메뉴 건너뛰기




Volumn , Issue , 2013, Pages

Endoplasmic reticulum stress and Parkinson's disease: The role of HRD1 in averting apoptosis in neurodegenerative disease

Author keywords

[No Author keywords available]

Indexed keywords

ANTIEPILEPTIC DRUGS; ENDOPLASMIC RETICULUM STRESS; NEURODEGENERATIVE DISORDERS; NEURONAL DEATH; PARKINSON'S DISEASE; RECENT PROGRESS; UBIQUITIN LIGASES; UBIQUITINATION;

EID: 84877302055     PISSN: 19420900     EISSN: 19420994     Source Type: Journal    
DOI: 10.1155/2013/239854     Document Type: Review
Times cited : (93)

References (75)
  • 2
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri K. F., Kroemer G., Organelle-specific initiation of cell death pathways. Nature Cell Biology 2001 3 E255 E263
    • (2001) Nature Cell Biology , vol.3
    • Ferri, K.F.1    Kroemer, G.2
  • 3
    • 10644233167 scopus 로고    scopus 로고
    • CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum
    • DOI 10.1101/gad.1250704
    • Marciniak S. J., Yun C. Y., Oyadomari S., Novoa I., Zhang Y., Jungreis R., Nagata K., Harding H. P., Ron D., CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum. Genes and Development 2004 18 24 3066 3077 2-s2.0-10644233167 10.1101/gad.1250704 (Pubitemid 39658175)
    • (2004) Genes and Development , vol.18 , Issue.24 , pp. 3066-3077
    • Marciniak, S.J.1    Yun, C.Y.2    Oyadomari, S.3    Novoa, I.4    Zhang, Y.5    Jungreis, R.6    Nagata, K.7    Harding, H.P.8    Ron, D.9
  • 4
    • 0035144493 scopus 로고    scopus 로고
    • Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bc12 and perturbing the cellular redox state
    • DOI 10.1128/MCB.21.4.1249-1259.2001
    • McCullough K. D., Martindale J. L., Klotz L. O., Aw T. Y., Holbrook N. J., Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bc12 and perturbing the cellular redox state. Molecular and Cellular Biology 2001 21 4 1249 1259 2-s2.0-0035144493 10.1128/MCB.21.4.1249-1259.2001 (Pubitemid 32114973)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.4 , pp. 1249-1259
    • McCullough, K.D.1    Martindale, J.L.2    Klotz, L.-O.3    Aw, T.-Y.4    Holbrook, N.J.5
  • 5
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
    • DOI 10.1038/47513
    • Nakagawa T., Zhu H., Morishima N., Li E., Xu J., Yankner B. A., Yuan J., Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid- β Nature 2000 403 6765 98 103 2-s2.0-0034610743 10.1038/47513 (Pubitemid 30038529)
    • (2000) Nature , vol.403 , Issue.6765 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 7
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding H. P., Novoa I., Zhang Y., Regulated translation initiation controls stress-induced gene expression in mammalian cells. Molecular Cell 2000 6 5 1099 1108
    • (2000) Molecular Cell , vol.6 , Issue.5 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3
  • 8
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • Haze K., Yoshida H., Yanagi H., Yura T., Mori K., Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Molecular Biology of the Cell 1999 10 11 3787 3799 2-s2.0-0032693671 (Pubitemid 29534025)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.11 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 9
    • 0033815971 scopus 로고    scopus 로고
    • ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response
    • 2-s2.0-0033815971 10.1128/MCB.20.18.6755-6767.2000
    • Yoshida H., Okada T., Haze K., Yanagi H., Yura T., Negishi M., Mori K., ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response. Molecular and Cellular Biology 2000 20 18 6755 6767 2-s2.0-0033815971 10.1128/MCB.20.18.6755-6767.2000
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.18 , pp. 6755-6767
    • Yoshida, H.1    Okada, T.2    Haze, K.3    Yanagi, H.4    Yura, T.5    Negishi, M.6    Mori, K.7
  • 10
    • 0033634641 scopus 로고    scopus 로고
    • Perk is essential for translational regulation and cell survival during the unfolded protein response
    • 2-s2.0-0033634641 10.1016/S1097-2765(00)80330-5
    • Harding H. P., Zhang Y., Bertolotti A., Zeng H., Ron D., Perk is essential for translational regulation and cell survival during the unfolded protein response. Molecular Cell 2000 5 5 897 904 2-s2.0-0033634641 10.1016/S1097-2765(00)80330-5
    • (2000) Molecular Cell , vol.5 , Issue.5 , pp. 897-904
    • Harding, H.P.1    Zhang, Y.2    Bertolotti, A.3    Zeng, H.4    Ron, D.5
  • 12
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 Regulates a Subset of Endoplasmic Reticulum Resident Chaperone Genes in the Unfolded Protein Response
    • DOI 10.1128/MCB.23.21.7448-7459.2003
    • Lee A. H., Iwakoshi N. N., Glimcher L. H., XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Molecular and Cellular Biology 2003 23 21 7448 7459 2-s2.0-0142059951 10.1128/MCB.23.21.7448-7459.2003 (Pubitemid 37271447)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.21 , pp. 7448-7459
    • Lee, A.-H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 13
    • 0031657807 scopus 로고    scopus 로고
    • The ubiquitin system
    • DOI 10.1146/annurev.biochem.67.1.425
    • Hershko A., Ciechanover A., The ubiquitin system. Annual Review of Biochemistry 1998 67 425 479 2-s2.0-0031657807 10.1146/annurev.biochem.67.1.425 (Pubitemid 28411135)
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 425-479
    • Hershko, A.1    Ciechanover, A.2
  • 14
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases
    • 2-s2.0-0034682718
    • Zheng N., Wang P., Jeffrey P. D., Pavletich N. P., Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell 2000 102 4 533 539 2-s2.0-0034682718
    • (2000) Cell , vol.102 , Issue.4 , pp. 533-539
    • Zheng, N.1    Wang, P.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 15
    • 4744374044 scopus 로고    scopus 로고
    • High ER stress in β-cells stimulates intracellular degradation of misfolded insulin
    • DOI 10.1016/j.bbrc.2004.09.035, PII S0006291X04020777
    • Allen J. R., Nguyen L. X., Sargent K. E. G., Lipson K. L., Hackett A., Urano F., High ER stress in β -cells stimulates intracellular degradation of misfolded insulin. Biochemical and Biophysical Research Communications 2004 324 1 166 170 2-s2.0-4744374044 10.1016/j.bbrc.2004.09.035 (Pubitemid 39311474)
    • (2004) Biochemical and Biophysical Research Communications , vol.324 , Issue.1 , pp. 166-170
    • Allen, J.R.1    Nguyen, L.X.2    Sargent, K.E.G.3    Lipson, K.L.4    Hackett, A.5    Urano, F.6
  • 19
    • 43049096083 scopus 로고    scopus 로고
    • Synoviolin promotes IRE1 ubiquitination and degradation in synovial fibroblasts from mice with collagen-induced arthritis
    • DOI 10.1038/embor.2008.37, PII EMBOR200837
    • Gao B., Lee S. M., Chen A., Zhang J., Zhang D. D., Kannan K., Ortmann R. A., Fang D., Synoviolin promotes IRE1 ubiquitination and degradation in synovial fibroblasts from mice with collagen-induced arthritis. EMBO Reports 2008 9 5 480 485 2-s2.0-43049096083 10.1038/embor.2008.37 (Pubitemid 351627287)
    • (2008) EMBO Reports , vol.9 , Issue.5 , pp. 480-485
    • Gao, B.1    Lee, S.-M.2    Chen, A.3    Zhang, J.4    Zhang, D.D.5    Kannan, K.6    Ortmann, R.A.7    Fang, D.8
  • 20
    • 0035967883 scopus 로고    scopus 로고
    • An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin
    • DOI 10.1016/S0092-8674(01)00407-X
    • Imai Y., Soda M., Inoue H., Hattori N., Mizuno Y., Takahashi R., An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell 2001 105 7 891 902 2-s2.0-0035967883 10.1016/S0092-8674(01)00407-X (Pubitemid 32635090)
    • (2001) Cell , vol.105 , Issue.7 , pp. 891-902
    • Imai, Y.1    Soda, M.2    Inoue, H.3    Hattori, N.4    Mizuno, Y.5    Takahashi, R.6
  • 21
    • 0035854437 scopus 로고    scopus 로고
    • Ubiquitination of a new form of α-synuclein by parkin from human brain: Implications for Parkinson's disease
    • DOI 10.1126/science.1060627
    • Shimura H., Schlossmacher M. G., Hattori N., Frosch M. P., Trockenbacher A., Schneider R., Mizuno Y., Kosik K. S., Selkoe D. J., Ubiquitination of a new form of α -synuclein by parkin from human brain: implications for Parkinson's disease. Science 2001 293 5528 263 269 2-s2.0-0035854437 10.1126/science.1060627 (Pubitemid 32694735)
    • (2001) Science , vol.293 , Issue.5528 , pp. 263-269
    • Shimura, H.1    Schlossmacher, M.G.2    Hattori, N.3    Frosch, M.P.4    Trockenbacher, A.5    Schneider, R.6    Mizuno, Y.7    Kosik, K.S.8    Selkoe, D.J.9
  • 22
    • 0038143287 scopus 로고    scopus 로고
    • Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons
    • DOI 10.1074/jbc.M211821200
    • Holtz W. A., O'Malley K. L., Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons. Journal of Biological Chemistry 2003 278 21 19367 19377 2-s2.0-0038143287 10.1074/jbc.M211821200 (Pubitemid 36799332)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.21 , pp. 19367-19377
    • Holtz, W.A.1    O'Malley, K.L.2
  • 24
    • 77949764687 scopus 로고    scopus 로고
    • Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid- β generation
    • 2-s2.0-77949764687 10.1523/JNEUROSCI.2422-09.2010
    • Kaneko M., Koike H., Saito R., Kitamura Y., Okuma Y., Nomura Y., Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid- β generation. Journal of Neuroscience 2010 30 11 3924 3932 2-s2.0-77949764687 10.1523/JNEUROSCI.2422-09.2010
    • (2010) Journal of Neuroscience , vol.30 , Issue.11 , pp. 3924-3932
    • Kaneko, M.1    Koike, H.2    Saito, R.3    Kitamura, Y.4    Okuma, Y.5    Nomura, Y.6
  • 25
    • 78650338184 scopus 로고    scopus 로고
    • The endoplasmic reticulum protein folding factory and its chaperones: New targets for drug discovery?
    • 2-s2.0-78650338184 10.1111/j.1476-5381.2010.01064.x
    • McLaughlin M., Vandenbroeck K., The endoplasmic reticulum protein folding factory and its chaperones: new targets for drug discovery? British Journal of Pharmacology 2011 162 2 328 345 2-s2.0-78650338184 10.1111/j.1476-5381.2010. 01064.x
    • (2011) British Journal of Pharmacology , vol.162 , Issue.2 , pp. 328-345
    • McLaughlin, M.1    Vandenbroeck, K.2
  • 26
    • 84856448928 scopus 로고    scopus 로고
    • Therapeutic targeting of the endoplasmic reticulum in Alzheimer's disease
    • Chadwick W., Mitchell N., Martin B., Maudsley S., Therapeutic targeting of the endoplasmic reticulum in Alzheimer's disease. Current Alzheimer Research 2012 9 1 110 119
    • (2012) Current Alzheimer Research , vol.9 , Issue.1 , pp. 110-119
    • Chadwick, W.1    Mitchell, N.2    Martin, B.3    Maudsley, S.4
  • 27
    • 84857539039 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and insulin resistance post-trauma: Similarities to type 2 diabetes
    • Jeschke M. G., Boehning D., Endoplasmic reticulum stress and insulin resistance post-trauma: similarities to type 2 diabetes. Journal of Cellular and Molecular Medicine 2012 16 3 437 444
    • (2012) Journal of Cellular and Molecular Medicine , vol.16 , Issue.3 , pp. 437-444
    • Jeschke, M.G.1    Boehning, D.2
  • 28
    • 0023769965 scopus 로고
    • Dementia, parkinsonism, and motor neuron disease: Neurochemical and neuropathological correlates
    • DOI 10.1002/ana.410240518
    • Gilbert J. J., Kish S. J., Chang L. J., Dementia, parkinsonism, and motor neuron disease: neurochemical and neuropathological correlates. Annals of Neurology 1988 24 5 688 691 (Pubitemid 18262675)
    • (1988) Annals of Neurology , vol.24 , Issue.5 , pp. 688-691
    • Gilbert, J.J.1    Kish, S.J.2    Chang, L.-J.3    Morito, C.4    Shannak, K.5    Hornykiewicz, O.6
  • 29
    • 0032816549 scopus 로고    scopus 로고
    • The substantia nigra of the human brain: II. Patterns of loss of dopamine-containing neurons in Parkinson's disease
    • DOI 10.1093/brain/122.8.1437
    • Damier P., Hirsch E. C., Agid Y., Graybiel A. M., The substantia nigra of the human brain: II. Patterns of loss of dopamine-containing neurons in Parkinson's disease. Brain 1999 122 8 1437 1448 2-s2.0-0032816549 10.1093/brain/122.8.1437 (Pubitemid 29374122)
    • (1999) Brain , vol.122 , Issue.8 , pp. 1437-1448
    • Damier, P.1    Hirsch, E.C.2    Agid, Y.3    Graybiel, A.M.4
  • 30
    • 63149090431 scopus 로고    scopus 로고
    • Parkinson's disease: From monogenic forms to genetic susceptibility factors
    • 2-s2.0-63149090431 10.1093/hmg/ddp012
    • Lesage S., Brice A., Parkinson's disease: from monogenic forms to genetic susceptibility factors. Human Molecular Genetics 2009 18 1 R48 R59 2-s2.0-63149090431 10.1093/hmg/ddp012
    • (2009) Human Molecular Genetics , vol.18 , Issue.1
    • Lesage, S.1    Brice, A.2
  • 31
    • 77953458926 scopus 로고    scopus 로고
    • Clinical implications of gene discovery in Parkinson's disease and parkinsonism
    • 2-s2.0-77953458926 10.1002/mds.22723
    • Wider C., Foroud T., Wszolek Z. K., Clinical implications of gene discovery in Parkinson's disease and parkinsonism. Movement Disorders 2010 25 1 S15 S20 2-s2.0-77953458926 10.1002/mds.22723
    • (2010) Movement Disorders , vol.25 , Issue.1
    • Wider, C.1    Foroud, T.2    Wszolek, Z.K.3
  • 32
    • 70549084415 scopus 로고    scopus 로고
    • Genome-wide association study identifies common variants at four loci as genetic risk factors for Parkinson's disease
    • Satake W., Nakabayashi Y., Mizuta I., Genome-wide association study identifies common variants at four loci as genetic risk factors for Parkinson's disease. Nature Genetics 2009 41 12 1303 1307
    • (2009) Nature Genetics , vol.41 , Issue.12 , pp. 1303-1307
    • Satake, W.1    Nakabayashi, Y.2    Mizuta, I.3
  • 33
    • 70549088602 scopus 로고    scopus 로고
    • Genome-wide association study reveals genetic risk underlying Parkinson's disease
    • Simon-Sanchez J., Schulte C., Bras J. M., Genome-wide association study reveals genetic risk underlying Parkinson's disease. Nature Genetics 2009 41 12 1308 1312
    • (2009) Nature Genetics , vol.41 , Issue.12 , pp. 1308-1312
    • Simon-Sanchez, J.1    Schulte, C.2    Bras, J.M.3
  • 34
    • 0034680913 scopus 로고    scopus 로고
    • Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity
    • 2-s2.0-0034680913 10.1074/jbc.C000447200
    • Imai Y., Soda M., Takahashi R., Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. Journal of Biological Chemistry 2000 275 46 35661 35664 2-s2.0-0034680913 10.1074/jbc.C000447200
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.46 , pp. 35661-35664
    • Imai, Y.1    Soda, M.2    Takahashi, R.3
  • 35
    • 67650164931 scopus 로고    scopus 로고
    • Regulation of LRRK2 stability by the E3 ubiquitin ligase CHIP
    • 2-s2.0-67650164931 10.1371/journal.pone.0005949 e5949
    • Ding X., Goldberg M. S., Regulation of LRRK2 stability by the E3 ubiquitin ligase CHIP. PLoS ONE 2009 4 6 2-s2.0-67650164931 10.1371/journal. pone.0005949 e5949
    • (2009) PLoS ONE , vol.4 , Issue.6
    • Ding, X.1    Goldberg, M.S.2
  • 38
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
    • DOI 10.1038/33416
    • Kitada T., Asakawa S., Hattori N., Matsumine H., Yamamura Y., Minoshima S., Yokochi M., Mizuno Y., Shimizu N., Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 1998 392 6676 605 608 2-s2.0-0032499264 10.1038/33416 (Pubitemid 28207717)
    • (1998) Nature , vol.392 , Issue.6676 , pp. 605-608
    • Kitada, T.1    Asakawa, S.2    Hattori, N.3    Matsumine, H.4    Yamamura, Y.5    Minoshima, S.6    Yokochi, M.7    Mizuno, Y.8    Shimizu, N.9
  • 39
    • 0031848638 scopus 로고    scopus 로고
    • Neurochemical and neurogenetic correlates of Parkinson's disease
    • Mizuno Y., Hattori N., Matsumine H., Neurochemical and neurogenetic correlates of Parkinson's disease. Journal of Neurochemistry 1998 71 3 893 902 2-s2.0-0031848638 (Pubitemid 28390243)
    • (1998) Journal of Neurochemistry , vol.71 , Issue.3 , pp. 893-902
    • Mizuno, Y.1    Hattori, N.2    Matsumine, H.3
  • 44
    • 51849134081 scopus 로고    scopus 로고
    • Pael-R transgenic mice crossed with parkin deficient mice displayed progressive and selective catecholaminergic neuronal loss
    • 2-s2.0-51849134081 10.1111/j.1471-4159.2008.05607.x
    • Wang H. Q., Imai Y., Inoue H., Kataoka A., Iita S., Nukina N., Takahashi R., Pael-R transgenic mice crossed with parkin deficient mice displayed progressive and selective catecholaminergic neuronal loss. Journal of Neurochemistry 2008 107 1 171 185 2-s2.0-51849134081 10.1111/j.1471-4159.2008. 05607.x
    • (2008) Journal of Neurochemistry , vol.107 , Issue.1 , pp. 171-185
    • Wang, H.Q.1    Imai, Y.2    Inoue, H.3    Kataoka, A.4    Iita, S.5    Nukina, N.6    Takahashi, R.7
  • 45
    • 55749090654 scopus 로고    scopus 로고
    • The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila
    • 2-s2.0-55749090654 10.1073/pnas.0803998105
    • Deng H., Dodson M. W., Huang H., Guo M., The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila. Proceedings of the National Academy of Sciences of the United States of America 2008 105 38 14503 14508 2-s2.0-55749090654 10.1073/pnas.0803998105
    • (2008) Proceedings of the National Academy of Sciences of the United States of America , vol.105 , Issue.38 , pp. 14503-14508
    • Deng, H.1    Dodson, M.W.2    Huang, H.3    Guo, M.4
  • 48
    • 84866072587 scopus 로고    scopus 로고
    • PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria
    • 1016
    • Okatsu K., Oka T., Iguchi M., PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria. Nature Communications 2012 3 1016
    • (2012) Nature Communications , vol.3
    • Okatsu, K.1    Oka, T.2    Iguchi, M.3
  • 49
    • 0037021416 scopus 로고    scopus 로고
    • Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation
    • DOI 10.1016/S0014-5793(02)03660-8, PII S0014579302036608
    • Kaneko M., Ishiguro M., Niinuma Y., Uesugi M., Nomura Y., Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation. FEBS Letters 2002 532 1-2 147 152 2-s2.0-0037021416 10.1016/S0014-5793(02)03660- 8 (Pubitemid 35375880)
    • (2002) FEBS Letters , vol.532 , Issue.1-2 , pp. 147-152
    • Kaneko, M.1    Ishiguro, M.2    Niinuma, Y.3    Uesugi, M.4    Nomura, Y.5
  • 50
    • 33746208871 scopus 로고    scopus 로고
    • A Luminal Surveillance Complex that Selects Misfolded Glycoproteins for ER-Associated Degradation
    • DOI 10.1016/j.cell.2006.05.045, PII S0092867406008610
    • Denic V., Quan E. M., Weissman J. S., A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Cell 2006 126 2 349 359 2-s2.0-33746208871 10.1016/j.cell.2006.05.045 (Pubitemid 44092967)
    • (2006) Cell , vol.126 , Issue.2 , pp. 349-359
    • Denic, V.1    Quan, E.M.2    Weissman, J.S.3
  • 51
    • 78149482323 scopus 로고    scopus 로고
    • Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase hrd1p
    • 2-s2.0-78149482323 10.1016/j.cell.2010.10.028
    • Carvalho P., Stanley A. M., Rapoport T. A., Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase hrd1p. Cell 2010 143 4 579 591 2-s2.0-78149482323 10.1016/j.cell.2010.10.028
    • (2010) Cell , vol.143 , Issue.4 , pp. 579-591
    • Carvalho, P.1    Stanley, A.M.2    Rapoport, T.A.3
  • 52
    • 0035815754 scopus 로고    scopus 로고
    • Membrane Topology and Function of Der3/Hrd1p as a Ubiquitin-Protein Ligase (E3) Involved in Endoplasmic Reticulum Degradation
    • DOI 10.1074/jbc.M008608200
    • Deak P. M., Wolf D. H., Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation. Journal of Biological Chemistry 2001 276 14 10663 10669 2-s2.0-0035815754 10.1074/jbc.M008608200 (Pubitemid 38089236)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.14 , pp. 10663-10669
    • Deak, P.M.1    Wolf, D.H.2
  • 53
    • 0242321271 scopus 로고    scopus 로고
    • ER signaling in unfolded protein response
    • DOI 10.1016/j.lfs.2003.09.007
    • Kaneko M., Nomura Y., ER signaling in unfolded protein response. Life Sciences 2003 74 2-3 199 205 (Pubitemid 37357051)
    • (2003) Life Sciences , vol.74 , Issue.2-3 , pp. 199-205
    • Kaneko, M.1    Nomura, Y.2
  • 54
    • 40249088336 scopus 로고    scopus 로고
    • OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1?SEL1L ubiquitin ligase complex for ERAD
    • DOI 10.1038/ncb1689, PII NCB1689
    • Christianson J. C., Shaler T. A., Tyler R. E., Kopito R. R., OS-9 and GRP94 deliver mutant α 1-antitrypsin to the Hrd1?SEL1L ubiquitin ligase complex for ERAD. Nature Cell Biology 2008 10 3 272 282 2-s2.0-40249088336 10.1038/ncb1689 (Pubitemid 351331014)
    • (2008) Nature Cell Biology , vol.10 , Issue.3 , pp. 272-282
    • Christianson, J.C.1    Shaler, T.A.2    Tyler, R.E.3    Kopito, R.R.4
  • 55
  • 57
    • 0035958015 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro
    • Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O., Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Research 2001 8 2 85 95 2-s2.0-0035958015 (Pubitemid 33617355)
    • (2001) DNA Research , vol.8 , Issue.2 , pp. 85-95
    • Nagase, T.1    Nakayama, M.2    Nakajima, D.3    Kikuno, R.4    Ohara, O.5
  • 58
    • 14244268370 scopus 로고    scopus 로고
    • Pathogenesis of prion diseases
    • DOI 10.1007/s00401-004-0953-9
    • Unterberger U., Voigtländer T., Budka H., Pathogenesis of prion diseases. Acta Neuropathologica 2005 109 1 32 48 2-s2.0-14244268370 10.1007/s00401-004-0953-9 (Pubitemid 40287788)
    • (2005) Acta Neuropathologica , vol.109 , Issue.1 , pp. 32-48
    • Unterberger, U.1    Voigtlander, T.2    Budka, H.3
  • 60
    • 79955085928 scopus 로고    scopus 로고
    • Movement disorders in spinocerebellar ataxias
    • 2-s2.0-79955085928 10.1002/mds.23584
    • van Gaalen J., Giunti P., van de Warrenburg B. P., Movement disorders in spinocerebellar ataxias. Movement Disorders 2011 26 5 792 800 2-s2.0-79955085928 10.1002/mds.23584
    • (2011) Movement Disorders , vol.26 , Issue.5 , pp. 792-800
    • Van Gaalen, J.1    Giunti, P.2    Van De Warrenburg, B.P.3
  • 61
    • 41549116799 scopus 로고    scopus 로고
    • Novel functions of ubiquitin ligase HRD1 with transmembrane and proline-rich domains
    • DOI 10.1254/jphs.08005FP
    • Omura T., Kaneko M., Onoguchi M., Koizumi S., Itami M., Ueyama M., Okuma Y., Nomura Y., Novel functions of ubiquitin ligase HRD1 with transmembrane and proline-rich domains. Journal of Pharmacological Sciences 2008 106 3 512 519 2-s2.0-41549116799 10.1254/jphs.08005FP (Pubitemid 351468605)
    • (2008) Journal of Pharmacological Sciences , vol.106 , Issue.3 , pp. 512-519
    • Omura, T.1    Kaneko, M.2    Onoguchi, M.3    Koizumi, S.4    Itami, M.5    Ueyama, M.6    Okuma, Y.7    Nomura, Y.8
  • 62
    • 77949751415 scopus 로고    scopus 로고
    • Wolfram syndrome 1 gene negatively regulates ER stress signaling in rodent and human cells
    • Fonseca S. G., Ishigaki S., Oslowski C. M., Wolfram syndrome 1 gene negatively regulates ER stress signaling in rodent and human cells. Journal of Clinical Investigation 2010 120 3 744 755
    • (2010) Journal of Clinical Investigation , vol.120 , Issue.3 , pp. 744-755
    • Fonseca, S.G.1    Ishigaki, S.2    Oslowski, C.M.3
  • 64
    • 77957316569 scopus 로고    scopus 로고
    • Restoring endoplasmic reticulum function by chemical chaperones: An emerging therapeutic approach for metabolic diseases
    • supplement 2 2-s2.0-77957316569 10.1111/j.1463-1326.2010.01282.x
    • Engin F., Hotamisligil G. S., Restoring endoplasmic reticulum function by chemical chaperones: an emerging therapeutic approach for metabolic diseases. Diabetes, Obesity and Metabolism 2010 12 supplement 2 108 115 2-s2.0-77957316569 10.1111/j.1463-1326.2010.01282.x
    • (2010) Diabetes, Obesity and Metabolism , vol.12 , pp. 108-115
    • Engin, F.1    Hotamisligil, G.S.2
  • 65
    • 78751550063 scopus 로고    scopus 로고
    • Chemical and pharmacological chaperones|application for recombinant protein production and protein folding diseases
    • 2-s2.0-78751550063 10.2174/092986711793979698
    • Rajan R. S., Tsumoto K., Tokunaga M., Tokunaga H., Kita Y., Arakawa T., Chemical and pharmacological chaperones|application for recombinant protein production and protein folding diseases. Current Medicinal Chemistry 2011 18 1 1 15 2-s2.0-78751550063 10.2174/092986711793979698
    • (2011) Current Medicinal Chemistry , vol.18 , Issue.1 , pp. 1-15
    • Rajan, R.S.1    Tsumoto, K.2    Tokunaga, M.3    Tokunaga, H.4    Kita, Y.5    Arakawa, T.6
  • 66
    • 33646581674 scopus 로고    scopus 로고
    • Suppressive effects of 4-phenylbutyrate on the aggregation of Pael receptors and endoplasmic reticulum stress
    • DOI 10.1111/j.1471-4159.2006.03782.x
    • Kubota K., Niinuma Y., Kaneko M., Okuma Y., Sugai M., Omura T., Uesugi M., Uehara T., Hosoi T., Nomura Y., Suppressive effects of 4-phenylbutyrate on the aggregation of Pael receptors and endoplasmic reticulum stress. Journal of Neurochemistry 2006 97 5 1259 1268 2-s2.0-33646581674 10.1111/j.1471-4159.2006. 03782.x (Pubitemid 43725566)
    • (2006) Journal of Neurochemistry , vol.97 , Issue.5 , pp. 1259-1268
    • Kubota, K.1    Niinuma, Y.2    Kaneko, M.3    Okuma, Y.4    Sugai, M.5    Omura, T.6    Uesugi, M.7    Uehara, T.8    Hosoi, T.9    Nomura, Y.10
  • 67
    • 84855708250 scopus 로고    scopus 로고
    • Protective effects of 4-phenylbutyrate derivatives on the neuronal cell death and endoplasmic reticulum stress
    • Mimori S., Okuma Y., Kaneko M., Protective effects of 4-phenylbutyrate derivatives on the neuronal cell death and endoplasmic reticulum stress. Biological and Pharmaceutical Bulletin 2012 35 1 84 90
    • (2012) Biological and Pharmaceutical Bulletin , vol.35 , Issue.1 , pp. 84-90
    • Mimori, S.1    Okuma, Y.2    Kaneko, M.3
  • 68
    • 70350150325 scopus 로고    scopus 로고
    • A chemical chaperone, sodium 4-phenylbutyric acid, attenuates the pathogenic potency in human α -synuclein A30P + A53T transgenic mice
    • 2-s2.0-70350150325 10.1016/j.parkreldis.2009.03.002
    • Ono K., Ikemoto M., Kawarabayashi T., Ikeda M., Nishinakagawa T., Hosokawa M., Shoji M., Takahashi M., Nakashima M., A chemical chaperone, sodium 4-phenylbutyric acid, attenuates the pathogenic potency in human α -synuclein A30P + A53T transgenic mice. Parkinsonism and Related Disorders 2009 15 9 649 654 2-s2.0-70350150325 10.1016/j.parkreldis.2009.03.002
    • (2009) Parkinsonism and Related Disorders , vol.15 , Issue.9 , pp. 649-654
    • Ono, K.1    Ikemoto, M.2    Kawarabayashi, T.3    Ikeda, M.4    Nishinakagawa, T.5    Hosokawa, M.6    Shoji, M.7    Takahashi, M.8    Nakashima, M.9
  • 69
    • 80053586271 scopus 로고    scopus 로고
    • Long-term phenylbutyrate administration prevents memory deficits in Tg2576 mice by decreasing Abeta
    • Ricobaraza A., Cuadrado-Tejedor M., Garcia-Osta A., Long-term phenylbutyrate administration prevents memory deficits in Tg2576 mice by decreasing Abeta. Frontiers in Bioscience (Elite Edition) 2011 3 1375 1384
    • (2011) Frontiers in Bioscience (Elite Edition) , vol.3 , pp. 1375-1384
    • Ricobaraza, A.1    Cuadrado-Tejedor, M.2    Garcia-Osta, A.3
  • 70
    • 84859158190 scopus 로고    scopus 로고
    • HRD1 levels increased by zonisamide prevented cell death and caspase-3 activation caused by endoplasmic reticulum stress in SH-SY5Y cells
    • Omura T., Asari M., Yamamoto J., HRD1 levels increased by zonisamide prevented cell death and caspase-3 activation caused by endoplasmic reticulum stress in SH-SY5Y cells. Journal of Molecular Neuroscience 2012 46 3 527 535
    • (2012) Journal of Molecular Neuroscience , vol.46 , Issue.3 , pp. 527-535
    • Omura, T.1    Asari, M.2    Yamamoto, J.3
  • 71
    • 0035656346 scopus 로고    scopus 로고
    • Zonisamide has beneficial effects on Parkinson's disease patients
    • PII S016801020100298X
    • Murata M., Horiuchi E., Kanazawa I., Zonisamide has beneficial effects on Parkinson's disease patients. Neuroscience Research 2001 41 4 397 399 2-s2.0-0035656346 (Pubitemid 33733759)
    • (2001) Neuroscience Research , vol.41 , Issue.4 , pp. 397-399
    • Murata, M.1    Horiuchi, E.2    Kanazawa, I.3
  • 73
    • 33645755812 scopus 로고    scopus 로고
    • The Parkinson's complex: Parkinsonism is just the tip of the Iceberg
    • 2-s2.0-33645755812 10.1002/ana.20834
    • Langston J. W., The Parkinson's complex: Parkinsonism is just the tip of the Iceberg. Annals of Neurology 2006 59 4 591 596 2-s2.0-33645755812 10.1002/ana.20834
    • (2006) Annals of Neurology , vol.59 , Issue.4 , pp. 591-596
    • Langston, J.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.