메뉴 건너뛰기




Volumn 29, Issue 1, 2006, Pages 9-19

Presenilin 1 forms aggresomal deposits in response to heat shock

Author keywords

Aggregate; Alzheimer's disease; Chaperone; Dislocation; Neurodegeneration

Indexed keywords

HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; PRESENILIN 1;

EID: 33744954445     PISSN: 08958696     EISSN: None     Source Type: Journal    
DOI: 10.1385/JMN:29:1:9     Document Type: Article
Times cited : (13)

References (51)
  • 1
    • 3142724742 scopus 로고    scopus 로고
    • UCH-L1 aggresome formation in response to proteasome impairment indicates a role in inclusion formation in Parkinson's disease
    • Ardley H.C., Scott G. B., Rose S. A., Tan N. G., and Robinson P.A. (2004) UCH-L1 aggresome formation in response to proteasome impairment indicates a role in inclusion formation in Parkinson's disease. J. Neurochem. 90, 379-391.
    • (2004) J. Neurochem. , vol.90 , pp. 379-391
    • Ardley, H.C.1    Scott, G.B.2    Rose, S.A.3    Tan, N.G.4    Robinson, P.A.5
  • 2
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N. F., Sampat R. M., and Kopito R. R. (2001) Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292, 1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 3
    • 0032544674 scopus 로고    scopus 로고
    • Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1
    • Bruijn L. I., Houseweart M. K., Kato S., et al. (1998) Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. Science 281, 1851-1854.
    • (1998) Science , vol.281 , pp. 1851-1854
    • Bruijn, L.I.1    Houseweart, M.K.2    Kato, S.3
  • 4
    • 0031006343 scopus 로고    scopus 로고
    • Neuronal localization of presenilin-1 and association with amyloid plaques and neurofibrillary tangles in Alzheimer's disease
    • Busciglio J., Hartmann H., Lorenzo A., et al. (1997) Neuronal localization of presenilin-1 and association with amyloid plaques and neurofibrillary tangles in Alzheimer's disease. J. Neurosci. 17, 5101-5107.
    • (1997) J. Neurosci. , vol.17 , pp. 5101-5107
    • Busciglio, J.1    Hartmann, H.2    Lorenzo, A.3
  • 5
    • 0027397058 scopus 로고
    • The roles of heat shock proteins and immediate early genes in central nervous system normal function and pathology
    • Chopp M. (1993) The roles of heat shock proteins and immediate early genes in central nervous system normal function and pathology. Curr. Opin. Neurol. Neurosurg. 6, 6-10.
    • (1993) Curr. Opin. Neurol. Neurosurg. , vol.6 , pp. 6-10
    • Chopp, M.1
  • 6
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • Cummings C.J., Mancini M.A., Antalffy B., DeFranco D.B., Orr H.T., and Zoghbi H.Y. (1998) Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat. Genet. 19, 148-154.
    • (1998) Nat. Genet. , vol.19 , pp. 148-154
    • Cummings, C.J.1    Mancini, M.A.2    Antalffy, B.3    DeFranco, D.B.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 7
    • 18544410106 scopus 로고    scopus 로고
    • Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation
    • Davies S.W., Turmaine M., Cozens B. A., et al. 1997. Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 90, 537-548.
    • (1997) Cell , vol.90 , pp. 537-548
    • Davies, S.W.1    Turmaine, M.2    Cozens, B.A.3
  • 8
    • 0035911163 scopus 로고    scopus 로고
    • Hsp70 and antifibrillogenic peptides promote degradation and inhibit intracellular aggregation of amyloidogenic light chains
    • Dul J. L., Davis D. P., Williamson E. K., Stevens F. J., and Argon Y. (2001) Hsp70 and antifibrillogenic peptides promote degradation and inhibit intracellular aggregation of amyloidogenic light chains. J. Cell Biol. 152, 705-716.
    • (2001) J. Cell Biol. , vol.152 , pp. 705-716
    • Dul, J.L.1    Davis, D.P.2    Williamson, E.K.3    Stevens, F.J.4    Argon, Y.5
  • 9
    • 0030777650 scopus 로고    scopus 로고
    • Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS
    • Durham H. D., Roy J., Dong L., and Figlewicz D. A. (1997) Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS. J. Neuropathol. Exp. Neurol. 56, 523-530.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 523-530
    • Durham, H.D.1    Roy, J.2    Dong, L.3    Figlewicz, D.A.4
  • 10
    • 0035680611 scopus 로고    scopus 로고
    • Aggresome formation in liver cells in response to different toxic mechanisms: Role of the ubiquitin-proteasome pathway and the frameshift mutant of ubiquitin
    • French B.A., van Leeuwen F., Riley N. E., et al. (2001) Aggresome formation in liver cells in response to different toxic mechanisms: role of the ubiquitin-proteasome pathway and the frameshift mutant of ubiquitin. Exp. Mol. Pathol. 71, 241-246.
    • (2001) Exp. Mol. Pathol. , vol.71 , pp. 241-246
    • French, B.A.1    Van Leeuwen, F.2    Riley, N.E.3
  • 11
    • 0344466781 scopus 로고    scopus 로고
    • Characterization and dynamics of aggresome formation by a cytosolic GFP- chimera
    • Garcia-Mata R., Bebok Z., Sorscher E. J., and Sztul E. S. (1999) Characterization and dynamics of aggresome formation by a cytosolic GFP- chimera. J. Cell Biol. 146, 1239-1254.
    • (1999) J. Cell Biol. , vol.146 , pp. 1239-1254
    • Garcia-Mata, R.1    Bebok, Z.2    Sorscher, E.J.3    Sztul, E.S.4
  • 12
    • 0036303981 scopus 로고    scopus 로고
    • Hassles with taking out the garbage: Aggravating aggresomes
    • Garcia-Mata R., Gao Y. S., and Sztul E. (2002) Hassles with taking out the garbage: aggravating aggresomes. Traffic 3, 388-396.
    • (2002) Traffic , vol.3 , pp. 388-396
    • Garcia-Mata, R.1    Gao, Y.S.2    Sztul, E.3
  • 13
    • 0036898485 scopus 로고    scopus 로고
    • Alzheimer disease gamma-secretase: A complex story of GxGD-type presenilin proteases
    • Haass C. and Steiner H. (2002) Alzheimer disease gamma-secretase: a complex story of GxGD-type presenilin proteases. Trends Cell Biol. 12, 556-562.
    • (2002) Trends Cell Biol. , vol.12 , pp. 556-562
    • Haass, C.1    Steiner, H.2
  • 14
    • 0035972239 scopus 로고    scopus 로고
    • Aggresomes resemble sites specialized for virus assembly
    • Heath C. M., Windsor M., and Wileman T. (2001) Aggresomes resemble sites specialized for virus assembly. J. Cell Biol. 153, 449-455.
    • (2001) J. Cell Biol. , vol.153 , pp. 449-455
    • Heath, C.M.1    Windsor, M.2    Wileman, T.3
  • 15
    • 0032079522 scopus 로고    scopus 로고
    • Involvement of heat shock protein 90 in the degradation of mutant insulin receptors by the proteasome
    • Imamura T., Haruta T., Takata Y., et al. (1998) Involvement of heat shock protein 90 in the degradation of mutant insulin receptors by the proteasome. J. Biol. Chem. 273, 11, 183-11, 188.
    • (1998) J. Biol. Chem. , vol.273
    • Imamura, T.1    Haruta, T.2    Takata, Y.3
  • 16
    • 2942604376 scopus 로고    scopus 로고
    • The gamma-secretase complex: Machinery for intramembrane proteolysis
    • Iwatsubo T. (2004) The gamma-secretase complex: machinery for intramembrane proteolysis. Curr. Opin. Neurobiol. 14, 379-383.
    • (2004) Curr. Opin. Neurobiol. , vol.14 , pp. 379-383
    • Iwatsubo, T.1
  • 17
    • 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., and 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
  • 18
    • 0033749379 scopus 로고    scopus 로고
    • Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis
    • Johnston J. A., Dalton M. J., Gurney M. E., and Kopito R.R. (2000) Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. USA 97, 12,571-12,576.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97
    • Johnston, J.A.1    Dalton, M.J.2    Gurney, M.E.3    Kopito, R.R.4
  • 19
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston J. A., Ward C. L., and Kopito R. R. 1998. Aggresomes: a cellular response to misfolded proteins. J. Cell Biol. 143, 1883-1898.
    • (1998) J. Cell Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 20
    • 0035129262 scopus 로고    scopus 로고
    • Biosynthesis of surfactant protein C: Characterization of aggresome formation by EGFP chimeras containing propeptide mutants lacking conserved cysteine residues
    • Kabore A.F., Wang W. J., Russo S. J., and Beers M. F. (2001) Biosynthesis of surfactant protein C: characterization of aggresome formation by EGFP chimeras containing propeptide mutants lacking conserved cysteine residues. J. Cell Sci. 114, 293-302.
    • (2001) J. Cell Sci. , vol.114 , pp. 293-302
    • Kabore, A.F.1    Wang, W.J.2    Russo, S.J.3    Beers, M.F.4
  • 21
    • 0032527991 scopus 로고    scopus 로고
    • Proteasome inhibition leads to the activation of all members of the heat-shock-factor family
    • Kawazoe Y., Nakai A., Tanabe M., and Nagata K. (1998) Proteasome inhibition leads to the activation of all members of the heat-shock-factor family. Eur. J. Biochem. 255, 356-362.
    • (1998) Eur. J. Biochem. , vol.255 , pp. 356-362
    • Kawazoe, Y.1    Nakai, A.2    Tanabe, M.3    Nagata, K.4
  • 22
    • 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., and Tanzi R.E. (1997) Endoproteolytic cleavage and proteasomal degradation of presenilin 2 in transfected cells. J. Biol. Chem. 272, 11,006-11,010.
    • (1997) J. Biol. Chem. , vol.272
    • Kim, T.W.1    Pettingell, W.H.2    Hallmark, O.G.3    Moir, R.D.4    Wasco, W.5    Tanzi, R.E.6
  • 23
    • 13344282063 scopus 로고    scopus 로고
    • Alzheimer-associated presenilins 1 and 2: Neuronal expression in brain and localization to intracellular membranes in mammalian cells
    • Kovacs D. M., Fausett H. J., Page K. J., et al. (1996) Alzheimer-associated presenilins 1 and 2: neuronal expression in brain and localization to intracellular membranes in mammalian cells. Nat. Med. 2, 224-229.
    • (1996) Nat. Med. , vol.2 , pp. 224-229
    • Kovacs, D.M.1    Fausett, H.J.2    Page, K.J.3
  • 24
    • 0032727864 scopus 로고    scopus 로고
    • Staurosporine-induced activation of caspase-3 is potentiated by presenilin 1 familial Alzheimer's disease mutations in human neuroglioma cells
    • Kovacs D. M., Mancini R., Henderson J., et al. (1999) Staurosporine-induced activation of caspase-3 is potentiated by presenilin 1 familial Alzheimer's disease mutations in human neuroglioma cells. J. Neurochem. 73, 2278-2285.
    • (1999) J. Neurochem. , vol.73 , pp. 2278-2285
    • Kovacs, D.M.1    Mancini, R.2    Henderson, J.3
  • 25
    • 0031714867 scopus 로고    scopus 로고
    • Monogenic determinants of familial Alzheimer's disease: Presenilin-1 mutations
    • Kovacs D. M. and Tanzi R.E. (1998) Monogenic determinants of familial Alzheimer's disease: presenilin-1 mutations. Cell Mol. Life Sci. 54, 902-909.
    • (1998) Cell Mol. Life Sci. , vol.54 , pp. 902-909
    • Kovacs, D.M.1    Tanzi, R.E.2
  • 26
    • 0002858113 scopus 로고    scopus 로고
    • Proteasome inhibitors cause induction of heat shock proteins and trehalose, which together confer thermotolerance in Saccharomyces cerevisiae
    • Lee D. H. and Goldberg A. L. (1998) Proteasome inhibitors cause induction of heat shock proteins and trehalose, which together confer thermotolerance in Saccharomyces cerevisiae. Mol. Cell Biol. 18, 30-38.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 30-38
    • Lee, D.H.1    Goldberg, A.L.2
  • 27
    • 0034681471 scopus 로고    scopus 로고
    • Dopaminergic loss and inclusion body formation in alpha-synuclein mice: Implications for neurodegenerative disorders
    • Masliah E., Rockenstein E., Veinbergs I., et al. (2000) Dopaminergic loss and inclusion body formation in alpha-synuclein mice: implications for neurodegenerative disorders. Science 287, 1265-1269.
    • (2000) Science , vol.287 , pp. 1265-1269
    • Masliah, E.1    Rockenstein, E.2    Veinbergs, I.3
  • 28
    • 0042536471 scopus 로고    scopus 로고
    • Neuronal and glial calcium signaling in Alzheimer's disease
    • Mattson M. P. and Chan S. L. (2003) Neuronal and glial calcium signaling in Alzheimer's disease. Cell Calcium 34, 385-397.
    • (2003) Cell Calcium , vol.34 , pp. 385-397
    • Mattson, M.P.1    Chan, S.L.2
  • 30
    • 0033559258 scopus 로고    scopus 로고
    • The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
    • Meacham G. C., Lu Z., King S., Sorscher E., Tousson A., and Cyr D. M. (1999) The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis. EMBO J. 18, 1492-1505.
    • (1999) EMBO J. , vol.18 , pp. 1492-1505
    • Meacham, G.C.1    Lu, Z.2    King, S.3    Sorscher, E.4    Tousson, A.5    Cyr, D.M.6
  • 31
    • 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
  • 32
    • 0023140474 scopus 로고
    • Ubiquitin is a component of paired helical filaments in Alzheimer's disease
    • Mori H., Kondo J., and 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
  • 33
    • 0036677215 scopus 로고    scopus 로고
    • Presenilin-binding protein forms aggresomes in monkey kidney COS-7 cells
    • Namekata K., Nishimura N., and Kimura H. (2002) Presenilin-binding protein forms aggresomes in monkey kidney COS-7 cells. J. Neurochem. 82, 819-827.
    • (2002) J. Neurochem. , vol.82 , pp. 819-827
    • Namekata, K.1    Nishimura, N.2    Kimura, H.3
  • 34
    • 0037389255 scopus 로고    scopus 로고
    • Heat shock proteins are present in mallory bodies (cytokeratin aggresomes) in human liver biopsy specimens
    • Riley N. E., Li J., McPhaul L. W., Bardag-Gorce F., Lue Y. H., and French S. W. (2003) Heat shock proteins are present in mallory bodies (cytokeratin aggresomes) in human liver biopsy specimens. Exp. Mol. Pathol. 74, 168-172.
    • (2003) Exp. Mol. Pathol. , vol.74 , pp. 168-172
    • Riley, N.E.1    Li, J.2    McPhaul, L.W.3    Bardag-Gorce, F.4    Lue, Y.H.5    French, S.W.6
  • 35
    • 0034638240 scopus 로고    scopus 로고
    • Expression of amyloid precursor protein in human astrocytes in vitro: Isoform-specific increases following heat shock
    • Shepherd C. E., Bowes S., Parkinson D., Cambray-Deakin M., and Pearson R. C. (2000) Expression of amyloid precursor protein in human astrocytes in vitro: isoform-specific increases following heat shock. Neuroscience 99, 317-325.
    • (2000) Neuroscience , vol.99 , pp. 317-325
    • Shepherd, C.E.1    Bowes, S.2    Parkinson, D.3    Cambray-Deakin, M.4    Pearson, R.C.5
  • 36
    • 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., et al. (1998) Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation. J. Biol. Chem. 273, 32,322-32,331.
    • (1998) J. Biol. Chem. , vol.273
    • Steiner, H.1    Capell, A.2    Pesold, B.3
  • 37
    • 1042266326 scopus 로고    scopus 로고
    • Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective
    • Tanaka M., Kim Y. M., Lee G., Junn E., Iwatsubo T., and Mouradian M. M. (2004) Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective. J. Biol. Chem. 279, 4625-4631.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4625-4631
    • Tanaka, M.1    Kim, Y.M.2    Lee, G.3    Junn, E.4    Iwatsubo, T.5    Mouradian, M.M.6
  • 38
    • 0033358871 scopus 로고    scopus 로고
    • Caspases land on APP: One small step for apoptosis, one giant leap for amyloidosis?
    • Tanzi R. E. (1999) Caspases land on APP: one small step for apoptosis, one giant leap for amyloidosis? [news]. Nat. Neurosci. 2, 585-586.
    • (1999) Nat. Neurosci. , vol.2 , pp. 585-586
    • Tanzi, R.E.1
  • 39
    • 0037388418 scopus 로고    scopus 로고
    • Aggresomes protect cells by enhancing the degradation of toxic polyglutamine-containing protein
    • Taylor J. P., Tanaka F., Robitschek J., et al. (2003) Aggresomes protect cells by enhancing the degradation of toxic polyglutamine-containing protein. Hum. Mol. Genet. 12, 749-757.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 749-757
    • Taylor, J.P.1    Tanaka, F.2    Robitschek, J.3
  • 40
    • 0032720123 scopus 로고    scopus 로고
    • The role of presenilins in Alzheimer's disease
    • Thinakaran G. (1999) The role of presenilins in Alzheimer's disease. J. Clin. Invest. 104, 1321-1327.
    • (1999) J. Clin. Invest. , vol.104 , pp. 1321-1327
    • Thinakaran, G.1
  • 41
    • 15844425969 scopus 로고    scopus 로고
    • Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo
    • Thinakaran G., Borchelt D.R., Lee M.K., et al. (1996) Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo. Neuron 17, 181-190.
    • (1996) Neuron , vol.17 , pp. 181-190
    • Thinakaran, G.1    Borchelt, D.R.2    Lee, M.K.3
  • 42
    • 0031920383 scopus 로고    scopus 로고
    • Stable association of presenilin derivatives and absence of presenilin interactions with APP
    • Thinakaran G., Regard J. B., Bouton C. M., et al. (1998) Stable association of presenilin derivatives and absence of presenilin interactions with APP Neurobiol. Dis. 4, 438-453.
    • (1998) Neurobiol. Dis. , vol.4 , pp. 438-453
    • Thinakaran, G.1    Regard, J.B.2    Bouton, C.M.3
  • 43
    • 0033064547 scopus 로고    scopus 로고
    • Identification of caspases that cleave presenilin-1 and presenilin-2. Five presenilin-1 (PS1) mutations do not alter the sensitivity of PS1 to caspases
    • van de Craen M., de Jonghe C., van den Brande I., et al. (1999) Identification of caspases that cleave presenilin-1 and presenilin-2. Five presenilin-1 (PS1) mutations do not alter the sensitivity of PS1 to caspases. FEBS Lett. 445, 149-154.
    • (1999) FEBS Lett. , vol.445 , pp. 149-154
    • Van De Craen, M.1    De Jonghe, C.2    Van Den Brande, I.3
  • 44
    • 0029911025 scopus 로고    scopus 로고
    • Heat shock causes protein aggregation and reduced protein solubility at the centrosome and other cytoplasmic locations
    • Vidair C. A., Huang R. N., and Doxsey S. J. (1996) Heat shock causes protein aggregation and reduced protein solubility at the centrosome and other cytoplasmic locations. Int. J. Hyperthermia 12, 681-695.
    • (1996) Int. J. Hyperthermia , vol.12 , pp. 681-695
    • Vidair, C.A.1    Huang, R.N.2    Doxsey, S.J.3
  • 45
    • 0034754875 scopus 로고    scopus 로고
    • Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation
    • Waelter S., Boeddrich A., Lurz R., et al. (2001) Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation. Mol. Biol. Cell. 12, 1393-1407.
    • (2001) Mol. Biol. Cell. , vol.12 , pp. 1393-1407
    • Waelter, S.1    Boeddrich, A.2    Lurz, R.3
  • 46
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward C. L., Omura S., and 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
  • 47
    • 0032487575 scopus 로고    scopus 로고
    • Prominent expression of presenilin-1 in senile plaques and reactive astrocytes in Alzheimer's disease brain
    • Weggen S., Diehlmann A., Buslei R., Beyreuther K., and Bayer T. A. 1998. Prominent expression of presenilin-1 in senile plaques and reactive astrocytes in Alzheimer's disease brain. Neuroreport 9, 3279-3283.
    • (1998) Neuroreport , vol.9 , pp. 3279-3283
    • Weggen, S.1    Diehlmann, A.2    Buslei, R.3    Beyreuther, K.4    Bayer, T.A.5
  • 48
    • 0345593387 scopus 로고    scopus 로고
    • Dynamic association of proteasomal machinery with the centrosome
    • Wigley W. C., Fabunmi R. P., Lee M.G., et al. (1999) Dynamic association of proteasomal machinery with the centrosome. J. Cell. Biol. 145, 481-490.
    • (1999) J. Cell. Biol. , vol.145 , pp. 481-490
    • Wigley, W.C.1    Fabunmi, R.P.2    Lee, M.G.3
  • 49
    • 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., Zhang J., Kholodenko D., et al. (1997) 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.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7977-7982
    • Xia, W.1    Zhang, J.2    Kholodenko, D.3
  • 50
    • 0027488993 scopus 로고
    • The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment
    • Yang Y., Janich S., Cohn J. A., and Wilson J. M. (1993) The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment. Proc. Natl. Acad. Sci. U. S. A. 90, 9480-9484.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 9480-9484
    • Yang, Y.1    Janich, S.2    Cohn, J.A.3    Wilson, J.M.4
  • 51
    • 0034757165 scopus 로고    scopus 로고
    • Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast
    • Zhang Y., Nijbroek G., Sullivan M. L., et al. (2001) Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast. Mol. Biol. Cell. 12, 1303-1314.
    • (2001) Mol. Biol. Cell. , vol.12 , pp. 1303-1314
    • Zhang, Y.1    Nijbroek, G.2    Sullivan, M.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.