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Volumn 28, Issue 10, 2008, Pages 1980-1988

TMP21 degradation is mediated by the ubiquitin-proteasome pathway

Author keywords

secretase complex; Alzheimer's disease; Human TMP21; Protein degradation

Indexed keywords

GAMMA SECRETASE; MEMBRANE PROTEIN; PROTEASOME; PROTEASOME INHIBITOR; TMP21 PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 55949127672     PISSN: 0953816X     EISSN: 14609568     Source Type: Journal    
DOI: 10.1111/j.1460-9568.2008.06497.x     Document Type: Article
Times cited : (31)

References (91)
  • 1
    • 0018826203 scopus 로고
    • Role of lysosomes in protein turnover: Catch-up proteolysis after release from NH4Cl inhibition
    • Amenta, J.S. Brocher, S.C. (1980) Role of lysosomes in protein turnover: catch-up proteolysis after release from NH4Cl inhibition. J. Cell. Physiol., 102, 259 266.
    • (1980) J. Cell. Physiol. , vol.102 , pp. 259-266
    • Amenta, J.S.1    Brocher, S.C.2
  • 2
    • 33750135226 scopus 로고    scopus 로고
    • Receptor-mediated tobacco toxicity: Cooperation of the Ras/Raf-1/MEK1/ERK and JAK-2/STAT-3 pathways downstream of alpha7 nicotinic receptor in oral keratinocytes
    • Arredondo, J., Chernyavsky, A.I., Jolkovsky, D.L., Pinkerton, K.E. Grando, S.A. (2006) Receptor-mediated tobacco toxicity: cooperation of the Ras/Raf-1/MEK1/ERK and JAK-2/STAT-3 pathways downstream of alpha7 nicotinic receptor in oral keratinocytes. FASEB J., 20, 2093 2101.
    • (2006) FASEB J. , vol.20 , pp. 2093-2101
    • Arredondo, J.1    Chernyavsky, A.I.2    Jolkovsky, D.L.3    Pinkerton, K.E.4    Grando, S.A.5
  • 3
    • 0035842897 scopus 로고    scopus 로고
    • Golgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatus
    • Barr, F.A., Preisinger, C., Kopajtich, R. Körner, R. (2001) Golgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatus. J. Cell Biol., 155, 885 891.
    • (2001) J. Cell Biol. , vol.155 , pp. 885-891
    • Barr, F.A.1    Preisinger, C.2    Kopajtich, R.3    Körner, R.4
  • 4
    • 1642336602 scopus 로고    scopus 로고
    • Pen-2 is sequestered in the endoplasmic reticulum and subjected to ubiquitylation and proteasome-mediated degradation in the absence of presenilin
    • Bergman, A., Hansson, E.M., Pursglove, S.E., Farmery, M.R., Lannfelt, L., Lendahl, U., Lundkvist, J. Näslund, J. (2004) Pen-2 is sequestered in the endoplasmic reticulum and subjected to ubiquitylation and proteasome-mediated degradation in the absence of presenilin. J. Biol. Chem., 279, 16744 16753.
    • (2004) J. Biol. Chem. , vol.279 , pp. 16744-16753
    • Bergman, A.1    Hansson, E.M.2    Pursglove, S.E.3    Farmery, M.R.4    Lannfelt, L.5    Lendahl, U.6    Lundkvist, J.7    Näslund, J.8
  • 5
    • 0030055357 scopus 로고    scopus 로고
    • Tmp21 and p24A, two type I proteins enriched in pancreatic microsomal membranes, are members of a protein family involved in vesicular trafficking
    • Blum, R., Feick, P., Puype, M., Vandekerckhove, J., Klengel, R., Nastainczyk, W. Schulz, I. (1996) Tmp21 and p24A, two type I proteins enriched in pancreatic microsomal membranes, are members of a protein family involved in vesicular trafficking. J. Biol. Chem., 271, 17183 17189.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17183-17189
    • Blum, R.1    Feick, P.2    Puype, M.3    Vandekerckhove, J.4    Klengel, R.5    Nastainczyk, W.6    Schulz, I.7
  • 9
    • 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
    • Chen, F., Gu, Y., Hasegawa, H., Ruan, X., Arawaka, S., Fraser, P., Westaway, D., Mount, H. George-Hyslop, P.S. (2002) Presenilin 1 mutations activate gamma 42-secretase but reciprocally inhibit epsilon-secretase cleavage of amyloid precursor protein (APP) and S3-cleavage of notch. J. Biol. Chem., 277, 36521 36526.
    • (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    George-Hyslop, P.S.9
  • 11
    • 0023200224 scopus 로고
    • Ubiquitin-protein conjugates in Alzheimer's lesions
    • Cole, G.M. Timiras, P.S. (1987) Ubiquitin-protein conjugates in Alzheimer's lesions. Neurosci. Lett., 79, 207 212.
    • (1987) Neurosci. Lett. , vol.79 , pp. 207-212
    • Cole, G.M.1    Timiras, P.S.2
  • 19
    • 33644781725 scopus 로고    scopus 로고
    • Catabolism of endogenous and overexpressed APH1a and PEN2: Evidence for artifactual involvement of the proteasome in the degradation of overexpressed proteins
    • Dunys, J., Kawarai, T., Wilk, S., St George-Hyslop, P., Alves da Costa, C. Checler, F. (2006) Catabolism of endogenous and overexpressed APH1a and PEN2: evidence for artifactual involvement of the proteasome in the degradation of overexpressed proteins. Biochem. J., 394, 501 509.
    • (2006) Biochem. J. , vol.394 , pp. 501-509
    • Dunys, J.1    Kawarai, T.2    Wilk, S.3    St George-Hyslop, P.4    Alves Da Costa, C.5    Checler, F.6
  • 22
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany, G., Standaert, R.F., Lane, W.S., Choi, S., Corey, E.J. Schreiber, S.L. (1995) Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science, 268, 726 731.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 23
    • 0029796074 scopus 로고    scopus 로고
    • Bimodal interaction of coatomer with the p24 family of putative cargo receptors
    • Fiedler, K., Veit, M., Stamnes, M.A. Rothman, J.E. (1996) Bimodal interaction of coatomer with the p24 family of putative cargo receptors. Science, 273, 1396 1399.
    • (1996) Science , vol.273 , pp. 1396-1399
    • Fiedler, K.1    Veit, M.2    Stamnes, M.A.3    Rothman, J.E.4
  • 26
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner, G.G. Wong, C.W. (1984) Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun., 120, 885 890.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 27
    • 0032971476 scopus 로고    scopus 로고
    • P24 and p23, the major transmembrane proteins of COPI-coated transport vesicles, form hetero-oligomeric complexes and cycle between the organelles of the early secretory pathway
    • Gommel, D., Orci, L., Emig, E.M., Hannah, M.J., Ravazzola, M., Nickel, W., Helms, J.B., Wieland, F.T. Sohn, K. (1999) p24 and p23, the major transmembrane proteins of COPI-coated transport vesicles, form hetero-oligomeric complexes and cycle between the organelles of the early secretory pathway. FEBS Lett., 447, 179 185.
    • (1999) FEBS Lett. , vol.447 , pp. 179-185
    • Gommel, D.1    Orci, L.2    Emig, E.M.3    Hannah, M.J.4    Ravazzola, M.5    Nickel, W.6    Helms, J.B.7    Wieland, F.T.8    Sohn, K.9
  • 28
    • 0019307389 scopus 로고
    • Chloroquine inhibits lysosomal enzyme pinocytosis and enhances lysosomal enzyme secretion by impairing receptor recycling
    • Gonzalez-Noriega, A., Grubb, J.H., Talkad, V. Sly, W.S. (1980) Chloroquine inhibits lysosomal enzyme pinocytosis and enhances lysosomal enzyme secretion by impairing receptor recycling. J. Cell Biol., 85, 839 852.
    • (1980) J. Cell Biol. , vol.85 , pp. 839-852
    • Gonzalez-Noriega, A.1    Grubb, J.H.2    Talkad, V.3    Sly, W.S.4
  • 29
    • 0019315920 scopus 로고
    • Ammonia inhibits phagosome-lysosome fusion in macrophages
    • Gordon, A.H., Hart, P.D. Young, M.R. (1980) Ammonia inhibits phagosome-lysosome fusion in macrophages. Nature, 286, 79 80.
    • (1980) Nature , vol.286 , pp. 79-80
    • Gordon, A.H.1    Hart, P.D.2    Young, M.R.3
  • 30
    • 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. 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. U.S.A., 99, 775 779.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 775-779
    • Goutte, C.1    Tsunozaki, M.2    Hale, V.A.3    Priess, J.R.4
  • 31
    • 0035929554 scopus 로고    scopus 로고
    • 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. (2001) Distinct intramembrane cleavage of the beta-amyloid precursor protein family resembling gamma-secretase-like cleavage of Notch. J. Biol. Chem., 276, 35235 35238.
    • (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
  • 33
    • 34247570016 scopus 로고    scopus 로고
    • Degradation of nicastrin involves both proteasome and lysosome
    • He, G., Qing, H., Tong, Y., Cai, F., Ishiura, S. Song, W. (2007) Degradation of nicastrin involves both proteasome and lysosome. J. Neurochem., 101, 982 992.
    • (2007) J. Neurochem. , vol.101 , pp. 982-992
    • He, G.1    Qing, H.2    Tong, Y.3    Cai, F.4    Ishiura, S.5    Song, W.6
  • 37
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen, T.J., Loo, M.A., Pind, S., Williams, D.B., Goldberg, A.L. Riordan, J.R. (1995) Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell, 83, 129 135.
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1    Loo, M.A.2    Pind, S.3    Williams, D.B.4    Goldberg, A.L.5    Riordan, J.R.6
  • 38
    • 0013945038 scopus 로고
    • Effect of cycloheximide on protein and ribonucleic acid synthesis in cultured human lymphocytes
    • Kay, J.E. Korner, A. (1966) Effect of cycloheximide on protein and ribonucleic acid synthesis in cultured human lymphocytes. Biochem. J., 100, 815 822.
    • (1966) Biochem. J. , vol.100 , pp. 815-822
    • Kay, J.E.1    Korner, A.2
  • 39
    • 0037381710 scopus 로고    scopus 로고
    • Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease
    • Keck, S., Nitsch, R., Grune, T. Ullrich, O. (2003) Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease. J. Neurochem., 85, 115 122.
    • (2003) J. Neurochem. , vol.85 , pp. 115-122
    • Keck, S.1    Nitsch, R.2    Grune, T.3    Ullrich, O.4
  • 40
    • 0034131044 scopus 로고    scopus 로고
    • Impaired proteasome function in Alzheimer's disease
    • Keller, J.N., Hanni, K.B. Markesbery, W.R. (2000) Impaired proteasome function in Alzheimer's disease. J. Neurochem., 75, 436 439.
    • (2000) J. Neurochem. , vol.75 , pp. 436-439
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 41
    • 0342596836 scopus 로고
    • The effect of actidione and other antifungal agents on nucleic acid and protein synthesis in Saccharomyces carlsbergensis
    • Kerridge, D. (1958) The effect of actidione and other antifungal agents on nucleic acid and protein synthesis in Saccharomyces carlsbergensis. J. Gen. Microbiol., 19, 497 506.
    • (1958) J. Gen. Microbiol. , vol.19 , pp. 497-506
    • Kerridge, D.1
  • 42
    • 0030890399 scopus 로고    scopus 로고
    • Endoproteolytic cleavage and proteasomal degradation of presenilin 2 in transfected cells
    • Kim, T.W., Pettingell, W.H., Hallmark, O.G., Moir, R.D., Wasco, W. Tanzi, R.E. (1997) Endoproteolytic cleavage and proteasomal degradation of presenilin 2 in transfected cells. J. Biol. Chem., 272, 11006 11010.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11006-11010
    • Kim, T.W.1    Pettingell, W.H.2    Hallmark, O.G.3    Moir, R.D.4    Wasco, W.5    Tanzi, R.E.6
  • 44
    • 0037160063 scopus 로고    scopus 로고
    • Mammalian APH-1 interacts with presenilin and nicastrin and is required for intramembrane proteolysis of amyloid-beta precursor protein and Notch
    • Lee, S.-F., Shah, S., Li, H., Yu, C., Han, W. Yu, G. (2002) Mammalian APH-1 interacts with presenilin and nicastrin and is required for intramembrane proteolysis of amyloid-beta precursor protein and Notch. J. Biol. Chem., 277, 45013 45019.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45013-45019
    • Lee, S.-F.1    Shah, S.2    Li, H.3    Yu, C.4    Han, W.5    Yu, G.6
  • 48
    • 0029618686 scopus 로고
    • Identification and expression analysis of a potential familial Alzheimer disease gene on chromosome 1 related to AD3
    • Li, J., Ma, J. Potter, H. (1995) Identification and expression analysis of a potential familial Alzheimer disease gene on chromosome 1 related to AD3. Proc. Natl. Acad. Sci. U.S.A., 92, 12180 12184.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 12180-12184
    • Li, J.1    Ma, J.2    Potter, H.3
  • 50
    • 33644920657 scopus 로고    scopus 로고
    • Control of APP processing and Abeta generation level by BACE1 enzymatic activity and transcription
    • Li, Y., Zhou, W., Tong, Y., He, G. Song, W. (2006) Control of APP processing and Abeta generation level by BACE1 enzymatic activity and transcription. FASEB J., 20, 285 292.
    • (2006) FASEB J. , vol.20 , pp. 285-292
    • Li, Y.1    Zhou, W.2    Tong, Y.3    He, G.4    Song, W.5
  • 51
    • 4544345125 scopus 로고    scopus 로고
    • Caspase-mediated specific cleavage of human histone deacetylase 4
    • Liu, F., Dowling, M., Yang, X.-J. Kao, G.D. (2004) Caspase-mediated specific cleavage of human histone deacetylase 4. J. Biol. Chem., 279, 34537 34546.
    • (2004) J. Biol. Chem. , vol.279 , pp. 34537-34546
    • Liu, F.1    Dowling, M.2    Yang, X.-J.3    Kao, G.D.4
  • 56
    • 0141429160 scopus 로고    scopus 로고
    • A CBP binding transcriptional repressor produced by the PS1/epsilon-cleavage of N-cadherin is inhibited by PS1 FAD mutations
    • Marambaud, P., Wen, P.H., Dutt, A., Shioi, J., Takashima, A., Siman, R. Robakis, N.K. (2003) A CBP binding transcriptional repressor produced by the PS1/epsilon-cleavage of N-cadherin is inhibited by PS1 FAD mutations. Cell, 114, 635 645.
    • (2003) Cell , vol.114 , 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
  • 57
    • 0023140474 scopus 로고
    • Ubiquitin is a component of paired helical filaments in Alzheimer's disease
    • Mori, H., Kondo, J. Ihara, Y. (1987) Ubiquitin is a component of paired helical filaments in Alzheimer's disease. Science, 235, 1641 1644.
    • (1987) Science , vol.235 , pp. 1641-1644
    • Mori, H.1    Kondo, J.2    Ihara, Y.3
  • 58
    • 0027024651 scopus 로고
    • A locus for familial early-onset Alzheimer's disease on the long arm of chromosome 14, proximal to the alpha 1-antichymotrypsin gene
    • Mullan, M., Houlden, H., Windelspecht, M., Fidani, L., Lombardi, C., Diaz, P., Rossor, M., Crook, R., Hardy, J., Duff, K. et al. (1992) A locus for familial early-onset Alzheimer's disease on the long arm of chromosome 14, proximal to the alpha 1-antichymotrypsin gene. Nat. Genet., 2, 340 342.
    • (1992) Nat. Genet. , vol.2 , pp. 340-342
    • Mullan, M.1    Houlden, H.2    Windelspecht, M.3    Fidani, L.4    Lombardi, C.5    Diaz, P.6    Rossor, M.7    Crook, R.8    Hardy, J.9    Duff, K.10
  • 60
    • 0030868332 scopus 로고    scopus 로고
    • P23, a major COPI-vesicle membrane protein, constitutively cycles through the early secretory pathway
    • Nickel, W., Sohn, K., Bünning, C. Wieland, F.T. (1997) p23, a major COPI-vesicle membrane protein, constitutively cycles through the early secretory pathway. Proc. Natl. Acad. Sci. U.S.A., 94, 11393 11398.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 11393-11398
    • Nickel, W.1    Sohn, K.2    Bünning, C.3    Wieland, F.T.4
  • 61
    • 0034797234 scopus 로고    scopus 로고
    • The C-terminal fragment of the Alzheimer's disease amyloid protein precursor is degraded by a proteasome-dependent mechanism distinct from gamma-secretase
    • Nunan, J., Shearman, M.S., Checler, F., Cappai, R., Evin, G., Beyreuther, K., Masters, C.L. Small, D.H. (2001) The C-terminal fragment of the Alzheimer's disease amyloid protein precursor is degraded by a proteasome-dependent mechanism distinct from gamma-secretase. Eur. J. Biochem., 268, 5329 5336.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5329-5336
    • Nunan, J.1    Shearman, M.S.2    Checler, F.3    Cappai, R.4    Evin, G.5    Beyreuther, K.6    Masters, C.L.7    Small, D.H.8
  • 62
    • 0242330370 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of the C-terminus of the Alzheimer's disease beta-amyloid protein precursor: Effect of C-terminal truncation on production of beta-amyloid protein
    • Nunan, J., Williamson, N.A., Hill, A.F., Sernee, M.F., Masters, C.L. Small, D.H. (2003) Proteasome-mediated degradation of the C-terminus of the Alzheimer's disease beta-amyloid protein precursor: effect of C-terminal truncation on production of beta-amyloid protein. J. Neurosci. Res., 74, 378 385.
    • (2003) J. Neurosci. Res. , vol.74 , pp. 378-385
    • Nunan, J.1    Williamson, N.A.2    Hill, A.F.3    Sernee, M.F.4    Masters, C.L.5    Small, D.H.6
  • 63
    • 2642714342 scopus 로고
    • Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents
    • Ohkuma, S. Poole, B. (1978) Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents. Proc. Natl. Acad. Sci. U.S.A., 75, 3327 3331.
    • (1978) Proc. Natl. Acad. Sci. U.S.A. , vol.75 , pp. 3327-3331
    • Ohkuma, S.1    Poole, B.2
  • 65
    • 0001521232 scopus 로고
    • Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains
    • Perry, G., Friedman, R., Shaw, G. Chau, V. (1987) Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains. Proc. Natl. Acad. Sci. U.S.A., 84, 3033 3036.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 3033-3036
    • Perry, G.1    Friedman, R.2    Shaw, G.3    Chau, V.4
  • 66
    • 0035005101 scopus 로고    scopus 로고
    • New protease inhibitors prevent gamma-secretase-mediated production of Abeta40/42 without affecting Notch cleavage
    • Petit, A., Bihel, F., da Costa, C.A., Pourquié, O., Checler, F. Kraus, J.L. (2001) New protease inhibitors prevent gamma-secretase-mediated production of Abeta40/42 without affecting Notch cleavage. Nat. Cell Biol., 3, 507 511.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 507-511
    • Petit, A.1    Bihel, F.2    Da Costa, C.A.3    Pourquié, O.4    Checler, F.5    Kraus, J.L.6
  • 67
    • 7444250507 scopus 로고    scopus 로고
    • Degradation of BACE by the ubiquitin-proteasome pathway
    • Qing, H., Zhou, W., Christensen, M.A., Sun, X., Tong, Y. Song, W. (2004) Degradation of BACE by the ubiquitin-proteasome pathway. FASEB J., 18, 1571 1573.
    • (2004) FASEB J. , vol.18 , pp. 1571-1573
    • Qing, H.1    Zhou, W.2    Christensen, M.A.3    Sun, X.4    Tong, Y.5    Song, W.6
  • 68
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock, K.L., Gramm, C., Rothstein, L., Clark, K., Stein, R., Dick, L., Hwang, D. Goldberg, A.L. (1994) Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell, 78, 761 771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 69
    • 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
  • 70
    • 0034033881 scopus 로고    scopus 로고
    • The transmembrane protein p23 contributes to the organization of the Golgi apparatus
    • Rojo, M., Emery, G., Marjomäki, V., McDowall, A.W., Parton, R.G. Gruenberg, J. (2000) The transmembrane protein p23 contributes to the organization of the Golgi apparatus. J. Cell Sci., 113 (Pt 6 1043 1057.
    • (2000) J. Cell Sci. , vol.113 , Issue.6 , pp. 1043-1057
    • Rojo, M.1    Emery, G.2    Marjomäki, V.3    McDowall, A.W.4    Parton, R.G.5    Gruenberg, J.6
  • 71
    • 0034774969 scopus 로고    scopus 로고
    • Presenilin-dependent gamma-secretase processing of beta-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch
    • Sastre, M., Steiner, H., Fuchs, K., Capell, A., Multhaup, G., Condron, M.M., Teplow, D.B. Haass, C. (2001) Presenilin-dependent gamma-secretase processing of beta-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch. EMBO Rep., 2, 835 841.
    • (2001) EMBO Rep. , vol.2 , pp. 835-841
    • Sastre, M.1    Steiner, H.2    Fuchs, K.3    Capell, A.4    Multhaup, G.5    Condron, M.M.6    Teplow, D.B.7    Haass, C.8
  • 74
    • 0034682465 scopus 로고    scopus 로고
    • Elongin BC complex prevents degradation of von Hippel-Lindau tumor suppressor gene products
    • Schoenfeld, A.R., Davidowitz, E.J. Burk, R.D. (2000) Elongin BC complex prevents degradation of von Hippel-Lindau tumor suppressor gene products. Proc. Natl. Acad. Sci. U.S.A., 97, 8507 8512.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8507-8512
    • Schoenfeld, A.R.1    Davidowitz, E.J.2    Burk, R.D.3
  • 75
    • 0023900638 scopus 로고
    • Ubiquitin and microtubule-associated protein tau immunoreactivity each define distinct structures with differing distributions and solubility properties in Alzheimer brain
    • Shaw, G. Chau, V. (1988) Ubiquitin and microtubule-associated protein tau immunoreactivity each define distinct structures with differing distributions and solubility properties in Alzheimer brain. Proc. Natl. Acad. Sci. U.S.A., 85, 2854 2858.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 2854-2858
    • Shaw, G.1    Chau, V.2
  • 77
    • 0034142022 scopus 로고    scopus 로고
    • A distinct ER/IC gamma-secretase competes with the proteasome for cleavage of APP
    • Skovronsky, D.M., Pijak, D.S., Doms, R.W. Lee, V.M. (2000) A distinct ER/IC gamma-secretase competes with the proteasome for cleavage of APP. Biochemistry, 39, 810 817.
    • (2000) Biochemistry , vol.39 , pp. 810-817
    • Skovronsky, D.M.1    Pijak, D.S.2    Doms, R.W.3    Lee, V.M.4
  • 79
    • 0033536072 scopus 로고    scopus 로고
    • Proteolytic release and nuclear translocation of Notch-1 are induced by presenilin-1 and impaired by pathogenic presenilin-1 mutations
    • Song, W., Nadeau, P., Yuan, M., Yang, X., Shen, J. Yankner, B.A. (1999) Proteolytic release and nuclear translocation of Notch-1 are induced by presenilin-1 and impaired by pathogenic presenilin-1 mutations. Proc. Natl. Acad. Sci. U.S.A., 96, 6959 6963.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 6959-6963
    • Song, W.1    Nadeau, P.2    Yuan, M.3    Yang, X.4    Shen, J.5    Yankner, B.A.6
  • 82
    • 0033610863 scopus 로고    scopus 로고
    • Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation
    • Steiner, H., Capell, A., Pesold, B., Citron, M., Kloetzel, P.M., Selkoe, D.J., Romig, H., Mendla, K. Haass, C. (1998) Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation. J. Biol. Chem., 273, 32322 32331.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32322-32331
    • Steiner, H.1    Capell, A.2    Pesold, B.3    Citron, M.4    Kloetzel, P.M.5    Selkoe, D.J.6    Romig, H.7    Mendla, K.8    Haass, C.9
  • 83
    • 0037131218 scopus 로고    scopus 로고
    • PEN-2 is an integral component of the gamma-secretase complex required for coordinated expression of presenilin and nicastrin
    • Steiner, H., Winkler, E., Edbauer, D., Prokop, S., Basset, G., Yamasaki, A., Kostka, M. Haass, C. (2002) PEN-2 is an integral component of the gamma-secretase complex required for coordinated expression of presenilin and nicastrin. J. Biol. Chem., 277, 39062 39065.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39062-39065
    • Steiner, H.1    Winkler, E.2    Edbauer, D.3    Prokop, S.4    Basset, G.5    Yamasaki, A.6    Kostka, M.7    Haass, C.8
  • 85
    • 0035872863 scopus 로고    scopus 로고
    • A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome
    • Touitou, R., Richardson, J., Bose, S., Nakanishi, M., Rivett, J. Allday, M.J. (2001) A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome. EMBO J., 20, 2367 2375.
    • (2001) EMBO J. , vol.20 , pp. 2367-2375
    • Touitou, R.1    Richardson, J.2    Bose, S.3    Nakanishi, M.4    Rivett, J.5    Allday, M.J.6
  • 86
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward, C.L., Omura, S. Kopito, R.R. (1995) Degradation of CFTR by the ubiquitin-proteasome pathway. Cell, 83, 121 127.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 87
    • 0037176727 scopus 로고    scopus 로고
    • A novel epsilon-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing
    • Weidemann, A., Eggert, S., Reinhard, F.B., Vogel, M., Paliga, K., Baier, G., Masters, C.L., Beyreuther, K. Evin, G. (2002) A novel epsilon-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing. Biochemistry, 41, 2825 2835.
    • (2002) Biochemistry , vol.41 , pp. 2825-2835
    • Weidemann, A.1    Eggert, S.2    Reinhard, F.B.3    Vogel, M.4    Paliga, K.5    Baier, G.6    Masters, C.L.7    Beyreuther, K.8    Evin, G.9
  • 89
    • 0033779635 scopus 로고    scopus 로고
    • Presenilins are required for gamma-secretase cleavage of beta-APP and transmembrane cleavage of Notch-1
    • Zhang, Z., Nadeau, P., Song, W., Donoviel, D., Yuan, M., Bernstein, A. Yankner, B.A. (2000) Presenilins are required for gamma-secretase cleavage of beta-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
  • 90
    • 33646244775 scopus 로고    scopus 로고
    • Leaky scanning and reinitiation regulate BACE1 gene expression
    • Zhou, W. Song, W. (2006) Leaky scanning and reinitiation regulate BACE1 gene expression. Mol. Cell. Biol., 26, 3353 3364.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3353-3364
    • Zhou, W.1    Song, W.2
  • 91
    • 19644389648 scopus 로고    scopus 로고
    • CD147 is a regulatory subunit of the gamma-secretase complex in Alzheimer's disease amyloid beta-peptide production
    • Zhou, S., Zhou, H., Walian, P.J. Jap, B.K. (2005) CD147 is a regulatory subunit of the gamma-secretase complex in Alzheimer's disease amyloid beta-peptide production. Proc. Natl. Acad. Sci. U.S.A., 102, 7499 7504.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , 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.