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Volumn 16, Issue 7, 2007, Pages 848-864

CHIP and HSPs interact with β-APP in a proteasome-dependent manner and influence Aβ metabolism

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; CARBOXY TERMINAL HEAT SHOCK PROTEIN 70 INTERACTING PROTEIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 70; SMALL INTERFERING RNA; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 34447297017     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddm030     Document Type: Article
Times cited : (133)

References (59)
  • 1
    • 0029823454 scopus 로고    scopus 로고
    • Extracellular deposition of beta-amyloid upon p53-dependert neuronal cell death in transgenic mice
    • LaFerla, F.M., Hall, C.K., Ngo, L. and Jay, G. (1996) Extracellular deposition of beta-amyloid upon p53-dependert neuronal cell death in transgenic mice. J. Clin. Invest., 98, 1626-1632.
    • (1996) J. Clin. Invest , vol.98 , pp. 1626-1632
    • LaFerla, F.M.1    Hall, C.K.2    Ngo, L.3    Jay, G.4
  • 2
    • 0032475957 scopus 로고    scopus 로고
    • The chaperone BiP/GRP78 binds to amyloid precursor protein and decreases Abeta40 and Abeta42 secretion
    • Yang, Y., Turner, R.S. and Gaut, J.R. (1998) The chaperone BiP/GRP78 binds to amyloid precursor protein and decreases Abeta40 and Abeta42 secretion. J. Biol. Chem., 273, 25552-22555.
    • (1998) J. Biol. Chem , vol.273 , pp. 25552-22555
    • Yang, Y.1    Turner, R.S.2    Gaut, J.R.3
  • 3
    • 0033540060 scopus 로고    scopus 로고
    • Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration
    • Patrick, G.N., Zukerberg, L., Nikolic, M., de la Monte, S., Dikkes, P. and Tsai, L.H. (1999) Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration. Nature, 402, 615-622.
    • (1999) Nature , vol.402 , pp. 615-622
    • Patrick, G.N.1    Zukerberg, L.2    Nikolic, M.3    de la Monte, S.4    Dikkes, P.5    Tsai, L.H.6
  • 5
    • 0034609516 scopus 로고    scopus 로고
    • The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain
    • Walsh, D.M., Tseng, B.P., Rydel, R.E., Podlisny, M.B. and Selkoe, D.J. (2000) The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain. Biochemistry, 39, 10831-10839.
    • (2000) Biochemistry , vol.39 , pp. 10831-10839
    • Walsh, D.M.1    Tseng, B.P.2    Rydel, R.E.3    Podlisny, M.B.4    Selkoe, D.J.5
  • 6
    • 0035120525 scopus 로고    scopus 로고
    • Evidence that neurones accumulating amyloid can undergo lysis to form amyloid plaques in Alzheimer's disease
    • D'Andrea, M.R., Nagele, R.G., Wang, H.Y., Peterson, P.A. and Lee, D.H. (2001) Evidence that neurones accumulating amyloid can undergo lysis to form amyloid plaques in Alzheimer's disease. Histopathology, 38 120-134.
    • (2001) Histopathology , vol.38 , pp. 120-134
    • D'Andrea, M.R.1    Nagele, R.G.2    Wang, H.Y.3    Peterson, P.A.4    Lee, D.H.5
  • 7
    • 0034745017 scopus 로고    scopus 로고
    • Intraneuronal abeta-amyloid precedes development of amyloid plaques in Down syndrome
    • Gyure, K.A., Durham, R., Stewart, W.F., Smialek, J.E. and Troncoso, J.C. (2001) Intraneuronal abeta-amyloid precedes development of amyloid plaques in Down syndrome. Arch. Pathol. Lab. Med., 125, 489-492.
    • (2001) Arch. Pathol. Lab. Med , vol.125 , pp. 489-492
    • Gyure, K.A.1    Durham, R.2    Stewart, W.F.3    Smialek, J.E.4    Troncoso, J.C.5
  • 8
    • 0037186074 scopus 로고    scopus 로고
    • Altered metabolism of the amyloid beta precursor protein is associated with mitochondrial dysfunction in Down's syndrome
    • Busciglio, J., Pelsman, A., Wong, C., Pigino, G., Yuan, M., Mori, H. and Yankner, B.A. (2002) Altered metabolism of the amyloid beta precursor protein is associated with mitochondrial dysfunction in Down's syndrome. Neuron, 33, 677-688.
    • (2002) Neuron , vol.33 , pp. 677-688
    • Busciglio, J.1    Pelsman, A.2    Wong, C.3    Pigino, G.4    Yuan, M.5    Mori, H.6    Yankner, B.A.7
  • 9
    • 0036165129 scopus 로고    scopus 로고
    • Alzheimer beta-amyloid peptides: Normal and abnormal localization
    • Takahashi, R.H., Nam, E.E., Edgar, M. and Gouras, G.K. (2002) Alzheimer beta-amyloid peptides: Normal and abnormal localization. Histol. Histopathol., 17, 239-246.
    • (2002) Histol. Histopathol , vol.17 , pp. 239-246
    • Takahashi, R.H.1    Nam, E.E.2    Edgar, M.3    Gouras, G.K.4
  • 10
    • 0037059040 scopus 로고    scopus 로고
    • Chaperoning brain degeneration
    • Bonini, N.M. (2002) Chaperoning brain degeneration. Proc. Natl Acad. Sci. USA, 99 (Suppl. 4), 16407-16411.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , Issue.SUPPL. 4 , pp. 16407-16411
    • Bonini, N.M.1
  • 11
    • 0037059042 scopus 로고    scopus 로고
    • Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
    • Sakahira, H., Breuer, P., Hayer-Hartl, M.K. and Hartl, F.U. (2002) Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity. Proc. Natl Acad. Sci. USA, 99 (Suppl. 4), 16412-16418.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , Issue.SUPPL. 4 , pp. 16412-16418
    • Sakahira, H.1    Breuer, P.2    Hayer-Hartl, M.K.3    Hartl, F.U.4
  • 12
    • 1042266624 scopus 로고    scopus 로고
    • CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival
    • Shimura, H., Schwartz, D., Gygi, S.P. and Kosik, K.S. (2004) CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival. J. Biol. Chem., 279, 4869-4876.
    • (2004) J. Biol. Chem , vol.279 , pp. 4869-4876
    • Shimura, H.1    Schwartz, D.2    Gygi, S.P.3    Kosik, K.S.4
  • 14
    • 1242274389 scopus 로고    scopus 로고
    • Heat shock protein 70 participates in the neuroprotective response to intracellularly expressed beta-amyloid in neurons
    • Magrane, J., Smith, R.C., Walsh, K. and Querfurth, H.W. (2004) Heat shock protein 70 participates in the neuroprotective response to intracellularly expressed beta-amyloid in neurons. J. Neurosci., 24, 1700-1706.
    • (2004) J. Neurosci , vol.24 , pp. 1700-1706
    • Magrane, J.1    Smith, R.C.2    Walsh, K.3    Querfurth, H.W.4
  • 15
    • 28044446528 scopus 로고    scopus 로고
    • Intraneuronal β-amyloid expression down-regulates the Akt survival pathway and suppresses the stress response
    • Magrané, J., Rosen, K.M., Smith, R.C., Walsh, K., Gouras G.K. and Querfurth, H.W. (2005) Intraneuronal β-amyloid expression down-regulates the Akt survival pathway and suppresses the stress response. J. Neurosci., 25, 10960-10969.
    • (2005) J. Neurosci , vol.25 , pp. 10960-10969
    • Magrané, J.1    Rosen, K.M.2    Smith, R.C.3    Walsh, K.4    Gouras, G.K.5    Querfurth, H.W.6
  • 16
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger, C.A., Connell, P., Wu, Y., Hu, Z., Thompson, L.J., Yin, L.Y. and Patterson, C. (1999) Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol. Cell. Biol., 19, 4535-4545.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.Y.6    Patterson, C.7
  • 18
    • 0038788824 scopus 로고    scopus 로고
    • Overexpression of the cochaperone CHIP enhances Hsp70-dependent folding activity in mammalian cells
    • Kampinga, H.H., Kanon, B., Salomons, F.A., Kabakov, A.E. and Patterson, C. (2003) Overexpression of the cochaperone CHIP enhances Hsp70-dependent folding activity in mammalian cells. Mol. Cell. Biol. 23, 4948-4958.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 4948-4958
    • Kampinga, H.H.1    Kanon, B.2    Salomons, F.A.3    Kabakov, A.E.4    Patterson, C.5
  • 20
    • 21744438271 scopus 로고    scopus 로고
    • C-terminus of beat shock protein 70 interacting protein facilitates degradation of apoptosis signal-regulating kinase1 and inhibits apoptosis signal-regulating kinase-1 dependent apoptosis
    • Hwang, J.R., Zhang, C. and Patterson, C. (2005) C-terminus of beat shock protein 70 interacting protein facilitates degradation of apoptosis signal-regulating kinase1 and inhibits apoptosis signal-regulating kinase-1 dependent apoptosis. Cell Stress Chaperones, 10, 147-156.
    • (2005) Cell Stress Chaperones , vol.10 , pp. 147-156
    • Hwang, J.R.1    Zhang, C.2    Patterson, C.3
  • 21
    • 0034708216 scopus 로고    scopus 로고
    • The U box is a modified RING finger - a common domain in ubiquitination
    • Aravind, L. and Koonin, E.V. (2000) The U box is a modified RING finger - a common domain in ubiquitination. Curr. Biol., 10, R132-R134.
    • (2000) Curr. Biol , vol.10
    • Aravind, L.1    Koonin, E.V.2
  • 22
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: Folding, refolding and degradation of proteins
    • Wickner, S., Maurizi, M. and Gottesman, S. (1999) Posttranslational quality control: Folding, refolding and degradation of proteins. Science, 286, 1888-1893.
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.2    Gottesman, S.3
  • 23
    • 0035147404 scopus 로고    scopus 로고
    • Molecular chaperones and the art of recognizing a lost cause
    • McClellan, A.J. and Frydman, J. (2001.) Molecular chaperones and the art of recognizing a lost cause. Nat. Cell Biol., 3, E51-E53.
    • (2001) Nat. Cell Biol , vol.3
    • McClellan, A.J.1    Frydman, J.2
  • 24
    • 1242291789 scopus 로고    scopus 로고
    • CHIP: A link between the chaperone and proteasome systems
    • McDonough, H. and Patterson, C. (2003) CHIP: A link between the chaperone and proteasome systems. Cell Stress Chaperones, 8, 303-308.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 303-308
    • McDonough, H.1    Patterson, C.2
  • 25
    • 15744387323 scopus 로고    scopus 로고
    • Co-chaperone CHIP associates with expanded polyglutamine proteins and promotes their degradation by proteasomes
    • Jana, N.R., Dikshit, P., Goswami, A., Kotliarova, S., Murata, S., Tanaka, K. and Nukina, N. (2005) Co-chaperone CHIP associates with expanded polyglutamine proteins and promotes their degradation by proteasomes. J. Biol. Chem., 280, 11635-11640.
    • (2005) J. Biol. Chem , vol.280 , pp. 11635-11640
    • Jana, N.R.1    Dikshit, P.2    Goswami, A.3    Kotliarova, S.4    Murata, S.5    Tanaka, K.6    Nukina, N.7
  • 26
    • 0036345454 scopus 로고    scopus 로고
    • CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity
    • Imai, Y., Soda, M., Hatakeyama, S., Akagi, T., Hashikawa, T., Nakayama, K.I. and Takahashi, R. (2002) CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Mol. Cell, 10, 55-67.
    • (2002) Mol. Cell , vol.10 , pp. 55-67
    • Imai, Y.1    Soda, M.2    Hatakeyama, S.3    Akagi, T.4    Hashikawa, T.5    Nakayama, K.I.6    Takahashi, R.7
  • 27
    • 21244499845 scopus 로고    scopus 로고
    • The co-chaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates alpha-synuclein degradation decisions between proteasomal and lysosomal pathways
    • Shin, Y., Klucken, J., Patterson, C., Hyman, B.T. and McLean, P.J. (2005) The co-chaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates alpha-synuclein degradation decisions between proteasomal and lysosomal pathways. J. Biol. Chem., 280, 23727-23734.
    • (2005) J. Biol. Chem , vol.280 , pp. 23727-23734
    • Shin, Y.1    Klucken, J.2    Patterson, C.3    Hyman, B.T.4    McLean, P.J.5
  • 28
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • Meacham, G.C., Patterson, C., Zhang, W., Younger, J.M. and Cyr, D.M. (2001) The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat. Cell Biol., 3, 100-105.
    • (2001) Nat. Cell Biol , vol.3 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 29
    • 11244349206 scopus 로고    scopus 로고
    • A foldable CFTR {Delta} F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHlP E3 ubiquitin ligase
    • Younger, J.M., Ren, H.Y., Chen, L., Fan, C.Y., Fields, A., Patterson, C. and Cyr, D.M. (2004) A foldable CFTR {Delta} F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHlP E3 ubiquitin ligase. J. Cell Biol., 167, 1075-1085.
    • (2004) J. Cell Biol , vol.167 , pp. 1075-1085
    • Younger, J.M.1    Ren, H.Y.2    Chen, L.3    Fan, C.Y.4    Fields, A.5    Patterson, C.6    Cyr, D.M.7
  • 30
    • 5444239863 scopus 로고    scopus 로고
    • U-box protein carboxyl terminus of Hsc70-interacting protein (CHIP) mediates poly-ubiquitylation preferentially on four-repeat tau and is involved in neurodegeneration of tauopathy
    • Hatakeyama, S., Matsumoto, M., Kamura, T., Murayama, M., Chui, D.H., Planel, E., Takahashi, R., Nakayama, K.I. and Takashima, A. (2004) U-box protein carboxyl terminus of Hsc70-interacting protein (CHIP) mediates poly-ubiquitylation preferentially on four-repeat tau and is involved in neurodegeneration of tauopathy. J. Neurochem., 91, 299-307.
    • (2004) J. Neurochem , vol.91 , pp. 299-307
    • Hatakeyama, S.1    Matsumoto, M.2    Kamura, T.3    Murayama, M.4    Chui, D.H.5    Planel, E.6    Takahashi, R.7    Nakayama, K.I.8    Takashima, A.9
  • 33
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones and negative regulators
    • Morimoto, R.I. (1998) Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones and negative regulators. Genes Dev., 12, 3788-3796.
    • (1998) Genes Dev , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 35
    • 33645293437 scopus 로고    scopus 로고
    • CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70
    • Qian, S.B., McDonough, H., Boellmann, F., Cyr, D.M. and Patterson, C. (2006) CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70. Nature, 440, 551-555.
    • (2006) Nature , vol.440 , pp. 551-555
    • Qian, S.B.1    McDonough, H.2    Boellmann, F.3    Cyr, D.M.4    Patterson, C.5
  • 36
    • 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. and 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
  • 37
    • 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. and 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
  • 38
    • 0038730933 scopus 로고    scopus 로고
    • Downregulation and increased turnover of beta-amyloid precursor protein in skeletal muscle cultures by neuregulin-1
    • Rosen, K.M., Ford, B.D. and Querfurth, H.W. (2003) Downregulation and increased turnover of beta-amyloid precursor protein in skeletal muscle cultures by neuregulin-1. Exp. Neurol., 181, 170-180.
    • (2003) Exp. Neurol , vol.181 , pp. 170-180
    • Rosen, K.M.1    Ford, B.D.2    Querfurth, H.W.3
  • 39
    • 0030898710 scopus 로고    scopus 로고
    • (19,97) Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance
    • Bush, K.T., Goldberg, A.L. and Nigam, S.K. (19,97) Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance. J. Biol. Chem., 272, 9086-9092.
    • J. Biol. Chem , vol.272 , pp. 9086-9092
    • Bush, K.T.1    Goldberg, A.L.2    Nigam, S.K.3
  • 40
    • 33749543406 scopus 로고    scopus 로고
    • Differential effects of mitochondrial Hsp60 and related molecular chaperones to prevent intracellular P-amyloid induced inhibition of complex IV and limit apoptosis
    • Veereshwarayya, V., Kumar, P., Rosen, K.M., Mestril, R. and Querfurth, H.W. (2006) Differential effects of mitochondrial Hsp60 and related molecular chaperones to prevent intracellular P-amyloid induced inhibition of complex IV and limit apoptosis. J. Biol. Chem., 281, 29468-29478.
    • (2006) J. Biol. Chem , vol.281 , pp. 29468-29478
    • Veereshwarayya, V.1    Kumar, P.2    Rosen, K.M.3    Mestril, R.4    Querfurth, H.W.5
  • 41
    • 0035899897 scopus 로고    scopus 로고
    • Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling
    • Demand, J., Alberti, S., Patterson, C. and Hohfeld, J. (2001) Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling. Curr. Biol., 11, 1569-1577.
    • (2001) Curr. Biol , vol.11 , pp. 1569-1577
    • Demand, J.1    Alberti, S.2    Patterson, C.3    Hohfeld, J.4
  • 42
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • Murata, S., Minami, Y., Minami, M., Chiba, T. and Tanaka, K. (2001) CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. EMBO Rep., 2, 1133-1138.
    • (2001) EMBO Rep , vol.2 , pp. 1133-1138
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 43
    • 0037401714 scopus 로고    scopus 로고
    • CHIP: A quality control E3 ligase collaborating with molecular chaperones
    • Murata, S., Chiba, T. and Tanaka, K. (2003) CHIP: A quality control E3 ligase collaborating with molecular chaperones. Int. J. Biochem. Cell. Biol., 35, 572-578.
    • (2003) Int. J. Biochem. Cell. Biol , vol.35 , pp. 572-578
    • Murata, S.1    Chiba, T.2    Tanaka, K.3
  • 45
    • 0033054564 scopus 로고    scopus 로고
    • C-terminal maturation fragments of presenilin 1 and 2 control secretion of APP alpha and A beta by human cells and are degraded by proteasome
    • da Costa, C.A., Ancolio, K. and Checler, F. (1999) C-terminal maturation fragments of presenilin 1 and 2 control secretion of APP alpha and A beta by human cells and are degraded by proteasome. Mol. Med., 5, 160-168.
    • (1999) Mol. Med , vol.5 , pp. 160-168
    • da Costa, C.A.1    Ancolio, K.2    Checler, F.3
  • 46
    • 0030667097 scopus 로고    scopus 로고
    • Constitutive and protein kinase C-regulated secretory cleavage of Alzheimer's beta-amyloid precursor protein: Different control of early and late events by the proteasome
    • Marambaud, P., Lopez-Perez, E., Wilk, S. and Checler, F. (1997) Constitutive and protein kinase C-regulated secretory cleavage of Alzheimer's beta-amyloid precursor protein: Different control of early and late events by the proteasome. J. Neurochem., 69, 2500-2505.
    • (1997) J. Neurochem , vol.69 , pp. 2500-2505
    • Marambaud, P.1    Lopez-Perez, E.2    Wilk, S.3    Checler, F.4
  • 47
    • 0026539090 scopus 로고
    • Processing of the amyloid protein precursor to potentially amyloidogenic derivatives
    • Golde, T.E., Estus, S., Younkin, L.H., Selkoe, D.J. and Younkin, S.G. (1992) Processing of the amyloid protein precursor to potentially amyloidogenic derivatives. Science, 255, 728-730.
    • (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
  • 48
    • 0026778656 scopus 로고
    • Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4/beta protein
    • Knauer, M.F., Soreghan, B., Burdick, D., Kosmoski, J. and Glabe, C.G. (1992) Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4/beta protein. Proc. Natl Acad Sci. USA, 89 7437-7441.
    • (1992) Proc. Natl Acad Sci. USA , vol.89 , pp. 7437-7441
    • Knauer, M.F.1    Soreghan, B.2    Burdick, D.3    Kosmoski, J.4    Glabe, C.G.5
  • 49
    • 0029112811 scopus 로고
    • Lysosomal processing of amyloid precursor protein to A beta peptides: A distinct role for cathepsin S
    • Munger, J.S., Haass, C., Lemere, C.A., Shi, G.P., Wong, W.S., Teplow, D.B., Selkoe, D.J. and Chapman, H.A. (1995) Lysosomal processing of amyloid precursor protein to A beta peptides: A distinct role for cathepsin S. Biochem. J., 311, 299-305.
    • (1995) Biochem. J , vol.311 , pp. 299-305
    • Munger, J.S.1    Haass, C.2    Lemere, C.A.3    Shi, G.P.4    Wong, W.S.5    Teplow, D.B.6    Selkoe, D.J.7    Chapman, H.A.8
  • 50
    • 0028866435 scopus 로고    scopus 로고
    • Haass, C., Lemere, C.A., Capell, A., Citron, M., Seubert, P., Schenk, D., Lannfelt, L. and Selkoe, D.J. (1995) The Swedish mutation causes early-onset Alzheimer's disease by beta-secretase cleavage within the secretory pathway. Nat. Med., 1, 1291-1296.
    • Haass, C., Lemere, C.A., Capell, A., Citron, M., Seubert, P., Schenk, D., Lannfelt, L. and Selkoe, D.J. (1995) The Swedish mutation causes early-onset Alzheimer's disease by beta-secretase cleavage within the secretory pathway. Nat. Med., 1, 1291-1296.
  • 51
    • 0034839287 scopus 로고    scopus 로고
    • The amyloid precursor protein (APP)-cytoplasmic fiagment generated by gamma-secretase is rapidly degraded but distributes partially in a nuclear fraction of neurones in culture
    • Cupers, P., Orlans, I., Craessaerts, K., Annaert, W. and De Strooper, B. (2001) The amyloid precursor protein (APP)-cytoplasmic fiagment generated by gamma-secretase is rapidly degraded but distributes partially in a nuclear fraction of neurones in culture. J. Neurochem. 78, 1168-1178.
    • (2001) J. Neurochem , vol.78 , pp. 1168-1178
    • Cupers, P.1    Orlans, I.2    Craessaerts, K.3    Annaert, W.4    De Strooper, B.5
  • 52
    • 0037698096 scopus 로고    scopus 로고
    • Presenilin-1, nicastrin, amyloid precursor protein, and gamma-secretase activity are co-localized in the lysosomal membrane
    • Pasternak, S.H., Bagshaw, R.D., Guiral, M., Zhang, S., Ackerley, C.A., Pak, B.J., Callahan, J.W. and Mahuran, D.J. (2003) Presenilin-1, nicastrin, amyloid precursor protein, and gamma-secretase activity are co-localized in the lysosomal membrane. J. Biol. Chem., 278, 26687-26694.
    • (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
  • 53
    • 0001181116 scopus 로고    scopus 로고
    • Alzheimer's disease: Molecular understanding predicts amyloid-based therapeutics
    • Selkoe, D.J. and Schenk, D. (2003) Alzheimer's disease: Molecular understanding predicts amyloid-based therapeutics. Annu. Rev. Pharmacol. Toxicol., 43, 545-584.
    • (2003) Annu. Rev. Pharmacol. Toxicol , vol.43 , pp. 545-584
    • Selkoe, D.J.1    Schenk, D.2
  • 54
    • 1042292018 scopus 로고    scopus 로고
    • Endoplasmic reticulum-localized amyloid beta-peptide is degraded in the cytosol by two distinct degradation pathways
    • Schmitz, A., Schneider, A., Kummer, M.P. and Herzog, V. (2004) Endoplasmic reticulum-localized amyloid beta-peptide is degraded in the cytosol by two distinct degradation pathways. Traffic, 5, 89-101.
    • (2004) Traffic , vol.5 , pp. 89-101
    • Schmitz, A.1    Schneider, A.2    Kummer, M.P.3    Herzog, V.4
  • 55
    • 33745959291 scopus 로고    scopus 로고
    • Deletion of the ubiquitin ligase CHIP leads to the accumulation, but not the aggregation, of both endogenous phospho- and Caspase-3-cleaved tau species
    • Dickey, C.A., Yue, M., Lin, W.L., Dickson, D.W., Dunmore, J.H., Lee, W.C., Zehr, C., West, G., Cao, S., Clark, A.M.K. et al. (2006) Deletion of the ubiquitin ligase CHIP leads to the accumulation, but not the aggregation, of both endogenous phospho- and Caspase-3-cleaved tau species. J. Neurosci., 26, 6985-6996.
    • (2006) J. Neurosci , vol.26 , pp. 6985-6996
    • Dickey, C.A.1    Yue, M.2    Lin, W.L.3    Dickson, D.W.4    Dunmore, J.H.5    Lee, W.C.6    Zehr, C.7    West, G.8    Cao, S.9    Clark, A.M.K.10
  • 56
    • 0035967883 scopus 로고    scopus 로고
    • An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin
    • Imai, Y., Soda, M., Inoue, H., Hattori, N., Mizuno, Y. and Takahashi, R. (2001) An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell, 105, 891-902.
    • (2001) Cell , vol.105 , pp. 891-902
    • Imai, Y.1    Soda, M.2    Inoue, H.3    Hattori, N.4    Mizuno, Y.5    Takahashi, R.6
  • 58
    • 0030987603 scopus 로고    scopus 로고
    • Caffeine stimulates amyloid beta-peptide release from beta-amyloid. precursor protein-transfected BEK293 cells
    • Querfurth, H.W., Jiang, J., Geiger, J.D. and Selkoe, D.J. (1997) Caffeine stimulates amyloid beta-peptide release from beta-amyloid. precursor protein-transfected BEK293 cells. J. Neurochem., 69 1580-1591.
    • (1997) J. Neurochem , vol.69 , pp. 1580-1591
    • Querfurth, H.W.1    Jiang, J.2    Geiger, J.D.3    Selkoe, D.J.4
  • 59
    • 1242314232 scopus 로고    scopus 로고
    • Overexpression of heat shock proteins differentially modulates protein kinase C expression in rat neonatal cardiomyocytes
    • Coaxum, S.D., Martin, J.L. and Mestril, R. (2003) Overexpression of heat shock proteins differentially modulates protein kinase C expression in rat neonatal cardiomyocytes. Cell Stress Chaperones., 8, 297-302.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 297-302
    • Coaxum, S.D.1    Martin, J.L.2    Mestril, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.