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Volumn 120, Issue 4, 2012, Pages 477-494

Hsp70.1 and related lysosomal factors for necrotic neuronal death

Author keywords

calpain cathepsin hypothesis; Hsp70; hydroxynonenal; lysosome; neuronal death; Niemann Pick disease

Indexed keywords

4 HYDROXYNONENAL; APOLIPOPROTEIN E; ARACHIDONIC ACID; BONE MORPHOGENETIC PROTEIN; CALPAIN 1; CATHEPSIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 72; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LINOLEIC ACID; NEUROTOXIN; REACTIVE OXYGEN METABOLITE; SPHINGOMYELIN; SPHINGOMYELIN PHOSPHODIESTERASE;

EID: 84855946896     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2011.07596.x     Document Type: Review
Times cited : (76)

References (159)
  • 1
    • 0019723109 scopus 로고
    • Tricyclic antidepressants induce sphingomyelinase deficiency in fibroblast and neuroblastoma cell cultures
    • Albouz S., et al. (1981) Tricyclic antidepressants induce sphingomyelinase deficiency in fibroblast and neuroblastoma cell cultures. Biomedicine 35, 218-220. (Pubitemid 12050793)
    • (1981) Biomedicine , vol.35 , Issue.7-8 , pp. 218-220
    • Albouz, S.1    Hauw, J.J.2    Berwald-Netter, Y.3
  • 2
    • 0029953488 scopus 로고    scopus 로고
    • Transacylase and phospholipases in the synthesis of bis(monoacylglycero) phosphate
    • DOI 10.1021/bi961164o
    • Amidon B., Brown A., and, Waite M., (1996) Transacylase and phospholipases in the synthesis of bis(monoacylglycero)phosphate. Biochemistry 35, 13995-14002. (Pubitemid 26374471)
    • (1996) Biochemistry , vol.35 , Issue.44 , pp. 13995-14002
    • Amidon, B.1    Brown, A.2    Waite, M.3
  • 3
    • 33646081999 scopus 로고    scopus 로고
    • Lysosomal biogenesis and function is critical for necrotic cell death in Caenorhabditis elegans
    • Artal-Sanz M., et al. (2006) Lysosomal biogenesis and function is critical for necrotic cell death in Caenorhabditis elegans. J. Cell Biol. 173, 231-239.
    • (2006) J. Cell Biol. , vol.173 , pp. 231-239
    • Artal-Sanz, M.1
  • 4
    • 0036570159 scopus 로고    scopus 로고
    • Oxidatively modified proteins in aging and disease
    • DOI 10.1016/S0891-5849(02)00780-3, PII S0891584902007803
    • Beal M. F., (2002) Oxidatively modified proteins in aging and disease. Free Radic. Biol. Med. 32, 797-803. (Pubitemid 34439250)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.9 , pp. 797-803
    • Beal M.Flint1
  • 5
    • 36849088609 scopus 로고    scopus 로고
    • Growth Arrest and Autophagy Are Required for Salivary Gland Cell Degradation in Drosophila
    • DOI 10.1016/j.cell.2007.10.048, PII S009286740701402X
    • Berry D. L., and, Baehrecke E. H., (2007) Growth arrest and autophagy are required for salivary gland cell degradation in Drosophila. Cell 131, 1137-1148. (Pubitemid 350235023)
    • (2007) Cell , vol.131 , Issue.6 , pp. 1137-1148
    • Berry, D.L.1    Baehrecke, E.H.2
  • 6
    • 41149174763 scopus 로고    scopus 로고
    • Mechanistic role of calpains in postischemic neurodegeneration
    • DOI 10.1038/sj.jcbfm.9600595, PII 9600595
    • Bevers M. B., and, Neumar R. W., (2008) Mechanistic role of calpains in postischemic neurodegeneration. J. Cereb. Blood Flow Metab. 28, 655-673. (Pubitemid 351432797)
    • (2008) Journal of Cerebral Blood Flow and Metabolism , vol.28 , Issue.4 , pp. 655-673
    • Bevers, M.B.1    Neumar, R.W.2
  • 7
    • 34047097917 scopus 로고    scopus 로고
    • Hsp70 protects against UVB induced apoptosis by preventing release of cathepsins and cytochrome c in human melanocytes
    • DOI 10.1093/carcin/bgl152
    • Bivik C., Rosdahl I., and, Öllinger K., (2007) Hsp70 protects against UVB induced apoptosis by preventing release of cathepsins and cytochrome c in human melanocytes. Carcinogenesis 28, 537-544. (Pubitemid 46523349)
    • (2007) Carcinogenesis , vol.28 , Issue.3 , pp. 537-544
    • Bivik, C.1    Rosdahl, I.2    Ollinger, K.3
  • 9
    • 54949137644 scopus 로고    scopus 로고
    • Lysosomal membrane permeabilization in cell death
    • Boya P., and, Kroemer G., (2008) Lysosomal membrane permeabilization in cell death. Oncogene 27, 6434-6451.
    • (2008) Oncogene , vol.27 , pp. 6434-6451
    • Boya, P.1    Kroemer, G.2
  • 11
    • 0016121227 scopus 로고
    • Novel stereoconfiguration in lyso-bis-phosphatidic acid of cultured BHK-cells
    • Brotherus J., et al. (1974) Novel stereoconfiguration in lyso-bis-phosphatidic acid of cultured BHK-cells. Chem. Phys. Lipids 13, 178-182.
    • (1974) Chem. Phys. Lipids , vol.13 , pp. 178-182
    • Brotherus, J.1
  • 12
    • 0032988381 scopus 로고    scopus 로고
    • Oxidative stress, growth factor starvation and Fas activation may all cause apoptosis through lysosomal leak
    • Brunk U. T., and, Svensson I., (1999) Oxidative stress, growth factor starvation and Fas activation may all cause apoptosis through lysosomal leak. Redox Rep. 4, 3-11. (Pubitemid 29296774)
    • (1999) Redox Report , vol.4 , Issue.1-2 , pp. 3-11
    • Brunk, U.T.1    Svensson, I.2
  • 13
    • 0030757986 scopus 로고    scopus 로고
    • Photo-oxidative disruption of lysosomal membranes causes apoptosis of cultured human fibroblasts
    • DOI 10.1016/S0891-5849(97)00007-5, PII S0891584997000075
    • Brunk U. T., et al. (1997) Photooxidative disruption of lysosomal membranes causes apoptosis of cultured human fibroblasts. Free Radic. Biol. Med. 23, 616-626. (Pubitemid 27287345)
    • (1997) Free Radical Biology and Medicine , vol.23 , Issue.4 , pp. 616-626
    • Brunk, U.T.1    Dalen, H.2    Roberg, K.3    Hellquist, H.B.4
  • 14
    • 0034983544 scopus 로고    scopus 로고
    • Lysosomal involvement in apoptosis
    • DOI 10.1179/135100001101536094
    • Brunk U. T., Neuzil J., and, Eaton J. W., (2001) Lysosomal involvement in apoptosis. Redox Rep. 6, 91-97. (Pubitemid 32519816)
    • (2001) Redox Report , vol.6 , Issue.2 , pp. 91-97
    • Brunk, U.T.1    Neuzil, J.2    Eaton, J.W.3
  • 15
    • 0036591849 scopus 로고    scopus 로고
    • Lipid peroxidation and protein oxidation in Alzheimer's disease brain: Potential causes and consequences involving amyloid β-peptide-associated free radical oxidative stress
    • DOI 10.1016/S0891-5849(02)00794-3, PII S0891584902007943
    • Butterfield D. A., and, Lauderback C. M., (2002) Lipid peroxidation and protein oxidation in Alzheimer's disease brain: potential causes and consequences involving amyloid ß-peptide-associated free radical oxidative stress. Free Radic. Biol. Med. 32, 1050-1060. (Pubitemid 34603342)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.11 , pp. 1050-1060
    • Butterfield D.Allan1    Lauderback, C.M.2
  • 16
    • 0035194145 scopus 로고    scopus 로고
    • Evidence of oxidative damage in Alzheimer's disease brain: Central role for amyloid β-peptide
    • DOI 10.1016/S1471-4914(01)02173-6, PII S1471491401021736
    • Butterfield D. A., et al. (2001) Evidence of oxidative damage in Alzheimer's disease brain: central role for amyloid ß-peptide. Trends Mol. Med. 7, 548-554. (Pubitemid 33127140)
    • (2001) Trends in Molecular Medicine , vol.7 , Issue.12 , pp. 548-554
    • Butterfield, D.A.1    Drake, J.2    Pocernich, C.3    Castegna, A.4
  • 18
    • 0035242357 scopus 로고    scopus 로고
    • The effect of mutating arginine-469 on the substrate binding and refolding activities of 70-kDa heat shock cognate protein
    • Chang T. C., et al. (2001) The effect of mutating arginine-469 on the substrate binding and refolding activities of 70-kDa heat shock cognate protein. Arch. Biochem. Biophys. 386, 30-36.
    • (2001) Arch. Biochem. Biophys. , vol.386 , pp. 30-36
    • Chang, T.C.1
  • 19
    • 0024975155 scopus 로고
    • A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins
    • Chiang H. L., et al. (1989) A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science 246, 382-385.
    • (1989) Science , vol.246 , pp. 382-385
    • Chiang, H.L.1
  • 20
    • 33344457969 scopus 로고    scopus 로고
    • Cathepsin-regulated apoptosis
    • DOI 10.1007/s10495-006-3486-y
    • Chwieralski C. E., Welte T., and, Bühling F., (2006) Cathepsin-regulated apoptosis. Apoptosis 11, 143-149. (Pubitemid 43291015)
    • (2006) Apoptosis , vol.11 , Issue.2 , pp. 143-149
    • Chwieralski, C.E.1    Welte, T.2    Buhling, F.3
  • 22
    • 0031005724 scopus 로고    scopus 로고
    • Global ischemia activates nuclear factor-kappa B in forebrain neurons of rats
    • discussion 1080-1071.
    • Clemens J. A., Stephenson D. T., Smalstig E. B., Dixon E. P., and, Little S. P., (1997) Global ischemia activates nuclear factor-kappa B in forebrain neurons of rats. Stroke 28, 1073-1080, discussion 1080-1071.
    • (1997) Stroke , vol.28 , pp. 1073-1080
    • Clemens, J.A.1    Stephenson, D.T.2    Smalstig, E.B.3    Dixon, E.P.4    Little, S.P.5
  • 23
    • 0031883733 scopus 로고    scopus 로고
    • Lysosomes, a meeting point of proteins, chaperones, and proteases
    • Cuervo A. M., and, Dice J. F., (1998) Lysosomes, a meeting point of proteins, chaperons, and proteases. J. Mol. Med. 76, 6-12. (Pubitemid 28085056)
    • (1998) Journal of Molecular Medicine , vol.76 , Issue.1 , pp. 6-12
    • Cuervo, A.M.1    Dice, J.F.2
  • 24
    • 34447528828 scopus 로고    scopus 로고
    • The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions
    • DOI 10.1016/j.febslet.2007.05.039, PII S0014579307005674, Cellular Stress
    • Daugaard M., Rohde M., and, Jäättelä M., (2007) The heat shock protein 70 family: highly homologous proteins with overlapping and distinct functions. FEBS Lett. 581, 3702-3710. (Pubitemid 47081009)
    • (2007) FEBS Letters , vol.581 , Issue.19 , pp. 3702-3710
    • Daugaard, M.1    Rohde, M.2    Jaattela, M.3
  • 25
    • 33646558596 scopus 로고    scopus 로고
    • NF-κB protects neurons from ischemic injury after middle cerebral artery occlusion in mice
    • DOI 10.1016/j.brainres.2006.02.103, PII S0006899306005233
    • Duckworth E. A. M., et al. (2006) NF-κB protects neurons from ischemic injury after middle cerebral artery occlusion in mice. Brain Res. 1088, 167-175. (Pubitemid 43729410)
    • (2006) Brain Research , vol.1088 , Issue.1 , pp. 167-175
    • Duckworth, E.A.M.1    Butler, T.2    Collier, L.3    Collier, S.4    Pennypacker, K.R.5
  • 26
    • 67650376373 scopus 로고    scopus 로고
    • Oxidized proteins: Mechanisms of removal and consequences of accumulation
    • Dunlop R. A., Brunk U. T., and, Rodgers K. J., (2009) Oxidized proteins: mechanisms of removal and consequences of accumulation. IUBMB Life 61, 522-527.
    • (2009) IUBMB Life , vol.61 , pp. 522-527
    • Dunlop, R.A.1    Brunk, U.T.2    Rodgers, K.J.3
  • 27
    • 0025363276 scopus 로고
    • Studies on the mechanisms of autophagy: Formation of the autophagic vacuole
    • Dunn Jr W. A., (1990a) Studies on the mechanisms of autophagy: formation of the autophagic vacuole. J. Cell Biol. 110, 1923-1933.
    • (1990) J. Cell Biol. , vol.110 , pp. 1923-1933
    • Dunn, Jr.W.A.1
  • 28
    • 0025340880 scopus 로고
    • Studies on the mechanisms of autophagy: Maturation of the autophagic vacuole
    • Dunn Jr W. A., (1990b) Studies on the mechanisms of autophagy: maturation of the autophagic vacuole. J. Cell Biol. 110, 1935-1945.
    • (1990) J. Cell Biol. , vol.110 , pp. 1935-1945
    • Dunn, Jr.W.A.1
  • 29
    • 33750475618 scopus 로고    scopus 로고
    • Current insights into the regulation of programmed cell death by NF-κB
    • DOI 10.1038/sj.onc.1209938, PII 1209938
    • Dutta J., Fan Y., Gupta N., Fan G., and, Gelinas C., (2006) Current insights into the regulation of programmed cell death by NF-kappaB. Oncogene 25, 6800-6816. (Pubitemid 44657853)
    • (2006) Oncogene , vol.25 , Issue.51 , pp. 6800-6816
    • Dutta, J.1    Fan, Y.2    Gupta, N.3    Fan, G.4    Gelinas, C.5
  • 30
    • 0002850020 scopus 로고
    • Lysosomes, a new group of cytoplasmic particles
    • in (Hayashi T. ed.), The Ronald Press Co. New York.
    • de Duve C., (1959) Lysosomes, a new group of cytoplasmic particles, in Subcellular Particles (, Hayashi T., ed.), pp. 128-159. The Ronald Press Co., New York.
    • (1959) Subcellular Particles , pp. 128-159
    • De Duve, C.1
  • 31
    • 77049229661 scopus 로고
    • Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue
    • de Duve C., et al. (1955) Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue. Biochem. J. 60, 604-617.
    • (1955) Biochem. J. , vol.60 , pp. 604-617
    • De Duve, C.1
  • 33
    • 0023668329 scopus 로고
    • Proteins as molecular chaperones
    • Ellis J., (1987) Proteins as molecular chaperones. Nature 328, 378-379.
    • (1987) Nature , vol.328 , pp. 378-379
    • Ellis, J.1
  • 35
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer H., Schaur R. J., and, Zollner H., (1991) Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic. Biol. Med. 11, 81-128. (Pubitemid 121003917)
    • (1991) Free Radical Biology and Medicine , vol.11 , Issue.1 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 36
    • 0029051966 scopus 로고
    • Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1
    • Freeman B. C., Myers M. P., Schumacher R., and, Morimoto R. I., (1995) Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. EMBO J. 14, 2281-2292.
    • (1995) EMBO J. , vol.14 , pp. 2281-2292
    • Freeman, B.C.1    Myers, M.P.2    Schumacher, R.3    Morimoto, R.I.4
  • 37
    • 67649460932 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in neuronal injury
    • Galluzzi L., Blomgren K., and, Kroemer G., (2009) Mitochondrial membrane permeabilization in neuronal injury. Nature Rev. Neurosci. 10, 481-494.
    • (2009) Nature Rev. Neurosci. , vol.10 , pp. 481-494
    • Galluzzi, L.1    Blomgren, K.2    Kroemer, G.3
  • 38
    • 0028962656 scopus 로고
    • Lysosomal storage diseases
    • Gieselmann V., (1995) Lysosomal storage diseases. Biochem. Biophys. Acta 1270, 103-136.
    • (1995) Biochem. Biophys. Acta , vol.1270 , pp. 103-136
    • Gieselmann, V.1
  • 39
    • 48849109369 scopus 로고    scopus 로고
    • Regulation of apoptotic and inflammatory cell signaling in cerebral ischemia: The complex roles of heat shock protein 70
    • Giffard R. G., Han R. Q., Emery J. F., Duan M., and, Pittet J. F., (2008) Regulation of apoptotic and inflammatory cell signaling in cerebral ischemia: the complex roles of heat shock protein 70. Anesthesiology 109, 339-348.
    • (2008) Anesthesiology , vol.109 , pp. 339-348
    • Giffard, R.G.1    Han, R.Q.2    Emery, J.F.3    Duan, M.4    Pittet, J.F.5
  • 40
    • 56949085541 scopus 로고    scopus 로고
    • Necrotic cell death: From reversible mitochondrial uncoupling to irreversible lysosomal permeabilization
    • Giusti C., Luciani M. F., Klein G., Aubry L., Tresse E., Kosta A., and, Golstein P., (2009) Necrotic cell death: from reversible mitochondrial uncoupling to irreversible lysosomal permeabilization. Exp. Cell Res. 315, 26-38.
    • (2009) Exp. Cell Res. , vol.315 , pp. 26-38
    • Giusti, C.1    Luciani, M.F.2    Klein, G.3    Aubry, L.4    Tresse, E.5    Kosta, A.6    Golstein, P.7
  • 42
    • 33846018602 scopus 로고    scopus 로고
    • Cell death by necrosis: towards a molecular definition
    • DOI 10.1016/j.tibs.2006.11.001, PII S0968000406003185
    • Golstein P., and, Kroemer G., (2007) Cell death by necrosis: towards a molecular definition. Trends Biochem. Sci. 32, 37-43. (Pubitemid 46043552)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.1 , pp. 37-43
    • Golstein, P.1    Kroemer, G.2
  • 43
    • 4344677922 scopus 로고    scopus 로고
    • Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease
    • DOI 10.1016/j.biocel.2004.04.020, PII S1357272504001670
    • Grune T., et al. (2004) Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease. Int. J. Biochem. Cell Biol. 36, 2519-2530. (Pubitemid 39119763)
    • (2004) International Journal of Biochemistry and Cell Biology , vol.36 , Issue.12 , pp. 2519-2530
    • Grune, T.1    Jung, T.2    Merker, K.3    Davies, K.J.A.4
  • 44
    • 2442476459 scopus 로고    scopus 로고
    • Lysosomes in cell death
    • DOI 10.1038/sj.onc.1207512
    • Guicciardi M. E., Leist M., and, Gores G. J., (2004) Lysosomes in cell death. Oncogene 23, 2881-2890. (Pubitemid 38638850)
    • (2004) Oncogene , vol.23 , Issue.16 REV. ISS. 2 , pp. 2881-2890
    • Guicciardi, M.E.1    Leist, M.2    Gores, G.J.3
  • 46
    • 33745013111 scopus 로고    scopus 로고
    • Oxidative stress and neurodegeneration: Where are we now?
    • DOI 10.1111/j.1471-4159.2006.03907.x
    • Halliwell B., (2006) Oxidative stress and neurodegeneration: where are we now? J. Neurochem. 97, 1634-1658. (Pubitemid 43873658)
    • (2006) Journal of Neurochemistry , vol.97 , Issue.6 , pp. 1634-1658
    • Halliwell, B.1
  • 47
    • 38549152194 scopus 로고    scopus 로고
    • Principles of bioactive lipid signalling: Lessons from sphingolipids
    • DOI 10.1038/nrm2329, PII NRM2329
    • Hannun Y. A., and, Obeid L. M., (2008) Principles of bioactive lipid signalling: lessons from sphingolipids. Nat. Rev. Mol. Cell Biol. 9, 139-150. (Pubitemid 351158911)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.2 , pp. 139-150
    • Hannun, Y.A.1    Obeid, L.M.2
  • 49
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl F. U., (1996) Molecular chaperones in cellular protein folding. Nature 381, 571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 50
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-kappaB signaling
    • Hayden M. S., and, Ghosh S., (2008) Shared principles in NF-kappaB signaling. Cell 132, 344-362.
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 51
    • 0036629206 scopus 로고    scopus 로고
    • A fluorescence-based, high-throughput sphingomyelin assay for the analysis of Niemann-Pick disease and other disorders of sphingomyelin metabolism
    • DOI 10.1006/abio.2002.5686
    • He X., et al. (2002) A fluorescence-based, highthroughput sphingomyelin assay for the analysis of Niemann-Pick disease and other disorders of sphingomyelin metabolism. Anal. Biochem. 306, 115-123. (Pubitemid 34722024)
    • (2002) Analytical Biochemistry , vol.306 , Issue.1 , pp. 115-123
    • He, X.1    Chen, F.2    McGovern, M.M.3    Schuchman, E.H.4
  • 53
    • 0033602394 scopus 로고    scopus 로고
    • Transacylase formation of bis(monoacylglycerol) phosphate
    • Heravi J., and, Waite M., (1999) Transacylase formation of bis(monoacylglycerol) phosphate. Biochim. Biophys. Acta 1437, 277-286.
    • (1999) Biochim. Biophys. Acta , vol.1437 , pp. 277-286
    • Heravi, J.1    Waite, M.2
  • 54
    • 0025281993 scopus 로고
    • Movement of internalized ligand-receptor complexes along a continuous endosomal reticulum
    • Hopkins C. R., et al. (1990) Movement of internalized ligand-receptor complexes along a continuous endosomal reticulum. Nature 346, 335-339.
    • (1990) Nature , vol.346 , pp. 335-339
    • Hopkins, C.R.1
  • 55
    • 0029012443 scopus 로고
    • Acid sphingomyelinase deficient mice: A model of types A and B Niemann-Pick disease
    • Horinouchi K., et al. (1995) Acid sphingomyelinase deficient mice: a model of types A and B Niemann-Pick disease. Nat. Genet. 10, 288-293.
    • (1995) Nat. Genet. , vol.10 , pp. 288-293
    • Horinouchi, K.1
  • 56
    • 75749139400 scopus 로고    scopus 로고
    • Cell biology: Stability in times of stress
    • Horváth I., and, Vígh L., (2010) Cell biology: stability in times of stress. Nature 463, 436-438.
    • (2010) Nature , vol.463 , pp. 436-438
    • Horváth, I.1    Vígh, L.2
  • 59
    • 0028468309 scopus 로고
    • The tricyclic antidepressant desipramine causes proteolytic degradation of lysosomal sphingomyelinase in human fibroblasts
    • Hurwitz R., Ferlinz K., and, Sandhoff K., (1994) The tricyclic antidepressant desipramine causes proteolytic degradation of lysosomal sphingomyelinase in human fibroblasts. Biol. Chem. Hoppe-Seyler 375, 447-450. (Pubitemid 2120332)
    • (1994) Biological Chemistry Hoppe-Seyler , vol.375 , Issue.7 , pp. 447-450
    • Hurwitz, R.1    Ferlinz, K.2    Sandhoff, K.3
  • 60
    • 0032768772 scopus 로고    scopus 로고
    • Heat shock proteins as cellular lifeguards
    • Jäättelä M., (1999) Heat shock proteins as cellular lifeguards. Ann. Med. 31, 261-271. (Pubitemid 29366608)
    • (1999) Annals of Medicine , vol.31 , Issue.4 , pp. 261-271
    • Jaattela, M.1
  • 61
    • 48249108314 scopus 로고    scopus 로고
    • Tumor suppression by autophagy through the management of metabolic stress
    • Jin S., and, White E., (2008) Tumor suppression by autophagy through the management of metabolic stress. Autophagy 4, 563-566.
    • (2008) Autophagy , vol.4 , pp. 563-566
    • Jin, S.1    White, E.2
  • 62
    • 77951666702 scopus 로고    scopus 로고
    • Regulation of apoptosis-associated lysosomal membrane permeabilization
    • Johansson A. C., et al. (2010) Regulation of apoptosis-associated lysosomal membrane permeabilization. Apoptosis 15, 527-540.
    • (2010) Apoptosis , vol.15 , pp. 527-540
    • Johansson, A.C.1
  • 63
    • 78449282609 scopus 로고    scopus 로고
    • Metals, oxidative stress and neurodegenerative disorders
    • Jomova K., Vondrakova D., Lawson M., and, Valko M., (2010) Metals, oxidative stress and neurodegenerative disorders. Mol. Cell. Biochem. 345, 91-104.
    • (2010) Mol. Cell. Biochem. , vol.345 , pp. 91-104
    • Jomova, K.1    Vondrakova, D.2    Lawson, M.3    Valko, M.4
  • 64
    • 0031963852 scopus 로고    scopus 로고
    • Isoform-specific effect of apolipoprotein E on cell survival and β- amyloid-induced toxicity in rat hippocampal pyramidal neuronal cultures
    • Jordán J., et al. (1998) Isoform-specific effect of apolipoprotein E on cell survival and ß-amyloid-induced toxicity in rat hippocampal pyramidal neuronal cultures. J. Neurosci. 18, 195-204. (Pubitemid 28046781)
    • (1998) Journal of Neuroscience , vol.18 , Issue.1 , pp. 195-204
    • Jordan, J.1    Galindo, M.F.2    Miller, R.J.3    Reardon, C.A.4    Getz, G.S.5    LaDu, M.J.6
  • 65
    • 0035887215 scopus 로고    scopus 로고
    • Sphingosine-induced apoptosis is dependent on lysosomal proteases
    • DOI 10.1042/0264-6021:3590335
    • KÃ¥gedal K., et al. (2001) Sphingosine-induced apoptosis is dependent on lysosomal proteases. Biochem. J. 359, 335-343. (Pubitemid 32999777)
    • (2001) Biochemical Journal , vol.359 , Issue.2 , pp. 335-343
    • Kagedal, K.1    Zhao, M.2    Svensson, I.3    Brunk, U.T.4
  • 66
    • 0017715433 scopus 로고
    • The preservation of ultrastructure in saturated phosphatidyl cholines by tannic acid in model systems and type II pneumocytes
    • DOI 10.1083/jcb.74.3.726
    • Kalina M., and, Pease D. C., (1977a) The preservation of ultrastructure in saturated phosphatidyl cholines by tannic acid in model systems and type II pneumocytes. J. Cell Biol. 74, 726-741. (Pubitemid 8193856)
    • (1977) Journal of Cell Biology , vol.74 , Issue.3 , pp. 726-741
    • Kalina, M.1    Pease, D.C.2
  • 67
    • 0017740362 scopus 로고
    • The probable role of phosphatidyl cholines in the tannic acid enhancement of cytomembrane electron contrast
    • DOI 10.1083/jcb.74.3.742
    • Kalina M., and, Pease D. C., (1977b) The probable role of phosphatidyl cholines in the tannic acid enhancement of cytomembrane electron contrast. J. Cell Biol. 74, 742-746. (Pubitemid 8193857)
    • (1977) Journal of Cell Biology , vol.74 , Issue.3 , pp. 742-746
    • Kalina, M.1    Pease, D.C.2
  • 69
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr J. F., Wyllie A. H., and, Currie A. R., (1972) Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26, 239-257.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 70
    • 62949128915 scopus 로고    scopus 로고
    • Lysosomal involvement in cell death and cancer
    • Kirkegaard T., and, Jäättelä M., (2009) Lysosomal involvement in cell death and cancer. Biochim. Biophys. Acta 1793, 746-754.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 746-754
    • Kirkegaard, T.1    Jäättelä, M.2
  • 71
    • 75749102680 scopus 로고    scopus 로고
    • Hsp70 stabilizes lysosomes and reverts Niemann-Pick disease-associated lysosomal pathology
    • Kirkegaard T., et al. (2010) Hsp70 stabilizes lysosomes and reverts Niemann-Pick disease-associated lysosomal pathology. Nature 463, 549-553.
    • (2010) Nature , vol.463 , pp. 549-553
    • Kirkegaard, T.1
  • 72
    • 0033988606 scopus 로고    scopus 로고
    • Niemann-Pick disease
    • DOI 10.1097/00062752-200001000-00009
    • Kolodny E. H., (2000) Niemann-Pick disease. Curr. Opin. Hematol. 7, 48-52. (Pubitemid 30007687)
    • (2000) Current Opinion in Hematology , vol.7 , Issue.1 , pp. 48-52
    • Kolodny, E.H.1
  • 73
    • 25444443570 scopus 로고    scopus 로고
    • Principles of lysosomal membrane digestion: Stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids
    • DOI 10.1146/annurev.cellbio.21.122303.120013
    • Kolter T., and, Sandhoff K., (2005) Principles of lysosomal membrane digestion: stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids. Annu. Rev. Cell Dev. Biol. 21, 81-103. (Pubitemid 41740628)
    • (2005) Annual Review of Cell and Developmental Biology , vol.21 , pp. 81-103
    • Kolter, T.1    Sandhoff, K.2
  • 74
    • 77951924919 scopus 로고    scopus 로고
    • Lysosomal degradation of membrane lipids
    • Kolter T., and, Sandhoff K., (2010) Lysosomal degradation of membrane lipids. FEBS Lett. 584, 1700-1712.
    • (2010) FEBS Lett. , vol.584 , pp. 1700-1712
    • Kolter, T.1    Sandhoff, K.2
  • 75
    • 0442323490 scopus 로고    scopus 로고
    • Interactions of acid sphingomyelinase and lipid bilayers in the presence of the tricyclic antidepressant desipramine
    • DOI 10.1016/S0014-5793(04)00033-X
    • Kölzer M., Werth N., and, Sandhoff K., (2004) Interactions of acid sphingomyelinase and lipid bilayers in the presence of the tricyclic antidepressant desipramine. FEBS Lett. 559, 96-98. (Pubitemid 38186710)
    • (2004) FEBS Letters , vol.559 , Issue.1-3 , pp. 96-98
    • Kolzer, M.1    Werth, N.2    Sandhoff, K.3
  • 78
    • 79952257741 scopus 로고    scopus 로고
    • Stat3 controls lysosomal-mediated cell death in vivo
    • Kreuzaler P. A., et al. (2011) Stat3 controls lysosomal-mediated cell death in vivo. Nat. Cell Biol. 13, 303-309.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 303-309
    • Kreuzaler, P.A.1
  • 79
    • 56749170677 scopus 로고    scopus 로고
    • Autophagic cell death: The story of a misnomer
    • Kroemer G., and, Levine B., (2008) Autophagic cell death: the story of a misnomer. Nat. Rev. Mol. Cell Biol. 9, 1004-1010.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 1004-1010
    • Kroemer, G.1    Levine, B.2
  • 80
    • 19444370566 scopus 로고    scopus 로고
    • The lipid composition of autophagic vacuoles regulates expression of multilamellar bodies
    • DOI 10.1242/jcs.02324
    • Lajoie P., et al. (2005) The lipid composition of autophagic vacuoles regulates expression of multilamellar bodies. J. Cell Sci. 118, 1991-2003. (Pubitemid 40723842)
    • (2005) Journal of Cell Science , vol.118 , Issue.9 , pp. 1991-2003
    • Lajoie, P.1    Guay, G.2    Dennis, J.W.3    Nabi, I.R.4
  • 81
    • 0026754019 scopus 로고
    • Autophagic vacuoles rapidly fuse with pre-existing lysosomes in cultured hepatocytes
    • Lawrence B. P., and, Brown W. J., (1992) Autophagic vacuoles rapidly fuse with pre-existing lysosomes in cultured hepatocytes. J. Cell Sci. 102, 515-526.
    • (1992) J. Cell Sci. , vol.102 , pp. 515-526
    • Lawrence, B.P.1    Brown, W.J.2
  • 82
    • 4344571747 scopus 로고    scopus 로고
    • Effects of Hsp70.1 gene knockout on the mitochondrial apoptotic pathway after focal cerebral ischemia
    • Lee S. H., et al. (2004) Effects of Hsp70.1 gene knockout on the mitochondrial apoptotic pathway after focal cerebral ischemia. Stroke 35, 2195-2199.
    • (2004) Stroke , vol.35 , pp. 2195-2199
    • Lee, S.H.1
  • 83
    • 0035038613 scopus 로고    scopus 로고
    • Triggering of apoptosis by cathepsins
    • DOI 10.1038/sj.cdd.4400859
    • Leist M., and, Jäättelä M., (2001) Triggering of apoptosis by cathepsins. Cell Death Differ. 8, 324-326. (Pubitemid 32409602)
    • (2001) Cell Death and Differentiation , vol.8 , Issue.4 , pp. 324-326
    • Leist, M.1    Jaattela, M.2
  • 84
    • 33244471589 scopus 로고    scopus 로고
    • Developmental apoptosis in C. elegans: A complex CEDnario
    • DOI 10.1038/nrm1836, PII NRM1836
    • Lettre G., and, Hengartner M. O., (2006) Developmental apoptosis in C. elegans: a complex CEDnario. Nature Rev. Mol. Cell Biol. 7, 97-108. (Pubitemid 43278293)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.2 , pp. 97-108
    • Lettre, G.1    Hengartner, M.O.2
  • 85
    • 0036569401 scopus 로고    scopus 로고
    • Carbonyl modified proteins in cellular regulation, aging, and disease
    • DOI 10.1016/S0891-5849(02)00765-7, PII S0891584902007657
    • Levine R. L., (2002) Carbonyl modified proteins in cellular regulation, aging, and disease. Free Radic. Biol. Med. 32, 790-796. (Pubitemid 34439249)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.9 , pp. 790-796
    • Levine, R.L.1
  • 88
    • 0035937146 scopus 로고    scopus 로고
    • Interfacial regulation of acid ceramidase activity. Stimulation of ceramide degradation by lysosomal lipids and sphingolipid activator proteins
    • Linke T., et al. (2001b) Interfacial regulation of acid ceramidase activity. Stimulation of ceramide degradation by lysosomal lipids and sphingolipid activator proteins. J. Biol. Chem. 276, 5760-5768.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5760-5768
    • Linke, T.1
  • 89
    • 0030714092 scopus 로고    scopus 로고
    • Elevated 4-hydroxynonenal in ventricular fluid in Alzheimer's disease
    • DOI 10.1016/S0197-4580(97)00108-5, PII S0197458097001085
    • Lovell M. A., et al. (1997) Elevated 4-hydroxynonenal in ventricular fluid in Alzheimer's disease. Neurobiol. Aging 18, 457-461. (Pubitemid 27497140)
    • (1997) Neurobiology of Aging , vol.18 , Issue.5 , pp. 457-461
    • Lovell, M.A.1    Ehmann, W.D.2    Mattson, M.P.3    Markesbery, W.R.4
  • 90
    • 79952259044 scopus 로고    scopus 로고
    • Necrotic cell death: Harnessing the dark side of the force in mammary gland involution
    • Luke C. J., and, Silverman G. A., (2007) Necrotic cell death: harnessing the dark side of the force in mammary gland involution. Nat. Cell Biol. 13, 197-199.
    • (2007) Nat. Cell Biol. , vol.13 , pp. 197-199
    • Luke, C.J.1    Silverman, G.A.2
  • 93
    • 56349145208 scopus 로고    scopus 로고
    • Neuropathology of the acid sphingomyelinase knockout mouse model of Niemann-Pick A disease including structure-function studies associated with cerebellar Purkinje cell degeneration
    • Macauley S. L., et al. (2008) Neuropathology of the acid sphingomyelinase knockout mouse model of Niemann-Pick A disease including structure-function studies associated with cerebellar Purkinje cell degeneration. Exp. Neurol. 214, 181-192.
    • (2008) Exp. Neurol. , vol.214 , pp. 181-192
    • MacAuley, S.L.1
  • 95
    • 0031020476 scopus 로고    scopus 로고
    • A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid β- peptide
    • Mark R. J., et al. (1997) A role for 4-hydroxynonenal, an aldehydic product of lipid peroxidation, in disruption of ion homeostasis and neuronal death induced by amyloid ß-peptide. J. Neurochem. 68, 255-264. (Pubitemid 26427315)
    • (1997) Journal of Neurochemistry , vol.68 , Issue.1 , pp. 255-264
    • Mark, R.J.1    Lovell, M.A.2    Markesbery, W.R.3    Uchida, K.4    Mattson, M.P.5
  • 96
    • 0034011261 scopus 로고    scopus 로고
    • Oxyradicals and DNA damage
    • Marnett L. J., (2000) Oxyradicals and DNA damage. Carcinogenesis 21, 361-370. (Pubitemid 30137921)
    • (2000) Carcinogenesis , vol.21 , Issue.3 , pp. 361-370
    • Marnett, L.J.1
  • 98
    • 0018786885 scopus 로고
    • Degradation of bis(monoacylglycero) phosphate by an acid phosphodiesterase in rat liver lysosomes
    • Matsuzawa Y., and, Hostetler K. Y., (1979) Degradation of bis(monoacylglycero) phosphate by an acid phosphodiesterase in rat liver lysosomes. J. Biol. Chem. 254, 5997-6001.
    • (1979) J. Biol. Chem. , vol.254 , pp. 5997-6001
    • Matsuzawa, Y.1    Hostetler, K.Y.2
  • 100
    • 2342651518 scopus 로고    scopus 로고
    • Molecular chaperones and the stress of oncogenesis
    • DOI 10.1038/sj.onc.1207529
    • Mosser D. D., and, Morimoto R. I., (2004) Molecular chaperones and the stress of oncogenesis. Oncogene 23, 2907-2918. (Pubitemid 38638852)
    • (2004) Oncogene , vol.23 , Issue.REV. ISS. 2 , pp. 2907-2918
    • Mosser, D.D.1    Morimoto, R.I.2
  • 105
    • 17844403545 scopus 로고    scopus 로고
    • Role of oxidative carbonylation in protein quality control and senescence
    • DOI 10.1038/sj.emboj.7600599
    • Nyström T., (2005) Role of oxidative carbonylation in protein quality control and senescence. EMBO J. 24, 1311-1317. (Pubitemid 40593052)
    • (2005) EMBO Journal , vol.24 , Issue.7 , pp. 1311-1317
    • Nystrom, T.1
  • 106
    • 67349091434 scopus 로고    scopus 로고
    • Proteomic identification of carbonylated proteins in the monkey hippocampus after ischemia-reperfusion
    • Oikawa S., et al. (2009) Proteomic identification of carbonylated proteins in the monkey hippocampus after ischemia-reperfusion. Free Radic. Biol. Med. 46, 1472-1477.
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 1472-1477
    • Oikawa, S.1
  • 107
    • 0029133790 scopus 로고
    • Cellular injury induced by oxidative stress is mediated through lysosomal damage
    • Öllinger K., and, Brunk U. T., (1995) Cellular injury induced by oxidative stress is mediated through lysosomal damage. Free Radical Biol. Med. 19, 565-574.
    • (1995) Free Radical Biol. Med. , vol.19 , pp. 565-574
    • Öllinger, K.1    Brunk, U.T.2
  • 108
    • 0034656016 scopus 로고    scopus 로고
    • Distribution of hydroxynonenal-modified proteins in the kainate-lesioned rat hippocampus: Evidence that hydroxynonenal formation precedes neuronal cell death
    • Ong W. Y., et al. (2000) Distribution of hydroxynonenal-modified proteins in the kainate-lesioned rat hippocampus: evidence that hydroxynonenal formation precedes neuronal cell death. Free Radic. Biol. Med. 28, 1214-1221.
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 1214-1221
    • Ong, W.Y.1
  • 109
    • 0029014350 scopus 로고
    • Acid sphingomyelinase-deficient mice mimic the neurovisceral form of human lysosomal storage disease (Niemann-Pick disease)
    • Otterbach B., and, Stoffel W., (1995) Acid sphingomyelinase-deficient mice mimic the neurovisceral form of human lysosomal storage disease (Niemann-Pick disease). Cell 81, 1053-1061.
    • (1995) Cell , vol.81 , pp. 1053-1061
    • Otterbach, B.1    Stoffel, W.2
  • 110
    • 0034063728 scopus 로고    scopus 로고
    • A mechanism for the neuroprotective effect of apolipoprotein E: Isoform- specific modification by the lipid peroxidation product 4-hydroxynonenal
    • DOI 10.1046/j.1471-4159.2000.0741426.x
    • Pedersen W. A., Chan S. L., and, Mattson M. P., (2000) A mechanism for the neuroprotective effect of apolipoprotein E: isoform-specific modification by the lipid peroxidation product 4-hydroxynonenal. J. Neurochem. 74, 1426-1433. (Pubitemid 30163962)
    • (2000) Journal of Neurochemistry , vol.74 , Issue.4 , pp. 1426-1433
    • Pedersen, W.A.1    Chan, S.L.2    Mattson, M.P.3
  • 111
    • 78649743957 scopus 로고    scopus 로고
    • HSP70 and lysosomal storage disorders: Novel therapeutic opportunities
    • Petersen N. H., and, Kirkegaard T., (2010) HSP70 and lysosomal storage disorders: novel therapeutic opportunities. Biochem. Soc. Trans. 38, 1479-1483.
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 1479-1483
    • Petersen, N.H.1    Kirkegaard, T.2
  • 112
    • 77954164469 scopus 로고    scopus 로고
    • Connecting Hsp70, sphingolipid metabolism and lysosomal stability
    • Petersen N. H. T., et al. (2010) Connecting Hsp70, sphingolipid metabolism and lysosomal stability. Cell Cycle 9, 2305-2309.
    • (2010) Cell Cycle , vol.9 , pp. 2305-2309
    • Petersen, N.H.T.1
  • 113
    • 57649146521 scopus 로고    scopus 로고
    • Post-ischemic brain damage: NF-kappaB dimer heterogeneity as a molecular determinant of neuron vulnerability
    • Pizzi M., Sarnico I., Lanzillotta A., Battistin L., and, Spano P., (2009) Post-ischemic brain damage: NF-kappaB dimer heterogeneity as a molecular determinant of neuron vulnerability. FEBS J. 276, 27-35.
    • (2009) FEBS J. , vol.276 , pp. 27-35
    • Pizzi, M.1    Sarnico, I.2    Lanzillotta, A.3    Battistin, L.4    Spano, P.5
  • 114
    • 62949097187 scopus 로고    scopus 로고
    • Delivery of endocytosed membrane proteins to the lysosome
    • Pryor P. R., and, Luzio J. P., (2009) Delivery of endocytosed membrane proteins to the lysosome. Biochim. Biophys. Acta 1793, 615-624.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 615-624
    • Pryor, P.R.1    Luzio, J.P.2
  • 115
    • 0038725886 scopus 로고    scopus 로고
    • Ischemic neuronal death in the rat hippocampus: The calpain-calpastatin- caspase hypothesis
    • DOI 10.1016/S0969-9961(03)00018-4
    • Rami A., (2003) Ischemic neuronal death in the rat hippocampus: the calpain-calpastatin-caspase hypothesis. Neurobiol. Dis. 13, 75-88. (Pubitemid 36793974)
    • (2003) Neurobiology of Disease , vol.13 , Issue.2 , pp. 75-88
    • Rami, A.1
  • 117
    • 78149358483 scopus 로고    scopus 로고
    • Lysosomal-mitochondrial cross-talk during cell death
    • Repnik U., and, Turk B., (2010) Lysosomal-mitochondrial cross-talk during cell death. Mitochondrion 10, 662-669.
    • (2010) Mitochondrion , vol.10 , pp. 662-669
    • Repnik, U.1    Turk, B.2
  • 118
    • 59349107204 scopus 로고    scopus 로고
    • NF-kappaB signaling in cerebral ischemia
    • Ridder D. A., and, Schwaninger M., (2009) NF-kappaB signaling in cerebral ischemia. Neuroscience 158, 995-1006.
    • (2009) Neuroscience , vol.158 , pp. 995-1006
    • Ridder, D.A.1    Schwaninger, M.2
  • 119
    • 34250561475 scopus 로고
    • A new puffing pattern induced by temperature shock and DNP in Drosophila
    • Ritossa F., (1962) A new puffing pattern induced by temperature shock and DNP in Drosophila. Cell. Mol. Life Sci. 18, 571-573.
    • (1962) Cell. Mol. Life Sci. , vol.18 , pp. 571-573
    • Ritossa, F.1
  • 120
    • 0031883782 scopus 로고    scopus 로고
    • A pre-embedding technique for immunocytochemical visualization of cathepsin D in cultured cells subjected to oxidative stress
    • Roberg K., and, Öllinger K., (1998) A pre-embedding technique for immunocytochemical visualization of cathepsin D in cultured cells subjected to oxidative stress. J. Histochem. Cytochem. 46, 411-418. (Pubitemid 28117392)
    • (1998) Journal of Histochemistry and Cytochemistry , vol.46 , Issue.3 , pp. 411-418
    • Roberg, K.1    Ollinger, K.2
  • 122
    • 77949488942 scopus 로고    scopus 로고
    • Calpain-mediated Hsp70.1 cleavage in hippocampal CA1 neuronal death
    • Sahara S., and, Yamashima T., (2010) Calpain-mediated Hsp70.1 cleavage in hippocampal CA1 neuronal death. Biochem. Biophys. Res. Commu. 393, 806-811.
    • (2010) Biochem. Biophys. Res. Commu. , vol.393 , pp. 806-811
    • Sahara, S.1    Yamashima, T.2
  • 124
    • 42449159755 scopus 로고    scopus 로고
    • Sphingomyelinase deficiency (Niemann-Pick disease) in a Hereford calf
    • DOI 10.1354/vp.45-2-201
    • Saunders G. K., and, Wenger D. A., (2008) Sphingomyelinase deficiency (Niemann-Pick disease) in a Hereford calf. Vet. Pathol. 45, 201-202. (Pubitemid 351571655)
    • (2008) Veterinary Pathology , vol.45 , Issue.2 , pp. 201-202
    • Saunders, G.K.1    Wenger, D.A.2
  • 126
    • 0025941838 scopus 로고
    • Structure and function of lamellar bodies, lipid-protein complexes involved in storage and secretion of cellular lipids
    • Schmitz G., and, Müller G., (1991) Structure and function of lamellar bodies, lipid-protein complexes involved in storage and secretion of cellular lipids. J. Lipid Res. 32, 1539-1570.
    • (1991) J. Lipid Res. , vol.32 , pp. 1539-1570
    • Schmitz, G.1    Müller, G.2
  • 127
    • 0001745899 scopus 로고    scopus 로고
    • Niemann-Pick disease types A and B: Acid sphingomyelinase deficiencies
    • in, 8th edn (Scriver C. R. Beaudet A. L. Sly W. S. and Valle D. eds), McGraw-Hill, New York.
    • Schuchman E. H., and, Desnick R. J., (2001) Niemann-Pick disease types A and B: acid sphingomyelinase deficiencies, in The Metabolic and Molecular Bases of Inherited Disease, 8th edn (, Scriver C. R., Beaudet A. L., Sly W. S., and, Valle D., eds), pp. 3589-3610. McGraw-Hill, New York.
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , pp. 3589-3610
    • Schuchman, E.H.1    Desnick, R.J.2
  • 128
    • 63149196645 scopus 로고    scopus 로고
    • Principles of lysosomal membrane degradation: Cellular topology and biochemistry of lysosomal lipid degradation
    • Schulze H., Kolter T., and, Sandhoff K., (2009) Principles of lysosomal membrane degradation: cellular topology and biochemistry of lysosomal lipid degradation. Biochim. Biophys. Acta 1793, 674-683.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 674-683
    • Schulze, H.1    Kolter, T.2    Sandhoff, K.3
  • 129
    • 0033538073 scopus 로고    scopus 로고
    • Inhibition of receptor internalization by monodansylcadaverine selectively blocks p55 tumor necrosis factor receptor death domain signaling
    • Schutze S., et al. (1999) Inhibition of receptor internalization by monodansylcadaverine selectively blocks p55 tumor necrosis factor receptor death domain signaling. J. Biol. Chem. 274, 10203-10212.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10203-10212
    • Schutze, S.1
  • 131
    • 0027032722 scopus 로고
    • The metabolism of 4-hydroxynonenal, a lipid peroxidation product, is dependent on tumor age in Ehrlich mouse ascites cells
    • Siems W. G., et al. (1992) The metabolism of 4-hydroxynonenal, a lipid peroxidation product, is dependent on tumor age in Ehrlich mouse ascites cells. Experientia 62, 124-135.
    • (1992) Experientia , vol.62 , pp. 124-135
    • Siems, W.G.1
  • 132
    • 0031891221 scopus 로고    scopus 로고
    • Metabolism of 4-hydroxynonenal, a cytotoxic lipid peroxidation product, in thymocytes as an effective secondary antioxidative defense mechanism
    • Siems W. G., et al. (1998) Metabolism of 4-hydroxynonenal, a cytotoxic lipid peroxidation product, in thymocytes as an effective secondary antioxidative defense mechanism. J. Biochem. 123, 534-539. (Pubitemid 28143511)
    • (1998) Journal of Biochemistry , vol.123 , Issue.3 , pp. 534-539
    • Siems, W.G.1    Pimenov, A.M.2    Esterbauer, H.3    Grune, T.4
  • 133
    • 54049092827 scopus 로고    scopus 로고
    • The unexpected role of acid sphingomyelinase in cell death and the pathophysiology of common diseases
    • Smith E. L., and, Schuchman E. H., (2008) The unexpected role of acid sphingomyelinase in cell death and the pathophysiology of common diseases. FASEB J. 22, 3419-3431.
    • (2008) FASEB J. , vol.22 , pp. 3419-3431
    • Smith, E.L.1    Schuchman, E.H.2
  • 134
    • 0031722955 scopus 로고    scopus 로고
    • Presence of 4-hydroxynonenal in cerebrospinal fluid of patients with sporadic amyotrophic lateral sclerosis
    • DOI 10.1002/ana.410440419
    • Smith R. G., et al. (1998) Presence of 4-hydroxynonenal in cerebrospinal fluid of patients with sporadic amyotrophic lateral sclerosis. Ann. Neurol. 44, 696-699. (Pubitemid 28477861)
    • (1998) Annals of Neurology , vol.44 , Issue.4 , pp. 696-699
    • Smith, R.G.1    Henry, Y.K.2    Mattson, M.P.3    Appel, S.H.4
  • 137
    • 0031010333 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • DOI 10.1021/tx960133r
    • Stadtman E. R., and, Berlett B. S., (1997) Reactive oxygen-mediated protein oxidation in aging and disease. Chem. Res. Toxicol. 10, 485-494. (Pubitemid 27217204)
    • (1997) Chemical Research in Toxicology , vol.10 , Issue.5 , pp. 485-494
    • Stadtman, E.R.1    Berlett, B.S.2
  • 138
    • 0031831270 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman E. R., and, Berlett B. S., (1998) Reactive oxygen-mediated protein oxidation in aging and disease. Drug Metab. Rev. 30, 225-243. (Pubitemid 28266861)
    • (1998) Drug Metabolism Reviews , vol.30 , Issue.2 , pp. 225-243
    • Stadtman, E.R.1    Berlett, B.S.2
  • 139
    • 34250020188 scopus 로고    scopus 로고
    • Lysosomal cysteine cathepsins: Signaling pathways in apoptosis
    • DOI 10.1515/BC.2007.064
    • Stoka V., Turk V., and, Turk B., (2007) Lysosomal cysteine cathepsins: signaling pathways in apoptosis. Biol. Chem. 388, 555-560. (Pubitemid 46883446)
    • (2007) Biological Chemistry , vol.388 , Issue.6 , pp. 555-560
    • Stoka, V.1    Turk, V.2    Turk, B.3
  • 140
    • 75149161571 scopus 로고    scopus 로고
    • Redox proteomic analysis of carbonylated brain proteins in mild cognitive impairment and early Alzheimer's disease
    • Sultana R., et al. (2010) Redox proteomic analysis of carbonylated brain proteins in mild cognitive impairment and early Alzheimer's disease. Antioxid. Redox Signal. 12, 327-336.
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 327-336
    • Sultana, R.1
  • 141
    • 0037206901 scopus 로고    scopus 로고
    • Specific aspartyl and calpain proteases are required for neurodegeneration in C. elegans
    • DOI 10.1038/nature01108
    • Syntichaki P., et al. (2002) Specific aspartyl and calpain proteases are required for neurodegeneration in C. elegans. Nature 419, 939-944. (Pubitemid 35339629)
    • (2002) Nature , vol.419 , Issue.6910 , pp. 939-944
    • Syntichaki, P.1    Xu, K.2    Driscoll, M.3    Tavernarakis, N.4
  • 142
    • 21844467751 scopus 로고    scopus 로고
    • +-ATPase mediates intracellular acidification required for neurodegeneration in C. elegans
    • DOI 10.1016/j.cub.2005.05.057, PII S0960982205006172
    • +-ATPase mediates intracellular acidification required for neurodegeneration in C. elegans. Curr. Biol. 15, 1249-1254. (Pubitemid 40950525)
    • (2005) Current Biology , vol.15 , Issue.13 , pp. 1249-1254
    • Syntichaki, P.1    Samara, C.2    Tavernarakis, N.3
  • 144
    • 33749146320 scopus 로고    scopus 로고
    • Lysosomal labilization
    • DOI 10.1080/15216540600904885, PII J375811642077257
    • Terman A., et al. (2006) Lysosomal labilization. IUBMB Life. 58, 531-539. (Pubitemid 44470239)
    • (2006) IUBMB Life , vol.58 , Issue.9 , pp. 531-539
    • Terman, A.1    Kurz, T.2    Gustafsson, B.3    Brunk, U.T.4
  • 145
    • 0016373748 scopus 로고
    • Protein synthesis in salivary glands of Drosophila melanogaster: Relation to chromosome puffs
    • Tissières A., Mitchell H. K., and, Tracy U. M. J., (1974) Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs. J. Mol. Biol. 84, 389-398.
    • (1974) J. Mol. Biol. , vol.84 , pp. 389-398
    • Tissières, A.1    Mitchell, H.K.2    Tracy, U.M.J.3
  • 146
    • 77954667267 scopus 로고    scopus 로고
    • Proteomic approaches to oxidative protein modifications implicated in the mechanism of aging
    • Toda T., et al. (2010) Proteomic approaches to oxidative protein modifications implicated in the mechanism of aging. Geriatr. Gerontol. Int. 10, S25-S31.
    • (2010) Geriatr. Gerontol. Int. , vol.10
    • Toda, T.1
  • 147
    • 69249140641 scopus 로고    scopus 로고
    • Lysosomes as "suicide bags" in cell death: Myth or reality?
    • Turk B., and, Turk V., (2009) Lysosomes as "suicide bags" in cell death: myth or reality? J. Biol. Chem. 284, 21783-21787.
    • (2009) J. Biol. Chem. , vol.284 , pp. 21783-21787
    • Turk, B.1    Turk, V.2
  • 148
    • 0026059280 scopus 로고
    • Membrane markers of endoplasmic reticulum preserved in autophagic vacuolar membranes isolated from leupeptin-administered rat liver
    • Ueno T., Muno D., and, Kominami E., (1991) Membrane markers of endoplasmic reticulum preserved in autophagic vacuolar membranes isolated from leupeptin-administered rat liver. J. Biol. Chem. 266, 18995-18999. (Pubitemid 21908181)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.28 , pp. 18995-18999
    • Ueno, T.1    Muno, D.2    Kominami, E.3
  • 150
    • 14144255733 scopus 로고    scopus 로고
    • Lysosomal storage disorders
    • DOI 10.1111/j.1365-2141.2004.05293.x
    • Vellodi A., (2005) Lysosomal storage disorders. Br. J. Haematol. 128, 413-431. (Pubitemid 40283160)
    • (2005) British Journal of Haematology , vol.128 , Issue.4 , pp. 413-431
    • Vellodi, A.1
  • 151
    • 0028919063 scopus 로고
    • Inhibition of proliferation and induction of apoptosis by abrogation of heat-shock protein (HSP) 70 expression in tumor cells
    • Wei Y. Q., et al. (1995) Inhibition of proliferation and induction of apoptosis by abrogation of heat-shock protein (HSP) 70 expression in tumor cells. Cancer Immunol. Immunother. 40, 73-78.
    • (1995) Cancer Immunol. Immunother. , vol.40 , pp. 73-78
    • Wei, Y.Q.1
  • 152
    • 0034739734 scopus 로고    scopus 로고
    • Implication of cysteine proteases calpain, cathepsin and caspase in ischemic neuronal death of primates
    • DOI 10.1016/S0301-0082(00)00006-X, PII S030100820000006X
    • Yamashima T., (2000) Implication of cysteine proteases calpain, cathepsin and caspase in ischemic neuronal death of primates. Prog. Neurobiol. 62, 273-295. (Pubitemid 30326777)
    • (2000) Progress in Neurobiology , vol.62 , Issue.3 , pp. 273-295
    • Yamashima, T.1
  • 153
    • 3342900223 scopus 로고    scopus 로고
    • 2+-dependent proteases in ischemic neuronal death. A conserved 'calpain-cathepsin cascade' from nematodes to primates
    • DOI 10.1016/j.ceca.2004.03.001, PII S0143416004000661
    • 2+-dependent proteases in ischemic neuronal death: a conserved 'calpain-cathepsin cascade' from nematodes to primates. Cell Calcium 36, 285-293. (Pubitemid 38992354)
    • (2004) Cell Calcium , vol.36 , Issue.3-4 , pp. 285-293
    • Yamashima, T.1
  • 154
    • 70450222302 scopus 로고    scopus 로고
    • The role of lysosomal rupture in neuronal death
    • Yamashima T., and, Oikawa S., (2009) The role of lysosomal rupture in neuronal death. Prog. Neurobiol. 89, 343-358.
    • (2009) Prog. Neurobiol. , vol.89 , pp. 343-358
    • Yamashima, T.1    Oikawa, S.2
  • 155
    • 0029784671 scopus 로고    scopus 로고
    • 2 and calpain responses prior to delayed neuronal death in monkeys
    • 2 and calpain responses prior to delayed neuronal death in monkeys. Eur. J. Neurosci. 8, 1932-1944.
    • (1996) Eur. J. Neurosci. , vol.8 , pp. 1932-1944
    • Yamashima, T.1
  • 156
    • 0031817004 scopus 로고    scopus 로고
    • Inhibition of ischaemic hippocampal neuronal death in primates with cathepsin B inhibitor CA-074: A novel strategy for neuroprotection based on 'calpain-cathepsin hypothesis'
    • Yamashima T., et al. (1998) Inhibition of ischaemic hippocampal neuronal death in primates with cathepsin B inhibitor CA-074: a novel strategy for neuroprotection based on 'calpain-cathepsin hypothesis'. Eur. J. Neurosci. 10, 1723-1733.
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 1723-1733
    • Yamashima, T.1
  • 157
    • 0242539781 scopus 로고    scopus 로고
    • Sustained calpain activation associated with lysosomal rupture executes necrosis of the postischemic CA1 neurons in primates
    • DOI 10.1002/hipo.10127
    • Yamashima T., et al. (2003) Sustained calpain activation associated with lysosomal rupture executes necrosis of the postischemic CA1 neurons in primates. Hippocampus 13, 791-800. (Pubitemid 37407965)
    • (2003) Hippocampus , vol.13 , Issue.7 , pp. 791-800
    • Yamashima, T.1    Tonchev, A.B.2    Tsukada, T.3    Saido, T.C.4    Imajoh-Ohmi, S.5    Momoi, T.6    Kominami, E.7
  • 158
    • 84863393821 scopus 로고    scopus 로고
    • Why are hippocampal CA1 neurons vulnerable but motor cortex neurons resistant to transient ischemia?
    • Zhu H., et al. (2012) Why are hippocampal CA1 neurons vulnerable but motor cortex neurons resistant to transient ischemia? J. Neurochem. 120, 574-585.
    • (2012) J. Neurochem. , vol.120 , pp. 574-585
    • Zhu, H.1
  • 159
    • 29944438881 scopus 로고    scopus 로고
    • Necrotic death as a cell fate
    • DOI 10.1101/gad.1376506
    • Zong W. X., and, Thompson C. B., (2006) Necrotic death as a cell fate. Genes Dev. 20, 1-15. (Pubitemid 43042662)
    • (2006) Genes and Development , vol.20 , Issue.1 , pp. 1-15
    • Zong, W.-X.1    Thompson, C.B.2


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