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Volumn 6, Issue 1, 2011, Pages

DJ-1 can inhibit microtubule associated protein 1 B formed aggregates

Author keywords

[No Author keywords available]

Indexed keywords

DJ 1 PROTEIN; MICROTUBULE ASSOCIATED PROTEIN 1;

EID: 79957901402     PISSN: None     EISSN: 17501326     Source Type: Journal    
DOI: 10.1186/1750-1326-6-38     Document Type: Article
Times cited : (16)

References (40)
  • 1
    • 0029937494 scopus 로고    scopus 로고
    • Epidemiology of Parkinson's disease
    • DOI 10.1016/S0733-8619(05)70259-0
    • Epidemiology of Parkinson's disease. CM Tanner SM Goldman, Neurol Clin 1996 14 317 335 10.1016/S0733-8619(05)70259-0 8827174 (Pubitemid 26157425)
    • (1996) Neurologic Clinics , vol.14 , Issue.2 , pp. 317-335
    • Tanner, C.M.1    Goldman, S.M.2
  • 2
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • 15272267
    • Protein aggregation and neurodegenerative disease. CA Ross MA Poirier, Nat Med 2004 10 Suppl 10 17 15272267
    • (2004) Nat Med , vol.10 , Issue.SUPPL. , pp. 10-17
    • Ross, C.A.1    Poirier, M.A.2
  • 3
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • 10.1016/S0962-8924(00)01852-3. 11121744
    • Aggresomes, inclusion bodies and protein aggregation. RR Kopito, Trends Cell Biol 2000 10 524 530 10.1016/S0962-8924(00)01852-3 11121744
    • (2000) Trends Cell Biol , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 4
    • 27644596641 scopus 로고    scopus 로고
    • What is the role of protein aggregation in neurodegeneration?
    • DOI 10.1038/nrm1742, PII N1742
    • Opinion: What is the role of protein aggregation in neurodegeneration? CA Ross MA Poirier, Nat Rev Mol Cell Biol 2005 6 891 898 10.1038/nrm1742 16167052 (Pubitemid 41568738)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.11 , pp. 891-898
    • Ross, C.A.1    Poirier, M.A.2
  • 5
    • 0037077040 scopus 로고    scopus 로고
    • Toxic proteins in neurodegenerative disease
    • DOI 10.1126/science.1067122
    • Toxic proteins in neurodegenerative disease. JP Taylor J Hardy KH Fischbeck, Science 2002 296 1991 1995 10.1126/science.1067122 12065827 (Pubitemid 34627514)
    • (2002) Science , vol.296 , Issue.5575 , pp. 1991-1995
    • Taylor, J.P.1    Hardy, J.2    Fischbeck, K.H.3
  • 6
    • 0022616904 scopus 로고
    • Cytoskeletal protein abnormalities in neurodegenerative diseases
    • Cytoskeletal protein abnormalities in neurodegenerative diseases. JE Goldman SH Yen, Ann Neurol 1986 19 209 223 10.1002/ana.410190302 3008639 (Pubitemid 16111070)
    • (1986) Annals of Neurology , vol.19 , Issue.3 , pp. 209-223
    • Goldman, J.E.1    Yen, S.-H.2
  • 7
    • 7944236911 scopus 로고    scopus 로고
    • The cytoskeleton in neurodegenerative diseases
    • DOI 10.1002/path.1650
    • The cytoskeleton in neurodegenerative diseases. NJ Cairns VM Lee JQ Trojanowski, J Pathol 2004 204 438 449 10.1002/path.1650 15495240 (Pubitemid 39468155)
    • (2004) Journal of Pathology , vol.204 , Issue.4 , pp. 438-449
    • Cairns, N.J.1    Lee, V.M.-Y.2    Trojanowski, J.Q.3
  • 8
    • 0030005625 scopus 로고    scopus 로고
    • Tau protein and the neurofibrillary pathology of Alzheimer's disease
    • Tau protein and the neurofibrillary pathology of Alzheimer's disease. M Goedert, Ann N Y Acad Sci 1996 777 121 131 10.1111/j.1749-6632.1996.tb34410.x 8624074 (Pubitemid 26149179)
    • (1996) Annals of the New York Academy of Sciences , vol.777 , pp. 121-131
    • Goedert, M.1
  • 9
    • 0242363670 scopus 로고    scopus 로고
    • Molecular pathways of neurodegeneration in Parkinson's disease
    • DOI 10.1126/science.1087753
    • Molecular pathways of neurodegeneration in Parkinson's disease. TM Dawson VL Dawson, Science 2003 302 819 822 10.1126/science.1087753 14593166 (Pubitemid 37339614)
    • (2003) Science , vol.302 , Issue.5646 , pp. 819-822
    • Dawson, T.M.1    Dawson, V.L.2
  • 11
    • 27744494043 scopus 로고    scopus 로고
    • Gigaxonin-controlled degradation of MAP1B light chain is critical to neuronal survival
    • DOI 10.1038/nature04256, PII N04256
    • Gigaxonin-controlled degradation of MAP1B light chain is critical to neuronal survival. E Allen J Ding W Wang S Pramanik J Chou V Yau Y Yang, Nature 2005 438 224 228 10.1038/nature04256 16227972 (Pubitemid 41599874)
    • (2005) Nature , vol.438 , Issue.7065 , pp. 224-228
    • Allen, E.1    Ding, J.2    Wang, W.3    Pramanik, S.4    Chou, J.5    Yau, V.6    Yang, Y.7
  • 12
    • 0346750742 scopus 로고    scopus 로고
    • Microtubule-Associated Protein 1B Function during Normal Development, Regeneration, and Pathological Conditions in the Nervous System
    • DOI 10.1002/neu.10283
    • Microtubule-associated protein 1B function during normal development, regeneration, and pathological conditions in the nervous system. C Gonzalez-Billault EM Jimenez-Mateos A Caceres J Diaz-Nido F Wandosell J Avila, J Neurobiol 2004 58 48 59 10.1002/neu.10283 14598369 (Pubitemid 37543337)
    • (2004) Journal of Neurobiology , vol.58 , Issue.1 , pp. 48-59
    • Gonzalez-Billault, C.1    Jimenez-Mateos, E.M.2    Caceres, A.3    Diaz-Nido, J.4    Wandosell, F.5    Avila, J.6
  • 13
    • 0030917033 scopus 로고    scopus 로고
    • Delayed development of nervous system in mice homozygous for disrupted microtubule-associated protein 1B (MAP1B) gene
    • DOI 10.1083/jcb.137.7.1615
    • Delayed development of nervous system in mice homozygous for disrupted microtubule-associated protein 1B (MAP1B) gene. Y Takei S Kondo A Harada S Inomata T Noda N Hirokawa, J Cell Biol 1997 137 1615 1626 10.1083/jcb.137.7.1615 9199175 (Pubitemid 27282241)
    • (1997) Journal of Cell Biology , vol.137 , Issue.7 , pp. 1615-1626
    • Takei, Y.1    Kondo, S.2    Harada, A.3    Inomata, S.4    Noda, T.5    Hirokawa, N.6
  • 14
    • 0034647557 scopus 로고    scopus 로고
    • Microtubule-associated protein 1B is a component of cortical Lewy bodies and binds α-synuclein filaments
    • DOI 10.1074/jbc.M000099200
    • Microtubule-associated protein 1B is a component of cortical Lewy bodies and binds alpha-synuclein filaments. PH Jensen K Islam J Kenney MS Nielsen J Power WP Gai, J Biol Chem 2000 275 21500 21507 10.1074/jbc.M000099200 10764738 (Pubitemid 30481854)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.28 , pp. 21500-21507
    • Jensen, P.H.1    Islam, K.2    Kenney, J.3    Nielsen, M.S.4    Power, J.5    Gai, W.P.6
  • 16
    • 1642379155 scopus 로고    scopus 로고
    • Linking DJ-1 to neurodegeneration offers novel insights for understanding the pathogenesis of Parkinson's disease
    • DOI 10.1007/s00109-003-0512-1
    • Linking DJ-1 to neurodegeneration offers novel insights for understanding the pathogenesis of Parkinson's disease. V Bonifati BA Oostra P Heutink, J Mol Med 2004 82 163 174 10.1007/s00109-003-0512-1 14712351 (Pubitemid 38392166)
    • (2004) Journal of Molecular Medicine , vol.82 , Issue.3 , pp. 163-174
    • Bonifati, V.1    Oostra, B.A.2    Heutink, P.3
  • 19
    • 0042232039 scopus 로고    scopus 로고
    • Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease
    • DOI 10.1074/jbc.M304221200
    • Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease. X Tao L Tong, J Biol Chem 2003 278 31372 31379 10.1074/jbc.M304221200 12761214 (Pubitemid 36994657)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.33 , pp. 31372-31379
    • Tao, X.1    Tong, L.2
  • 20
    • 13944267769 scopus 로고    scopus 로고
    • DJ-1 Is a redox-dependent molecular chaperone that inhibits α-synuclein aggregate formation
    • DOI 10.1371/journal.pbio.0020362
    • DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation. S Shendelman A Jonason C Martinat T Leete A Abeliovich, PLoS Biol 2004 2 362 10.1371/journal.pbio.0020362 (Pubitemid 40280476)
    • (2004) PLoS Biology , vol.2 , Issue.11
    • Shendelman, S.1    Jonason, A.2    Martinat, C.3    Leete, T.4    Abeliovich, A.5
  • 21
    • 44849093321 scopus 로고    scopus 로고
    • DJ-1 modulates α-synuclein aggregation state in a cellular model of oxidative stress: Relevance for Parkinson's Disease and involvement of HSP70
    • DOI 10.1371/journal.pone.0001884
    • DJ-1 modulates alpha-synuclein aggregation state in a cellular model of oxidative stress: relevance for Parkinson's disease and involvement of HSP70. S Batelli D Albani R Rametta L Polito F Prato M Pesaresi A Negro G Forloni, PLoS One 2008 3 1884 10.1371/journal.pone.0001884 (Pubitemid 351943824)
    • (2008) PLoS ONE , vol.3 , Issue.4
    • Batelli, S.1    Albani, D.2    Rametta, R.3    Polito, L.4    Prato, F.5    Pesaresi, M.6    Negro, A.7    Forloni, G.8
  • 22
    • 34249704608 scopus 로고    scopus 로고
    • Identification of novel proteins associated with both α-synuclein and DJ-1
    • DOI 10.1074/mcp.M600182-MCP200
    • Identification of novel proteins associated with both alpha-synuclein and DJ-1. J Jin GJ Li J Davis D Zhu Y Wang C Pan J Zhang, Mol Cell Proteomics 2007 6 845 859 10.1074/mcp.M600182-MCP200 16854843 (Pubitemid 46831936)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.5 , pp. 845-859
    • Jin, J.1    Li, G.J.2    Davis, J.3    Zhu, D.4    Wang, Y.5    Pan, C.6    Zhang, J.7
  • 23
    • 0346434141 scopus 로고    scopus 로고
    • A missense mutation (L166P) in DJ-1, linked to familial Parkinson's disease, confers reduced protein stability and impairs homo-oligomerization
    • A missense mutation (L166P) in DJ-1, linked to familial Parkinson's disease, confers reduced protein stability and impairs homo-oligomerization. DJ Moore L Zhang TM Dawson VL Dawson, J Neurochem 2003 87 1558 1567 10.1111/j.1471-4159.2003.02265.x 14713311 (Pubitemid 38020589)
    • (2003) Journal of Neurochemistry , vol.87 , Issue.6 , pp. 1558-1567
    • Moore, D.J.1    Zhang, L.2    Dawson, T.M.3    Dawson, V.L.4
  • 25
    • 0345357664 scopus 로고    scopus 로고
    • Down regulation of DJ-1 enhances cell death by oxidative stress, ER stress, and proteasome inhibition
    • DOI 10.1016/j.bbrc.2003.11.056
    • Down regulation of DJ-1 enhances cell death by oxidative stress, ER stress, and proteasome inhibition. T Yokota K Sugawara K Ito R Takahashi H Ariga H Mizusawa, Biochem Biophys Res Commun 2003 312 1342 1348 10.1016/j.bbrc.2003. 11.056 14652021 (Pubitemid 37490964)
    • (2003) Biochemical and Biophysical Research Communications , vol.312 , Issue.4 , pp. 1342-1348
    • Yokota, T.1    Sugawara, K.2    Ito, K.3    Takahashi, R.4    Ariga, H.5    Mizusawa, H.6
  • 27
    • 26444442450 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress: Cell life and death decisions
    • DOI 10.1172/JCI26373
    • Endoplasmic reticulum stress: cell life and death decisions. C Xu B Bailly-Maitre JC Reed, J Clin Invest 2005 115 2656 2664 10.1172/JCI26373 16200199 (Pubitemid 41434389)
    • (2005) Journal of Clinical Investigation , vol.115 , Issue.10 , pp. 2656-2664
    • Xu, C.1    Bailly-Maitre, B.2    Reed, J.C.3
  • 29
    • 0033634641 scopus 로고    scopus 로고
    • Perk is essential for translational regulation and cell survival during the unfolded protein response
    • 10.1016/S1097-2765(00)80330-5. 10882126
    • Perk is essential for translational regulation and cell survival during the unfolded protein response. HP Harding Y Zhang A Bertolotti H Zeng D Ron, Mol Cell 2000 5 897 904 10.1016/S1097-2765(00)80330-5 10882126
    • (2000) Mol Cell , vol.5 , pp. 897-904
    • Harding, H.P.1    Zhang, Y.2    Bertolotti, A.3    Zeng, H.4    Ron, D.5
  • 30
    • 0035692636 scopus 로고    scopus 로고
    • DJ-1 is an indicator for endogenous reactive oxygen species elicited by endotoxin
    • DJ-1 is an indicator for endogenous reactive oxygen species elicited by endotoxin. A Mitsumoto Y Nakagawa, Free Radic Res 2001 35 885 893 10.1080/10715760100301381 11811539 (Pubitemid 34065677)
    • (2001) Free Radical Research , vol.35 , Issue.6 , pp. 885-893
    • Mitsumoto, A.1    Nakagawa, Y.2
  • 31
    • 24044506249 scopus 로고    scopus 로고
    • Roles of Drosophila DJ-1 in survival of dopaminergic neurons and oxidative stress
    • DOI 10.1016/j.cub.2005.07.036, PII S0960982205007918
    • Roles of Drosophila DJ-1 in survival of dopaminergic neurons and oxidative stress. FM Menzies SC Yenisetti KT Min, Curr Biol 2005 15 1578 1582 10.1016/j.cub.2005.07.036 16139214 (Pubitemid 41219598)
    • (2005) Current Biology , vol.15 , Issue.17 , pp. 1578-1582
    • Menzies, F.M.1    Yenisetti, S.C.2    Min, K.-T.3
  • 32
    • 24044472010 scopus 로고    scopus 로고
    • Drosophila DJ-1 mutants are selectively sensitive to environmental toxins associated with Parkinson's disease
    • DOI 10.1016/j.cub.2005.07.064, PII S0960982205008481
    • Drosophila DJ-1 mutants are selectively sensitive to environmental toxins associated with Parkinson's disease. M Meulener AJ Whitworth CE Armstrong-Gold P Rizzu P Heutink PD Wes LJ Pallanck NM Bonini, Curr Biol 2005 15 1572 1577 10.1016/j.cub.2005.07.064 16139213 (Pubitemid 41219597)
    • (2005) Current Biology , vol.15 , Issue.17 , pp. 1572-1577
    • Meulener, M.1    Whitworth, A.J.2    Armstrong-Gold, C.E.3    Rizzu, P.4    Heutink, P.5    Wes, P.D.6    Pallanck, L.J.7    Bonini, N.M.8
  • 33
    • 1642527499 scopus 로고    scopus 로고
    • DJ-1 has a role in antioxidative stress to prevent cell death
    • DOI 10.1038/sj.embor.7400074
    • DJ-1 has a role in antioxidative stress to prevent cell death. T Taira Y Saito T Niki SM Iguchi-Ariga K Takahashi H Ariga, EMBO Rep 2004 5 213 218 10.1038/sj.embor.7400074 14749723 (Pubitemid 38401204)
    • (2004) EMBO Reports , vol.5 , Issue.2 , pp. 213-218
    • Taira, T.1    Saito, Y.2    Niki, T.3    Iguchi-Ariga, S.M.M.4    Takahashi, K.5    Ariga, H.6
  • 34
    • 13944279784 scopus 로고    scopus 로고
    • Sensitivity to oxidative stress in DJ-1-deficient dopamine neurons: An ES- derived cell model of primary Parkinsonism
    • DOI 10.1371/journal.pbio.0020327
    • Sensitivity to oxidative stress in DJ-1-deficient dopamine neurons: an ES- derived cell model of primary Parkinsonism. C Martinat S Shendelman A Jonason T Leete MF Beal L Yang T Floss A Abeliovich, PLoS Biol 2004 2 327 10.1371/journal.pbio.0020327 (Pubitemid 40280475)
    • (2004) PLoS Biology , vol.2 , Issue.11
    • Martinat, C.1    Shendelman, S.2    Jonason, A.3    Leete, T.4    Beal, M.F.5    Yang, L.6    Floss, T.7    Abeliovich, A.8
  • 36
    • 63149175877 scopus 로고    scopus 로고
    • Endoplasmic reticulum protein quality control in neurodegenerative disease: The good, the bad and the therapy
    • 10.2174/092986709787458506. 19199926
    • Endoplasmic reticulum protein quality control in neurodegenerative disease: the good, the bad and the therapy. W Scheper JJ Hoozemans, Curr Med Chem 2009 16 615 626 10.2174/092986709787458506 19199926
    • (2009) Curr Med Chem , vol.16 , pp. 615-626
    • Scheper, W.1    Hoozemans, J.J.2
  • 37
    • 77952299672 scopus 로고    scopus 로고
    • DJ-1 deficient mice demonstrate similar vulnerability to pathogenic Ala53Thr human alpha-syn toxicity
    • DJ-1 deficient mice demonstrate similar vulnerability to pathogenic Ala53Thr human alpha-syn toxicity. CP Ramsey E Tsika H Ischiropoulos BI Giasson, Hum Mol Genet 19 1425 1437
    • Hum Mol Genet , vol.19 , pp. 1425-1437
    • Ramsey, C.P.1    Tsika, E.2    Ischiropoulos, H.3    Giasson, B.I.4
  • 39
    • 34250334136 scopus 로고    scopus 로고
    • Absence of dopaminergic neuronal degeneration and oxidative damage in aged DJ-1-deficient mice
    • 10.1186/1750-1326-2-10. 17535435
    • Absence of dopaminergic neuronal degeneration and oxidative damage in aged DJ-1-deficient mice. H Yamaguchi J Shen, Mol Neurodegener 2007 2 10 10.1186/1750-1326-2-10 17535435
    • (2007) Mol Neurodegener , vol.2 , pp. 10
    • Yamaguchi, H.1    Shen, J.2


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