메뉴 건너뛰기




Volumn 6, Issue 5, 2007, Pages 845-859

Identification of novel proteins associated with both α-synuclein and DJ-1

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; CALNEXIN; CLATHRIN; DJ 1 PROTEIN; GLUCOSE REGULATED PROTEIN 94; NUCLEOLIN; ROTENONE;

EID: 34249704608     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M600182-MCP200     Document Type: Article
Times cited : (158)

References (69)
  • 1
    • 0033035762 scopus 로고    scopus 로고
    • Managing late complications of Parkinson's disease
    • Stacy M. (1999) Managing late complications of Parkinson's disease. Med. Clin. North Am. 83, 469-481
    • (1999) Med. Clin. North Am , vol.83 , pp. 469-481
    • Stacy, M.1
  • 2
    • 0029688041 scopus 로고    scopus 로고
    • Electron microscopy of Lewy bodies in the amygdala-parahippocampal region. Comparison with inclusion bodies in the MPTP-treated squirrel monkey
    • Forno, L. S., DeLanney, L. E., Irwin, I., and Langston, J. W. (1996) Electron microscopy of Lewy bodies in the amygdala-parahippocampal region. Comparison with inclusion bodies in the MPTP-treated squirrel monkey. Adv. Neurol. 69, 217-228
    • (1996) Adv. Neurol , vol.69 , pp. 217-228
    • Forno, L.S.1    DeLanney, L.E.2    Irwin, I.3    Langston, J.W.4
  • 3
    • 0031910093 scopus 로고    scopus 로고
    • Aggregation of neurofilament and α-synuclein proteins in Lewy bodies: Implications for the pathogenesis of Parkinson disease and Lewy body dementia
    • Trojanowski, J. Q., and Lee, V. M. (1998) Aggregation of neurofilament and α-synuclein proteins in Lewy bodies: implications for the pathogenesis of Parkinson disease and Lewy body dementia. Arch. Neurol. 55, 151-152
    • (1998) Arch. Neurol , vol.55 , pp. 151-152
    • Trojanowski, J.Q.1    Lee, V.M.2
  • 6
    • 33645833848 scopus 로고    scopus 로고
    • Detection of oligomeric forms of α-synuclein protein in human plasma as a potential biomarker for Parkinson's disease
    • El-Agnaf, O. M., Salem, S. A., Paleologou, K. E., Curran, M. D., Gibson, M. J., Court, J. A., Schlossmacher, M. G., and Allsop, D. (2006) Detection of oligomeric forms of α-synuclein protein in human plasma as a potential biomarker for Parkinson's disease. FASEB J. 20, 419-425
    • (2006) FASEB J , vol.20 , pp. 419-425
    • El-Agnaf, O.M.1    Salem, S.A.2    Paleologou, K.E.3    Curran, M.D.4    Gibson, M.J.5    Court, J.A.6    Schlossmacher, M.G.7    Allsop, D.8
  • 8
    • 24944525045 scopus 로고    scopus 로고
    • Molecular pathogenesis of Parkinson's disease
    • Gandhi, S., and Wood, N. W. (2005) Molecular pathogenesis of Parkinson's disease. Hum. Mol. Genet. 14, 2749 -2755
    • (2005) Hum. Mol. Genet , vol.14 , pp. 2749-2755
    • Gandhi, S.1    Wood, N.W.2
  • 11
    • 0242524434 scopus 로고    scopus 로고
    • The DJ-1L166P mutant protein associated with early onset Parkinson's disease is unstable and forms higher-order protein complexes
    • Macedo, M. G., Anar, B., Bronner, I. F., Cannella, M., Squitieri, F., Bonifati, V., Hoogeveen, A., Heutink, P., and Rizzu, P. (2003) The DJ-1L166P mutant protein associated with early onset Parkinson's disease is unstable and forms higher-order protein complexes. Hum. Mol. Genet. 12, 2807-2816
    • (2003) Hum. Mol. Genet , vol.12 , pp. 2807-2816
    • Macedo, M.G.1    Anar, B.2    Bronner, I.F.3    Cannella, M.4    Squitieri, F.5    Bonifati, V.6    Hoogeveen, A.7    Heutink, P.8    Rizzu, P.9
  • 12
    • 0034906096 scopus 로고    scopus 로고
    • Oxidized forms of peroxiredoxins and DJ-1 on two-dimensional gels increased in response to sublethal levels of paraquat
    • Mitsumoto, A., Nakagawa, Y., Takeuchi, A., Okawa, K., Iwamatsu, A., and Takanezawa, Y. (2001) Oxidized forms of peroxiredoxins and DJ-1 on two-dimensional gels increased in response to sublethal levels of paraquat. Free Radic. Res. 35, 301-310
    • (2001) Free Radic. Res , vol.35 , pp. 301-310
    • Mitsumoto, A.1    Nakagawa, Y.2    Takeuchi, A.3    Okawa, K.4    Iwamatsu, A.5    Takanezawa, Y.6
  • 13
    • 1842740232 scopus 로고    scopus 로고
    • Cysteine-106 of DJ-1 is the most sensitive cysteine residue to hydrogen peroxide-mediated oxidation in vivo in human umbilical vein endothelial cells
    • Kinumi, T., Kimata, J., Taira, T., Ariga, H., and Niki, E. (2004) Cysteine-106 of DJ-1 is the most sensitive cysteine residue to hydrogen peroxide-mediated oxidation in vivo in human umbilical vein endothelial cells. Biochem. Biophys. Res. Commun. 317, 722-728
    • (2004) Biochem. Biophys. Res. Commun , vol.317 , pp. 722-728
    • Kinumi, T.1    Kimata, J.2    Taira, T.3    Ariga, H.4    Niki, E.5
  • 15
    • 0345357664 scopus 로고    scopus 로고
    • Down regulation of DJ-1 enhances cell death by oxidative stress, ER stress, and proteasome inhibition
    • Yokota, T., Sugawara, K., Ito, K., Takahashi, R., Ariga, H., and Mizusawa, H. (2003) Down regulation of DJ-1 enhances cell death by oxidative stress, ER stress, and proteasome inhibition. Biochem. Biophys. Res. Commun. 312, 1342-1348
    • (2003) Biochem. Biophys. Res. Commun , vol.312 , pp. 1342-1348
    • Yokota, T.1    Sugawara, K.2    Ito, K.3    Takahashi, R.4    Ariga, H.5    Mizusawa, H.6
  • 16
    • 13944267769 scopus 로고    scopus 로고
    • DJ-1 is a redox-dependent molecular chaperone that inhibits α-synuclein aggregate formation
    • Shendelman, S., Jonason, A., Martinat, C., Leete, T., and Abeliovich, A. (2004) DJ-1 is a redox-dependent molecular chaperone that inhibits α-synuclein aggregate formation. PLoS Biol. 2, 1764-1773
    • (2004) PLoS Biol , vol.2 , pp. 1764-1773
    • Shendelman, S.1    Jonason, A.2    Martinat, C.3    Leete, T.4    Abeliovich, A.5
  • 17
    • 30044449754 scopus 로고    scopus 로고
    • DJ-1 up-regulates glutathione synthesis during oxidative stress and inhibits A53T α-synuclein toxicity
    • Zhou, W., and Freed, C. R. (2005) DJ-1 up-regulates glutathione synthesis during oxidative stress and inhibits A53T α-synuclein toxicity. J. Biol. Chem. 280, 43150-43158
    • (2005) J. Biol. Chem , vol.280 , pp. 43150-43158
    • Zhou, W.1    Freed, C.R.2
  • 18
    • 31344464179 scopus 로고    scopus 로고
    • The oxidation state of DJ-1 regulates its chaperone activity toward α-synuclein
    • Zhou, W., Zhu, M., Wilson, M. A., Petsko, G. A., and Fink, A. L. (2006) The oxidation state of DJ-1 regulates its chaperone activity toward α-synuclein. J. Mol. Biol. 356, 1036-10483
    • (2006) J. Mol. Biol , vol.356 , pp. 1036-10483
    • Zhou, W.1    Zhu, M.2    Wilson, M.A.3    Petsko, G.A.4    Fink, A.L.5
  • 19
    • 20744454444 scopus 로고    scopus 로고
    • DJ-1 is present in a large molecular complex in human brain tissue and interacts with α-synuclein
    • Meulener, M. C., Graves, C. L., Sampathu, D. M., Armstrong-Gold, C. E., Bonini, N. M., and Giasson, B. I. (2005) DJ-1 is present in a large molecular complex in human brain tissue and interacts with α-synuclein. J. Neurochem. 93, 1524-1532
    • (2005) J. Neurochem , vol.93 , pp. 1524-1532
    • Meulener, M.C.1    Graves, C.L.2    Sampathu, D.M.3    Armstrong-Gold, C.E.4    Bonini, N.M.5    Giasson, B.I.6
  • 21
    • 2942689352 scopus 로고    scopus 로고
    • Pathological properties of the Parkinson's disease-associated protein DJ-1 in α-synucleinopathies and tauopathies: Relevance for multiple system atrophy and Pick's disease
    • Neumann, M., Muller, V., Gorner, K., Kretzschmar, H. A., Haass, C., and Kahle, P. J. (2004) Pathological properties of the Parkinson's disease-associated protein DJ-1 in α-synucleinopathies and tauopathies: relevance for multiple system atrophy and Pick's disease. Acta Neuropathol. (Berl.) 107, 489-496
    • (2004) Acta Neuropathol. (Berl.) , vol.107 , pp. 489-496
    • Neumann, M.1    Muller, V.2    Gorner, K.3    Kretzschmar, H.A.4    Haass, C.5    Kahle, P.J.6
  • 22
    • 15544374722 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of mitochondrial proteins: Relevance to Lewy body formation and Parkinson's disease
    • Jin, J., Meredith, G. E., Chen, L., Zhou, Y., Xu, J., Shie, F. S., Lockhart, P., and Zhang, J. (2005) Quantitative proteomic analysis of mitochondrial proteins: relevance to Lewy body formation and Parkinson's disease. Brain Res, Mol. Brain Res. 134, 119-138
    • (2005) Brain Res, Mol. Brain Res , vol.134 , pp. 119-138
    • Jin, J.1    Meredith, G.E.2    Chen, L.3    Zhou, Y.4    Xu, J.5    Shie, F.S.6    Lockhart, P.7    Zhang, J.8
  • 24
    • 0034056940 scopus 로고    scopus 로고
    • The dynamic range of protein expression: A challenge for proteomic research
    • Corthals, G. L., Wasinger, V. C., Hochstrasser, D. F., and Sanchez, J. C. (2000) The dynamic range of protein expression: a challenge for proteomic research. Electrophoresis 21, 1104-1115
    • (2000) Electrophoresis , vol.21 , pp. 1104-1115
    • Corthals, G.L.1    Wasinger, V.C.2    Hochstrasser, D.F.3    Sanchez, J.C.4
  • 26
    • 0026781572 scopus 로고
    • A novel N18TG2X mesencephalon cell hybrid expresses properties that suggest a dopaminergic cell line of substantia nigra origin
    • Crawford, G. C., Le, W., Smith, R. G., Xie, W. J., Stefani, E., and Appel, S. H. (1992) A novel N18TG2X mesencephalon cell hybrid expresses properties that suggest a dopaminergic cell line of substantia nigra origin. J. Neurosci. 12, 3392-3398
    • (1992) J. Neurosci , vol.12 , pp. 3392-3398
    • Crawford, G.C.1    Le, W.2    Smith, R.G.3    Xie, W.J.4    Stefani, E.5    Appel, S.H.6
  • 27
    • 0032581347 scopus 로고    scopus 로고
    • Secondary excitotoxicity contributes to dopamine-induced apoptosis of dopaminergic neuronal cultures
    • Zhang, J., Price, J. O., Graham, D. G., and Montine, T. J. (1998) Secondary excitotoxicity contributes to dopamine-induced apoptosis of dopaminergic neuronal cultures. Biochem. Biophys. Res. Commun. 248, 812-816
    • (1998) Biochem. Biophys. Res. Commun , vol.248 , pp. 812-816
    • Zhang, J.1    Price, J.O.2    Graham, D.G.3    Montine, T.J.4
  • 28
    • 0033952292 scopus 로고    scopus 로고
    • Enhancement of dopaminergic neurotoxicity by the mercapturate of dopamine: Relevance to Parkinson's disease
    • Zhang, J., Kravtsov, V., Amarnath, V., Picklo, M. J., Graham, D. G., and Montine, T. J. (2000) Enhancement of dopaminergic neurotoxicity by the mercapturate of dopamine: relevance to Parkinson's disease. J. Neurochem. 74, 970-978
    • (2000) J. Neurochem , vol.74 , pp. 970-978
    • Zhang, J.1    Kravtsov, V.2    Amarnath, V.3    Picklo, M.J.4    Graham, D.G.5    Montine, T.J.6
  • 29
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., and Mann, M. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1, 376-386
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 30
    • 33646011523 scopus 로고    scopus 로고
    • Proteomic analysis of microglial contribution to mouse strain-dependent dopaminergic neurotoxicity
    • McLaughlin, P., Zhou, Y., Ma, T., Liu, J., Zhang, W., Hong, J. S., Kovacs, M., and Zhang, J. (2006) Proteomic analysis of microglial contribution to mouse strain-dependent dopaminergic neurotoxicity. Glia 53, 567-582
    • (2006) Glia , vol.53 , pp. 567-582
    • McLaughlin, P.1    Zhou, Y.2    Ma, T.3    Liu, J.4    Zhang, W.5    Hong, J.S.6    Kovacs, M.7    Zhang, J.8
  • 33
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of pepticle identifications made by MS/MS and database search
    • Keller, A., Nesvizhskii, A. I., Kolker, E., and Aebersold, R. (2002) Empirical statistical model to estimate the accuracy of pepticle identifications made by MS/MS and database search. Anal. Chem. 74, 5383-5392
    • (2002) Anal. Chem , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 35
    • 0344737959 scopus 로고    scopus 로고
    • Automated statistical analysis of protein abundance ratios from data generated by stable-isotope dilution and tandem mass spectrometry
    • Li, X. J., Zhang, H., Ranish, J. A., and Aebersold, R. (2003) Automated statistical analysis of protein abundance ratios from data generated by stable-isotope dilution and tandem mass spectrometry. Anal. Biochem. 75, 6648-6657
    • (2003) Anal. Biochem , vol.75 , pp. 6648-6657
    • Li, X.J.1    Zhang, H.2    Ranish, J.A.3    Aebersold, R.4
  • 36
    • 33746296891 scopus 로고    scopus 로고
    • Proteomic identification of a stress protein, mortalin/ mthsp70/ GRP75: Relevance to Parkinson disease
    • Jin, J., Hulette, C., Wang, Y., Zhang, T., Pan, C., Wadhwa, R., and Zhang, J. (2006) Proteomic identification of a stress protein, mortalin/ mthsp70/ GRP75: relevance to Parkinson disease. Mol. Cell. Proteomics 5, 1193-1204
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1193-1204
    • Jin, J.1    Hulette, C.2    Wang, Y.3    Zhang, T.4    Pan, C.5    Wadhwa, R.6    Zhang, J.7
  • 37
    • 15544374722 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of mitochondrial proteins: Relevance to Lewy body formation and Parkinson's disease
    • Jin, J., Meredith, G., Chen, L., Zhou, Y., Xu, J., Xie, F., Lockhart, P., and Zhang, J. (2005) Quantitative proteomic analysis of mitochondrial proteins: relevance to Lewy body formation and Parkinson's disease. Mol. Brain Res. 24, 119-138
    • (2005) Mol. Brain Res , vol.24 , pp. 119-138
    • Jin, J.1    Meredith, G.2    Chen, L.3    Zhou, Y.4    Xu, J.5    Xie, F.6    Lockhart, P.7    Zhang, J.8
  • 38
    • 27644559809 scopus 로고    scopus 로고
    • Microglial activation induced by neurodegeneration: A proteomic analysis
    • Zhou, Y., Wang, Y., Kovacs, M., Jin, J., and Zhang, J. (2005) Microglial activation induced by neurodegeneration: a proteomic analysis. Mol. Cell. Proteomics 4, 1471-1479
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1471-1479
    • Zhou, Y.1    Wang, Y.2    Kovacs, M.3    Jin, J.4    Zhang, J.5
  • 39
    • 14844314804 scopus 로고    scopus 로고
    • Advances in protein complex analysis using mass spectrometry
    • Gingras, A. C., Aebersold, R., and Raught, B. (2005) Advances in protein complex analysis using mass spectrometry. J. Physiol. 563, 11-21
    • (2005) J. Physiol , vol.563 , pp. 11-21
    • Gingras, A.C.1    Aebersold, R.2    Raught, B.3
  • 40
    • 0037337310 scopus 로고    scopus 로고
    • A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling
    • Blagoev, B., Kratchmarova, I., Ong, S. E., Nielsen, M., Foster, L. J., and Mann, M. (2003) A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nat. Biotechnol. 21, 315-318
    • (2003) Nat. Biotechnol , vol.21 , pp. 315-318
    • Blagoev, B.1    Kratchmarova, I.2    Ong, S.E.3    Nielsen, M.4    Foster, L.J.5    Mann, M.6
  • 42
    • 0038342507 scopus 로고    scopus 로고
    • Association of the cytoskeletal GTP-binding protein Sept4/H5 with cytoplasmic inclusions found in Parkinson's disease and other synucleinopathies
    • lhara, M., Tomimoto, H., Kitayama, H., Morioka, Y., Akiguchi, I., Shibasaki, H., Noda, M., and Kinoshita, M. (2003) Association of the cytoskeletal GTP-binding protein Sept4/H5 with cytoplasmic inclusions found in Parkinson's disease and other synucleinopathies. J. Biol. Chem. 278, 24095-24102
    • (2003) J. Biol. Chem , vol.278 , pp. 24095-24102
    • lhara, M.1    Tomimoto, H.2    Kitayama, H.3    Morioka, Y.4    Akiguchi, I.5    Shibasaki, H.6    Noda, M.7    Kinoshita, M.8
  • 43
    • 20944437573 scopus 로고    scopus 로고
    • The Parkinson's disease-associated DJ-1 protein is a transcriptional co-activator that protects against neuronal apoptosis
    • Xu, J., Zhong, N., Wang, H., Elias, J. E., Kim, C. Y., Woldman, I., Pifl, C., Gygi, S. P., Geula, C., and Yankner, B. A. (2005) The Parkinson's disease-associated DJ-1 protein is a transcriptional co-activator that protects against neuronal apoptosis. Hum. Mol. Genet. 14 1231-1241
    • (2005) Hum. Mol. Genet , vol.14 , pp. 1231-1241
    • Xu, J.1    Zhong, N.2    Wang, H.3    Elias, J.E.4    Kim, C.Y.5    Woldman, I.6    Pifl, C.7    Gygi, S.P.8    Geula, C.9    Yankner, B.A.10
  • 44
    • 25444514752 scopus 로고    scopus 로고
    • Association of DJ-1 with chaperones and enhanced association and colocalization with mitochondrial Hsp70 by oxidative stress
    • Li, H. M., Niki, T., Taira, T., Iguchi-Ariga, S. M., and Ariga, H. (2005) Association of DJ-1 with chaperones and enhanced association and colocalization with mitochondrial Hsp70 by oxidative stress. Free Radic. Res. 39, 1091-1099
    • (2005) Free Radic. Res , vol.39 , pp. 1091-1099
    • Li, H.M.1    Niki, T.2    Taira, T.3    Iguchi-Ariga, S.M.4    Ariga, H.5
  • 45
    • 22144465488 scopus 로고    scopus 로고
    • Interaction of DJ-1 with Daxx inhibits apoptosis signal-regulating kinase activity 1 and cell death
    • Junn, E., Taniguchi, H., Jeong, B. S., Zhao, X., Ichijo, H., and Mouradian, M. M. (2005) Interaction of DJ-1 with Daxx inhibits apoptosis signal-regulating kinase activity 1 and cell death. Proc. Natl. Aced. Sci. U. S. A. 102, 9691-9696
    • (2005) Proc. Natl. Aced. Sci. U. S. A , vol.102 , pp. 9691-9696
    • Junn, E.1    Taniguchi, H.2    Jeong, B.S.3    Zhao, X.4    Ichijo, H.5    Mouradian, M.M.6
  • 46
    • 18844404686 scopus 로고    scopus 로고
    • Rotenone induces aggregation of γ-tubulin protein and subsequent disorganization of the centrosome: Relevance to formation of inclusion bodies and neurodegeneration
    • Diaz-Corrales, F. J., Asanuma, M., Miyazaki, I., Miyoshi, K., and Ogawa, (2005) Rotenone induces aggregation of γ-tubulin protein and subsequent disorganization of the centrosome: relevance to formation of inclusion bodies and neurodegeneration. Neuroscience 133, 117-135
    • (2005) Neuroscience , vol.133 , pp. 117-135
    • Diaz-Corrales, F.J.1    Asanuma, M.2    Miyazaki, I.3    Miyoshi, K.4    Ogawa5
  • 47
    • 33646833056 scopus 로고    scopus 로고
    • Basic fibroblast growth factor protects against rotenone-induced dopaminergic cell death through activation of extracellular signal-regulated kinases 1/2 and phosphaticlylinositol-3 kinase pathways
    • Hsuan, S. L., Klintworth, H. M., and Xia, Z. (2006) Basic fibroblast growth factor protects against rotenone-induced dopaminergic cell death through activation of extracellular signal-regulated kinases 1/2 and phosphaticlylinositol-3 kinase pathways. J. Neurosci. 26, 4481-4491
    • (2006) J. Neurosci , vol.26 , pp. 4481-4491
    • Hsuan, S.L.1    Klintworth, H.M.2    Xia, Z.3
  • 48
    • 3042822563 scopus 로고    scopus 로고
    • Altered expression of protein p421P4/centaurin-α1 in Alzheimer's disease brains and possible interaction of p421P4 with nucleolin
    • Reiser, G., and Bernstein, H. G. (2004) Altered expression of protein p421P4/centaurin-α1 in Alzheimer's disease brains and possible interaction of p421P4 with nucleolin. Neuroreport 15, 147-148
    • (2004) Neuroreport , vol.15 , pp. 147-148
    • Reiser, G.1    Bernstein, H.G.2
  • 50
    • 0033210210 scopus 로고    scopus 로고
    • GRP94, an ER chaperone with protein and peptide binding properties
    • Argon, Y., and Simen, B. B. (1999) GRP94, an ER chaperone with protein and peptide binding properties. Semin. Cell Dev. Biol. 10, 495-505
    • (1999) Semin. Cell Dev. Biol , vol.10 , pp. 495-505
    • Argon, Y.1    Simen, B.B.2
  • 52
    • 23944438373 scopus 로고    scopus 로고
    • Cellular functions of endoplasmic reticulum chaperones calreticulin, calnexin, and ERp57
    • Bedard, K., Szabo, E., Michalak, M., and Opas, M. (2005) Cellular functions of endoplasmic reticulum chaperones calreticulin, calnexin, and ERp57. Int. Rev. Cytol. 245, 91-121
    • (2005) Int. Rev. Cytol , vol.245 , pp. 91-121
    • Bedard, K.1    Szabo, E.2    Michalak, M.3    Opas, M.4
  • 53
    • 33645141853 scopus 로고    scopus 로고
    • ER stress and neurodegenerative diseases
    • Lindholm, D., Wootz, H., and Korhonen, L. (2006) ER stress and neurodegenerative diseases. Cell Death Differ. 13, 385-392
    • (2006) Cell Death Differ , vol.13 , pp. 385-392
    • Lindholm, D.1    Wootz, H.2    Korhonen, L.3
  • 54
    • 0037114971 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease
    • Ryu, E. J., Harding, H. P., Angelastro, J. M., Vitolo, O. V., Ron, D., and Greene, L. A. (2002) Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease. J. Neurosci. 22, 10690-10698
    • (2002) J. Neurosci , vol.22 , pp. 10690-10698
    • Ryu, E.J.1    Harding, H.P.2    Angelastro, J.M.3    Vitolo, O.V.4    Ron, D.5    Greene, L.A.6
  • 57
    • 0033520474 scopus 로고    scopus 로고
    • α-Synuclein binds to Tau and stimulates the protein kinase A-catalyzed tau phosphorylation of serine residues 262 and 356
    • Jensen, P. H., Hager, H., Nielsen, M. S., Hojrup, P., Gliemann, J., and Jakes, R. (1999) α-Synuclein binds to Tau and stimulates the protein kinase A-catalyzed tau phosphorylation of serine residues 262 and 356. J. Biol. Chem. 274 25481-25489
    • (1999) J. Biol. Chem , vol.274 , pp. 25481-25489
    • Jensen, P.H.1    Hager, H.2    Nielsen, M.S.3    Hojrup, P.4    Gliemann, J.5    Jakes, R.6
  • 58
    • 0036161596 scopus 로고    scopus 로고
    • Mass spectrometry in coupling with affinity capture-release and isotope-coded affinity tags for quantitative protein analysis
    • Turecek, F. (2002) Mass spectrometry in coupling with affinity capture-release and isotope-coded affinity tags for quantitative protein analysis. J. Mass Spectrom. 37, 11-114
    • (2002) J. Mass Spectrom , vol.37 , pp. 11-114
    • Turecek, F.1
  • 62
    • 0035813135 scopus 로고    scopus 로고
    • DJ-1 positively regulates the androgen receptor by impairing the binding of PIASxα to the receptor
    • Takahashi, K., Taira, T., Niki, T., Seino, C., Iguchi-Ariga, S. M., and Ariga, H. (2001) DJ-1 positively regulates the androgen receptor by impairing the binding of PIASxα to the receptor. J. Biol. Chem. 276, 37556-37563
    • (2001) J. Biol. Chem , vol.276 , pp. 37556-37563
    • Takahashi, K.1    Taira, T.2    Niki, T.3    Seino, C.4    Iguchi-Ariga, S.M.5    Ariga, H.6
  • 63
    • 18144420749 scopus 로고    scopus 로고
    • DJ-1 restores p53 transcription activity inhibited by Topors/ p53BP3
    • Shinbo, Y., Taira, T., Niki, T., Iguchi-Ariga, S. M., and Ariga, H. (2005) DJ-1 restores p53 transcription activity inhibited by Topors/ p53BP3. Int. J. Oncol. 26, 641-648
    • (2005) Int. J. Oncol , vol.26 , pp. 641-648
    • Shinbo, Y.1    Taira, T.2    Niki, T.3    Iguchi-Ariga, S.M.4    Ariga, H.5
  • 67
    • 0030957355 scopus 로고    scopus 로고
    • Clathrin-coated vesicle formation and protein sorting: An integrated process
    • Schmid, S. L. (1997) Clathrin-coated vesicle formation and protein sorting: an integrated process. Annu. Rev. Biochem. 66, 511-548
    • (1997) Annu. Rev. Biochem , vol.66 , pp. 511-548
    • Schmid, S.L.1
  • 68
    • 13444263549 scopus 로고    scopus 로고
    • Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling
    • Le Roy, C., and Wrana, J. L. (2005) Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling. Nat. Rev. Mol. Cell. Biol. 6, 112-126
    • (2005) Nat. Rev. Mol. Cell. Biol , vol.6 , pp. 112-126
    • Le Roy, C.1    Wrana, J.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.