메뉴 건너뛰기




Volumn 55, Issue 11, 2014, Pages 2198-2210

Lysosomal storage diseases and the heat shock response: Convergences and therapeutic opportunities

Author keywords

Glycosphingolipids; Heat shock proteins; Molecular chaperones; Sphingolipids; Stress response

Indexed keywords

ARIMOCLOMOL; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; CALCIUM CHANNEL BLOCKING AGENT; CELASTROL; CHAPERONE; GLUCOSYLCERAMIDASE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HEAT SHOCK TRANSCRIPTION FACTOR 1; HISTONE DEACETYLASE INHIBITOR; PROTEASOME INHIBITOR; PSYCHOSINE; REACTIVE OXYGEN METABOLITE; CALCIUM;

EID: 84929513267     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.R048090     Document Type: Review
Times cited : (33)

References (180)
  • 2
    • 69249227502 scopus 로고    scopus 로고
    • Lysosome biogenesis and lysosomal membrane proteins: Trafficking meets function
    • Saftig, P., and J. Klumperman. 2009. Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function. Nat. Rev. Mol. Cell Biol. 10: 623-635.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 623-635
    • Saftig, P.1    Klumperman, J.2
  • 4
    • 77954225471 scopus 로고    scopus 로고
    • Common and uncommon pathogenic cascades in lysosomal storage diseases
    • Vitner, E. B., F. M. Platt, and A. H. Futerman. 2010. Common and uncommon pathogenic cascades in lysosomal storage diseases. J. Biol. Chem. 285: 20423-20427.
    • (2010) J. Biol. Chem. , vol.285 , pp. 20423-20427
    • Vitner, E.B.1    Platt, F.M.2    Futerman, A.H.3
  • 5
    • 84871960929 scopus 로고    scopus 로고
    • The cell biology of disease: Lysosomal storage disorders: The cellular impact of lysosomal dysfunction
    • Platt, F. M., B. Boland, and C. van der Spoel. 2012. The cell biology of disease: lysosomal storage disorders: the cellular impact of lysosomal dysfunction. J. Cell Biol. 199: 723-734.
    • (2012) J. Cell Biol. , vol.199 , pp. 723-734
    • Platt, F.M.1    Boland, B.2    Van Der Spoel, C.3
  • 6
    • 84896713980 scopus 로고    scopus 로고
    • Emerging therapies and therapeutic concepts for lysosomal storage diseases
    • Kirkegaard, T. 2013. Emerging therapies and therapeutic concepts for lysosomal storage diseases. Expert Opin. Orphan Drugs. 1: 385-404.
    • (2013) Expert Opin. Orphan Drugs , vol.1 , pp. 385-404
    • Kirkegaard, T.1
  • 7
    • 50249175120 scopus 로고    scopus 로고
    • Chemical and biological approaches synergize to ameliorate protein-folding diseases
    • Mu, T. W., D. S. Ong, Y. J. Wang, W. E. Balch, J. R. Yates, L. Segatori, and J. W. Kelly. 2008. Chemical and biological approaches synergize to ameliorate protein-folding diseases. Cell. 134: 769-781.
    • (2008) Cell. , vol.134 , pp. 769-781
    • Mu, T.W.1    Ong, D.S.2    Wang, Y.J.3    Balch, W.E.4    Yates, J.R.5    Segatori, L.6    Kelly, J.W.7
  • 8
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F. U., A. Bracher, and M. Hayer-Hartl. 2011. Molecular chaperones in protein folding and proteostasis. Nature. 475: 324-332.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 9
    • 0037099046 scopus 로고    scopus 로고
    • Chaperoning signaling pathways: Molecular chaperones as stress-sensing "heat shock" proteins
    • Nollen, E. A.A., and R. I. Morimoto. 2002. Chaperoning signaling pathways: molecular chaperones as stress-sensing "heat shock" proteins. J. Cell Sci. 115: 2809-2816.
    • (2002) J. Cell Sci. , vol.115 , pp. 2809-2816
    • Nollen, E.A.A.1    Morimoto, R.I.2
  • 10
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • Morimoto, R. I. 2008. Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev. 22: 1427-1438.
    • (2008) Genes Dev. , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 11
    • 34047097917 scopus 로고    scopus 로고
    • Hsp70 protects against UVB induced apoptosis by preventing release of cathepsins and cytochrome c in human melanocytes
    • Bivik, C., I. Rosdahl, and K. Ollinger. 2007. Hsp70 protects against UVB induced apoptosis by preventing release of cathepsins and cytochrome c in human melanocytes. Carcinogenesis. 28: 537-544.
    • (2007) Carcinogenesis , vol.28 , pp. 537-544
    • Bivik, C.1    Rosdahl, I.2    Ollinger, K.3
  • 13
    • 62949128915 scopus 로고    scopus 로고
    • Lysosomal involvement in cell death and cancer
    • Kirkegaard, T., and M. Jäättelä. 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
  • 14
    • 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.
    • (1999) Ann. Med. , vol.31 , pp. 261-271
    • Jäättelä, M.1
  • 15
    • 40149095757 scopus 로고    scopus 로고
    • Partial restoration of mutant enzyme homeostasis in three distinct lysosomal storage disease cell lines by altering calcium homeostasis
    • Mu, T-W., D. M. Fowler, and J. W. Kelly. 2008. Partial restoration of mutant enzyme homeostasis in three distinct lysosomal storage disease cell lines by altering calcium homeostasis. PLoS Biol. 6: e26.
    • (2008) PLoS Biol. , vol.6 , pp. e26
    • Mu, T.-W.1    Fowler, D.M.2    Kelly, J.W.3
  • 16
    • 79954416821 scopus 로고    scopus 로고
    • Chemical and/or biological therapeutic strategies to ameliorate protein misfolding diseases
    • Ong, D. S. T., and J. W. Kelly. 2011. Chemical and/or biological therapeutic strategies to ameliorate protein misfolding diseases. Curr. Opin. Cell Biol. 23: 231-238.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 231-238
    • Ong, D.S.T.1    Kelly, J.W.2
  • 17
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • Muchowski, P. J., and J. L. Wacker. 2005. Modulation of neurodegeneration by molecular chaperones. Nat. Rev. Neurosci. 6: 11-22.
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 18
    • 84890560755 scopus 로고    scopus 로고
    • The role of heat shock proteins in amyotrophic lateral sclerosis: The therapeutic potential of Arimoclomol
    • Kalmar, B., C-H. Lu, and L. Greensmith. 2014. The role of heat shock proteins in amyotrophic lateral sclerosis: the therapeutic potential of Arimoclomol. Pharmacol. Ther. 141: 40-54.
    • (2014) Pharmacol. Ther. , vol.141 , pp. 40-54
    • Kalmar, B.1    Lu, C.-H.2    Greensmith, L.3
  • 19
    • 84866329572 scopus 로고    scopus 로고
    • Pathogenesis and therapy of inclusion body myositis
    • Greenberg, S. A. 2012. Pathogenesis and therapy of inclusion body myositis. Curr. Opin. Neurol. 25: 630-639.
    • (2012) Curr. Opin. Neurol. , vol.25 , pp. 630-639
    • Greenberg, S.A.1
  • 21
    • 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
  • 22
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • Hartl, F. U., and M. Hayer-Hartl. 2009. Converging concepts of protein folding in vitro and in vivo. Nat. Struct. Mol. Biol. 16: 574-581.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 23
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • Scheufler, C., A. Brinker, G. Bourenkov, S. Pegoraro, L. Moroder, H. Bartunik, F. U. Hartl, and I. Moarefi. 2000. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell. 101: 199-210.
    • (2000) Cell. , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl, F.U.7    Moarefi, I.8
  • 24
    • 78649357985 scopus 로고    scopus 로고
    • Protein quality control in the cytosol and the endoplasmic reticulum: Brothers in arms
    • Buchberger, A., B. Bukau, and T. Sommer. 2010. Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms. Mol. Cell. 40: 238-252.
    • (2010) Mol. Cell. , vol.40 , pp. 238-252
    • Buchberger, A.1    Bukau, B.2    Sommer, T.3
  • 25
    • 0033612302 scopus 로고    scopus 로고
    • BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane
    • Matlack, K. E., B. Misselwitz, K. Plath, and T. A. Rapoport. 1999. BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane. Cell. 97: 553-564.
    • (1999) Cell. , vol.97 , pp. 553-564
    • Matlack, K.E.1    Misselwitz, B.2    Plath, K.3    Rapoport, T.A.4
  • 27
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron, D., and P. Walter. 2007. Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8: 519-529.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 28
    • 84864318195 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: A unique way to enter the lysosome world
    • Kaushik, S., and A. M. Cuervo. 2012. Chaperone-mediated autophagy: a unique way to enter the lysosome world. Trends Cell Biol. 22: 407-417.
    • (2012) Trends Cell Biol. , vol.22 , pp. 407-417
    • Kaushik, S.1    Cuervo, A.M.2
  • 29
    • 79959463520 scopus 로고    scopus 로고
    • Regulation of HSF1 function in the heat stress response: Implications in aging and disease
    • Anckar, J., and L. Sistonen. 2011. Regulation of HSF1 function in the heat stress response: implications in aging and disease. Annu. Rev. Biochem. 80: 1089-1115.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 1089-1115
    • Anckar, J.1    Sistonen, L.2
  • 30
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • Zou, J., Y. Guo, T. Guettouche, D. F. Smith, and R. Voellmy. 1998. Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell. 94: 471-480.
    • (1998) Cell. , vol.94 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5
  • 31
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou, C., S. M. Roe, R. O'Brien, J. E. Ladbury, P. W. Piper, and L. H. Pearl. 1997. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell. 90: 65-75.
    • (1997) Cell. , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 32
    • 0025744556 scopus 로고
    • Induction of hsp 72/73 by herbimycin A, an inhibitor of transformation by tyrosine kinase oncogenes
    • Murakami, Y., Y. Uehara, C. Yamamoto, H. Fukazawa, and S. Mizuno. 1991. Induction of hsp 72/73 by herbimycin A, an inhibitor of transformation by tyrosine kinase oncogenes. Exp. Cell Res. 195: 338-344.
    • (1991) Exp. Cell Res. , vol.195 , pp. 338-344
    • Murakami, Y.1    Uehara, Y.2    Yamamoto, C.3    Fukazawa, H.4    Mizuno, S.5
  • 33
    • 1942486792 scopus 로고    scopus 로고
    • Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice
    • Kieran, D., B. Kalmar, J. R. T. Dick, J. Riddoch-Contreras, G. Burnstock, and L. Greensmith. 2004. Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice. Nat. Med. 10: 402-405.
    • (2004) Nat. Med. , vol.10 , pp. 402-405
    • Kieran, D.1    Kalmar, B.2    Dick, J.R.T.3    Riddoch-Contreras, J.4    Burnstock, G.5    Greensmith, L.6
  • 35
    • 84874901074 scopus 로고    scopus 로고
    • Co-induction of the heat shock response ameliorates disease progression in a mouse model of human spinal and bulbar muscular atrophy: Implications for therapy
    • Malik, B., N. Nirmalananthan, A. L. Gray, A. R. La Spada, M. G. Hanna, and L. Greensmith. 2013. Co-induction of the heat shock response ameliorates disease progression in a mouse model of human spinal and bulbar muscular atrophy: implications for therapy. Brain. 136: 926-943.
    • (2013) Brain , vol.136 , pp. 926-943
    • Malik, B.1    Nirmalananthan, N.2    Gray, A.L.3    La Spada, A.R.4    Hanna, M.G.5    Greensmith, L.6
  • 36
    • 76749160942 scopus 로고    scopus 로고
    • Activation of mutant enzyme function in vivo by proteasome inhibitors and treatments that induce Hsp70
    • Singh, L. R., S. Gupta, N. H. Honig, J. P. Kraus, and W. D. Kruger. 2010. Activation of mutant enzyme function in vivo by proteasome inhibitors and treatments that induce Hsp70. PLoS Genet. 6: e1000807.
    • (2010) PLoS Genet. , vol.6
    • Singh, L.R.1    Gupta, S.2    Honig, N.H.3    Kraus, J.P.4    Kruger, W.D.5
  • 39
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease
    • Auluck, P. K., H. Y. E. Chan, J. Q. Trojanowski, V. M. Y. Lee, and N. M. Bonini. 2002. Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease. Science. 295: 865-868.
    • (2002) Science , vol.295 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.E.2    Trojanowski, J.Q.3    Lee, V.M.Y.4    Bonini, N.M.5
  • 40
    • 26444609722 scopus 로고    scopus 로고
    • ER retention and degradation as the molecular basis underlying Gaucher disease heterogeneity
    • Ron, I., and M. Horowitz. 2005. ER retention and degradation as the molecular basis underlying Gaucher disease heterogeneity. Hum. Mol. Genet. 14: 2387-2398.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2387-2398
    • Ron, I.1    Horowitz, M.2
  • 42
    • 0033018496 scopus 로고    scopus 로고
    • Accelerated transport and maturation of lysosomal alpha-galactosidase A in Fabry lymphoblasts by an enzyme inhibitor
    • Fan, J. Q., S. Ishii, N. Asano, and Y. Suzuki. 1999. Accelerated transport and maturation of lysosomal alpha-galactosidase A in Fabry lymphoblasts by an enzyme inhibitor. Nat. Med. 5: 112-115.
    • (1999) Nat. Med. , vol.5 , pp. 112-115
    • Fan, J.Q.1    Ishii, S.2    Asano, N.3    Suzuki, Y.4
  • 43
    • 84890320564 scopus 로고    scopus 로고
    • Treatment of human fibroblasts carrying NPC1 missense mutations with MG132 leads to an improvement of intracellular cholesterol trafficking
    • Zampieri, S., B. Bembi, N. Rosso, M. Filocamo, and A. Dardis. 2012. Treatment of human fibroblasts carrying NPC1 missense mutations with MG132 leads to an improvement of intracellular cholesterol trafficking. JIMD Rep. 2: 59-69.
    • (2012) JIMD Rep. , vol.2 , pp. 59-69
    • Zampieri, S.1    Bembi, B.2    Rosso, N.3    Filocamo, M.4    Dardis, A.5
  • 45
    • 84872541302 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors increase glucocerebrosidase activity in Gaucher disease by modulation of molecular chaperones
    • Yang, C., S. Rahimpour, J. Lu, K. Pacak, B. Ikejiri, R. O. Brady, and Z. Zhuang. 2013. Histone deacetylase inhibitors increase glucocerebrosidase activity in Gaucher disease by modulation of molecular chaperones. Proc. Natl. Acad. Sci. USA. 110: 966-971.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 966-971
    • Yang, C.1    Rahimpour, S.2    Lu, J.3    Pacak, K.4    Ikejiri, B.5    Brady, R.O.6    Zhuang, Z.7
  • 46
    • 66849109082 scopus 로고    scopus 로고
    • Transcriptional induction of GRP78/BiP by histone deacetylase inhibitors and resistance to histone deacetylase inhibitor-induced apoptosis
    • Baumeister, P., D. Dong, Y. Fu, and A. S. Lee. 2009. Transcriptional induction of GRP78/BiP by histone deacetylase inhibitors and resistance to histone deacetylase inhibitor-induced apoptosis. Mol. Cancer Ther. 8: 1086-1094.
    • (2009) Mol. Cancer Ther. , vol.8 , pp. 1086-1094
    • Baumeister, P.1    Dong, D.2    Fu, Y.3    Lee, A.S.4
  • 47
    • 0032513215 scopus 로고    scopus 로고
    • Proteasome inhibitors activate stress kinases and induce Hsp72. Diverse effects on apoptosis
    • Meriin, A. B., V. L. Gabai, J. Yaglom, V. I. Shifrin, and M. Y. Sherman. 1998. Proteasome inhibitors activate stress kinases and induce Hsp72. Diverse effects on apoptosis. J. Biol. Chem. 273: 6373-6379.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6373-6379
    • Meriin, A.B.1    Gabai, V.L.2    Yaglom, J.3    Shifrin, V.I.4    Sherman, M.Y.5
  • 48
    • 84891929380 scopus 로고    scopus 로고
    • Celastrol increases glucocerebrosidase activity in Gaucher disease by modulating molecular chaperones
    • Yang, C., C. L. Swallows, C. Zhang, J. Lu, H. Xiao, R. O. Brady, and Z. Zhuang. 2014. Celastrol increases glucocerebrosidase activity in Gaucher disease by modulating molecular chaperones. Proc. Natl. Acad. Sci. USA. 111: 249-254.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 249-254
    • Yang, C.1    Swallows, C.L.2    Zhang, C.3    Lu, J.4    Xiao, H.5    Brady, R.O.6    Zhuang, Z.7
  • 49
    • 84866156846 scopus 로고    scopus 로고
    • The therapeutic potential of pharmacological chaperones and proteosomal inhibitors, Celastrol and MG132 in the treatment of sialidosis
    • O'Leary, E. M., and S. A. Igdoura. 2012. The therapeutic potential of pharmacological chaperones and proteosomal inhibitors, Celastrol and MG132 in the treatment of sialidosis. Mol. Genet. Metab. 107: 173-185.
    • (2012) Mol. Genet. Metab. , vol.107 , pp. 173-185
    • O'Leary, E.M.1    Igdoura, S.A.2
  • 50
    • 84862965909 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors prevent the degradation and restore the activity of glucocerebrosidase in Gaucher disease
    • Lu, J., C. Yang, M. Chen, D. Y. Ye, R. R. Lonser, R. O. Brady, and Z. Zhuang. 2011. Histone deacetylase inhibitors prevent the degradation and restore the activity of glucocerebrosidase in Gaucher disease. Proc. Natl. Acad. Sci. USA. 108: 21200-21205.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 21200-21205
    • Lu, J.1    Yang, C.2    Chen, M.3    Ye, D.Y.4    Lonser, R.R.5    Brady, R.O.6    Zhuang, Z.7
  • 52
    • 77951924919 scopus 로고    scopus 로고
    • Lysosomal degradation of membrane lipids
    • Kolter, T., and K. Sandhoff. 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
  • 53
    • 77953499076 scopus 로고    scopus 로고
    • Multi-system disorders of glycosphingolipid and ganglioside metabolism
    • Xu, Y.-H., S. Barnes, Y. Sun, and G. A. Grabowski. 2010. Multi-system disorders of glycosphingolipid and ganglioside metabolism. J. Lipid Res. 51: 1643-1675.
    • (2010) J. Lipid Res. , vol.51 , pp. 1643-1675
    • Xu, Y.-H.1    Barnes, S.2    Sun, Y.3    Grabowski, G.A.4
  • 54
    • 62949156035 scopus 로고    scopus 로고
    • Secondary lipid accumulation in lysosomal disease
    • Walkley, S. U., and M. T. Vanier. 2009. Secondary lipid accumulation in lysosomal disease. Biochim. Biophys. Acta. 1793: 726-736.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 726-736
    • Walkley, S.U.1    Vanier, M.T.2
  • 55
    • 82755181717 scopus 로고    scopus 로고
    • The cellular pathology of lysosomal diseases
    • Cox, T. M., and M. B. Cachón-González. 2012. The cellular pathology of lysosomal diseases. J. Pathol. 226: 241-254.
    • (2012) J. Pathol. , vol.226 , pp. 241-254
    • Cox, T.M.1    Cachón-González, M.B.2
  • 56
    • 77951727293 scopus 로고    scopus 로고
    • Lipids on trial: The search for the offending metabolite in Niemann-Pick type C disease
    • Lloyd-Evans, E., and F. M. Platt. 2010. Lipids on trial: the search for the offending metabolite in Niemann-Pick type C disease. Traffic. 11: 419-428.
    • (2010) Traffic , vol.11 , pp. 419-428
    • Lloyd-Evans, E.1    Platt, F.M.2
  • 59
    • 84899957348 scopus 로고    scopus 로고
    • High sphingomyelin levels induce lysosomal damage and autophagy dysfunction in Niemann Pick disease type A
    • Gabandé-Rodríguez, E., P. Boya, V. Labrador, C. G. Dotti, and M. D. Ledesma. 2014. High sphingomyelin levels induce lysosomal damage and autophagy dysfunction in Niemann Pick disease type A. Cell Death Differ. 21: 864-875.
    • (2014) Cell Death Differ , vol.21 , pp. 864-875
    • Gabandé-Rodríguez, E.1    Boya, P.2    Labrador, V.3    Dotti, C.G.4    Ledesma, M.D.5
  • 60
    • 77954164469 scopus 로고    scopus 로고
    • Connecting Hsp70, sphingolipid metabolism and lysosomal stability
    • Petersen, N. H. T., T. Kirkegaard, O. D. Olsen, and M. Jäättelä. 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    Kirkegaard, T.2    Olsen, O.D.3    Jäättelä, M.4
  • 61
    • 77953142003 scopus 로고    scopus 로고
    • Improvement in lipid and protein trafficking in Niemann-Pick C1 cells by correction of a secondary enzyme defect
    • Devlin, C., N. H. Pipalia, X. Liao, E. H. Schuchman, F. R. Maxfield, and I. Tabas. 2010. Improvement in lipid and protein trafficking in Niemann-Pick C1 cells by correction of a secondary enzyme defect. Traffic. 11: 601-615.
    • (2010) Traffic , vol.11 , pp. 601-615
    • Devlin, C.1    Pipalia, N.H.2    Liao, X.3    Schuchman, E.H.4    Maxfield, F.R.5    Tabas, I.6
  • 62
    • 78649743957 scopus 로고    scopus 로고
    • HSP70 and lysosomal storage disorders: Novel therapeutic opportunities
    • Petersen, N. H. T., and T. Kirkegaard. 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.T.1    Kirkegaard, T.2
  • 63
    • 62949116803 scopus 로고    scopus 로고
    • Lysosomal disorders: From storage to cellular damage
    • Ballabio, A., and V. Gieselmann. 2009. Lysosomal disorders: from storage to cellular damage. Biochim. Biophys. Acta. 1793: 684-696.
    • (2009) Biochim. Biophys. Acta. , vol.1793 , pp. 684-696
    • Ballabio, A.1    Gieselmann, V.2
  • 64
    • 84882254367 scopus 로고    scopus 로고
    • The role of autophagy in neurodegenerative disease
    • Nixon, R. A. 2013. The role of autophagy in neurodegenerative disease. Nat. Med. 19: 983-997.
    • (2013) Nat. Med. , vol.19 , pp. 983-997
    • Nixon, R.A.1
  • 65
    • 84893639063 scopus 로고    scopus 로고
    • Stuck in traffic: An emerging theme in diseases of the nervous system
    • Neefjes, J., and R. van der Kant. 2014. Stuck in traffic: an emerging theme in diseases of the nervous system. Trends Neurosci. 37: 66-76.
    • (2014) Trends Neurosci. , vol.37 , pp. 66-76
    • Neefjes, J.1    Van Der Kant, R.2
  • 67
    • 84879309945 scopus 로고    scopus 로고
    • Lysosomal membrane permeability stimulates protein aggregate formation in neurons of a lysosomal disease
    • Micsenyi, M. C., J. Sikora, G. Stephney, K. Dobrenis, and S. U. Walkley. 2013. Lysosomal membrane permeability stimulates protein aggregate formation in neurons of a lysosomal disease. J. Neurosci. 33: 10815-10827.
    • (2013) J. Neurosci. , vol.33 , pp. 10815-10827
    • Micsenyi, M.C.1    Sikora, J.2    Stephney, G.3    Dobrenis, K.4    Walkley, S.U.5
  • 69
    • 73549105909 scopus 로고    scopus 로고
    • Increased activity and altered subcellular distribution of lysosomal enzymes determine neuronal vulnerability in Niemann-Pick type C1-deficient mice
    • Amritraj, A., K. Peake, A. Kodam, C. Salio, A. Merighi, J. E. Vance, and S. Kar. 2009. Increased activity and altered subcellular distribution of lysosomal enzymes determine neuronal vulnerability in Niemann-Pick type C1-deficient mice. Am. J. Pathol. 175: 2540-2556.
    • (2009) Am. J. Pathol. , vol.175 , pp. 2540-2556
    • Amritraj, A.1    Peake, K.2    Kodam, A.3    Salio, C.4    Merighi, A.5    Vance, J.E.6    Kar, S.7
  • 70
    • 33646442373 scopus 로고    scopus 로고
    • Co-localization hypothesis: A mechanism for the intrapancreatic activation of digestive enzymes during the early phases of acute pancreatitis
    • van Acker, G. J., G. Perides, and M. L. Steer. 2006. Co-localization hypothesis: a mechanism for the intrapancreatic activation of digestive enzymes during the early phases of acute pancreatitis. World J. Gastroenterol. 12: 1985-1990.
    • (2006) World J. Gastroenterol. , vol.12 , pp. 1985-1990
    • Van Acker, G.J.1    Perides, G.2    Steer, M.L.3
  • 71
    • 84878643872 scopus 로고    scopus 로고
    • Lysosomal cell death at a glance
    • Aits, S., and M. Jäättelä. 2013. Lysosomal cell death at a glance. J. Cell Sci. 126: 1905-1912.
    • (2013) J. Cell Sci. , vol.126 , pp. 1905-1912
    • Aits, S.1    Jäättelä, M.2
  • 72
    • 77954519532 scopus 로고    scopus 로고
    • Redox activity within the lysosomal compartment: Implications for aging and apoptosis
    • Kurz, T., J. W. Eaton, and U. T. Brunk. 2010. Redox activity within the lysosomal compartment: implications for aging and apoptosis. Antioxid. Redox Signal. 13: 511-523.
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 511-523
    • Kurz, T.1    Eaton, J.W.2    Brunk, U.T.3
  • 74
    • 33745205646 scopus 로고    scopus 로고
    • Intralysosomal iron chelation protects against oxidative stress-induced cellular damage
    • Kurz, T., B. Gustafsson, and U. T. Brunk. 2006. Intralysosomal iron chelation protects against oxidative stress-induced cellular damage. FEBS J. 273: 3106-3117.
    • (2006) FEBS J , vol.273 , pp. 3106-3117
    • Kurz, T.1    Gustafsson, B.2    Brunk, U.T.3
  • 75
    • 53749095321 scopus 로고    scopus 로고
    • Globotriaosylceramide induces oxidative stress and up-regulates cell adhesion molecule expression in Fabry disease endothelial cells
    • Shen, J-S. 2008. Globotriaosylceramide induces oxidative stress and up-regulates cell adhesion molecule expression in Fabry disease endothelial cells. Mol. Genet. Metab. 95: 163-168.
    • (2008) Mol. Genet. Metab. , vol.95 , pp. 163-168
    • Shen, J.-S.1
  • 76
    • 84861552789 scopus 로고    scopus 로고
    • Contribution of brain inflammation to neuronal cell death in neuronopathic forms of Gaucher's disease
    • Vitner, E. B., T. Farfel-Becker, R. Eilam, I. Biton, and A. H. Futerman. 2012. Contribution of brain inflammation to neuronal cell death in neuronopathic forms of Gaucher's disease. Brain. 135: 1724-1735.
    • (2012) Brain , vol.135 , pp. 1724-1735
    • Vitner, E.B.1    Farfel-Becker, T.2    Eilam, R.3    Biton, I.4    Futerman, A.H.5
  • 81
    • 64049091512 scopus 로고    scopus 로고
    • Hsp70 and cardiac surgery: Molecular chaperone and inflammatory regulator with compartmentalized effects
    • de Jong, P. R., A. W. L. Schadenberg, N. J. G. Jansen, and B. J. Prakken. 2009. Hsp70 and cardiac surgery: molecular chaperone and inflammatory regulator with compartmentalized effects. Cell Stress Chaperones. 14: 117-131.
    • (2009) Cell Stress Chaperones , vol.14 , pp. 117-131
    • De Jong, P.R.1    Schadenberg, A.W.L.2    Jansen, N.J.G.3    Prakken, B.J.4
  • 82
    • 0035887215 scopus 로고    scopus 로고
    • Sphingosine-induced apoptosis is dependent on lysosomal proteases
    • Kågedal, K., M. Zhao, I. Svensson, and U. T. Brunk. 2001. Sphingosine-induced apoptosis is dependent on lysosomal proteases. Biochem. J. 359: 335-343.
    • (2001) Biochem. J. , vol.359 , pp. 335-343
    • Kågedal, K.1    Zhao, M.2    Svensson, I.3    Brunk, U.T.4
  • 84
    • 84861436735 scopus 로고    scopus 로고
    • Sphingosine mediates TNFα-induced lysosomal membrane permeabilization and ensuing programmed cell death in hepatoma cells
    • Ullio, C., J. Casas, U. T. Brunk, G. Sala, G. Fabriàs, R. Ghidoni, G. Bonelli, F. M. Baccino, and R. Autelli. 2012. Sphingosine mediates TNFα-induced lysosomal membrane permeabilization and ensuing programmed cell death in hepatoma cells. J. Lipid Res. 53: 1134-1143.
    • (2012) J. Lipid Res. , vol.53 , pp. 1134-1143
    • Ullio, C.1    Casas, J.2    Brunk, U.T.3    Sala, G.4    Fabriàs, G.5    Ghidoni, R.6    Bonelli, G.7    Baccino, F.M.8    Autelli, R.9
  • 86
    • 33746099657 scopus 로고    scopus 로고
    • Effects of arachidonic acid on the lysosomal ion permeability and osmotic stability
    • Zhang, G., Y-P. Yi, and G-J. Zhang. 2006. Effects of arachidonic acid on the lysosomal ion permeability and osmotic stability. J. Bioenerg. Biomembr. 38: 75-82.
    • (2006) J. Bioenerg. Biomembr. , vol.38 , pp. 75-82
    • Zhang, G.1    Yi, Y.-P.2    Zhang, G.-J.3
  • 87
    • 77951910348 scopus 로고    scopus 로고
    • Ceramide-rich platforms in transmembrane signaling
    • Stancevic, B., and R. Kolesnick. 2010. Ceramide-rich platforms in transmembrane signaling. FEBS Lett. 584: 1728-1740.
    • (2010) FEBS Lett. , vol.584 , pp. 1728-1740
    • Stancevic, B.1    Kolesnick, R.2
  • 89
    • 0026703222 scopus 로고
    • Major heat shock protein hsp70 protects tumor cells from tumor necrosis factor cytotoxicity
    • Jäättelä, M., D. Wissing, P. A. Bauer, and G. C. Li. 1992. Major heat shock protein hsp70 protects tumor cells from tumor necrosis factor cytotoxicity. EMBO J. 11: 3507-3512.
    • (1992) EMBO J , vol.11 , pp. 3507-3512
    • Jäättelä, M.1    Wissing, D.2    Bauer, P.A.3    Li, G.C.4
  • 90
    • 38449100535 scopus 로고    scopus 로고
    • Extracellular heat shock proteins in cell signaling and immunity
    • Calderwood, S. K., S. S. Mambula, and P. J. Gray, Jr. 2007. Extracellular heat shock proteins in cell signaling and immunity. Ann. N. Y. Acad. Sci. 1113: 28-39
    • (2007) Ann. N. Y. Acad. Sci. , vol.1113 , pp. 28-39
    • Calderwood, S.K.1    Mambula, S.S.2    Gray, P.J.3
  • 91
    • 10044269628 scopus 로고    scopus 로고
    • Defective lysosomal exocytosis and plasma membrane repair in Chediak-Higashi/beige cells
    • Huynh, C., D. Roth, D. M. Ward, J. Kaplan, and N. W. Andrews. 2004. Defective lysosomal exocytosis and plasma membrane repair in Chediak-Higashi/beige cells. Proc. Natl. Acad. Sci. USA. 101: 16795-16800.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16795-16800
    • Huynh, C.1    Roth, D.2    Ward, D.M.3    Kaplan, J.4    Andrews, N.W.5
  • 94
    • 0942265544 scopus 로고    scopus 로고
    • Selective disruption of lysosomes in HeLa cells triggers apoptosis mediated by cleavage of Bid by multiple papain-like lysosomal cathepsins
    • Cirman, T., K. Oresic, G. D. Mazovec, V. Turk, J. C. Reed, R. M. Myers, G. S. Salvesen, and B. Turk. 2004. Selective disruption of lysosomes in HeLa cells triggers apoptosis mediated by cleavage of Bid by multiple papain-like lysosomal cathepsins. J. Biol. Chem. 279: 3578-3587.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3578-3587
    • Cirman, T.1    Oresic, K.2    Mazovec, G.D.3    Turk, V.4    Reed, J.C.5    Myers, R.M.6    Salvesen, G.S.7    Turk, B.8
  • 95
    • 0030757986 scopus 로고    scopus 로고
    • Photo-oxidative disruption of lysosomal membranes causes apoptosis of cultured human fibroblasts
    • Brunk, U. T., H. Dalen, K. Roberg, and H. B. Hellquist. 1997. Photo-oxidative disruption of lysosomal membranes causes apoptosis of cultured human fibroblasts. Free Radic. Biol. Med. 23: 616-626.
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 616-626
    • Brunk, U.T.1    Dalen, H.2    Roberg, K.3    Hellquist, H.B.4
  • 96
    • 0035366499 scopus 로고    scopus 로고
    • Apoptosis induced by exposure to a low steady-state concentration of H2O2 is a consequence of lysosomal rupture
    • Antunes, F., E. Cadenas, and U. T. Brunk. 2001. Apoptosis induced by exposure to a low steady-state concentration of H2O2 is a consequence of lysosomal rupture. Biochem. J. 356: 549-555.
    • (2001) Biochem. J. , vol.356 , pp. 549-555
    • Antunes, F.1    Cadenas, E.2    Brunk, U.T.3
  • 98
    • 0032476668 scopus 로고    scopus 로고
    • Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases
    • Jäättelä, M., D. Wissing, K. Kokholm, T. Kallunki, and M. Egeblad. 1998. Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases. EMBO J. 17: 6124-6134.
    • (1998) EMBO J. , vol.17 , pp. 6124-6134
    • Jäättelä, M.1    Wissing, D.2    Kokholm, K.3    Kallunki, T.4    Egeblad, M.5
  • 103
    • 84988024893 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof.
  • 106
    • 84876113312 scopus 로고    scopus 로고
    • Role of endogenous psychosine accumulation in oligodendrocyte differentiation and survival: Implication for Krabbe disease
    • Won, J-S., J. Kim, M. K. Paintlia, I. Singh, and A. K. Singh. 2013. Role of endogenous psychosine accumulation in oligodendrocyte differentiation and survival: implication for Krabbe disease. Brain Res. 1508: 44-52.
    • (2013) Brain Res. , vol.1508 , pp. 44-52
    • Won, J.-S.1    Kim, J.2    Paintlia, M.K.3    Singh, I.4    Singh, A.K.5
  • 107
    • 33746050965 scopus 로고    scopus 로고
    • Krabbe disease: Psychosine-mediated activation of phospholipase A2 in oligodendrocyte cell death
    • Giri, S., M. Khan, R. Rattan, I. Singh, and A. K. Singh. 2006. Krabbe disease: psychosine-mediated activation of phospholipase A2 in oligodendrocyte cell death. J. Lipid Res. 47: 1478-1492.
    • (2006) J. Lipid Res. , vol.47 , pp. 1478-1492
    • Giri, S.1    Khan, M.2    Rattan, R.3    Singh, I.4    Singh, A.K.5
  • 110
    • 0032988381 scopus 로고    scopus 로고
    • Oxidative stress, growth factor starvation and Fas activation may all cause apoptosis through lysosomal leak
    • Brunk, U. T., and I. Svensson. 1999. Oxidative stress, growth factor starvation and Fas activation may all cause apoptosis through lysosomal leak. Redox Rep. 4: 3-11.
    • (1999) Redox Rep. , vol.4 , pp. 3-11
    • Brunk, U.T.1    Svensson, I.2
  • 112
    • 0028108015 scopus 로고
    • Functional dichotomy of neutral and acidic sphingomyelinases in tumor necrosis factor signaling
    • Wiegmann, K., S. Schutze, T. Machleidt, D. Witte, and M. Kronke. 1994. Functional dichotomy of neutral and acidic sphingomyelinases in tumor necrosis factor signaling. Cell. 78: 1005-1015.
    • (1994) Cell. , vol.78 , pp. 1005-1015
    • Wiegmann, K.1    Schutze, S.2    Machleidt, T.3    Witte, D.4    Kronke, M.5
  • 114
    • 20444506408 scopus 로고    scopus 로고
    • Tumor necrosis factor induces the loss of sphingosine kinase-1 by a cathepsin B-dependent mechanism
    • Taha, T. A., K. Kitatani, J. Bielawski, W. Cho, Y. A. Hannun, and L. M. Obeid. 2005. Tumor necrosis factor induces the loss of sphingosine kinase-1 by a cathepsin B-dependent mechanism. J. Biol. Chem. 280: 17196-17202.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17196-17202
    • Taha, T.A.1    Kitatani, K.2    Bielawski, J.3    Cho, W.4    Hannun, Y.A.5    Obeid, L.M.6
  • 116
    • 0037131352 scopus 로고    scopus 로고
    • Cathepsin B mediates tumor necrosis factor-induced arachidonic acid release in tumor cells
    • Foghsgaard, L., U. Lademann, D. Wissing, B. Poulsen, and M. Jäättelä. 2002. Cathepsin B mediates tumor necrosis factor-induced arachidonic acid release in tumor cells. J. Biol. Chem. 277: 39499-39506.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39499-39506
    • Foghsgaard, L.1    Lademann, U.2    Wissing, D.3    Poulsen, B.4    Jäättelä, M.5
  • 118
    • 84987982982 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof.
  • 119
    • 0043032816 scopus 로고    scopus 로고
    • Inhibition of calcium uptake via the sarco/endoplasmic reticulum Ca2+-ATPase in a mouse model of Sandhoff disease and prevention by treatment with N-butyldeoxynojirimycin
    • Pelled, D., E. Lloyd-Evans, C. Riebeling, M. Jeyakumar, F. M. Platt, and A. H. Futerman. 2003. Inhibition of calcium uptake via the sarco/endoplasmic reticulum Ca2+-ATPase in a mouse model of Sandhoff disease and prevention by treatment with N-butyldeoxynojirimycin. J. Biol. Chem. 278: 29496-29501.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29496-29501
    • Pelled, D.1    Lloyd-Evans, E.2    Riebeling, C.3    Jeyakumar, M.4    Platt, F.M.5    Futerman, A.H.6
  • 120
    • 29144444023 scopus 로고    scopus 로고
    • Defective calcium homeostasis in the cerebellum in a mouse model of Niemann-Pick A disease
    • Ginzburg, L., and A. H. Futerman. 2005. Defective calcium homeostasis in the cerebellum in a mouse model of Niemann-Pick A disease. J. Neurochem. 95: 1619-1628.
    • (2005) J. Neurochem. , vol.95 , pp. 1619-1628
    • Ginzburg, L.1    Futerman, A.H.2
  • 121
    • 84855946896 scopus 로고    scopus 로고
    • Hsp70.1 and related lysosomal factors for necrotic neuronal death
    • Yamashima, T. 2012. Hsp70.1 and related lysosomal factors for necrotic neuronal death. J. Neurochem. 120: 477-494.
    • (2012) J. Neurochem. , vol.120 , pp. 477-494
    • Yamashima, T.1
  • 122
    • 77949488942 scopus 로고    scopus 로고
    • Calpain-mediated Hsp70.1 cleavage in hippocampal CA1 neuronal death
    • Sahara, S., and T. Yamashima. 2010. Calpain-mediated Hsp70.1 cleavage in hippocampal CA1 neuronal death. Biochem. Biophys. Res. Commun. 393: 806-811.
    • (2010) Biochem. Biophys. Res. Commun. , vol.393 , pp. 806-811
    • Sahara, S.1    Yamashima, T.2
  • 123
    • 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., Y. Kohda, K. Tsuchiya, T. Ueno, J. Yamashita, T. Yoshioka, and E. Kominami. 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    Kohda, Y.2    Tsuchiya, K.3    Ueno, T.4    Yamashita, J.5    Yoshioka, T.6    Kominami, E.7
  • 124
    • 0037206901 scopus 로고    scopus 로고
    • Specific aspartyl and calpain proteases are required for neurodegeneration in C. elegans
    • Syntichaki, P., K. Xu, M. Driscoll, and N. Tavernarakis. 2002. Specific aspartyl and calpain proteases are required for neurodegeneration in C. elegans. Nature. 419: 939-944.
    • (2002) Nature , vol.419 , pp. 939-944
    • Syntichaki, P.1    Xu, K.2    Driscoll, M.3    Tavernarakis, N.4
  • 125
    • 0037184523 scopus 로고    scopus 로고
    • NAADP mobilizes Ca(2+) from reserve granules, lysosome-related organelles, in sea urchin eggs
    • Churchill, G. C., Y. Okada, J. M. Thomas, A. A. Genazzani, S. Patel, and A. Galione. 2002. NAADP mobilizes Ca(2+) from reserve granules, lysosome-related organelles, in sea urchin eggs. Cell. 111: 703-708.
    • (2002) Cell. , vol.111 , pp. 703-708
    • Churchill, G.C.1    Okada, Y.2    Thomas, J.M.3    Genazzani, A.A.4    Patel, S.5    Galione, A.6
  • 129
    • 84884559258 scopus 로고    scopus 로고
    • Interplay between autophagy and programmed cell death in mammalian neural stem cells
    • Chung, K. M., and S-W. Yu. 2013. Interplay between autophagy and programmed cell death in mammalian neural stem cells. BMB Rep. 46: 383-390.
    • (2013) BMB Rep. , vol.46 , pp. 383-390
    • Chung, K.M.1    Yu, S.-W.2
  • 130
    • 77649211816 scopus 로고    scopus 로고
    • Disease pathogenesis explained by basic science: Lysosomal storage diseases as autophagocytic disorders
    • Ballabio, A. 2009. Disease pathogenesis explained by basic science: lysosomal storage diseases as autophagocytic disorders. Int. J. Clin. Pharmacol. Ther. 47 ( Suppl 1 ): S34-S38.
    • (2009) Int. J. Clin. Pharmacol. Ther. , vol.47 , pp. S34-S38
    • Ballabio, A.1
  • 131
    • 59649104665 scopus 로고    scopus 로고
    • Monitoring autophagy in lysosomal storage disorders
    • Raben, N., L. Shea, V. Hill, and P. Plotz. 2009. Monitoring autophagy in lysosomal storage disorders. Methods Enzymol. 453: 417-449.
    • (2009) Methods Enzymol. , vol.453 , pp. 417-449
    • Raben, N.1    Shea, L.2    Hill, V.3    Plotz, P.4
  • 132
    • 79551609332 scopus 로고    scopus 로고
    • BAG3 mediates chaperone-based aggresome-targeting and selective autophagy of misfolded proteins
    • Gamerdinger, M., A. M. Kaya, U. Wolfrum, A. M. Clement, and C. Behl. 2011. BAG3 mediates chaperone-based aggresome-targeting and selective autophagy of misfolded proteins. EMBO Rep. 12: 149-156.
    • (2011) EMBO Rep. , vol.12 , pp. 149-156
    • Gamerdinger, M.1    Kaya, A.M.2    Wolfrum, U.3    Clement, A.M.4    Behl, C.5
  • 133
    • 66149118221 scopus 로고    scopus 로고
    • HSF1-mediated BAG3 expression attenuates apoptosis in 4-hydroxynonenal-treated colon cancer cells via stabilization of anti-apoptotic Bcl-2 proteins
    • Jacobs, A. T., and L. J. Marnett. 2009. HSF1-mediated BAG3 expression attenuates apoptosis in 4-hydroxynonenal-treated colon cancer cells via stabilization of anti-apoptotic Bcl-2 proteins. J. Biol. Chem. 284: 9176-9183.
    • (2009) J. Biol. Chem. , vol.284 , pp. 9176-9183
    • Jacobs, A.T.1    Marnett, L.J.2
  • 134
    • 84878225041 scopus 로고    scopus 로고
    • Regulatory coordination between two major intracellular homeostatic systems: Heat shock response and autophagy
    • Dokladny, K., M. N. Zuhl, M. Mandell, D. Bhattacharya, S. Schneider, V. Deretic, and P. L. Moseley. 2013. Regulatory coordination between two major intracellular homeostatic systems: heat shock response and autophagy. J. Biol. Chem. 288: 14959-14972.
    • (2013) J. Biol. Chem. , vol.288 , pp. 14959-14972
    • Dokladny, K.1    Zuhl, M.N.2    Mandell, M.3    Bhattacharya, D.4    Schneider, S.5    Deretic, V.6    Moseley, P.L.7
  • 135
    • 84873578783 scopus 로고    scopus 로고
    • Alterations in ROS activity and lysosomal pH account for distinct patterns of macroautophagy in LINCL and JNCL fibroblasts
    • Vidal-Donet, J. M., J. Cárcel-Trullols, B. Casanova, C. Aguado, and E. Knecht. 2013. Alterations in ROS activity and lysosomal pH account for distinct patterns of macroautophagy in LINCL and JNCL fibroblasts. PLoS ONE. 8:e55526.
    • (2013) PLoS ONE , vol.8
    • Vidal-Donet, J.M.1    Cárcel-Trullols, J.2    Casanova, B.3    Aguado, C.4    Knecht, E.5
  • 136
    • 77953319336 scopus 로고    scopus 로고
    • GT1b-induced neurotoxicity is mediated by the Akt/GSK-3/tau signaling pathway but not caspase-3 in mesencephalic dopaminergic neurons
    • Chung, E. S., E. Bok, S. Sohn, Y. D. Lee, H. H. Baik, and B. K. Jin. 2010. GT1b-induced neurotoxicity is mediated by the Akt/GSK-3/tau signaling pathway but not caspase-3 in mesencephalic dopaminergic neurons. BMC Neurosci. 11: 74.
    • (2010) BMC Neurosci , vol.11 , pp. 74
    • Chung, E.S.1    Bok, E.2    Sohn, S.3    Lee, Y.D.4    Baik, H.H.5    Jin, B.K.6
  • 137
    • 0036544646 scopus 로고    scopus 로고
    • Trisialoganglioside GT1b induces in vivo degeneration of nigral dopaminergic neurons: Role of microglia
    • Ryu, J. K., W. H. Shin, J. Kim, E. H. Joe, Y. B. Lee, K. G. Cho, Y. J. Oh, S. U. Kim, and B. K. Jin. 2002. Trisialoganglioside GT1b induces in vivo degeneration of nigral dopaminergic neurons: role of microglia. Glia. 38: 15-23.
    • (2002) Glia , vol.38 , pp. 15-23
    • Ryu, J.K.1    Shin, W.H.2    Kim, J.3    Joe, E.H.4    Lee, Y.B.5    Cho, K.G.6    Oh, Y.J.7    Kim, S.U.8    Jin, B.K.9
  • 138
    • 77951885857 scopus 로고    scopus 로고
    • Brain gangliosides in axon-myelin stability and axon regeneration
    • Schnaar, R. L. 2010. Brain gangliosides in axon-myelin stability and axon regeneration. FEBS Lett. 584: 1741-1747.
    • (2010) FEBS Lett. , vol.584 , pp. 1741-1747
    • Schnaar, R.L.1
  • 140
    • 30844445379 scopus 로고    scopus 로고
    • Inhibitory effect of ganglioside GD1b on K+ current in hippocampal neurons and its involvement in apoptosis suppression
    • Chen, X., S. Chi, M. Liu, W. Yang, T. Wei, Z. Qi, and F. Yang. 2005. Inhibitory effect of ganglioside GD1b on K+ current in hippocampal neurons and its involvement in apoptosis suppression. J. Lipid Res. 46: 2580-2585.
    • (2005) J. Lipid Res. , vol.46 , pp. 2580-2585
    • Chen, X.1    Chi, S.2    Liu, M.3    Yang, W.4    Wei, T.5    Qi, Z.6    Yang, F.7
  • 143
    • 70449088871 scopus 로고    scopus 로고
    • GM1-ganglioside accumulation at the mitochondria-associated ER membranes links ER stress to Ca2+-dependent mitochondrial apoptosis
    • Sano, R., I. Annunziata, A. Patterson, S. Moshiach, E. Gomero, J. Opferman, M. Forte, and A. d'Azzo. 2009. GM1-ganglioside accumulation at the mitochondria-associated ER membranes links ER stress to Ca2+-dependent mitochondrial apoptosis. Mol. Cell. 36: 500-511.
    • (2009) Mol. Cell. , vol.36 , pp. 500-511
    • Sano, R.1    Annunziata, I.2    Patterson, A.3    Moshiach, S.4    Gomero, E.5    Opferman, J.6    Forte, M.7    D'Azzo, A.8
  • 144
    • 0032792684 scopus 로고    scopus 로고
    • Antagonistic effect of ganglioside GM1 and GM3 on the activity and conformation of sarcoplasmic reticulum Ca(2+)-ATPase
    • Wang, Y., Z. Tsui, and F. Yang. 1999. Antagonistic effect of ganglioside GM1 and GM3 on the activity and conformation of sarcoplasmic reticulum Ca(2+)-ATPase. FEBS Lett. 457: 144-148.
    • (1999) FEBS Lett. , vol.457 , pp. 144-148
    • Wang, Y.1    Tsui, Z.2    Yang, F.3
  • 145
    • 0030804867 scopus 로고    scopus 로고
    • Gangliosides enhance KCl-induced Ca2+ influx and acetylcholine release in brain synaptosomes
    • Tanaka, Y., H. Waki, K. Kon, and S. Ando. 1997. Gangliosides enhance KCl-induced Ca2+ influx and acetylcholine release in brain synaptosomes. Neuroreport. 8: 2203-2207.
    • (1997) Neuroreport , vol.8 , pp. 2203-2207
    • Tanaka, Y.1    Waki, H.2    Kon, K.3    Ando, S.4
  • 147
    • 33645237744 scopus 로고    scopus 로고
    • Gangliosides of the nuclear membrane: A crucial locus of cytoprotective modulation
    • Ledeen, R. W., and G. Wu. 2006. Gangliosides of the nuclear membrane: a crucial locus of cytoprotective modulation. J. Cell. Biochem. 97: 893-903.
    • (2006) J. Cell. Biochem. , vol.97 , pp. 893-903
    • Ledeen, R.W.1    Wu, G.2
  • 148
    • 0031760241 scopus 로고    scopus 로고
    • Effect of the mono- and tetrasialogangliosides, GM1 and GQ1b, on long-term potentiation in the CA1 hippocampal neurons of the guinea pig
    • Furuse, H., H. Waki, K. Kaneko, S. Fujii, M. Miura, H. Sasaki, K-I. Ito, H. Kato, and S. Ando. 1998. Effect of the mono- and tetrasialogangliosides, GM1 and GQ1b, on long-term potentiation in the CA1 hippocampal neurons of the guinea pig. Exp. Brain Res. 123: 307-314.
    • (1998) Exp. Brain Res. , vol.123 , pp. 307-314
    • Furuse, H.1    Waki, H.2    Kaneko, K.3    Fujii, S.4    Miura, M.5    Sasaki, H.6    Ito, K.-I.7    Kato, H.8    Ando, S.9
  • 149
    • 7244242544 scopus 로고    scopus 로고
    • Susceptibility of cerebellar granule neurons from GM2/GD2 synthase-null mice to apoptosis induced by glutamate excitotoxicity and elevated KCl: Rescue by GM1 and LIGA20
    • Wu, G., Z-H. Lu, X. Xie, and R. W. Ledeen. 2004. Susceptibility of cerebellar granule neurons from GM2/GD2 synthase-null mice to apoptosis induced by glutamate excitotoxicity and elevated KCl: rescue by GM1 and LIGA20. Glycoconj. J. 21: 305-313.
    • (2004) Glycoconj. J. , vol.21 , pp. 305-313
    • Wu, G.1    Lu, Z.-H.2    Xie, X.3    Ledeen, R.W.4
  • 150
    • 0034928839 scopus 로고    scopus 로고
    • GM2 ganglioside regulates the function of ciliary neurotrophic factor receptor in murine immortalized motor neuron-like cells (NSC-34)
    • Usuki, S., J. Ren, I. Utsunomiya, N. R. Cashman, J. Inokuchi, and T. Miyatake. 2001. GM2 ganglioside regulates the function of ciliary neurotrophic factor receptor in murine immortalized motor neuron-like cells (NSC-34). Neurochem. Res. 26: 375-382.
    • (2001) Neurochem. Res. , vol.26 , pp. 375-382
    • Usuki, S.1    Ren, J.2    Utsunomiya, I.3    Cashman, N.R.4    Inokuchi, J.5    Miyatake, T.6
  • 151
    • 0032950195 scopus 로고    scopus 로고
    • GM2 promotes ciliary neurotrophic factor-dependent rescue of immortalized motor neuron-like cell (NSC-34)
    • Usuki, S., N. R. Cashman, and T. Miyatake. 1999. GM2 promotes ciliary neurotrophic factor-dependent rescue of immortalized motor neuron-like cell (NSC-34). Neurochem. Res. 24: 281-286.
    • (1999) Neurochem. Res. , vol.24 , pp. 281-286
    • Usuki, S.1    Cashman, N.R.2    Miyatake, T.3
  • 153
    • 0035976976 scopus 로고    scopus 로고
    • Regulation of apoptosis during neuronal differentiation by ceramide and b-series complex gangliosides
    • Bieberich, E., S. MacKinnon, J. Silva, and R. K. Yu. 2001. Regulation of apoptosis during neuronal differentiation by ceramide and b-series complex gangliosides. J. Biol. Chem. 276: 44396-44404.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44396-44404
    • Bieberich, E.1    MacKinnon, S.2    Silva, J.3    Yu, R.K.4
  • 155
    • 67650088127 scopus 로고    scopus 로고
    • Neurotrophic and neuroprotective actions of an enhancer of ganglioside biosynthesis
    • Inokuchi, J. 2009. Neurotrophic and neuroprotective actions of an enhancer of ganglioside biosynthesis. Int. Rev. Neurobiol. 85: 319-336.
    • (2009) Int. Rev. Neurobiol. , vol.85 , pp. 319-336
    • Inokuchi, J.1
  • 156
    • 77951211369 scopus 로고    scopus 로고
    • GD3 synthase overexpression sensitizes hepatocarcinoma cells to hypoxia and reduces tumor growth by suppressing the cSrc/NF-kappaB survival pathway
    • Lluis, J. M., L. Llacuna, C. von Montfort, C. Bárcena, C. Enrich, A. Morales, and J. C. Fernandez-Checa. 2009. GD3 synthase overexpression sensitizes hepatocarcinoma cells to hypoxia and reduces tumor growth by suppressing the cSrc/NF-kappaB survival pathway. PLoS ONE. 4:e8059.
    • (2009) PLoS ONE , vol.4
    • Lluis, J.M.1    Llacuna, L.2    Von Montfort, C.3    Bárcena, C.4    Enrich, C.5    Morales, A.6    Fernandez-Checa, J.C.7
  • 157
    • 66149137283 scopus 로고    scopus 로고
    • GD3, an overexpressed tumor-derived ganglioside, mediates the apoptosis of activated but not resting T cells
    • Sa, G., T. Das, C. Moon, C. M. Hilston, P.A. Rayman, B. I. Rini, C. S. Tannenbaum, and J. H. Finke. 2009. GD3, an overexpressed tumor-derived ganglioside, mediates the apoptosis of activated but not resting T cells. Cancer Res. 69:3095-3104.
    • (2009) Cancer Res. , vol.69 , pp. 3095-3104
    • Sa, G.1    Das, T.2    Moon, C.3    Hilston, C.M.4    Rayman, P.A.5    Rini, B.I.6    Tannenbaum, C.S.7    Finke, J.H.8
  • 158
    • 0035906841 scopus 로고    scopus 로고
    • Synthesis of ganglioside GD3 and its comparison with bovine GD3 with regard to oligodendrocyte apoptosis mitochondrial damage
    • Castro-Palomino, J. C., B. Simon, O. Speer, M. Leist, and R. R. Schmidt. 2001. Synthesis of ganglioside GD3 and its comparison with bovine GD3 with regard to oligodendrocyte apoptosis mitochondrial damage. Chemistry. 7: 2178-2184.
    • (2001) Chemistry , vol.7 , pp. 2178-2184
    • Castro-Palomino, J.C.1    Simon, B.2    Speer, O.3    Leist, M.4    Schmidt, R.R.5
  • 160
    • 21644474053 scopus 로고    scopus 로고
    • Glycosphingolipid accumulation inhibits cholesterol efflux via the ABCA1/apolipoprotein A-I pathway: 1-phenyl-2-decanoylamino-3-morpholino-1-propanol is a novel cholesterol efflux accelerator
    • Glaros, E. N., W. S. Kim, C. M. Quinn, J. Wong, I. Gelissen, W. Jessup, and B. Garner. 2005. Glycosphingolipid accumulation inhibits cholesterol efflux via the ABCA1/apolipoprotein A-I pathway: 1-phenyl-2-decanoylamino-3-morpholino-1-propanol is a novel cholesterol efflux accelerator. J. Biol. Chem. 280: 24515-24523.
    • (2005) J. Biol. Chem. , vol.280 , pp. 24515-24523
    • Glaros, E.N.1    Kim, W.S.2    Quinn, C.M.3    Wong, J.4    Gelissen, I.5    Jessup, W.6    Garner, B.7
  • 161
    • 41649103930 scopus 로고    scopus 로고
    • Fusogenicity of membranes: The impact of acid sphingomyelinase on innate immune responses
    • Utermöhlen, O., J. Herz, M. Schramm, and M. Krönke. 2008. Fusogenicity of membranes: the impact of acid sphingomyelinase on innate immune responses. Immunobiology. 213: 307-314.
    • (2008) Immunobiology , vol.213 , pp. 307-314
    • Utermöhlen, O.1    Herz, J.2    Schramm, M.3    Krönke, M.4
  • 163
    • 58849160520 scopus 로고    scopus 로고
    • Ceramide and neurodegeneration: Susceptibility of neurons and oligodendrocytes to cell damage and death
    • Jana, A., E. L. Hogan, and K. Pahan. 2009. Ceramide and neurodegeneration: susceptibility of neurons and oligodendrocytes to cell damage and death. J. Neurol. Sci. 278: 5-15.
    • (2009) J. Neurol. Sci. , vol.278 , pp. 5-15
    • Jana, A.1    Hogan, E.L.2    Pahan, K.3
  • 164
    • 0032579511 scopus 로고    scopus 로고
    • Sphingomyelinase and ceramide stimulate the expression of inducible nitric-oxide synthase in rat primary astrocytes
    • Pahan, K. 1998. Sphingomyelinase and ceramide stimulate the expression of inducible nitric-oxide synthase in rat primary astrocytes. J. Biol. Chem. 273: 2591-2600.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2591-2600
    • Pahan, K.1
  • 165
    • 42649083647 scopus 로고    scopus 로고
    • Suppression of sphingomyelin synthase 1 by small interference RNA is associated with enhanced ceramide production and apoptosis after photodamage
    • Separovic, D. 2008. Suppression of sphingomyelin synthase 1 by small interference RNA is associated with enhanced ceramide production and apoptosis after photodamage. Exp. Cell Res. 314: 1860-1868.
    • (2008) Exp. Cell Res. , vol.314 , pp. 1860-1868
    • Separovic, D.1
  • 166
    • 84871250128 scopus 로고    scopus 로고
    • Sphingolipids: Regulators of crosstalk between apoptosis and autophagy
    • Young, M. M., M. Kester, and H-G. Wang. 2013. Sphingolipids: regulators of crosstalk between apoptosis and autophagy. J. Lipid Res. 54: 5-19.
    • (2013) J. Lipid Res. , vol.54 , pp. 5-19
    • Young, M.M.1    Kester, M.2    Wang, H.-G.3
  • 167
    • 54049092827 scopus 로고    scopus 로고
    • The unexpected role of acid sphingomyelinase in cell death and the pathophysiology of common diseases
    • Smith, E. L., and E. H. Schuchman. 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
  • 168
    • 0032939644 scopus 로고    scopus 로고
    • Ceramides in phospholipid membranes: Effects on bilayer stability and transition to nonlamellar phases
    • Veiga, M. P., J. L. Arrondo, F. M. Goñi, and A. Alonso. 1999. Ceramides in phospholipid membranes: effects on bilayer stability and transition to nonlamellar phases. Biophys. J. 76: 342-350.
    • (1999) Biophys. J. , vol.76 , pp. 342-350
    • Veiga, M.P.1    Arrondo, J.L.2    Goñi, F.M.3    Alonso, A.4
  • 170
    • 79952097851 scopus 로고    scopus 로고
    • Myelination in the absence of UDP-galactose:ceramide galactosyl-transferase and fatty acid 2 -hydroxylase
    • Meixner, M., J. Jungnickel, C. Grothe, V. Gieselmann, and M. Eckhardt. 2011. Myelination in the absence of UDP-galactose:ceramide galactosyl-transferase and fatty acid 2 -hydroxylase. BMC Neurosci. 12: 22.
    • (2011) BMC Neurosci. , vol.12 , pp. 22
    • Meixner, M.1    Jungnickel, J.2    Grothe, C.3    Gieselmann, V.4    Eckhardt, M.5
  • 171
    • 79959813959 scopus 로고    scopus 로고
    • Intracerebroventricular enzyme infusion corrects central nervous system pathology and dysfunction in a mouse model of metachromatic leukodystrophy
    • Stroobants, S., D. Gerlach, F. Matthes, D. Hartmann, J. Fogh, V. Gieselmann, R. D'Hooge, and U. Matzner. 2011. Intracerebroventricular enzyme infusion corrects central nervous system pathology and dysfunction in a mouse model of metachromatic leukodystrophy. Hum. Mol. Genet. 20: 2760-2769.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 2760-2769
    • Stroobants, S.1    Gerlach, D.2    Matthes, F.3    Hartmann, D.4    Fogh, J.5    Gieselmann, V.6    D'Hooge, R.7    Matzner, U.8
  • 172
    • 73249141580 scopus 로고    scopus 로고
    • Interleukin-2 gene transfer potentiates the alpha-galactosylceramide-stimulated antitumor effect by the induction of TRAIL in NKT and NK cells in mouse models of subcutaneous and metastatic carcinoma
    • Nishihori, Y., K. Kato, M. Tanaka, T. Okamoto, S. Hagiwara, N. Araki, K. Kogawa, K. Kuribayashi, K. Nakamura, and Y. Niitsu. 2009. Interleukin-2 gene transfer potentiates the alpha-galactosylceramide-stimulated antitumor effect by the induction of TRAIL in NKT and NK cells in mouse models of subcutaneous and metastatic carcinoma. Cancer Biol. Ther. 8: 1763-1770.
    • (2009) Cancer Biol. Ther. , vol.8 , pp. 1763-1770
    • Nishihori, Y.1    Kato, K.2    Tanaka, M.3    Okamoto, T.4    Hagiwara, S.5    Araki, N.6    Kogawa, K.7    Kuribayashi, K.8    Nakamura, K.9    Niitsu, Y.10
  • 173
    • 82455162407 scopus 로고    scopus 로고
    • Higher apoptotic state in Fabry disease peripheral blood mononuclear cells: Effect of globotriaosylceramide
    • De Francesco, P. N., J. M. Mucci, R. Ceci, C. A. Fossati, and P. A. Rozenfeld. 2011. Higher apoptotic state in Fabry disease peripheral blood mononuclear cells: effect of globotriaosylceramide. Mol. Genet. Metab. 104: 319-324.
    • (2011) Mol. Genet. Metab. , vol.104 , pp. 319-324
    • De Francesco, P.N.1    Mucci, J.M.2    Ceci, R.3    Fossati, C.A.4    Rozenfeld, P.A.5
  • 174
    • 84869456811 scopus 로고    scopus 로고
    • Possible role of transforming growth factor-β1 and vascular endothelial growth factor in Fabry disease nephropathy
    • Lee, M. H., E. N. Choi, Y. J. Jeon, and S-C. Jung. 2012. Possible role of transforming growth factor-β1 and vascular endothelial growth factor in Fabry disease nephropathy. Int. J. Mol. Med. 30: 1275-1280.
    • (2012) Int. J. Mol. Med. , vol.30 , pp. 1275-1280
    • Lee, M.H.1    Choi, E.N.2    Jeon, Y.J.3    Jung, S.-C.4
  • 178
    • 15744378799 scopus 로고    scopus 로고
    • Altered cholesterol metabolism in Niemann-Pick type C1 mouse brains affects mitochondrial function
    • Yu, W., J-S. Gong, M. Ko, W. S. Garver, K. Yanagisawa, and M. Michikawa. 2005. Altered cholesterol metabolism in Niemann-Pick type C1 mouse brains affects mitochondrial function. J. Biol. Chem. 280: 11731-11739.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11731-11739
    • Yu, W.1    Gong, J.-S.2    Ko, M.3    Garver, W.S.4    Yanagisawa, K.5    Michikawa, M.6
  • 179
    • 79959654327 scopus 로고    scopus 로고
    • Unesterified cholesterol accumulation in late endosomes/lysosomes causes neurodegeneration and is prevented by driving cholesterol export from this compartment
    • Aqul, A., B. Liu, C. M. Ramirez, A. A. Pieper, S. J. Estill, D. K. Burns, B. Liu, J. J. Repa, S. D. Turley, and J. M. Dietschy. 2011. Unesterified cholesterol accumulation in late endosomes/lysosomes causes neurodegeneration and is prevented by driving cholesterol export from this compartment. J. Neurosci. 31: 9404-9413.
    • (2011) J. Neurosci. , vol.31 , pp. 9404-9413
    • Aqul, A.1    Liu, B.2    Ramirez, C.M.3    Pieper, A.A.4    Estill, S.J.5    Burns, D.K.6    Liu, B.7    Repa, J.J.8    Turley, S.D.9    Dietschy, J.M.10
  • 180
    • 33644937289 scopus 로고    scopus 로고
    • Neuronal cell death caused by inhibition of intracellular cholesterol trafficking is caspase dependent and associated with activation of the mitochondrial apoptosis pathway
    • Huang, Z., Q. Hou, N. S. Cheung, and Q-T. Li. 2006. Neuronal cell death caused by inhibition of intracellular cholesterol trafficking is caspase dependent and associated with activation of the mitochondrial apoptosis pathway. J. Neurochem. 97:280-291.
    • (2006) J. Neurochem. , vol.97 , pp. 280-291
    • Huang, Z.1    Hou, Q.2    Cheung, N.S.3    Li, Q.-T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.