA. 100:6382-6387. http ://dx.doi.org/10.1073/pnas.1037392100
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6382-6387
    • Kimberly, W.T.1    LaVoie, M.J.2    Ostaszewski, B.L.3    Ye, W.4    Wolfe, M.S.5    Selkoe, D.J.6
  • 32
    • 0029950149 scopus 로고    scopus 로고
    • Trafficking of cell-surface amyloid beta-protein precursor I. Secretion, endocytosis and recycling as detected by labeled monoclonal antibody
    • Koo, E.H., S.L. Squazzo, D.J. Selkoe, and C.H. Koo. 1996. Trafficking of cell-surface amyloid beta-protein precursor. I. Secretion, endocytosis and recycling as detected by labeled monoclonal antibody. J. Cell Sci. 109:991-998.
    • (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
  • 33
    • 77956392552 scopus 로고    scopus 로고
    • ADAM10 is the physiologically relevant, constitutive α-secretase of the amyloid precursor protein in primary neurons
    • Kuhn, P.H., H. Wang, B. Dislich, A. Colombo, U. Zeitschel, J.W. Ellwart, E. Kremmer, S. Rossner, and S.F. Lichtenthaler. 2010. ADAM10 is the physiologically relevant, constitutive α-secretase of the amyloid precursor protein in primary neurons. EMBO J. 29:3020-3032. http ://dx.doi.org/10.1038/emboj.2010.167
    • (2010) EMBO J , vol.29 , pp. 3020-3032
    • Kuhn, P.H.1    Wang, H.2    Dislich, B.3    Colombo, A.4    Zeitschel, U.5    Ellwart, J.W.6    Kremmer, E.7    Rossner, S.8    Lichtenthaler, S.F.9
  • 34
    • 0141733241 scopus 로고    scopus 로고
    • Assembly of the γ-secretase complex involves early formation of an intermediate subcomplex of Aph-1 and nicastrin
    • LaVoie, M.J., P.C. Fraering, B.L. Ostaszewski, W. Ye, W.T. Kimberly, M.S. Wolfe, and D.J. Selkoe. 2003. Assembly of the γ-secretase complex involves early formation of an intermediate subcomplex of Aph-1 and nicastrin. J. Biol. Chem. 278:37213-37222. http ://dx.doi.org/10.1074/jbc.M303941200
    • (2003) J. Biol. Chem , vol.278 , pp. 37213-37222
    • LaVoie, M.J.1    Fraering, P.C.2    Ostaszewski, B.L.3    Ye, W.4    Kimberly, W.T.5    Wolfe, M.S.6    Selkoe, D.J.7
  • 37
    • 0027104001 scopus 로고
    • Dynamics of three-dimensional replication patterns during the S-phase, analysed by double labelling of DNA and confocal microscopy
    • Manders, E.M., J. Stap, G.J. Brakenhoff, R. van Driel, and J.A. Aten. 1992. Dynamics of three-dimensional replication patterns during the S-phase, analysed by double labelling of DNA and confocal microscopy. J. Cell Sci. 103:857-862.
    • (1992) J. Cell Sci , vol.103 , pp. 857-862
    • Manders, E.M.1    Stap, J.2    Brakenhoff, G.J.3    van Driel, R.4    Aten, J.A.5
  • 40
    • 0026176190 scopus 로고
    • Homology of the amyloid beta protein precursor in monkey and human supports a primate model for beta amyloidosis in Alzheimer's disease
    • Podlisny, M.B., D.R. Tolan, and D.J. Selkoe. 1991. Homology of the amyloid beta protein precursor in monkey and human supports a primate model for beta amyloidosis in Alzheimer's disease. Am. J. Pathol. 138:1423-1435.
    • (1991) Am. J. Pathol , vol.138 , pp. 1423-1435
    • Podlisny, M.B.1    Tolan, D.R.2    Selkoe, D.J.3
  • 41
    • 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., M. Citron, P. Amarante, R. Sherrington, W. Xia, J. Zhang, T. Diehl, G. Levesque, P. Fraser, C. Haass, 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. http ://dx.doi.org/10.1006/nbdi.1997.0129
    • (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
  • 44
    • 0033579505 scopus 로고    scopus 로고
    • Cell surface presenilin-1 participates in the γ-secretase-like proteolysis of Notch
    • Ray, W.J., M. Yao, J. Mumm, E.H. Schroeter, P. Saftig, M. Wolfe, D.J. Selkoe, R. Kopan, and A.M. Goate. 1999. Cell surface presenilin-1 participates in the γ-secretase-like proteolysis of Notch. J. Biol. Chem. 274:36801-36807. http ://dx.doi.org/10.1074/jbc.274.51.36801
    • (1999) J. Biol. Chem , vol.274 , pp. 36801-36807
    • Ray, W.J.1    Yao, M.2    Mumm, J.3    Schroeter, E.H.4    Saftig, P.5    Wolfe, M.6    Selkoe, D.J.7    Kopan, R.8    Goate, A.M.9
  • 45
    • 84867268345 scopus 로고    scopus 로고
    • Pancortins interact with amyloid precursor protein and modulate cortical cell migration
    • Rice, H.C., M. Townsend, J. Bai, S. Suth, W. Cavanaugh, D.J. Selkoe, and T.L. Young-Pearse. 2012. Pancortins interact with amyloid precursor protein and modulate cortical cell migration. Development. 139:3986-3996. http ://dx.doi.org/10.1242/dev.082909
    • (2012) Development , vol.139 , pp. 3986-3996
    • Rice, H.C.1    Townsend, M.2    Bai, J.3    Suth, S.4    Cavanaugh, W.5    Selkoe, D.J.6    Young-Pearse, T.L.7
  • 47
    • 0038541768 scopus 로고    scopus 로고
    • Intracellular maturation and localization of the tumour necrosis factor alpha convertase (TACE)
    • Schlöndorff, J., J.D. Becherer, and C.P. Blobel. 2000. Intracellular maturation and localization of the tumour necrosis factor alpha convertase (TACE). Biochem. J. 347:131-138. http ://dx.doi.org/10.1042/bj3470131
    • (2000) Biochem. J , vol.347 , pp. 131-138
    • Schlöndorff, J.1    Becherer, J.D.2    Blobel, C.P.3
  • 48
    • 4744375540 scopus 로고    scopus 로고
    • Identification of distinct γ-secretase complexes with different APH-1 variants
    • Shirotani, K., D. Edbauer, S. Prokop, C. Haass, and H. Steiner. 2004. Identification of distinct γ-secretase complexes with different APH-1 variants. J. Biol. Chem. 279:41340-41345. http ://dx.doi.org/10.1074/jbc.M405768200
    • (2004) J. Biol. Chem , vol.279 , pp. 41340-41345
    • Shirotani, K.1    Edbauer, D.2    Prokop, S.3    Haass, C.4    Steiner, H.5
  • 50
    • 66449103810 scopus 로고    scopus 로고
    • ADAM10, the rate-limiting protease of regulated intramembrane proteolysis of Notch and other proteins, is processed by ADA MS-9, ADA MS-15, and the γ-secretase
    • Tousseyn, T., A. Thathiah, E. Jorissen, T. Raemaekers, U. Konietzko, K. Reiss, E. Maes, A. Snellinx, L. Serneels, O. Nyabi, et al. 2009. ADAM10, the rate-limiting protease of regulated intramembrane proteolysis of Notch and other proteins, is processed by ADA MS-9, ADA MS-15, and the γ-secretase. J. Biol. Chem. 284:11738-11747. http ://dx.doi.org/10.1074/jbc.M805894200
    • (2009) J. Biol. Chem , vol.284 , pp. 11738-11747
    • Tousseyn, T.1    Thathiah, A.2    Jorissen, E.3    Raemaekers, T.4    Konietzko, U.5    Reiss, K.6    Maes, E.7    Snellinx, A.8    Serneels, L.9    Nyabi, O.10
  • 51
    • 0033595706 scopus 로고    scopus 로고
    • β-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • Vassar, R., B.D. Bennett, S. Babu-Khan, S. Kahn, E.A. Mendiaz, P. Denis, D.B. Teplow, S. Ross, P. Amarante, R. Loeloff, et al. 1999. β-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science. 286:735-741. http ://dx.doi.org/10.1126/science.286.5440.735
    • (1999) Science , vol.286 , pp. 735-741
    • Vassar, R.1    Bennett, B.D.2    Babu-Khan, S.3    Kahn, S.4    Mendiaz, E.A.5    Denis, P.6    Teplow, D.B.7    Ross, S.8    Amarante, P.9    Loeloff, R.10
  • 52
    • 84878847155 scopus 로고    scopus 로고
    • Presenilin-1 adopts pathogenic conformation in normal aging and in sporadic Alzheimer's disease
    • Wahlster, L., M. Arimon, N. Nasser-Ghodsi, K.L. Post, A. Serrano-Pozo, K. Uemura, and O. Berezovska. 2013. Presenilin-1 adopts pathogenic conformation in normal aging and in sporadic Alzheimer's disease. Acta Neuropathol. 125:187-199. http ://dx.doi.org/10.1007/s00401-012-1065-6
    • (2013) Acta Neuropathol , vol.125 , pp. 187-199
    • Wahlster, L.1    Arimon, M.2    Nasser-Ghodsi, N.3    Post, K.L.4    Serrano-Pozo, A.5    Uemura, K.6    Berezovska, O.7
  • 54
    • 84866487100 scopus 로고    scopus 로고
    • Ectodomain shedding and ADAMs in development
    • Weber, S., and P. Saftig. 2012. Ectodomain shedding and ADAMs in development. Development. 139:3693-3709. http ://dx.doi.org/10.1242/dev.076398
    • (2012) Development , vol.139 , pp. 3693-3709
    • Weber, S.1    Saftig, P.2
  • 55
    • 16944365745 scopus 로고    scopus 로고
    • Enhanced production and oligomerization of the 42-residue amyloid β-protein by Chinese hamster ovary cells stably expressing mutant presenilins
    • Xia, W., J. Zhang, D. Kholodenko, M. Citron, M.B. Podlisny, D.B. Teplow, C. Haass, P. Seubert, E.H. Koo, and D.J. Selkoe. 1997a. Enhanced production and oligomerization of the 42-residue amyloid β-protein by Chinese hamster ovary cells stably expressing mutant presenilins. J. Biol. Chem. 272:7977-7982. http ://dx.doi.org/10.1074/jbc.272.12.7977
    • (1997) J. Biol. Chem , vol.272 , pp. 7977-7982
    • Xia, W.1    Zhang, J.2    Kholodenko, D.3    Citron, M.4    Podlisny, M.B.5    Teplow, D.B.6    Haass, C.7    Seubert, P.8    Koo, E.H.9    Selkoe, D.J.10
  • 56
    • 0030753089 scopus 로고    scopus 로고
    • Interaction between amyloid precursor protein and presenilins in mammalian cells: implications for the pathogenesis of Alzheimer disease
    • Xia, W., J. Zhang, R. Perez, E.H. Koo, and D.J. Selkoe. 1997b. Interaction between amyloid precursor protein and presenilins in mammalian cells: implications for the pathogenesis of Alzheimer disease. Proc. Natl. Acad. Sci. USA. 94:8208-8213. http ://dx.doi.org/10.1073/pnas.94.15.8208
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8208-8213
    • Xia, W.1    Zhang, J.2    Perez, R.3    Koo, E.H.4    Selkoe, D.J.5
  • 57
    • 70350528991 scopus 로고    scopus 로고
    • Tetraspanin12 regulates ADAM10-dependent cleavage of amyloid precursor protein
    • Xu, D., C. Sharma, and M.E. Hemler. 2009. Tetraspanin12 regulates ADAM10-dependent cleavage of amyloid precursor protein. FAS EB J. 23:3674-3681. http ://dx.doi.org/10.1096/fj.09-133462
    • (2009) FAS EB J , vol.23 , pp. 3674-3681
    • Xu, D.1    Sharma, C.2    Hemler, M.E.3
  • 58
    • 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., F. Chen, G. Levesque, M. Nishimura, D.M. Zhang, L. Levesque, E. Rogaeva, D. Xu, Y. Liang, M. Duthie, 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. http ://dx.doi.org/10.1074/jbc.273.26.16470
    • (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
  • 59
    • 19644389648 scopus 로고    scopus 로고
    • CD147 is a regulatory subunit of the γ-secretase complex in Alzheimer's disease amyloid β-peptide production
    • Zhou, S., H. Zhou, P.J. Walian, and B.K. Jap. 2005. CD147 is a regulatory subunit of the γ-secretase complex in Alzheimer's disease amyloid β-peptide production. Proc. Natl. Acad. Sci. USA. 102:7499-7504. http ://dx.doi.org/10.1073/pnas.0502768102
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 7499-7504
    • Zhou, S.1    Zhou, H.2    Walian, P.J.3    Jap, B.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.