메뉴 건너뛰기




Volumn 13, Issue 10, 2012, Pages 1371-1387

Lipids and lysosomes

Author keywords

Lipids; Lysosomal hydrolysis and lysosomal trafficking; Lysosomes

Indexed keywords

ABC TRANSPORTER A1; ADENOSINE TRIPHOSPHATE; CHOLESTEROL; GLYCEROPHOSPHOLIPID; HYDROLASE; LIPID; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 2; PHOSPHATIDIC ACID; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLINOSITOL; PHOSPHATIDYLSERINE; PHOSPHOLIPASE A2; SNARE PROTEIN; SPHINGOLIPID ACTIVATOR PROTEIN; SPHINGOMYELIN;

EID: 84870415840     PISSN: 13892002     EISSN: 18755453     Source Type: Journal    
DOI: 10.2174/138920012803762684     Document Type: Article
Times cited : (28)

References (261)
  • 2
    • 0037334339 scopus 로고    scopus 로고
    • At the acidic edge: Emerging functions for lysosomal membrane proteins
    • Eskelinen, E.L.; Tanaka, Y.; Saftig, P. At the acidic edge: emerging functions for lysosomal membrane proteins. Trends Cell Biol., 2003, 13, 137-145.
    • (2003) Trends Cell Biol. , vol.13 , pp. 137-145
    • Eskelinen, E.L.1    Tanaka, Y.2    Saftig, P.3
  • 3
    • 43149104361 scopus 로고    scopus 로고
    • Molecular physiology and pathophysiology of lysosomal membrane transporters
    • Sagne, C.; Gasnier, B. Molecular physiology and pathophysiology of lysosomal membrane transporters. J. Inherit Metab. Dis., 2008, 31, 258-266.
    • (2008) J. Inherit Metab. Dis. , vol.31 , pp. 258-266
    • Sagne, C.1    Gasnier, B.2
  • 4
    • 2942687937 scopus 로고    scopus 로고
    • The cell biology of lysosomal storage disorders
    • Futerman, A.H.; van Meer, G. The cell biology of lysosomal storage disorders. Nat. Rev. Mol. Cell Biol., 2004, 5, 554-565.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 554-565
    • Futerman, A.H.1    Van Meer, G.2
  • 6
    • 77952934647 scopus 로고    scopus 로고
    • Lipids and cholesterol as regulators of traffic in the endomembrane system
    • Lippincott-Schwartz, J.; Phair, R.D. Lipids and cholesterol as regulators of traffic in the endomembrane system. Annu. Rev. Biophys., 2010, 39, 559-578.
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 559-578
    • Lippincott-Schwartz, J.1    Phair, R.D.2
  • 7
    • 53549122990 scopus 로고    scopus 로고
    • Function and dysfunction of the PI system in membrane trafficking
    • Vicinanza, M.; D'Angelo, G.; Di Campli, A.; De Matteis, M.A. Function and dysfunction of the PI system in membrane trafficking. Embo. J., 2008, 27, 2457-2470.
    • (2008) Embo. J. , vol.27 , pp. 2457-2470
    • Vicinanza, M.1    D'Angelo, G.2    Di Campli, A.3    De Matteis, M.A.4
  • 8
    • 37049019270 scopus 로고    scopus 로고
    • Endocytic trafficking of sphingomyelin depends on its acyl chain length
    • Koivusalo, M.; Jansen, M.; Somerharju, P.; Ikonen, E. Endocytic trafficking of sphingomyelin depends on its acyl chain length. Mol. Biol. Cell, 2007, 18, 5113-5123.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 5113-5123
    • Koivusalo, M.1    Jansen, M.2    Somerharju, P.3    Ikonen, E.4
  • 9
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood, D.; Simons, K. Lipid rafts as a membrane-organizing principle. Science, 2010, 327, 46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 10
    • 0032174579 scopus 로고    scopus 로고
    • Lipids, lipid domains and lipid-protein interactions in endocytic membrane traffic
    • Kobayashi, T.; Gu, F.; Gruenberg, J. Lipids, lipid domains and lipid-protein interactions in endocytic membrane traffic. Semin. Cell Dev. Biol., 1998, 9, 517-526.
    • (1998) Semin. Cell Dev. Biol. , vol.9 , pp. 517-526
    • Kobayashi, T.1    Gu, F.2    Gruenberg, J.3
  • 12
    • 12344305490 scopus 로고    scopus 로고
    • Saposin C-LBPA interaction in lateendosomes/lysosomes
    • Chu, Z.; Witte, D.P.; Qi, X. Saposin C-LBPA interaction in lateendosomes/lysosomes. Exp. Cell Res., 2005, 303, 300-307.
    • (2005) Exp. Cell Res. , vol.303 , pp. 300-307
    • Chu, Z.1    Witte, D.P.2    Qi, X.3
  • 14
    • 0032510559 scopus 로고    scopus 로고
    • A lipid associated with the antiphospholipid syndrome regulates endosome structure and function
    • Kobayashi, T.; Stang, E.; Fang, K.S.; de Moerloose, P.; Parton, R.G.; Gruenberg, J. A lipid associated with the antiphospholipid syndrome regulates endosome structure and function. Nature, 1998, 392, 193-197.
    • (1998) Nature , vol.392 , pp. 193-197
    • Kobayashi, T.1    Stang, E.2    Fang, K.S.3    De Moerloose, P.4    Parton, R.G.5    Gruenberg, J.6
  • 15
  • 16
    • 30444456831 scopus 로고    scopus 로고
    • EGF stimulates annexin 1-dependent inward vesiculation in a multivesicular endosome subpopulation
    • White, I.J.; Bailey, L.M.; Aghakhani, M.R.; Moss, S.E.; Futter, C.E. EGF stimulates annexin 1-dependent inward vesiculation in a multivesicular endosome subpopulation. Embo. J., 2006, 25, 1-12.
    • (2006) Embo. J. , vol.25 , pp. 1-12
    • White, I.J.1    Bailey, L.M.2    Aghakhani, M.R.3    Moss, S.E.4    Futter, C.E.5
  • 18
    • 0038620205 scopus 로고    scopus 로고
    • Recycling compartments and the internal vesicles of multivesicular bodies harbor most of the cholesterol found in the endocytic pathway
    • Mobius, W.; van Donselaar, E.; Ohno-Iwashita, Y.; Shimada, Y.; Heijnen, H.F.; Slot, J.W.; Geuze, H.J. Recycling compartments and the internal vesicles of multivesicular bodies harbor most of the cholesterol found in the endocytic pathway. Traffic, 2003, 4, 222-231.
    • (2003) Traffic , vol.4 , pp. 222-231
    • Mobius, W.1    Van Donselaar, E.2    Ohno-Iwashita, Y.3    Shimada, Y.4    Heijnen, H.F.5    Slot, J.W.6    Geuze, H.J.7
  • 19
    • 57749172710 scopus 로고    scopus 로고
    • Sortilin and prosaposin localize to detergent-resistant membrane microdomains
    • Canuel, M.; Bhattacharyya, N.; Balbis, A.; Yuan, L.; Morales, C.R. Sortilin and prosaposin localize to detergent-resistant membrane microdomains. Exp. Cell Res., 2009, 315, 240-247.
    • (2009) Exp. Cell Res. , vol.315 , pp. 240-247
    • Canuel, M.1    Bhattacharyya, N.2    Balbis, A.3    Yuan, L.4    Morales, C.R.5
  • 20
    • 33748374920 scopus 로고    scopus 로고
    • Lysosome membrane lipid microdomains: Novel regulators of chaperone-mediated autophagy
    • Kaushik, S.; Massey, A.C.; Cuervo, A.M. Lysosome membrane lipid microdomains: novel regulators of chaperone-mediated autophagy. Embo. J., 2006, 25, 3921-3933.
    • (2006) Embo. J. , vol.25 , pp. 3921-3933
    • Kaushik, S.1    Massey, A.C.2    Cuervo, A.M.3
  • 24
    • 63149196645 scopus 로고    scopus 로고
    • Principles of lysosomal membrane degradation: Cellular topology and biochemistry of lysosomal lipid degradation
    • Schulze, H.; Kolter, T.; Sandhoff, K. Principles of lysosomal membrane degradation: Cellular topology and biochemistry of lysosomal lipid degradation. Biochim. Biophys. Acta, 2009, 1793, 674-683.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 674-683
    • Schulze, H.1    Kolter, T.2    Sandhoff, K.3
  • 25
    • 24044519647 scopus 로고    scopus 로고
    • Displacement of sterols from sterol/sphingomyelin domains in fluid bilayer membranes by competing molecules
    • Alanko, S.M.; Halling, K.K.; Maunula, S.; Slotte, J.P.; Ramstedt, B. Displacement of sterols from sterol/sphingomyelin domains in fluid bilayer membranes by competing molecules. Biochim. Biophys. Acta, 2005, 1715, 111-121.
    • (2005) Biochim. Biophys. Acta , vol.1715 , pp. 111-121
    • Alanko, S.M.1    Halling, K.K.2    Maunula, S.3    Slotte, J.P.4    Ramstedt, B.5
  • 26
    • 27744514250 scopus 로고    scopus 로고
    • Activation of membrane cholesterol by displacement from phospholipids
    • Lange, Y.; Ye, J.; Steck, T.L. Activation of membrane cholesterol by displacement from phospholipids. J. Biol. Chem., 2005, 280, 36126-36131.
    • (2005) J. Biol. Chem. , vol.280 , pp. 36126-36131
    • Lange, Y.1    Ye, J.2    Steck, T.L.3
  • 27
    • 1642293929 scopus 로고    scopus 로고
    • Ceramide selectively displaces cholesterol from ordered lipid domains (rafts): Implications for lipid raft structure and function
    • London, M.; London, E. Ceramide selectively displaces cholesterol from ordered lipid domains (rafts): implications for lipid raft structure and function. J. Biol. Chem., 2004, 279, 9997-10004.
    • (2004) J. Biol. Chem. , vol.279 , pp. 9997-10004
    • London, M.1    London, E.2
  • 28
    • 25444443570 scopus 로고    scopus 로고
    • Principles of lysosomal membrane digestion: Stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids
    • Kolter, T.; Sandhoff, K. Principles of lysosomal membrane digestion: stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids. Annu. Rev. Cell Dev. Biol., 2005, 21, 81-103.
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 81-103
    • Kolter, T.1    Sandhoff, K.2
  • 31
    • 0018179763 scopus 로고
    • Conversion of diphosphatidylglycerol to bis(monoacylglyceryl)phosphate by lysosomes
    • Poorthuis, B.J.; Hostetler, K.Y. Conversion of diphosphatidylglycerol to bis(monoacylglyceryl)phosphate by lysosomes. J. Lipid Res., 1978, 19, 309-315.
    • (1978) J. Lipid Res. , vol.19 , pp. 309-315
    • Poorthuis, B.J.1    Hostetler, K.Y.2
  • 32
    • 0018951796 scopus 로고
    • Conversion of phosphatidylglycerol lipids to bis(monoacylglycero) phosphate in vivo
    • Somerharju, P.; Renkonen, O. Conversion of phosphatidylglycerol lipids to bis(monoacylglycero)phosphate in vivo. Biochim. Biophys. Acta, 1980, 618, 407-419.
    • (1980) Biochim. Biophys. Acta , vol.618 , pp. 407-419
    • Somerharju, P.1    Renkonen, O.2
  • 33
    • 0029953488 scopus 로고    scopus 로고
    • Transacylase and phospholipases in the synthesis of bis(monoacylglycero) phosphate
    • Amidon, B.; Brown, A.; Waite, M. Transacylase and phospholipases in the synthesis of bis(monoacylglycero)phosphate. Biochemistry, 1996, 35, 13995-14002.
    • (1996) Biochemistry , vol.35 , pp. 13995-14002
    • Amidon, B.1    Brown, A.2    Waite, M.3
  • 36
    • 77954957013 scopus 로고    scopus 로고
    • Membrane budding and scission by the ESCRT machinery: It's all in the neck
    • Hurley, J.H.; Hanson, P.I. Membrane budding and scission by the ESCRT machinery: it's all in the neck. Nat. Rev. Mol. Cell Biol., 2010, 11, 556-566.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 556-566
    • Hurley, J.H.1    Hanson, P.I.2
  • 37
    • 63649086486 scopus 로고    scopus 로고
    • The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
    • Raiborg, C.; Stenmark, H. The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins. Nature, 2009, 458, 445-452.
    • (2009) Nature , vol.458 , pp. 445-452
    • Raiborg, C.1    Stenmark, H.2
  • 40
    • 0041488656 scopus 로고    scopus 로고
    • Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes
    • Bache, K.G.; Brech, A.; Mehlum, A.; Stenmark, H. Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes. J. Cell Biol., 2003, 162, 435-442.
    • (2003) J. Cell Biol. , vol.162 , pp. 435-442
    • Bache, K.G.1    Brech, A.2    Mehlum, A.3    Stenmark, H.4
  • 42
    • 33745929286 scopus 로고    scopus 로고
    • Distinct roles for Tsg101 and Hrs in multivesicular body formation and inward vesiculation
    • Razi, M.; Futter, C.E. Distinct roles for Tsg101 and Hrs in multivesicular body formation and inward vesiculation. Mol. Biol. Cell, 2006, 17, 3469-3483.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3469-3483
    • Razi, M.1    Futter, C.E.2
  • 43
    • 2342423251 scopus 로고    scopus 로고
    • ATPase-deficient hVPS4 impairs formation of internal endosomal vesicles and stabilizes bilayered clathrin coats on endosomal vacuoles
    • Sachse, M.; Strous, G.J.; Klumperman, J. ATPase-deficient hVPS4 impairs formation of internal endosomal vesicles and stabilizes bilayered clathrin coats on endosomal vacuoles. J. Cell Sci., 2004, 117, 1699-1708.
    • (2004) J. Cell Sci. , vol.117 , pp. 1699-1708
    • Sachse, M.1    Strous, G.J.2    Klumperman, J.3
  • 44
    • 77953379422 scopus 로고    scopus 로고
    • Cell-free reconstitution of multivesicular body formation and receptor sorting
    • Sun, W.; Vida, T.A.; Sirisaengtaksin, N.; Merrill, S.A.; Hanson, P.I.; Bean, A.J. Cell-free reconstitution of multivesicular body formation and receptor sorting. Traffic, 2010, 11, 867-876.
    • (2010) Traffic , vol.11 , pp. 867-876
    • Sun, W.1    Vida, T.A.2    Sirisaengtaksin, N.3    Merrill, S.A.4    Hanson, P.I.5    Bean, A.J.6
  • 45
    • 77950863406 scopus 로고    scopus 로고
    • Molecular mechanism of multivesicular body biogenesis by ESCRT complexes
    • Wollert, T.; Hurley, J.H. Molecular mechanism of multivesicular body biogenesis by ESCRT complexes. Nature, 2010, 464, 864-869.
    • (2010) Nature , vol.464 , pp. 864-869
    • Wollert, T.1    Hurley, J.H.2
  • 47
    • 34147179868 scopus 로고    scopus 로고
    • Evidence of cholesterol accumulated in high curvature regions: Implication to the curvature elastic energy for lipid mixtures
    • Wang, W.; Yang, L.; Huang, H.W. Evidence of cholesterol accumulated in high curvature regions: implication to the curvature elastic energy for lipid mixtures. Biophys. J., 2007, 92, 2819-2830.
    • (2007) Biophys. J. , vol.92 , pp. 2819-2830
    • Wang, W.1    Yang, L.2    Huang, H.W.3
  • 48
    • 0037926403 scopus 로고    scopus 로고
    • Annexin II regulates multivesicular endosome biogenesis in the degradation pathway of animal cells
    • Mayran, N.; Parton, R.G.; Gruenberg, J. Annexin II regulates multivesicular endosome biogenesis in the degradation pathway of animal cells. Embo. J., 2003, 22, 3242-3253.
    • (2003) Embo. J. , vol.22 , pp. 3242-3253
    • Mayran, N.1    Parton, R.G.2    Gruenberg, J.3
  • 49
    • 61749095982 scopus 로고    scopus 로고
    • Annexin A2-dependent polymerization of actin mediates endosome biogenesis
    • Morel, E.; Parton, R.G.; Gruenberg, J. Annexin A2-dependent polymerization of actin mediates endosome biogenesis. Dev. Cell, 2009, 16, 445-457.
    • (2009) Dev. Cell , vol.16 , pp. 445-457
    • Morel, E.1    Parton, R.G.2    Gruenberg, J.3
  • 50
    • 58149280810 scopus 로고    scopus 로고
    • In vitro budding of intralumenal vesicles into late endosomes is regulated by Alix and Tsg101
    • Falguieres, T.; Luyet, P.P.; Bissig, C.; Scott, C.C.; Velluz, M.C.; Gruenberg, J. In vitro budding of intralumenal vesicles into late endosomes is regulated by Alix and Tsg101. Mol. Biol. Cell, 2008, 19, 4942-4955.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4942-4955
    • Falguieres, T.1    Luyet, P.P.2    Bissig, C.3    Scott, C.C.4    Velluz, M.C.5    Gruenberg, J.6
  • 52
    • 65549118370 scopus 로고    scopus 로고
    • Bis(monoacylglycero)phosphate forms stable small lamellar vesicle structures: Insights into vesicular body formation in endosomes
    • Frederick, T.E.; Chebukati, J.N.; Mair, C.E.; Goff, P.C.; Fanucci, G.E. Bis(monoacylglycero)phosphate forms stable small lamellar vesicle structures: insights into vesicular body formation in endosomes. Biophys. J., 2009, 96, 1847-1855.
    • (2009) Biophys. J. , vol.96 , pp. 1847-1855
    • Frederick, T.E.1    Chebukati, J.N.2    Mair, C.E.3    Goff, P.C.4    Fanucci, G.E.5
  • 54
    • 67949097489 scopus 로고    scopus 로고
    • Exosomes-vesicular carriers for intercellular communication
    • Simons, M.; Raposo, G. Exosomes-vesicular carriers for intercellular communication. Curr. Opin. Cell Biol., 2009, 21, 575-581.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 575-581
    • Simons, M.1    Raposo, G.2
  • 56
    • 13944258097 scopus 로고    scopus 로고
    • Endocytic delivery to lysosomes mediated by concurrent fusion and kissing events in living cells
    • Bright, N.A.; Gratian, M.J.; Luzio, J.P. Endocytic delivery to lysosomes mediated by concurrent fusion and kissing events in living cells. Curr. Biol., 2005, 15, 360-365.
    • (2005) Curr. Biol. , vol.15 , pp. 360-365
    • Bright, N.A.1    Gratian, M.J.2    Luzio, J.P.3
  • 57
    • 0034729167 scopus 로고    scopus 로고
    • The role of intraorganellar Ca(2+) in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles
    • Pryor, P.R.; Mullock, B.M.; Bright, N.A.; Gray, S.R.; Luzio, J.P. The role of intraorganellar Ca(2+) in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles. J. Cell Biol., 2000, 149, 1053-1062.
    • (2000) J. Cell Biol. , vol.149 , pp. 1053-1062
    • Pryor, P.R.1    Mullock, B.M.2    Bright, N.A.3    Gray, S.R.4    Luzio, J.P.5
  • 59
    • 79956070911 scopus 로고    scopus 로고
    • Pairing phosphoinositides with calcium ions in endolysosomal dynamics: Phosphoinositides control the direction and specificity of membrane trafficking by regulating the activity of calcium channels in the endolysosomes
    • Shen, D.; Wang, X.; Xu, H. Pairing phosphoinositides with calcium ions in endolysosomal dynamics: phosphoinositides control the direction and specificity of membrane trafficking by regulating the activity of calcium channels in the endolysosomes. Bioessays., 2011, 33, 448-457.
    • (2011) Bioessays. , vol.33 , pp. 448-457
    • Shen, D.1    Wang, X.2    Xu, H.3
  • 60
    • 77957020175 scopus 로고    scopus 로고
    • Membrane fusion: Five lipids, four SNAREs, three chaperones, two nucleotides, and a Rab, all dancing in a ring on yeast vacuoles
    • Wickner, W. Membrane fusion: five lipids, four SNAREs, three chaperones, two nucleotides, and a Rab, all dancing in a ring on yeast vacuoles. Annu. Rev. Cell Dev. Biol., 2010, 26, 115-136.
    • (2010) Annu. Rev. Cell Dev. Biol. , vol.26 , pp. 115-136
    • Wickner, W.1
  • 61
    • 65549087110 scopus 로고    scopus 로고
    • Fusion step-specific influence of cholesterol on SNARE-mediated membrane fusion
    • Chang, J.; Kim, S.A.; Lu, X.; Su, Z.; Kim, S.K.; Shin, Y.K. Fusion step-specific influence of cholesterol on SNARE-mediated membrane fusion. Biophys. J., 2009, 96, 1839-1846.
    • (2009) Biophys. J. , vol.96 , pp. 1839-1846
    • Chang, J.1    Kim, S.A.2    Lu, X.3    Su, Z.4    Kim, S.K.5    Shin, Y.K.6
  • 62
    • 65249144553 scopus 로고    scopus 로고
    • A scissors mechanism for stimulation of SNARE-mediated lipid mixing by cholesterol
    • Tong, J.; Borbat, P.P.; Freed, J.H.; Shin, Y.K. A scissors mechanism for stimulation of SNARE-mediated lipid mixing by cholesterol. Proc. Natl. Acad. Sci. U. S. A., 2009, 106, 5141-5146.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 5141-5146
    • Tong, J.1    Borbat, P.P.2    Freed, J.H.3    Shin, Y.K.4
  • 63
    • 79959346132 scopus 로고    scopus 로고
    • Distinct autophagosomal-lysosomal fusion mechanism revealed by thapsigargin-induced autophagy arrest
    • Ganley, I.G.; Wong, P.M.; Gammoh, N.; Jiang, X. Distinct autophagosomal-lysosomal fusion mechanism revealed by thapsigargin-induced autophagy arrest. Mol. Cell, 2011, 42, 731-743.
    • (2011) Mol. Cell , vol.42 , pp. 731-743
    • Ganley, I.G.1    Wong, P.M.2    Gammoh, N.3    Jiang, X.4
  • 64
    • 78649751019 scopus 로고    scopus 로고
    • The role of ESCRT proteins in fusion events involving lysosomes, endosomes and autophagosomes
    • Metcalf, D.; Isaacs, A.M. The role of ESCRT proteins in fusion events involving lysosomes, endosomes and autophagosomes. Biochem. Soc. Trans., 2010, 38, 1469-1473.
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 1469-1473
    • Metcalf, D.1    Isaacs, A.M.2
  • 66
    • 77955789211 scopus 로고    scopus 로고
    • Altered lipid content inhibits autophagic vesicular fusion
    • Koga, H.; Kaushik, S.; Cuervo, A.M. Altered lipid content inhibits autophagic vesicular fusion. FASEB. J, 2010, 24, 3052-3065.
    • (2010) FASEB. J , vol.24 , pp. 3052-3065
    • Koga, H.1    Kaushik, S.2    Cuervo, A.M.3
  • 67
    • 0037175388 scopus 로고    scopus 로고
    • Membrane proximal lysosomes are the major vesicles responsible for calcium-dependent exocytosis in nonsecretory cells
    • Jaiswal, J.K.; Andrews, N.W.; Simon, S.M. Membrane proximal lysosomes are the major vesicles responsible for calcium-dependent exocytosis in nonsecretory cells. J. Cell Biol., 2002, 159, 625-635.
    • (2002) J. Cell Biol. , vol.159 , pp. 625-635
    • Jaiswal, J.K.1    Andrews, N.W.2    Simon, S.M.3
  • 68
    • 0035958557 scopus 로고    scopus 로고
    • Plasma membrane repair is mediated by Ca(2+)-regulated exocytosis of lysosomes
    • Reddy, A.; Caler, E.V.; Andrews, N.W. Plasma membrane repair is mediated by Ca(2+)-regulated exocytosis of lysosomes. Cell, 2001, 106, 157-169.
    • (2001) Cell , vol.106 , pp. 157-169
    • Reddy, A.1    Caler, E.V.2    Andrews, N.W.3
  • 69
    • 0030615262 scopus 로고    scopus 로고
    • Lysosomes behave as Ca2+-regulated exocytic vesicles in fibroblasts and epithelial cells
    • Rodriguez, A.; Webster, P.; Ortego, J.; Andrews, N.W. Lysosomes behave as Ca2+-regulated exocytic vesicles in fibroblasts and epithelial cells. J. Cell Biol., 1997, 137, 93-104.
    • (1997) J. Cell Biol. , vol.137 , pp. 93-104
    • Rodriguez, A.1    Webster, P.2    Ortego, J.3    Andrews, N.W.4
  • 70
    • 78049511240 scopus 로고    scopus 로고
    • Palmitoylation-dependent association with CD63 targets the Ca2+ sensor synaptotagmin VII to lysosomes
    • Flannery, A.R.; Czibener, C.; Andrews, N.W. Palmitoylation-dependent association with CD63 targets the Ca2+ sensor synaptotagmin VII to lysosomes. J. Cell Biol., 2010, 191, 599-613.
    • (2010) J. Cell Biol. , vol.191 , pp. 599-613
    • Flannery, A.R.1    Czibener, C.2    Andrews, N.W.3
  • 71
    • 19344375822 scopus 로고    scopus 로고
    • Synaptotagmin VII restricts fusion pore expansion during lysosomal exocytosis
    • Jaiswal, J.K.; Chakrabarti, S.; Andrews, N.W.; Simon, S.M. Synaptotagmin VII restricts fusion pore expansion during lysosomal exocytosis. PLoS Biol., 2004, 2, E233.
    • (2004) PLoS Biol. , vol.2
    • Jaiswal, J.K.1    Chakrabarti, S.2    Andrews, N.W.3    Simon, S.M.4
  • 73
    • 2442584514 scopus 로고    scopus 로고
    • Identification of SNAREs involved in synaptotagmin VIIregulated lysosomal exocytosis
    • Rao, S.K.; Huynh, C.; Proux-Gillardeaux, V.; Galli, T.; Andrews, N.W. Identification of SNAREs involved in synaptotagmin VIIregulated lysosomal exocytosis. J. Biol. Chem., 2004, 279, 20471-20479.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20471-20479
    • Rao, S.K.1    Huynh, C.2    Proux-Gillardeaux, V.3    Galli, T.4    Andrews, N.W.5
  • 74
    • 40849118150 scopus 로고    scopus 로고
    • Repair of injured plasma membrane by rapid Ca2+- dependent endocytosis
    • Idone, V.; Tam, C.; Goss, J.W.; Toomre, D.; Pypaert, M.; Andrews, N.W. Repair of injured plasma membrane by rapid Ca2+- dependent endocytosis. J. Cell Biol., 2008, 180, 905-914.
    • (2008) J. Cell Biol. , vol.180 , pp. 905-914
    • Idone, V.1    Tam, C.2    Goss, J.W.3    Toomre, D.4    Pypaert, M.5    Andrews, N.W.6
  • 76
    • 33646544088 scopus 로고    scopus 로고
    • Apolipoprotein e recycling: Implications for dyslipidemia and atherosclerosis
    • Heeren, J.; Beisiegel, U.; Grewal, T. Apolipoprotein E recycling: implications for dyslipidemia and atherosclerosis. Arterioscler. Thromb. Vasc. Biol., 2006, 26, 442-448.
    • (2006) Arterioscler. Thromb. Vasc. Biol. , vol.26 , pp. 442-448
    • Heeren, J.1    Beisiegel, U.2    Grewal, T.3
  • 77
    • 55849135236 scopus 로고    scopus 로고
    • Molecular processes that handle - And mishandle - Dietary lipids
    • Williams, K.J. Molecular processes that handle - and mishandle - dietary lipids. J. Clin. Invest., 2008, 118, 3247-3259.
    • (2008) J. Clin. Invest. , vol.118 , pp. 3247-3259
    • Williams, K.J.1
  • 78
    • 77952335030 scopus 로고    scopus 로고
    • Recent insights into factors affecting remnant lipoprotein uptake
    • Williams, K.J.; Chen, K. Recent insights into factors affecting remnant lipoprotein uptake. Curr. Opin. Lipidol., 2010, 21, 218-228.
    • (2010) Curr. Opin. Lipidol. , vol.21 , pp. 218-228
    • Williams, K.J.1    Chen, K.2
  • 80
    • 0022549920 scopus 로고
    • A receptor-mediated pathway for cholesterol homeostasis
    • Brown, M.S.; Goldstein, J.L. A receptor-mediated pathway for cholesterol homeostasis. Science, 1986, 232, 34-47.
    • (1986) Science , vol.232 , pp. 34-47
    • Brown, M.S.1    Goldstein, J.L.2
  • 81
    • 15744390047 scopus 로고    scopus 로고
    • Modulation of endosomal cholesteryl ester metabolism by membrane cholesterol
    • Wang, Y.; Castoreno, A.B.; Stockinger, W.; Nohturfft, A. Modulation of endosomal cholesteryl ester metabolism by membrane cholesterol. J. Biol. Chem., 2005, 280, 11876-11886.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11876-11886
    • Wang, Y.1    Castoreno, A.B.2    Stockinger, W.3    Nohturfft, A.4
  • 82
    • 0021691363 scopus 로고
    • Uptake and processing of remnants of chylomicrons and very low density lipoproteins by rat liver
    • Jones, A.L.; Hradek, G.T.; Hornick, C.; Renaud, G.; Windler, E.E.; Havel, R.J. Uptake and processing of remnants of chylomicrons and very low density lipoproteins by rat liver. J. Lipid Res., 1984, 25, 1151-1158.
    • (1984) J. Lipid Res. , vol.25 , pp. 1151-1158
    • Jones, A.L.1    Hradek, G.T.2    Hornick, C.3    Renaud, G.4    Windler, E.E.5    Havel, R.J.6
  • 83
    • 43249086500 scopus 로고    scopus 로고
    • Conversion of low density lipoprotein-associated phosphatidylcholine to triacylglycerol by primary hepatocytes
    • Minahk, C.; Kim, K.W.; Nelson, R.; Trigatti, B.; Lehner, R.; Vance, D.E. Conversion of low density lipoprotein-associated phosphatidylcholine to triacylglycerol by primary hepatocytes. J. Biol. Chem., 2008, 283, 6449-6458.
    • (2008) J. Biol. Chem. , vol.283 , pp. 6449-6458
    • Minahk, C.1    Kim, K.W.2    Nelson, R.3    Trigatti, B.4    Lehner, R.5    Vance, D.E.6
  • 85
    • 0030046797 scopus 로고    scopus 로고
    • Identification of scavenger receptor SR-BI as a high density lipoprotein receptor
    • Acton, S.; Rigotti, A.; Landschulz, K.T.; Xu, S.; Hobbs, H.H.; Krieger, M. Identification of scavenger receptor SR-BI as a high density lipoprotein receptor. Science, 1996, 271, 518-520.
    • (1996) Science , vol.271 , pp. 518-520
    • Acton, S.1    Rigotti, A.2    Landschulz, K.T.3    Xu, S.4    Hobbs, H.H.5    Krieger, M.6
  • 86
    • 78650606471 scopus 로고    scopus 로고
    • Scavenger receptor BI: A multi-purpose player in cholesterol and steroid metabolism
    • Hoekstra, M.; Van Berkel, T.J.; Van Eck, M. Scavenger receptor BI: a multi-purpose player in cholesterol and steroid metabolism. World J. Gastroenterol., 2010, 16, 5916-5924.
    • (2010) World J. Gastroenterol. , vol.16 , pp. 5916-5924
    • Hoekstra, M.1    Van Berkel, T.J.2    Van Eck, M.3
  • 87
    • 11144246298 scopus 로고    scopus 로고
    • Scavenger receptor class B type i is solely responsible for the selective uptake of cholesteryl esters from HDL by the liver and the adrenals in mice
    • Out, R.; Hoekstra, M.; Spijkers, J.A.; Kruijt, J.K.; van Eck, M.; Bos, I.S.; Twisk, J.; Van Berkel, T.J. Scavenger receptor class B type I is solely responsible for the selective uptake of cholesteryl esters from HDL by the liver and the adrenals in mice. J. Lipid Res., 2004, 45, 2088-2095.
    • (2004) J. Lipid Res. , vol.45 , pp. 2088-2095
    • Out, R.1    Hoekstra, M.2    Spijkers, J.A.3    Kruijt, J.K.4    Van Eck, M.5    Bos, I.S.6    Twisk, J.7    Van Berkel, T.J.8
  • 89
    • 12144286290 scopus 로고    scopus 로고
    • Different transport routes for high density lipoprotein and its associated free sterol in polarized hepatic cells
    • Wustner, D.; Mondal, M.; Huang, A.; Maxfield, F.R. Different transport routes for high density lipoprotein and its associated free sterol in polarized hepatic cells. J. Lipid Res., 2004, 45, 427-437.
    • (2004) J. Lipid Res. , vol.45 , pp. 427-437
    • Wustner, D.1    Mondal, M.2    Huang, A.3    Maxfield, F.R.4
  • 91
    • 0036775845 scopus 로고    scopus 로고
    • Sequestration of aggregated low-density lipoproteins by macrophages
    • Kruth, H.S. Sequestration of aggregated low-density lipoproteins by macrophages. Curr. Opin. Lipidol., 2002, 13, 483-488.
    • (2002) Curr. Opin. Lipidol. , vol.13 , pp. 483-488
    • Kruth, H.S.1
  • 92
    • 0035813170 scopus 로고    scopus 로고
    • The uptake and degradation of matrix-bound lipoproteins by macrophages require an intact actin Cytoskeleton, Rho family GTPases, and myosin ATPase activity
    • Sakr, S.W.; Eddy, R.J.; Barth, H.; Wang, F.; Greenberg, S.; Maxfield, F.R.; Tabas, I. The uptake and degradation of matrix-bound lipoproteins by macrophages require an intact actin Cytoskeleton, Rho family GTPases, and myosin ATPase activity. J. Biol. Chem., 2001, 276, 37649-37658.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37649-37658
    • Sakr, S.W.1    Eddy, R.J.2    Barth, H.3    Wang, F.4    Greenberg, S.5    Maxfield, F.R.6    Tabas, I.7
  • 100
    • 77953019480 scopus 로고    scopus 로고
    • Niemann-Pick disease type C
    • Vanier, M.T. Niemann-Pick disease type C. Orphanet. J. Rare Dis., 2010, 5, 16.
    • (2010) Orphanet. J. Rare Dis. , vol.5 , pp. 16
    • Vanier, M.T.1
  • 101
    • 80052010267 scopus 로고    scopus 로고
    • Loss of Niemann-Pick C1 or C2 protein results in similar biochemical changes suggesting that these proteins function in a common lysosomal pathway
    • Dixit, S.S.; Jadot, M.; Sohar, I.; Sleat, D.E.; Stock, A.M.; Lobel, P. Loss of Niemann-Pick C1 or C2 protein results in similar biochemical changes suggesting that these proteins function in a common lysosomal pathway. PLoS One, 2011, 6, e23677.
    • (2011) PLoS One , vol.6
    • Dixit, S.S.1    Jadot, M.2    Sohar, I.3    Sleat, D.E.4    Stock, A.M.5    Lobel, P.6
  • 102
    • 73349138621 scopus 로고    scopus 로고
    • Cyclodextrin overcomes deficient lysosome-toendoplasmic reticulum transport of cholesterol in Niemann-Pick type C cells
    • Abi-Mosleh, L.; Infante, R.E.; Radhakrishnan, A.; Goldstein, J.L.; Brown, M.S. Cyclodextrin overcomes deficient lysosome-toendoplasmic reticulum transport of cholesterol in Niemann-Pick type C cells. Proc. Natl. Acad. Sci. U. S. A., 2009, 106, 19316-19321.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 19316-19321
    • Abi-Mosleh, L.1    Infante, R.E.2    Radhakrishnan, A.3    Goldstein, J.L.4    Brown, M.S.5
  • 103
    • 77950402392 scopus 로고    scopus 로고
    • Endocytosis of beta-cyclodextrins is responsible for cholesterol reduction in Niemann-Pick type C mutant cells
    • Rosenbaum, A.I.; Zhang, G.; Warren, J.D.; Maxfield, F.R. Endocytosis of beta-cyclodextrins is responsible for cholesterol reduction in Niemann-Pick type C mutant cells. Proc. Natl. Acad. Sci. U. S. A., 2010, 107, 5477-5482.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 5477-5482
    • Rosenbaum, A.I.1    Zhang, G.2    Warren, J.D.3    Maxfield, F.R.4
  • 105
    • 67549105629 scopus 로고    scopus 로고
    • Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol
    • Kwon, H.J.; Abi-Mosleh, L.; Wang, M.L.; Deisenhofer, J.; Goldstein, J.L.; Brown, M.S.; Infante, R.E. Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol. Cell, 2009, 137, 1213-1224.
    • (2009) Cell , vol.137 , pp. 1213-1224
    • Kwon, H.J.1    Abi-Mosleh, L.2    Wang, M.L.3    Deisenhofer, J.4    Goldstein, J.L.5    Brown, M.S.6    Infante, R.E.7
  • 106
    • 80053085866 scopus 로고    scopus 로고
    • Amino acid substitution in NPC1 that abolishes cho lesterol binding reproduces phenotype of complete NPC1 deficiency in mice
    • Xie, X.; Brown, M.S.; Shelton, J.M.; Richardson, J.A.; Goldstein, J.L.; Liang, G. Amino acid substitution in NPC1 that abolishes cho lesterol binding reproduces phenotype of complete NPC1 deficiency in mice. Proc. Natl. Acad. Sci. U.S. A., 2011, 108, 15330-15335.
    • (2011) Proc. Natl. Acad. Sci. U.S. A. , vol.108 , pp. 15330-15335
    • Xie, X.1    Brown, M.S.2    Shelton, J.M.3    Richardson, J.A.4    Goldstein, J.L.5    Liang, G.6
  • 107
    • 0034704244 scopus 로고    scopus 로고
    • Transmembrane molecular pump activity of Niemann-Pick C1 protein
    • Davies, J.P.; Chen, F.W.; Ioannou, Y.A. Transmembrane molecular pump activity of Niemann-Pick C1 protein. Science, 2000, 290, 2295-2298.
    • (2000) Science , vol.290 , pp. 2295-2298
    • Davies, J.P.1    Chen, F.W.2    Ioannou, Y.A.3
  • 108
    • 15444376731 scopus 로고    scopus 로고
    • Flux of fatty acids through NPC1 lysosomes
    • Passeggio, J.; Liscum, L. Flux of fatty acids through NPC1 lysosomes. J. Biol. Chem., 2005, 280, 10333-10339.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10333-10339
    • Passeggio, J.1    Liscum, L.2
  • 109
    • 25144444288 scopus 로고    scopus 로고
    • NPC1 late endosomes contain elevated levels of non-esterified ('free') fatty acids and an abnormally glycosylated form of the NPC2 protein
    • Chen, F.W.; Gordon, R.E.; Ioannou, Y.A. NPC1 late endosomes contain elevated levels of non-esterified ('free') fatty acids and an abnormally glycosylated form of the NPC2 protein. Biochem. J., 2005, 390, 549-561.
    • (2005) Biochem. J. , vol.390 , pp. 549-561
    • Chen, F.W.1    Gordon, R.E.2    Ioannou, Y.A.3
  • 110
    • 0041700117 scopus 로고    scopus 로고
    • Cholesterol accumulation in NPC1-deficient neurons is ganglioside dependent
    • Gondre-Lewis, M.C.; McGlynn, R.; Walkley, S.U. Cholesterol accumulation in NPC1-deficient neurons is ganglioside dependent. Curr. Biol., 2003, 13, 1324-1329.
    • (2003) Curr. Biol. , vol.13 , pp. 1324-1329
    • Gondre-Lewis, M.C.1    McGlynn, R.2    Walkley, S.U.3
  • 112
    • 77951727293 scopus 로고    scopus 로고
    • Lipids on trial: The search for the offending metabolite in Niemann-Pick type C disease
    • Lloyd-Evans, E.; Platt, F.M. Lipids on trial: the search for the offending metabolite in Niemann-Pick type C disease. Traffic, 2010, 11, 419-428.
    • (2010) Traffic , vol.11 , pp. 419-428
    • Lloyd-Evans, E.1    Platt, F.M.2
  • 113
    • 23944442427 scopus 로고    scopus 로고
    • Guilty until proven innocent: The case of NPC1 and cholesterol
    • Ioannou, Y.A. Guilty until proven innocent: the case of NPC1 and cholesterol. Trends Biochem. Sci., 2005, 30, 498-505.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 498-505
    • Ioannou, Y.A.1
  • 114
    • 54049127788 scopus 로고    scopus 로고
    • Niemann-Pick C1 functions in regulating lysosomal amine content
    • Kaufmann, A.M.; Krise, J.P. Niemann-Pick C1 functions in regulating lysosomal amine content. J. Biol. Chem., 2008, 283, 24584-24593.
    • (2008) J. Biol. Chem. , vol.283 , pp. 24584-24593
    • Kaufmann, A.M.1    Krise, J.P.2
  • 115
    • 77951158568 scopus 로고    scopus 로고
    • Niemann-Pick C1 functions independently of Niemann-Pick C2 in the initial stage of retrograde transport of membrane-impermeable lysosomal cargo
    • Goldman, S.D.; Krise, J.P. Niemann-Pick C1 functions independently of Niemann-Pick C2 in the initial stage of retrograde transport of membrane-impermeable lysosomal cargo. J. Biol. Chem., 2010, 285, 4983-4994.
    • (2010) J. Biol. Chem. , vol.285 , pp. 4983-4994
    • Goldman, S.D.1    Krise, J.P.2
  • 116
    • 33845994402 scopus 로고    scopus 로고
    • NPC2, the protein deficient in Niemann-Pick C2 disease, consists of multiple glycoforms that bind a variety of sterols
    • Liou, H.L.; Dixit, S.S.; Xu, S.; Tint, G.S.; Stock, A.M.; Lobel, P. NPC2, the protein deficient in Niemann-Pick C2 disease, consists of multiple glycoforms that bind a variety of sterols. J. Biol. Chem., 2006, 281, 36710-36723.
    • (2006) J. Biol. Chem. , vol.281 , pp. 36710-36723
    • Liou, H.L.1    Dixit, S.S.2    Xu, S.3    Tint, G.S.4    Stock, A.M.5    Lobel, P.6
  • 117
    • 33750318425 scopus 로고    scopus 로고
    • Mechanism of cholesterol transfer from the Niemann-Pick type C2 protein to model membranes supports a role in lysosomal cholesterol transport
    • Cheruku, S.R.; Xu, Z.; Dutia, R.; Lobel, P.; Storch, J. Mechanism of cholesterol transfer from the Niemann-Pick type C2 protein to model membranes supports a role in lysosomal cholesterol transport. J. Biol. Chem., 2006, 281, 31594-31604.
    • (2006) J. Biol. Chem. , vol.281 , pp. 31594-31604
    • Cheruku, S.R.1    Xu, Z.2    Dutia, R.3    Lobel, P.4    Storch, J.5
  • 118
    • 54349098469 scopus 로고    scopus 로고
    • Regulation of sterol transport between membranes and NPC2
    • Xu, Z.; Farver, W.; Kodukula, S.; Storch, J. Regulation of sterol transport between membranes and NPC2. Biochemistry, 2008, 47, 11134-11143.
    • (2008) Biochemistry , vol.47 , pp. 11134-11143
    • Xu, Z.1    Farver, W.2    Kodukula, S.3    Storch, J.4
  • 119
    • 0344838432 scopus 로고    scopus 로고
    • The integrity of a cholesterol-binding pocket in Niemann-Pick C2 protein is necessary to control lysosome cholesterol levels
    • Ko, D.C.; Binkley, J.; Sidow, A.; Scott, M.P. The integrity of a cholesterol-binding pocket in Niemann-Pick C2 protein is necessary to control lysosome cholesterol levels. Proc. Natl. Acad. Sci. U. S. A., 2003, 100, 2518-2525.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 2518-2525
    • Ko, D.C.1    Binkley, J.2    Sidow, A.3    Scott, M.P.4
  • 120
    • 34548192003 scopus 로고    scopus 로고
    • Structural basis of sterol binding by NPC2, a lysosomal protein deficient in Niemann-Pick type C2 disease
    • Xu, S.; Benoff, B.; Liou, H.L.; Lobel, P.; Stock, A.M. Structural basis of sterol binding by NPC2, a lysosomal protein deficient in Niemann-Pick type C2 disease. J. Biol. Chem., 2007, 282, 23525-23531.
    • (2007) J. Biol. Chem. , vol.282 , pp. 23525-23531
    • Xu, S.1    Benoff, B.2    Liou, H.L.3    Lobel, P.4    Stock, A.M.5
  • 121
    • 78649916808 scopus 로고    scopus 로고
    • Identification of surface residues on Niemann-Pick C2 essential for hydrophobic handoff of cholesterol to NPC1 in lysosomes
    • Wang, M.L.; Motamed, M.; Infante, R.E.; Abi-Mosleh, L.; Kwon, H.J.; Brown, M.S.; Goldstein, J.L. Identification of surface residues on Niemann-Pick C2 essential for hydrophobic handoff of cholesterol to NPC1 in lysosomes. Cell Metab., 2010, 12, 166-173.
    • (2010) Cell Metab. , vol.12 , pp. 166-173
    • Wang, M.L.1    Motamed, M.2    Infante, R.E.3    Abi-Mosleh, L.4    Kwon, H.J.5    Brown, M.S.6    Goldstein, J.L.7
  • 122
    • 82755197370 scopus 로고    scopus 로고
    • Niemann-Pick type C 1 function requires lumenal domain residues that mediate cholesterol-dependent NPC2 binding
    • Deffieu, M.S.; Pfeffer, S.R. Niemann-Pick type C 1 function requires lumenal domain residues that mediate cholesterol-dependent NPC2 binding. Proc. Natl. Acad. Sci. USA, 2011, 108, 18932-18936.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 18932-18936
    • Deffieu, M.S.1    Pfeffer, S.R.2
  • 124
    • 77957352699 scopus 로고    scopus 로고
    • The diverse functions of oxysterolbinding proteins
    • Raychaudhuri, S.; Prinz, W.A. The diverse functions of oxysterolbinding proteins. Annu. Rev. Cell Dev. Biol., 2010, 26, 157-177.
    • (2010) Annu. Rev. Cell Dev. Biol. , vol.26 , pp. 157-177
    • Raychaudhuri, S.1    Prinz, W.A.2
  • 125
    • 38549141572 scopus 로고    scopus 로고
    • Cellular cholesterol trafficking and compartmentalization
    • Ikonen, E. Cellular cholesterol trafficking and compartmentalization. Nat. Rev. Mol. Cell Biol., 2008, 9, 125-138.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 125-138
    • Ikonen, E.1
  • 126
    • 0034064138 scopus 로고    scopus 로고
    • Structure and lipid transport mechanism of a StAR-related domain
    • Tsujishita, Y.; Hurley, J.H. Structure and lipid transport mechanism of a StAR-related domain. Nat. Struct. Biol., 2000, 7, 408-414.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 408-414
    • Tsujishita, Y.1    Hurley, J.H.2
  • 127
    • 77951087930 scopus 로고    scopus 로고
    • MLN64 mediates egress of cholesterol from endosomes to mitochondria in the absence of functional Niemann-Pick Type C1 protein
    • Charman, M.; Kennedy, B.E.; Osborne, N.; Karten, B. MLN64 mediates egress of cholesterol from endosomes to mitochondria in the absence of functional Niemann-Pick Type C1 protein. J. Lipid Res., 2010, 51, 1023-1034.
    • (2010) J. Lipid Res. , vol.51 , pp. 1023-1034
    • Charman, M.1    Kennedy, B.E.2    Osborne, N.3    Karten, B.4
  • 128
    • 67649600680 scopus 로고    scopus 로고
    • Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 Glued and late endosome positioning
    • Rocha, N.; Kuijl, C.; van der Kant, R.; Janssen, L.; Houben, D.; Janssen, H.; Zwart, W.; Neefjes, J. Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 Glued and late endosome positioning. J. Cell Biol., 2009, 185, 1209-1225.
    • (2009) J. Cell Biol. , vol.185 , pp. 1209-1225
    • Rocha, N.1    Kuijl, C.2    Van Der Kant, R.3    Janssen, L.4    Houben, D.5    Janssen, H.6    Zwart, W.7    Neefjes, J.8
  • 132
  • 133
    • 0037336348 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptors: New twists in the tale
    • Ghosh, P.; Dahms, N.M.; Kornfeld, S. Mannose 6-phosphate receptors: new twists in the tale. Nat. Rev. Mol. Cell Biol., 2003, 4, 202-212.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 202-212
    • Ghosh, P.1    Dahms, N.M.2    Kornfeld, S.3
  • 135
    • 0141876961 scopus 로고    scopus 로고
    • Telomerase immortalization upregulates Rab9 expression and restores LDL cholesterol egress from Niemann-Pick C1 late endosomes
    • Walter, M.; Davies, J.P.; Ioannou, Y.A. Telomerase immortalization upregulates Rab9 expression and restores LDL cholesterol egress from Niemann-Pick C1 late endosomes. J. Lipid Res., 2003, 44, 243-253.
    • (2003) J. Lipid Res. , vol.44 , pp. 243-253
    • Walter, M.1    Davies, J.P.2    Ioannou, Y.A.3
  • 136
    • 33745846377 scopus 로고    scopus 로고
    • Cholesterol accumulation sequesters Rab9 and disrupts late endosome function in NPC1-deficient cells
    • Ganley, I.G.; Pfeffer, S.R. Cholesterol accumulation sequesters Rab9 and disrupts late endosome function in NPC1-deficient cells. J. Biol. Chem., 2006, 281, 17890-17899.
    • (2006) J. Biol. Chem. , vol.281 , pp. 17890-17899
    • Ganley, I.G.1    Pfeffer, S.R.2
  • 138
    • 60049091317 scopus 로고    scopus 로고
    • Endosomal lipid accumulation in NPC1 leads to inhibition of PKC, hypophosphorylation of vimentin and Rab9 entrapment
    • Walter, M.; Chen, F.W.; Tamari, F.; Wang, R.; Ioannou, Y.A. Endosomal lipid accumulation in NPC1 leads to inhibition of PKC, hypophosphorylation of vimentin and Rab9 entrapment. Biol. Cell, 2009, 101, 141-152.
    • (2009) Biol. Cell , vol.101 , pp. 141-152
    • Walter, M.1    Chen, F.W.2    Tamari, F.3    Wang, R.4    Ioannou, Y.A.5
  • 139
    • 23844485910 scopus 로고    scopus 로고
    • PEST deletion mutant of ABCA1 shows impaired internalization and defective cholesterol efflux from late endosomes
    • Chen, W.; Wang, N.; Tall, A.R. A PEST deletion mutant of ABCA1 shows impaired internalization and defective cholesterol efflux from late endosomes. J. Biol. Chem., 2005, 280, 29277-29281.
    • (2005) J. Biol. Chem. , vol.280 , pp. 29277-29281
    • Chen, W.1    Wang, N.2    Tall, A.R.A.3
  • 143
    • 47049089673 scopus 로고    scopus 로고
    • ATP-binding cassette A1-mediated lipidation of apolipoprotein A-I occurs at the plasma membrane and not in the endocytic compartments
    • Denis, M.; Landry, Y.D.; Zha, X. ATP-binding cassette A1-mediated lipidation of apolipoprotein A-I occurs at the plasma membrane and not in the endocytic compartments. J. Biol. Chem., 2008, 283, 16178-16186.
    • (2008) J. Biol. Chem. , vol.283 , pp. 16178-16186
    • Denis, M.1    Landry, Y.D.2    Zha, X.3
  • 144
    • 67549139908 scopus 로고    scopus 로고
    • Vesicular trafficking and autophagosome formation
    • Longatti, A.; Tooze, S.A. Vesicular trafficking and autophagosome formation. Cell Death Differ., 2009, 16, 956-965.
    • (2009) Cell Death Differ. , vol.16 , pp. 956-965
    • Longatti, A.1    Tooze, S.A.2
  • 145
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima, N.; Levine, B.; Cuervo, A.M.; Klionsky, D.J. Autophagy fights disease through cellular self-digestion. Nature, 2008, 451, 1069-1075.
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 146
    • 43949143804 scopus 로고    scopus 로고
    • The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy
    • Fujita, N.; Itoh, T.; Omori, H.; Fukuda, M.; Noda, T.; Yoshimori, T. The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy. Mol. Biol. Cell, 2008, 19, 2092-2100.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2092-2100
    • Fujita, N.1    Itoh, T.2    Omori, H.3    Fukuda, M.4    Noda, T.5    Yoshimori, T.6
  • 147
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • Axe, E.L.; Walker, S.A.; Manifava, M.; Chandra, P.; Roderick, H.L.; Habermann, A.; Griffiths, G.; Ktistakis, N.T. Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum. J. Cell Biol., 2008, 182, 685-701.
    • (2008) J. Cell Biol. , vol.182 , pp. 685-701
    • Axe, E.L.1    Walker, S.A.2    Manifava, M.3    Chandra, P.4    Roderick, H.L.5    Habermann, A.6    Griffiths, G.7    Ktistakis, N.T.8
  • 149
    • 71649112895 scopus 로고    scopus 로고
    • 3D tomography reveals connections between the phagophore and endoplasmic reticulum
    • Yla-Anttila, P.; Vihinen, H.; Jokitalo, E.; Eskelinen, E.L. 3D tomography reveals connections between the phagophore and endoplasmic reticulum. Autophagy, 2009, 5, 1180-1185.
    • (2009) Autophagy , vol.5 , pp. 1180-1185
    • Yla-Anttila, P.1    Vihinen, H.2    Jokitalo, E.3    Eskelinen, E.L.4
  • 150
    • 71649091524 scopus 로고    scopus 로고
    • The EmERgence of autophagosomes
    • Reggiori, F.; Tooze, S.A. The EmERgence of autophagosomes. Dev. Cell, 2009, 17, 747-748.
    • (2009) Dev. Cell , vol.17 , pp. 747-748
    • Reggiori, F.1    Tooze, S.A.2
  • 154
    • 77955131007 scopus 로고    scopus 로고
    • Plasma membrane contributes to the formation of preautophagosomal structures
    • Ravikumar, B.; Moreau, K.; Jahreiss, L.; Puri, C.; Rubinsztein, D.C. Plasma membrane contributes to the formation of preautophagosomal structures. Nat. Cell Biol., 2010, 12, 747-757.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 747-757
    • Ravikumar, B.1    Moreau, K.2    Jahreiss, L.3    Puri, C.4    Rubinsztein, D.C.5
  • 157
  • 158
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin, V.; McEwan, D.G.; Novak, I.; Dikic, I. A role for ubiquitin in selective autophagy. Mol Cell, 2009, 34, 259-269.
    • (2009) Mol Cell , vol.34 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 159
    • 64049118343 scopus 로고    scopus 로고
    • A role for ubiquitin ligases and Spartin/SPG20 in lipid droplet turnover
    • Eastman, S.W.; Yassaee, M.; Bieniasz, P.D. A role for ubiquitin ligases and Spartin/SPG20 in lipid droplet turnover. J. Cell Biol., 2009, 184, 881-894.
    • (2009) J. Cell Biol. , vol.184 , pp. 881-894
    • Eastman, S.W.1    Yassaee, M.2    Bieniasz, P.D.3
  • 160
    • 77952616841 scopus 로고    scopus 로고
    • Spartin activates atrophin-1-interacting protein 4 (AIP4) E3 ubiquitin ligase and promotes ubiquitination of adipophilin on lipid droplets
    • Hooper, C.; Puttamadappa, S.S.; Loring, Z.; Shekhtman, A.; Bakowska, J.C. Spartin activates atrophin-1-interacting protein 4 (AIP4) E3 ubiquitin ligase and promotes ubiquitination of adipophilin on lipid droplets. BMC Biol., 2010, 8, 72.
    • (2010) BMC Biol. , vol.8 , pp. 72
    • Hooper, C.1    Puttamadappa, S.S.2    Loring, Z.3    Shekhtman, A.4    Bakowska, J.C.5
  • 162
    • 1842639444 scopus 로고    scopus 로고
    • Effects of cholesterol depletion and increased lipid unsaturation on the properties of endocytic membranes
    • Hao, M.; Mukherjee, S.; Sun, Y.; Maxfield, F.R. Effects of cholesterol depletion and increased lipid unsaturation on the properties of endocytic membranes. J. Biol. Chem., 2004, 279, 14171-14178.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14171-14178
    • Hao, M.1    Mukherjee, S.2    Sun, Y.3    Maxfield, F.R.4
  • 163
    • 0344791683 scopus 로고    scopus 로고
    • Endocytic sorting of lipid analogues differing solely in the chemistry of their hydrophobic tails
    • Mukherjee, S.; Soe, T.T.; Maxfield, F.R. Endocytic sorting of lipid analogues differing solely in the chemistry of their hydrophobic tails. J. Cell Biol., 1999, 144, 1271-1284.
    • (1999) J. Cell Biol. , vol.144 , pp. 1271-1284
    • Mukherjee, S.1    Soe, T.T.2    Maxfield, F.R.3
  • 164
    • 1142274307 scopus 로고    scopus 로고
    • Partitioning of pyrene-labeled phospho- and sphingolipids between ordered and disordered bilayer domains
    • Koivusalo, M.; Alvesalo, J.; Virtanen, J.A.; Somerharju, P. Partitioning of pyrene-labeled phospho- and sphingolipids between ordered and disordered bilayer domains. Biophys. J., 2004, 86, 923-935.
    • (2004) Biophys. J. , vol.86 , pp. 923-935
    • Koivusalo, M.1    Alvesalo, J.2    Virtanen, J.A.3    Somerharju, P.4
  • 165
    • 77951924919 scopus 로고    scopus 로고
    • Lysosomal degradation of membrane lipids
    • Kolter, T.; Sandhoff, K. Lysosomal degradation of membrane lipids. FEBS Lett., 2010, 584, 1700-1712.
    • (2010) FEBS Lett. , vol.584 , pp. 1700-1712
    • Kolter, T.1    Sandhoff, K.2
  • 166
    • 0025287536 scopus 로고
    • Characterization and cloning of lgp110, a lysosomal membrane glycoprotein from mouse and rat cells
    • Granger, B.L.; Green, S.A.; Gabel, C.A.; Howe, C.L.; Mellman, I.; Helenius, A. Characterization and cloning of lgp110, a lysosomal membrane glycoprotein from mouse and rat cells. J. Biol. Chem., 1990, 265, 12036-12043.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12036-12043
    • Granger, B.L.1    Green, S.A.2    Gabel, C.A.3    Howe, C.L.4    Mellman, I.5    Helenius, A.6
  • 167
    • 0032742816 scopus 로고    scopus 로고
    • Asparagine-linked oligosaccharides protect Lamp-1 and Lamp-2 from intracellular proteolysis
    • Kundra, R.; Kornfeld, S. Asparagine-linked oligosaccharides protect Lamp-1 and Lamp-2 from intracellular proteolysis. J. Biol. Chem., 1999, 274, 31039-31046.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31039-31046
    • Kundra, R.1    Kornfeld, S.2
  • 168
    • 0016836751 scopus 로고
    • Role of lysosomal acid lipase in the metabolism of plasma low density lipoprotein. Observations in cultured fibroblasts from a patient with cholesteryl ester storage disease
    • Goldstein, J.L.; Dana, S.E.; Faust, J.R.; Beaudet, A.L.; Brown, M.S. Role of lysosomal acid lipase in the metabolism of plasma low density lipoprotein. Observations in cultured fibroblasts from a patient with cholesteryl ester storage disease. J. Biol. Chem., 1975, 250, 8487-8495.
    • (1975) J. Biol. Chem. , vol.250 , pp. 8487-8495
    • Goldstein, J.L.1    Dana, S.E.2    Faust, J.R.3    Beaudet, A.L.4    Brown, M.S.5
  • 169
    • 0019446127 scopus 로고
    • Purification of the lysosomal acid lipase from human liver and its role in lysosomal lipid hydrolysis
    • Warner, T.G.; Dambach, L.M.; Shin, J.H.; O'Brien, J.S. Purification of the lysosomal acid lipase from human liver and its role in lysosomal lipid hydrolysis. J. Biol. Chem., 1981, 256, 2952-2957.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2952-2957
    • Warner, T.G.1    Dambach, L.M.2    Shin, J.H.3    O'Brien, J.S.4
  • 170
    • 0022968919 scopus 로고
    • Synthesis and hydrolysis of cholesteryl esters by isolated rat-liver lysosomes and cell-free extracts of human lung fibroblasts
    • Slotte, J.P.; Ekman, S. Synthesis and hydrolysis of cholesteryl esters by isolated rat-liver lysosomes and cell-free extracts of human lung fibroblasts.
    • (1986) Biochim. Biophys. Acta , vol.879 , pp. 221-228
    • Slotte, J.P.1    Ekman, S.2
  • 171
    • 0023432449 scopus 로고
    • Effects of substrate composition on the esterification and hydrolysis activity of lysosomal acid sterol ester hydrolase
    • Ekman, S.; Slotte, J.P. Effects of substrate composition on the esterification and hydrolysis activity of lysosomal acid sterol ester hydrolase. Chem. Phys. Lipids, 1987, 45, 13-25.
    • (1987) Chem. Phys. Lipids , vol.45 , pp. 13-25
    • Ekman, S.1    Slotte, J.P.2
  • 172
    • 0031692456 scopus 로고    scopus 로고
    • Molecular and enzymatic analyses of lysosomal acid lipase in cholesteryl ester storage disease
    • Du, H.; Sheriff, S.; Bezerra, J.; Leonova, T.; Grabowski, G.A. Molecular and enzymatic analyses of lysosomal acid lipase in cholesteryl ester storage disease. Mol. Genet. Metab., 1998, 64, 126-134.
    • (1998) Mol. Genet. Metab. , vol.64 , pp. 126-134
    • Du, H.1    Sheriff, S.2    Bezerra, J.3    Leonova, T.4    Grabowski, G.A.5
  • 173
    • 0025323370 scopus 로고
    • Cholesterol esters selectively taken up from high-density lipoproteins are hydrolyzed extralysosomally
    • Sparrow, C.P.; Pittman, R.C. Cholesterol esters selectively taken up from high-density lipoproteins are hydrolyzed extralysosomally. Biochim. Biophys. Acta, 1990, 1043, 203-210.
    • (1990) Biochim. Biophys. Acta , vol.1043 , pp. 203-210
    • Sparrow, C.P.1    Pittman, R.C.2
  • 174
    • 0030470972 scopus 로고    scopus 로고
    • Metabolic fate of oleic acid derived from lysosomal degradation of cholesteryl oleate in human fibroblasts
    • Groener, J.E.; Bax, W.; Poorthuis, B.J. Metabolic fate of oleic acid derived from lysosomal degradation of cholesteryl oleate in human fibroblasts. J. Lipid Res., 1996, 37, 2271-2279.
    • (1996) J. Lipid Res. , vol.37 , pp. 2271-2279
    • Groener, J.E.1    Bax, W.2    Poorthuis, B.J.3
  • 175
    • 0024308504 scopus 로고
    • Hydrolysis of dolichyl esters by rat liver lysosomes
    • Tollbom, O.; Chojnacki, T.; Dallner, G. Hydrolysis of dolichyl esters by rat liver lysosomes. J. Biol. Chem., 1989, 264, 9836-9841.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9836-9841
    • Tollbom, O.1    Chojnacki, T.2    Dallner, G.3
  • 176
    • 34047093981 scopus 로고    scopus 로고
    • Defect in fatty acid esterification of dolichol in Niemann-Pick type C1 mouse livers in vivo
    • Turunen, M.; Schedin-Weiss, S. Defect in fatty acid esterification of dolichol in Niemann-Pick type C1 mouse livers in vivo. Biochim. Biophys. Acta, 2007, 1771, 506-513.
    • (2007) Biochim. Biophys. Acta , vol.1771 , pp. 506-513
    • Turunen, M.1    Schedin-Weiss, S.2
  • 177
    • 0015219599 scopus 로고
    • Identification of phospholipase A 1 and A 2 in the soluble fraction of rat liver lysosomes
    • Franson, R.; Waite, M.; LaVia, M. Identification of phospholipase A 1 and A 2 in the soluble fraction of rat liver lysosomes. Biochemistry, 1971, 10, 1942-1946.
    • (1971) Biochemistry , vol.10 , pp. 1942-1946
    • Franson, R.1    Waite, M.2    Lavia, M.3
  • 178
    • 0029891058 scopus 로고    scopus 로고
    • A novel enzyme that catalyzes the esterification of N-acetylsphingosine. Metabolism of C2-ceramides
    • Abe, A.; Shayman, J.A.; Radin, N.S. A novel enzyme that catalyzes the esterification of N-acetylsphingosine. Metabolism of C2-ceramides. J. Biol. Chem., 1996, 271, 14383-14389.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14383-14389
    • Abe, A.1    Shayman, J.A.2    Radin, N.S.3
  • 179
    • 78649794770 scopus 로고    scopus 로고
    • Group XV phospholipase A(2), a lysosomal phospholipase A(2)
    • Shayman, J.A.; Kelly, R.; Kollmeyer, J.; He, Y.; Abe, A. Group XV phospholipase A(2), a lysosomal phospholipase A(2). Prog Lipid Res., 2011, 50, 1-13.
    • (2011) Prog Lipid Res. , vol.50 , pp. 1-13
    • Shayman, J.A.1    Kelly, R.2    Kollmeyer, J.3    He, Y.4    Abe, A.5
  • 180
    • 0018871467 scopus 로고
    • Properties of phospholipase C isolated from rat liver lysosomes
    • Matsuzawa, Y.; Hostetler, K.Y. Properties of phospholipase C isolated from rat liver lysosomes. J. Biol. Chem., 1980, 255, 646-652.
    • (1980) J. Biol. Chem. , vol.255 , pp. 646-652
    • Matsuzawa, Y.1    Hostetler, K.Y.2
  • 181
    • 0032474821 scopus 로고    scopus 로고
    • Phospholipase D1 localises to secretory granules and lysosomes and is plasmamembrane translocated on cellular stimulation
    • Brown, F.D.; Thompson, N.; Saqib, K.M.; Clark, J.M.; Powner, D.; Thompson, N.T.; Solari, R.; Wakelam, M.J. Phospholipase D1 localises to secretory granules and lysosomes and is plasmamembrane translocated on cellular stimulation. Curr. Biol., 1998, 8, 835-838.
    • (1998) Curr. Biol. , vol.8 , pp. 835-838
    • Brown, F.D.1    Thompson, N.2    Saqib, K.M.3    Clark, J.M.4    Powner, D.5    Thompson, N.T.6    Solari, R.7    Wakelam, M.J.8
  • 182
    • 0032934814 scopus 로고    scopus 로고
    • Colocalization of phospholipase D1 and GTP-binding-defective mutant of ADP-ribosylation factor 6 to endosomes and lysosomes
    • Toda, K.; Nogami, M.; Murakami, K.; Kanaho, Y.; Nakayama, K. Colocalization of phospholipase D1 and GTP-binding-defective mutant of ADP-ribosylation factor 6 to endosomes and lysosomes. FEBS Lett., 1999, 442, 221-225.
    • (1999) FEBS Lett. , vol.442 , pp. 221-225
    • Toda, K.1    Nogami, M.2    Murakami, K.3    Kanaho, Y.4    Nakayama, K.5
  • 183
    • 0021245299 scopus 로고
    • Degradation of lysophosphatidylcholine by lysosomes. Stimulation of lysophospholipase C by taurocholate and deficiency in Niemann-Pick fibroblasts
    • Huterer, S.; Wherrett, J.R. Degradation of lysophosphatidylcholine by lysosomes. Stimulation of lysophospholipase C by taurocholate and deficiency in Niemann-Pick fibroblasts. Biochim. Biophys. Acta, 1984, 794, 1-8.
    • (1984) Biochim. Biophys. Acta , vol.794 , pp. 1-8
    • Huterer, S.1    Wherrett, J.R.2
  • 184
    • 0018164561 scopus 로고
    • The hydrolysis of phosphatidylinositol by lysosomal enzymes of rat liver and brain
    • Irvine, R.F.; Hemington, N.; Dawson, R.M. The hydrolysis of phosphatidylinositol by lysosomal enzymes of rat liver and brain. Biochem. J., 1978, 176, 475-484.
    • (1978) Biochem. J. , vol.176 , pp. 475-484
    • Irvine, R.F.1    Hemington, N.2    Dawson, R.M.3
  • 185
    • 0019989749 scopus 로고
    • Hydrolytic degradation of phosphatidylethanolamine and phosphatidylcholine by isolated rat-liver lysosomes
    • Kunze, H.; Hesse, B.; Bohn, E. Hydrolytic degradation of phosphatidylethanolamine and phosphatidylcholine by isolated rat-liver lysosomes. Biochim. Biophys. Acta, 1982, 711, 10-18.
    • (1982) Biochim. Biophys. Acta , vol.711 , pp. 10-18
    • Kunze, H.1    Hesse, B.2    Bohn, E.3
  • 186
    • 0027312942 scopus 로고
    • Intralysosomal glycerophospholipid catabolism in liver: Hydrolysis of amino alcohol-containing phospholipids and their metabolites
    • Kunze, H. Intralysosomal glycerophospholipid catabolism in liver: hydrolysis of amino alcohol-containing phospholipids and their metabolites. Biochim. Biophys. Acta, 1993, 1169, 273-279.
    • (1993) Biochim. Biophys. Acta , vol.1169 , pp. 273-279
    • Kunze, H.1
  • 187
    • 0023664425 scopus 로고
    • Fractionation, biochemical characterization and lysosomal phospholipases of human liver
    • Loffler, B.M.; Kunze, H. Fractionation, biochemical characterization and lysosomal phospholipases of human liver. FEBS Lett., 1987, 216, 51-56.
    • (1987) FEBS Lett. , vol.216 , pp. 51-56
    • Loffler, B.M.1    Kunze, H.2
  • 188
    • 0018688289 scopus 로고
    • Hydrolysis of membrane phospholipids by phospholipases of rat liver lysosomes
    • Richards, D.E.; Irvine, R.F.; Dawson, R.M. Hydrolysis of membrane phospholipids by phospholipases of rat liver lysosomes. Biochem. J., 1979, 182, 599-606.
    • (1979) Biochem. J. , vol.182 , pp. 599-606
    • Richards, D.E.1    Irvine, R.F.2    Dawson, R.M.3
  • 189
    • 0019811653 scopus 로고
    • Endogenous lipolytic activities during autolysis of highly enriched hepatic lysosomes
    • Beckman, J.K.; Owens, K.; Weglicki, W.B. Endogenous lipolytic activities during autolysis of highly enriched hepatic lysosomes. Lipids, 1981, 16, 796-799.
    • (1981) Lipids , vol.16 , pp. 796-799
    • Beckman, J.K.1    Owens, K.2    Weglicki, W.B.3
  • 191
    • 0016121227 scopus 로고
    • Novel stereoconfiguration in lyso-bis-phosphatidic acid of cultured BHKcells
    • Brotherus, J.; Renkonen, O.; Fischer, W.; Herrmann, J. Novel stereoconfiguration in lyso-bis-phosphatidic acid of cultured BHKcells. Chem. Phys. Lipids, 1974, 13, 178-182.
    • (1974) Chem. Phys. Lipids , vol.13 , pp. 178-182
    • Brotherus, J.1    Renkonen, O.2    Fischer, W.3    Herrmann, J.4
  • 192
    • 0018786885 scopus 로고
    • Degradation of bis(monoacylglycero)phosphate by an acid phosphodiesterase in rat liver lysosomes
    • Matsuzawa, Y.; Hostetler, K.Y. Degradation of bis(monoacylglycero) phosphate by an acid phosphodiesterase in rat liver lysosomes. J. Biol. Chem., 1979, 254, 5997-6001.
    • (1979) J. Biol. Chem. , vol.254 , pp. 5997-6001
    • Matsuzawa, Y.1    Hostetler, K.Y.2
  • 193
    • 0033602394 scopus 로고    scopus 로고
    • Transacylase formation of bis(monoacylglycerol)phosphate
    • Heravi, J.; Waite, M. Transacylase formation of bis(monoacylglycerol) phosphate. Biochim. Biophys. Acta, 1999, 1437, 277-286.
    • (1999) Biochim. Biophys. Acta , vol.1437 , pp. 277-286
    • Heravi, J.1    Waite, M.2
  • 194
    • 78649720042 scopus 로고    scopus 로고
    • Molecular mechanisms of pathogenesis in a glycosphingolipid and a glycoprotein storage disease
    • d'Azzo, A.; Bonten, E. Molecular mechanisms of pathogenesis in a glycosphingolipid and a glycoprotein storage disease. Biochem. Soc. Trans., 2010, 38, 1453-1457.
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 1453-1457
    • D'Azzo, A.1    Bonten, E.2
  • 197
    • 12844280581 scopus 로고    scopus 로고
    • A mutation in the saposin A coding region of the prosaposin gene in an infant presenting as Krabbe disease: First report of saposin A deficiency in humans
    • Spiegel, R.; Bach, G.; Sury, V.; Mengistu, G.; Meidan, B.; Shalev, S.; Shneor, Y.; Mandel, H.; Zeigler, M. A mutation in the saposin A coding region of the prosaposin gene in an infant presenting as Krabbe disease: first report of saposin A deficiency in humans. Mol. Genet. Metab., 2005, 84, 160-166.
    • (2005) Mol. Genet. Metab. , vol.84 , pp. 160-166
    • Spiegel, R.1    Bach, G.2    Sury, V.3    Mengistu, G.4    Meidan, B.5    Shalev, S.6    Shneor, Y.7    Mandel, H.8    Zeigler, M.9
  • 199
    • 0035937146 scopus 로고    scopus 로고
    • Interfacial regulation of acid ceramidase activity. Stimulation of ceramide degradation by lysosomal lipids and sphingolipid activator proteins
    • Linke, T.; Wilkening, G.; Sadeghlar, F.; Mozcall, H.; Bernardo, K.; Schuchman, E.; Sandhoff, K. Interfacial regulation of acid ceramidase activity. Stimulation of ceramide degradation by lysosomal lipids and sphingolipid activator proteins. J. Biol. Chem., 2001, 276, 5760-5768.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5760-5768
    • Linke, T.1    Wilkening, G.2    Sadeghlar, F.3    Mozcall, H.4    Bernardo, K.5    Schuchman, E.6    Sandhoff, K.7
  • 201
    • 77953499076 scopus 로고    scopus 로고
    • Multi-system disorders of glycosphingolipid and ganglioside metabolism
    • Xu, Y.H.; Barnes, S.; Sun, Y.; Grabowski, G.A. Multi-system disorders of glycosphingolipid and ganglioside metabolism. J. Lipid Res., 2010, 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
  • 204
    • 69449087070 scopus 로고    scopus 로고
    • Endocytosis of lipid-anchored proteins: Excluding GEECs from the crowd
    • Nichols, B. Endocytosis of lipid-anchored proteins: excluding GEECs from the crowd. J. Cell Biol., 2009, 186, 457-459.
    • (2009) J. Cell Biol. , vol.186 , pp. 457-459
    • Nichols, B.1
  • 206
    • 0036232040 scopus 로고    scopus 로고
    • GPI-anchored proteins are delivered to recycling endosomes via a distinct cdc42-regulated, clathrin-independent pinocytic pathway
    • Sabharanjak, S.; Sharma, P.; Parton, R.G.; Mayor, S. GPI-anchored proteins are delivered to recycling endosomes via a distinct cdc42-regulated, clathrin-independent pinocytic pathway. Dev. Cell, 2002, 2, 411-423.
    • (2002) Dev. Cell , vol.2 , pp. 411-423
    • Sabharanjak, S.1    Sharma, P.2    Parton, R.G.3    Mayor, S.4
  • 207
    • 0029796521 scopus 로고    scopus 로고
    • Subcellular distribution of glycosylphosphatidylinositol-specific phospholipase D in rat liver
    • Hari, T.; Kunze, H.; Bohn, E.; Brodbeck, U.; Butikofer, P. Subcellular distribution of glycosylphosphatidylinositol-specific phospholipase D in rat liver. Biochem. J., 1996, 320 (Pt 1), 315-319.
    • (1996) Biochem. J. , vol.320 , Issue.PART 1 , pp. 315-319
    • Hari, T.1    Kunze, H.2    Bohn, E.3    Brodbeck, U.4    Butikofer, P.5
  • 208
    • 33746075254 scopus 로고    scopus 로고
    • Thematic review series: Lipid posttranslational modifications. Lysosomal metabolism of lipid-modified proteins
    • Lu, J.Y.; Hofmann, S.L. Thematic review series: lipid posttranslational modifications. Lysosomal metabolism of lipid-modified proteins. J. Lipid Res., 2006, 47, 1352-1357.
    • (2006) J. Lipid Res. , vol.47 , pp. 1352-1357
    • Lu, J.Y.1    Hofmann, S.L.2
  • 210
    • 0035865135 scopus 로고    scopus 로고
    • Rabinteracting lysosomal protein (RILP): The Rab7 effector required for transport to lysosomes
    • Cantalupo, G.; Alifano, P.; Roberti, V.; Bruni, C.B.; Bucci, C. Rabinteracting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes. Embo J, 2001, 20, 683-693.
    • (2001) Embo J , vol.20 , pp. 683-693
    • Cantalupo, G.1    Alifano, P.2    Roberti, V.3    Bruni, C.B.4    Bucci, C.5
  • 211
    • 0028803110 scopus 로고
    • The rab7 GTPase resides on a vesicular compartment connected to lysosomes
    • Meresse, S.; Gorvel, J.P.; Chavrier, P. The rab7 GTPase resides on a vesicular compartment connected to lysosomes. J. Cell Sci., 1995, 108 (Pt 11), 3349-3358.
    • (1995) J. Cell Sci. , vol.108 , Issue.PART 11 , pp. 3349-3358
    • Meresse, S.1    Gorvel, J.P.2    Chavrier, P.3
  • 212
    • 0035163949 scopus 로고    scopus 로고
    • Dynamic movements of organelles containing Niemann-Pick C1 protein: NPC1 involvement in late endocytic events
    • Ko, D.C.; Gordon, M.D.; Jin, J.Y.; Scott, M.P. Dynamic movements of organelles containing Niemann-Pick C1 protein: NPC1 involvement in late endocytic events. Mol. Biol. Cell, 2001, 12, 601-614.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 601-614
    • Ko, D.C.1    Gordon, M.D.2    Jin, J.Y.3    Scott, M.P.4
  • 214
    • 55549111249 scopus 로고    scopus 로고
    • Coordinated lipid transfer between the endoplasmic reticulum and the Golgi complex requires the VAP proteins and is essential for Golgi-mediated transport
    • Peretti, D.; Dahan, N.; Shimoni, E.; Hirschberg, K.; Lev, S. Coordinated lipid transfer between the endoplasmic reticulum and the Golgi complex requires the VAP proteins and is essential for Golgi-mediated transport. Mol. Biol. Cell, 2008, 19, 3871-3884.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3871-3884
    • Peretti, D.1    Dahan, N.2    Shimoni, E.3    Hirschberg, K.4    Lev, S.5
  • 215
    • 28644446115 scopus 로고    scopus 로고
    • The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments
    • Johansson, M.; Lehto, M.; Tanhuanpaa, K.; Cover, T.L.; Olkkonen, V.M. The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments. Mol. Biol. Cell, 2005, 16, 5480-5492.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5480-5492
    • Johansson, M.1    Lehto, M.2    Tanhuanpaa, K.3    Cover, T.L.4    Olkkonen, V.M.5
  • 216
    • 18444381428 scopus 로고    scopus 로고
    • Structural basis for recruitment of RILP by small GTPase Rab7
    • Wu, M.; Wang, T.; Loh, E.; Hong, W.; Song, H. Structural basis for recruitment of RILP by small GTPase Rab7. Embo. J., 2005, 24, 1491-1501.
    • (2005) Embo. J. , vol.24 , pp. 1491-1501
    • Wu, M.1    Wang, T.2    Loh, E.3    Hong, W.4    Song, H.5
  • 217
    • 33847003020 scopus 로고    scopus 로고
    • Activation of endosomal dynein motors by stepwise assembly of Rab7-RILP-p150Glued, ORP1L, and the receptor betalll spectrin
    • Johansson, M.; Rocha, N.; Zwart, W.; Jordens, I.; Janssen, L.; Kuijl, C.; Olkkonen, V.M.; Neefjes, J. Activation of endosomal dynein motors by stepwise assembly of Rab7-RILP-p150Glued, ORP1L, and the receptor betalll spectrin. J. Cell Biol., 2007, 176, 459-471.
    • (2007) J. Cell Biol. , vol.176 , pp. 459-471
    • Johansson, M.1    Rocha, N.2    Zwart, W.3    Jordens, I.4    Janssen, L.5    Kuijl, C.6    Olkkonen, V.M.7    Neefjes, J.8
  • 220
    • 0032563304 scopus 로고    scopus 로고
    • Circulation of cholesterol between lysosomes and the plasma membrane
    • Lange, Y.; Ye, J.; Steck, T.L. Circulation of cholesterol between lysosomes and the plasma membrane. J. Biol. Chem., 1998, 273, 18915-18922.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18915-18922
    • Lange, Y.1    Ye, J.2    Steck, T.L.3
  • 222
    • 4644263342 scopus 로고    scopus 로고
    • Elevated endosomal cholesterol levels in Niemann-Pick cells inhibit rab4 and perturb membrane recycling
    • Choudhury, A.; Sharma, D.K.; Marks, D.L.; Pagano, R.E. Elevated endosomal cholesterol levels in Niemann-Pick cells inhibit rab4 and perturb membrane recycling. Mol. Biol. Cell, 2004, 15, 4500-4511.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4500-4511
    • Choudhury, A.1    Sharma, D.K.2    Marks, D.L.3    Pagano, R.E.4
  • 223
    • 0033203501 scopus 로고    scopus 로고
    • Cholesterol modulates membrane traffic along the endocytic pathway in sphingolipid-storage diseases
    • Puri, V.; Watanabe, R.; Dominguez, M.; Sun, X.; Wheatley, C.L.; Marks, D.L.; Pagano, R.E. Cholesterol modulates membrane traffic along the endocytic pathway in sphingolipid-storage diseases. Nat. Cell Biol., 1999, 1, 386-388.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 386-388
    • Puri, V.1    Watanabe, R.2    Dominguez, M.3    Sun, X.4    Wheatley, C.L.5    Marks, D.L.6    Pagano, R.E.7
  • 224
    • 0034329025 scopus 로고    scopus 로고
    • Membrane traffic in sphingolipid storage diseases
    • Pagano, R.E.; Puri, V.; Dominguez, M.; Marks, D.L. Membrane traffic in sphingolipid storage diseases. Traffic, 2000, 1, 807-815.
    • (2000) Traffic , vol.1 , pp. 807-815
    • Pagano, R.E.1    Puri, V.2    Dominguez, M.3    Marks, D.L.4
  • 225
    • 33846224732 scopus 로고    scopus 로고
    • Sterol, protein and lipid trafficking in Chinese hamster ovary cells with Niemann-Pick type C1 defect
    • Pipalia, N.H.; Hao, M.; Mukherjee, S.; Maxfield, F.R. Sterol, protein and lipid trafficking in Chinese hamster ovary cells with Niemann-Pick type C1 defect. Traffic, 2007, 8, 130-141.
    • (2007) Traffic , vol.8 , pp. 130-141
    • Pipalia, N.H.1    Hao, M.2    Mukherjee, S.3    Maxfield, F.R.4
  • 226
    • 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.; Pipalia, N.H.; Liao, X.; Schuchman, E.H.; Maxfield, F.R.; Tabas, I. Improvement in lipid and protein trafficking in Niemann-Pick C1 cells by correction of a secondary enzyme defect. Traffic, 2010, 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
  • 229
    • 34548860918 scopus 로고    scopus 로고
    • Cholesterol accumulation is associated with lysosomal dysfunction and autophagic stress in Npc1 -/- mouse brain
    • Liao, G.; Yao, Y.; Liu, J.; Yu, Z.; Cheung, S.; Xie, A.; Liang, X.; Bi, X. Cholesterol accumulation is associated with lysosomal dysfunction and autophagic stress in Npc1 -/- mouse brain. Am. J. Pathol., 2007, 171, 962-975.
    • (2007) Am. J. Pathol. , vol.171 , pp. 962-975
    • Liao, G.1    Yao, Y.2    Liu, J.3    Yu, Z.4    Cheung, S.5    Xie, A.6    Liang, X.7    Bi, X.8
  • 233
    • 77957294848 scopus 로고    scopus 로고
    • Autophagic pathways and metabolic stress
    • Kaushik, S.; Singh, R.; Cuervo, A.M. Autophagic pathways and metabolic stress. Diabetes Obes. Metab., 2010, 12 Suppl 2, 4-14.
    • (2010) Diabetes Obes. Metab. , vol.12 , Issue.SUPPL. 2 , pp. 4-14
    • Kaushik, S.1    Singh, R.2    Cuervo, A.M.3
  • 234
    • 0029837453 scopus 로고    scopus 로고
    • A receptor for the selective uptake and degradation of proteins by lysosomes
    • Cuervo, A.M.; Dice, J.F. A receptor for the selective uptake and degradation of proteins by lysosomes. Science, 1996, 273, 501-503.
    • (1996) Science , vol.273 , pp. 501-503
    • Cuervo, A.M.1    Dice, J.F.2
  • 235
    • 0037413688 scopus 로고    scopus 로고
    • Cathepsin A regulates chaperone-mediated autophagy through cleavage of the lysosomal receptor
    • Cuervo, A.M.; Mann, L.; Bonten, E.J.; d'Azzo, A.; Dice, J.F. Cathepsin A regulates chaperone-mediated autophagy through cleavage of the lysosomal receptor. Embo. J., 2003, 22, 47-59.
    • (2003) Embo. J. , vol.22 , pp. 47-59
    • Cuervo, A.M.1    Mann, L.2    Bonten, E.J.3    D'Azzo, A.4    Dice, J.F.5
  • 238
    • 33744948514 scopus 로고    scopus 로고
    • Free fatty acids induce JNK-dependent hepatocyte lipoapoptosis
    • Malhi, H.; Bronk, S.F.; Werneburg, N.W.; Gores, G.J. Free fatty acids induce JNK-dependent hepatocyte lipoapoptosis. J. Biol. Chem., 2006, 281, 12093-12101.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12093-12101
    • Malhi, H.1    Bronk, S.F.2    Werneburg, N.W.3    Gores, G.J.4
  • 239
    • 0034755341 scopus 로고    scopus 로고
    • Nutritional and metabolic considerations in the etiology of nonalcoholic steatohepatitis
    • Nehra, V.; Angulo, P.; Buchman, A.L.; Lindor, K.D. Nutritional and metabolic considerations in the etiology of nonalcoholic steatohepatitis. Dig. Dis. Sci., 2001, 46, 2347-2352.
    • (2001) Dig. Dis. Sci. , vol.46 , pp. 2347-2352
    • Nehra, V.1    Angulo, P.2    Buchman, A.L.3    Lindor, K.D.4
  • 240
    • 33845490856 scopus 로고    scopus 로고
    • Review: The role of insulin resistance in nonalcoholic fatty liver disease
    • Utzschneider, K.M.; Kahn, S.E. Review: The role of insulin resistance in nonalcoholic fatty liver disease. J. Clin. Endocrinol. Metab., 2006, 91, 4753-4761.
    • (2006) J. Clin. Endocrinol. Metab. , vol.91 , pp. 4753-4761
    • Utzschneider, K.M.1    Kahn, S.E.2
  • 241
    • 0031947715 scopus 로고    scopus 로고
    • Steatohepatitis: A tale of two "hits"?
    • Day, C.P.; James, O.F. Steatohepatitis: a tale of two "hits"? Gastroenterology, 1998, 114, 842-845.
    • (1998) Gastroenterology , vol.114 , pp. 842-845
    • Day, C.P.1    James, O.F.2
  • 243
    • 34250356015 scopus 로고    scopus 로고
    • Inhibiting triglyceride synthesis improves hepatic steatosis but exacerbates liver damage and fibrosis in obese mice with nonalcoholic steatohepatitis
    • Yamaguchi, K.; Yang, L.; McCall, S.; Huang, J.; Yu, X.X.; Pandey, S.K.; Bhanot, S.; Monia, B.P.; Li, Y.X.; Diehl, A.M. Inhibiting triglyceride synthesis improves hepatic steatosis but exacerbates liver damage and fibrosis in obese mice with nonalcoholic steatohepatitis. Hepatology, 2007, 45, 1366-1374.
    • (2007) Hepatology , vol.45 , pp. 1366-1374
    • Yamaguchi, K.1    Yang, L.2    McCall, S.3    Huang, J.4    Yu, X.X.5    Pandey, S.K.6    Bhanot, S.7    Monia, B.P.8    Li, Y.X.9    Diehl, A.M.10
  • 244
    • 65549136260 scopus 로고    scopus 로고
    • Hepatic lipid partitioning and liver damage in nonalcoholic fatty liver disease: Role of stearoyl-CoA desaturase
    • Li, Z.Z.; Berk, M.; McIntyre, T.M.; Feldstein, A.E. Hepatic lipid partitioning and liver damage in nonalcoholic fatty liver disease: role of stearoyl-CoA desaturase. J. Biol. Chem., 2009, 284, 5637-5644.
    • (2009) J. Biol. Chem. , vol.284 , pp. 5637-5644
    • Li, Z.Z.1    Berk, M.2    McIntyre, T.M.3    Feldstein, A.E.4
  • 245
    • 70049089646 scopus 로고    scopus 로고
    • Lipotoxicity in nonalcoholic fatty liver disease: Not all lipids are created equal
    • Alkhouri, N.; Dixon, L.J.; Feldstein, A.E. Lipotoxicity in nonalcoholic fatty liver disease: not all lipids are created equal. Expert Rev. Gastroenterol. Hepatol., 2009, 3, 445-451.
    • (2009) Expert Rev. Gastroenterol. Hepatol. , vol.3 , pp. 445-451
    • Alkhouri, N.1    Dixon, L.J.2    Feldstein, A.E.3
  • 246
    • 56649094325 scopus 로고    scopus 로고
    • Molecular mechanisms of lipotoxicity in nonalcoholic fatty liver disease
    • Malhi, H.; Gores, G.J. Molecular mechanisms of lipotoxicity in nonalcoholic fatty liver disease. Semin Liver Dis., 2008, 28, 360-369.
    • (2008) Semin Liver Dis. , vol.28 , pp. 360-369
    • Malhi, H.1    Gores, G.J.2
  • 248
    • 34547193134 scopus 로고    scopus 로고
    • Free fatty acids sensitise hepatocytes to TRAIL mediated cytotoxicity
    • Malhi, H.; Barreyro, F.J.; Isomoto, H.; Bronk, S.F.; Gores, G.J. Free fatty acids sensitise hepatocytes to TRAIL mediated cytotoxicity. Gut, 2007, 56, 1124-1131.
    • (2007) Gut , vol.56 , pp. 1124-1131
    • Malhi, H.1    Barreyro, F.J.2    Isomoto, H.3    Bronk, S.F.4    Gores, G.J.5
  • 250
    • 43949108922 scopus 로고    scopus 로고
    • The lysosomal-mitochondrial axis in free fatty acid-induced hepatic lipotoxicity
    • Li, Z.; Berk, M.; McIntyre, T.M.; Gores, G.J.; Feldstein, A.E. The lysosomal-mitochondrial axis in free fatty acid-induced hepatic lipotoxicity. Hepatology, 2008, 47, 1495-1503.
    • (2008) Hepatology , vol.47 , pp. 1495-1503
    • Li, Z.1    Berk, M.2    McIntyre, T.M.3    Gores, G.J.4    Feldstein, A.E.5
  • 253
    • 78149358483 scopus 로고    scopus 로고
    • Lysosomal-mitochondrial cross-talk during cell death
    • Repnik, U.; Turk, B. Lysosomal-mitochondrial cross-talk during cell death. Mitochondrion, 2010, 10, 662-669.
    • (2010) Mitochondrion , vol.10 , pp. 662-669
    • Repnik, U.1    Turk, B.2
  • 255
    • 41149115987 scopus 로고    scopus 로고
    • Secondary necrosis in multicellular animals: An outcome of apoptosis with pathogenic implications
    • Silva, M.T.; do Vale, A.; dos Santos, N.M. Secondary necrosis in multicellular animals: an outcome of apoptosis with pathogenic implications. Apoptosis, 2008, 13, 463-482.
    • (2008) Apoptosis , vol.13 , pp. 463-482
    • Silva, M.T.1    Do Vale, A.2    Dos Santos, N.M.3
  • 257
    • 77955690182 scopus 로고    scopus 로고
    • Hepatic lipotoxicity and the pathogenesis of nonalcoholic steatohepatitis: The central role of nontriglyceride fatty acid metabolites
    • Neuschwander-Tetri, B.A. Hepatic lipotoxicity and the pathogenesis of nonalcoholic steatohepatitis: the central role of nontriglyceride fatty acid metabolites. Hepatology, 2010, 52, 774-788.
    • (2010) Hepatology , vol.52 , pp. 774-788
    • Neuschwander-Tetri, B.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.