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Volumn 15, Issue 9, 2004, Pages 4031-4042

PrPC association with lipid rafts in the early secretory pathway stabilizes its cellular conformation

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR PRION PROTEIN; CHOLESTEROL; GLYCOPROTEIN; ISOPROTEIN; PRION PROTEIN; PROTEIN PRECURSOR; SCRAPIE PRION PROTEIN; SPHINGOLIPID; UNCLASSIFIED DRUG;

EID: 4344632252     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E03-05-0271     Document Type: Article
Times cited : (118)

References (85)
  • 1
    • 0035847623 scopus 로고    scopus 로고
    • Transport of endosomal early antigen 1 in the rat sciatic nerve and location in cultured neurons
    • Bartlett, S.E., Reynolds, A.J., Weible, M., 2nd, Noakes, P.G., and Hendry, I.A. (2001). Transport of endosomal early antigen 1 in the rat sciatic nerve and location in cultured neurons. Neuroreport 12, 281-284.
    • (2001) Neuroreport , vol.12 , pp. 281-284
    • Bartlett, S.E.1    Reynolds, A.J.2    Weible II, M.3    Noakes, P.G.4    Hendry, I.A.5
  • 2
    • 0037064026 scopus 로고    scopus 로고
    • Stimulation of PrP(C) retrograde transport toward the endoplasmic reticulum increases accumulation of PrP(Sc) in prion-infected cells
    • Beranger, F., Mange, A., Goud, B., and Lehmann, S. (2002). Stimulation of PrP(C) retrograde transport toward the endoplasmic reticulum increases accumulation of PrP(Sc) in prion-infected cells. J. Biol. Chem. 277, 38972-38977.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38972-38977
    • Beranger, F.1    Mange, A.2    Goud, B.3    Lehmann, S.4
  • 3
    • 0033601291 scopus 로고    scopus 로고
    • Lipid-assisted protein folding
    • Bogdanov, M., and Dowhan, W. (1999). Lipid-assisted protein folding. J. Biol. Chem. 274, 36827-36830.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36827-36830
    • Bogdanov, M.1    Dowhan, W.2
  • 4
    • 0025304678 scopus 로고
    • Scrapie and cellular prion protein differ in their kinetics of synthesis and topology in cultured cells
    • Borchelt, D.R., Scott, M., Taraboulos, A., Stahl, N., and Prusiner, S.B. (1990). Scrapie and cellular prion protein differ in their kinetics of synthesis and topology in cultured cells. J. Cell Biol. 110, 743-752.
    • (1990) J. Cell Biol. , vol.110 , pp. 743-752
    • Borchelt, D.R.1    Scott, M.2    Taraboulos, A.3    Stahl, N.4    Prusiner, S.B.5
  • 5
    • 0026775909 scopus 로고
    • Evidence for synthesis of scrapie prion proteins in the endocytic pathway
    • Borchelt, D.R., Taraboulos, A., and Prusiner, S.B. (1992). Evidence for synthesis of scrapie prion proteins in the endocytic pathway. J. Biol. Chem. 267, 16188-16199.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16188-16199
    • Borchelt, D.R.1    Taraboulos, A.2    Prusiner, S.B.3
  • 6
    • 0024433592 scopus 로고
    • Mechanism of membrane anchoring affects polarized expression of two proteins in MDCK cells
    • Brown, D.A., Crise, B., and Rose, J.K. (1989). Mechanism of membrane anchoring affects polarized expression of two proteins in MDCK cells. Science 245, 1499-1501.
    • (1989) Science , vol.245 , pp. 1499-1501
    • Brown, D.A.1    Crise, B.2    Rose, J.K.3
  • 7
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown, D.A., and London, E. (1998). Functions of lipid rafts in biological membranes. Annu. Rev. Cell Dev. Biol. 14, 111-136.
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 8
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown, D.A., and Rose, J.H. (1992). Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68, 533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.H.2
  • 10
    • 0024545093 scopus 로고
    • Prion protein biosynthesis in scrapie-infected and uninfected neuroblastoma cells
    • Caughey, B., Race, R.E., Ernst, D., Buchmeier, M.J., and Chesebro, B. (1989). Prion protein biosynthesis in scrapie-infected and uninfected neuroblastoma cells. J. Virol. 63, 175-181.
    • (1989) J. Virol. , vol.63 , pp. 175-181
    • Caughey, B.1    Race, R.E.2    Ernst, D.3    Buchmeier, M.J.4    Chesebro, B.5
  • 11
    • 0025991466 scopus 로고
    • The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive
    • Caughey, B., and Raymond, G.J. (1991). The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive. J. Biol. Chem. 266, 18217-18223.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18217-18223
    • Caughey, B.1    Raymond, G.J.2
  • 12
    • 0025876226 scopus 로고
    • N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): Implication regarding the site of conversion of PrP to the protease-resistant state
    • Caughey, B., Raymond, G.J., Ernst, D., and Race, R.E. (1991). N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): implication regarding the site of conversion of PrP to the protease-resistant state. J. Virol. 65, 6597-6603.
    • (1991) J. Virol. , vol.65 , pp. 6597-6603
    • Caughey, B.1    Raymond, G.J.2    Ernst, D.3    Race, R.E.4
  • 13
    • 0032775473 scopus 로고    scopus 로고
    • Species-independent inhibition of abnormal prion protein (PrP) formation by a peptide containing a conserved PrP sequence
    • Chabry, J., Priola, S.A., Wehrly, K., Nishio, J., Hope, J., and Chesebro, B. (1999). Species-independent inhibition of abnormal prion protein (PrP) formation by a peptide containing a conserved PrP sequence. J. Virol. 73, 6245-6250.
    • (1999) J. Virol. , vol.73 , pp. 6245-6250
    • Chabry, J.1    Priola, S.A.2    Wehrly, K.3    Nishio, J.4    Hope, J.5    Chesebro, B.6
  • 14
    • 0031054785 scopus 로고    scopus 로고
    • The interaction of the Alzheimer amyloid beta peptide and ganglioside GM1-containing membranes
    • Choo-Smith, L.P., and Surewicz, W.K. (1997). The interaction of the Alzheimer amyloid beta peptide and ganglioside GM1-containing membranes. FEBS Lett. 402, 95-98.
    • (1997) FEBS Lett. , vol.402 , pp. 95-98
    • Choo-Smith, L.P.1    Surewicz, W.K.2
  • 15
    • 0037201936 scopus 로고    scopus 로고
    • Role of sphingomyelinase and ceramide in modulating rafts: Do biophysical properties determine biologic outcome?
    • Cremesti, A.E., Goni, F.M., and Kolesnick, R. (2002). Role of sphingomyelinase and ceramide in modulating rafts: do biophysical properties determine biologic outcome? FEBS Lett. 531, 47-53.
    • (2002) FEBS Lett. , vol.531 , pp. 47-53
    • Cremesti, A.E.1    Goni, F.M.2    Kolesnick, R.3
  • 16
    • 0030896803 scopus 로고    scopus 로고
    • Identification of intermediate steps in the conversion of a mutant prion protein to a scrapie-like form in cultured cells
    • Daude, N., Lehmann, S., and Harris, D.A. (1997). Identification of intermediate steps in the conversion of a mutant prion protein to a scrapie-like form in cultured cells. J. Biol. Chem. 272, 11604-11612.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11604-11612
    • Daude, N.1    Lehmann, S.2    Harris, D.A.3
  • 17
    • 0034703034 scopus 로고    scopus 로고
    • Lipid raft association of carboxypeptidase E is necessary for its function as a regulated secretory pathway sorting receptor
    • Dhanvantari, S., and Loh, Y.P. (2000). Lipid raft association of carboxypeptidase E is necessary for its function as a regulated secretory pathway sorting receptor. J. Biol. Chem. 275, 29887-29893.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29887-29893
    • Dhanvantari, S.1    Loh, Y.P.2
  • 18
    • 0033493244 scopus 로고    scopus 로고
    • Cell fractionation analysis of human CD8 glycoprotein transport between endoplasmic reticulum, intermediate compartment and Golgi complex in tissue cultured cells
    • Erra, M.C., Iodice, L., Lotti, L.V., and Bonatti, S. (1999). Cell fractionation analysis of human CD8 glycoprotein transport between endoplasmic reticulum, intermediate compartment and Golgi complex in tissue cultured cells. Cell. Biol. Intern. 23, 571-577.
    • (1999) Cell. Biol. Intern. , vol.23 , pp. 571-577
    • Erra, M.C.1    Iodice, L.2    Lotti, L.V.3    Bonatti, S.4
  • 19
    • 0032802332 scopus 로고    scopus 로고
    • Cellular biology of prion diseases
    • Harris, D.A. (1999). Cellular biology of prion diseases. Clin. Microbiol. Rev. 12, 429-444.
    • (1999) Clin. Microbiol. Rev. , vol.12 , pp. 429-444
    • Harris, D.A.1
  • 20
    • 0033564204 scopus 로고    scopus 로고
    • Specific binding of normal prion protein to the scrapie form via a localized domain initiates its conversion to the protease-resistant state
    • Horiuchi, M., and Caughey, B. (1999). Specific binding of normal prion protein to the scrapie form via a localized domain initiates its conversion to the protease-resistant state. EMBO J. 18, 3193-3203.
    • (1999) EMBO J. , vol.18 , pp. 3193-3203
    • Horiuchi, M.1    Caughey, B.2
  • 21
    • 0032080795 scopus 로고    scopus 로고
    • Glucosylceramide synthase and glycosphingolipid synthesis
    • Ichikawa, S., and Hirabayashi, Y. (1998). Glucosylceramide synthase and glycosphingolipid synthesis. Trends Cell Biol. 8, 198-202.
    • (1998) Trends Cell Biol. , vol.8 , pp. 198-202
    • Ichikawa, S.1    Hirabayashi, Y.2
  • 22
    • 0035834680 scopus 로고    scopus 로고
    • Mutant prion proteins are partially retained in the endoplasmic reticulum
    • Ivanova, L., Barmada, S., Kummer, T., and Harris, D.A. (2001). Mutant prion proteins are partially retained in the endoplasmic reticulum. J. Biol. Chem. 276, 42409-42421.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42409-42421
    • Ivanova, L.1    Barmada, S.2    Kummer, T.3    Harris, D.A.4
  • 23
    • 0028181429 scopus 로고
    • Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90)
    • Jackson, M.R., Cohen-Doyle, M.F., Peterson, P.A., and Williams, D.B. (1994). Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90). Science 263, 384-387.
    • (1994) Science , vol.263 , pp. 384-387
    • Jackson, M.R.1    Cohen-Doyle, M.F.2    Peterson, P.A.3    Williams, D.B.4
  • 24
    • 0033947543 scopus 로고    scopus 로고
    • Sites of prion protein accumulation in scrapie-infected mouse spleen revealed by immuno-electron microscopy
    • Jeffrey, M., McGovern, G., Goodsir, C.M., Brown, K.L., and Bruce, M.E. (2000). Sites of prion protein accumulation in scrapie-infected mouse spleen revealed by immuno-electron microscopy. J. Pathol. 197, 323-332.
    • (2000) J. Pathol. , vol.197 , pp. 323-332
    • Jeffrey, M.1    McGovern, G.2    Goodsir, C.M.3    Brown, K.L.4    Bruce, M.E.5
  • 25
    • 0030964917 scopus 로고    scopus 로고
    • COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform
    • Kaneko, K., Vey, M., Scott, M., Pilkuhn, S., Cohen, F.E., and Prusiner, S.B. (1997). COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform. Proc. Natl. Acad. Sci. USA 94, 2333-2338.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2333-2338
    • Kaneko, K.1    Vey, M.2    Scott, M.3    Pilkuhn, S.4    Cohen, F.E.5    Prusiner, S.B.6
  • 26
    • 0036500837 scopus 로고    scopus 로고
    • The small GTPase Rab22 interacts with EEA1 and controls endosomal membrane trafficking
    • Kauppi, M., Simonsen, A., Bremnes, B., Vieira, A., Callaghan, J., Stenmark, H., and Olkkonen, V.M. (2002). The small GTPase Rab22 interacts with EEA1 and controls endosomal membrane trafficking. J. Cell Sci. 115(Pt 5), 899-911.
    • (2002) J. Cell Sci. , vol.115 , Issue.PART 5 , pp. 899-911
    • Kauppi, M.1    Simonsen, A.2    Bremnes, B.3    Vieira, A.4    Callaghan, J.5    Stenmark, H.6    Olkkonen, V.M.7
  • 27
    • 0032559854 scopus 로고    scopus 로고
    • Cholesterol is required for surface transport of influenza virus hemagglutinin
    • Keller, P., and Simons, K. (1998). Cholesterol is required for surface transport of influenza virus hemagglutinin. J. Cell Biol. 140, 1357-1367.
    • (1998) J. Cell Biol. , vol.140 , pp. 1357-1367
    • Keller, P.1    Simons, K.2
  • 28
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • Klausner, R.D., Donaldson, J.G., and Lippincott-Schwartz, J. (1992). Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biol. 116, 1071-1080.
    • (1992) J. Cell Biol. , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 29
    • 0031843985 scopus 로고    scopus 로고
    • Prion rods contain small amounts of two host sphingolipids as revealed by thin-layer chromatography and mass spectrometry
    • Klein, T.R., Kirsch, D., Kaufmann, R., and Riesner, D. (1998), Prion rods contain small amounts of two host sphingolipids as revealed by thin-layer chromatography and mass spectrometry. Biol. Chem. 379, 655-666.
    • (1998) Biol. Chem. , vol.379 , pp. 655-666
    • Klein, T.R.1    Kirsch, D.2    Kaufmann, R.3    Riesner, D.4
  • 32
    • 0026605853 scopus 로고
    • Lysosomes as key organelles in the pathogenesis of prion encephalopathies
    • Laszlo, L. et al. (1992). Lysosomes as key organelles in the pathogenesis of prion encephalopathies. J. Pathol. 166, 333-341.
    • (1992) J. Pathol. , vol.166 , pp. 333-341
    • Laszlo, L.1
  • 33
    • 0030006902 scopus 로고    scopus 로고
    • Two mutant prion proteins expressed in cultured cells acquire biochemical properties reminiscent of the scrapie isoform
    • Lehmann, S., and Harris, D.A. (1996a). Two mutant prion proteins expressed in cultured cells acquire biochemical properties reminiscent of the scrapie isoform. Proc. Natl. Acad. Sci. USA 93, 5610-5614.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5610-5614
    • Lehmann, S.1    Harris, D.A.2
  • 34
    • 0030050733 scopus 로고    scopus 로고
    • Mutant and infectious prion proteins display common biochemical properties in cultured cells
    • Lehmann, S., and Harris, D.A. (1996b). Mutant and infectious prion proteins display common biochemical properties in cultured cells. J. Biol. Chem. 271, 1633-1637.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1633-1637
    • Lehmann, S.1    Harris, D.A.2
  • 35
    • 0030799062 scopus 로고    scopus 로고
    • Blockade of glycosylation promotes acquisition of scrapie-like properties by the prion protein in cultured cells
    • Lehmann, S., and Harris, D.A. (1997). Blockade of glycosylation promotes acquisition of scrapie-like properties by the prion protein in cultured cells. J. Biol. Chem. 272, 21479-21487.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21479-21487
    • Lehmann, S.1    Harris, D.A.2
  • 36
    • 0034003908 scopus 로고    scopus 로고
    • Detergent insoluble GPI-anchored proteins are apically sorted in Fisher rat thyroid cells, but interference with cholesterol or sphingolipids differentially affects detergent insolubility and apical sorting
    • Lipardi, C., Nitsch, L., and Zurzolo, C. (2000). Detergent insoluble GPI-anchored proteins are apically sorted in Fisher rat thyroid cells, but interference with cholesterol or sphingolipids differentially affects detergent insolubility and apical sorting. Mol. Biol. Cell 11, 531-542.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 531-542
    • Lipardi, C.1    Nitsch, L.2    Zurzolo, C.3
  • 37
    • 0024591235 scopus 로고
    • Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: Evidence for membrane cycling from Golgi to ER
    • Lippincott-Schwartz, J., Yuan, L.C., Bonifacino, J.S., and Klausner, R.D. (1989). Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER. Cell 56, 801-813.
    • (1989) Cell , vol.56 , pp. 801-813
    • Lippincott-Schwartz, J.1    Yuan, L.C.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 38
    • 0024468669 scopus 로고
    • A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial cells
    • Lisanti, M.P., Caras, J.W., Davitz, M.A., and Rodriguez-Boulan, E. (1989). A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial cells. J. Cell Biol. 109, 2145-2156.
    • (1989) J. Cell Biol. , vol.109 , pp. 2145-2156
    • Lisanti, M.P.1    Caras, J.W.2    Davitz, M.A.3    Rodriguez-Boulan, E.4
  • 39
    • 0035910069 scopus 로고    scopus 로고
    • Wild-type and mutant associated with prion disease are subjected to retrograde transport and proteasome degradation
    • Ma, J., and Lindquist, S. (2001). Wild-type and mutant associated with prion disease are subjected to retrograde transport and proteasome degradation. Proc. Natl. Acad. Sci. USA 98, 4955-4960.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4955-4960
    • Ma, J.1    Lindquist, S.2
  • 40
    • 0037195617 scopus 로고    scopus 로고
    • Sc-like conformation in the cytosol
    • Sc-like conformation in the cytosol. Science 298, 1785-1788.
    • (2002) Science , vol.298 , pp. 1785-1788
    • Ma, J.1    Lindquist, S.2
  • 41
    • 0037195647 scopus 로고    scopus 로고
    • Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol
    • Ma, J., Wollmann, R., and Lindquist, S. (2002). Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 298, 1781-1785.
    • (2002) Science , vol.298 , pp. 1781-1785
    • Ma, J.1    Wollmann, R.2    Lindquist, S.3
  • 43
    • 0037192816 scopus 로고    scopus 로고
    • Identification of a common sphingolipid-binding domain in Alzheimer, Prion and HIV proteins
    • Mahfoud, R., Garmy, N., Maresca, M., Yahi, N., Puigserver, A., and Fantini, J. (2002). Identification of a common sphingolipid-binding domain in Alzheimer, Prion and HIV proteins. J. Biol. Chem. 277, 11292-11296.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11292-11296
    • Mahfoud, R.1    Garmy, N.2    Maresca, M.3    Yahi, N.4    Puigserver, A.5    Fantini, J.6
  • 44
    • 0029044628 scopus 로고
    • Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment
    • Mayor, S., and Maxfield, F.R. (1995). Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment. Mol. Biol. Cell 6, 929-944.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 929-944
    • Mayor, S.1    Maxfield, F.R.2
  • 45
    • 0035951401 scopus 로고    scopus 로고
    • Protein sorting upon exit from endoplasmic reticulum
    • Muniz, M., Morsomme, P., and Riezman, H. (2001). Protein sorting upon exit from endoplasmic reticulum. Cell 104, 313-320.
    • (2001) Cell , vol.104 , pp. 313-320
    • Muniz, M.1    Morsomme, P.2    Riezman, H.3
  • 47
    • 0242331275 scopus 로고    scopus 로고
    • Protein disulfide isomerase, a multifunctional protein chaperone, shows copper-binding activity
    • Narindrasorasak, S., Yao, P., and Sarkar, B. (2003). Protein disulfide isomerase, a multifunctional protein chaperone, shows copper-binding activity. Biochem. Biophys. Res. Commun. 311, 405-414.
    • (2003) Biochem. Biophys. Res. Commun. , vol.311 , pp. 405-414
    • Narindrasorasak, S.1    Yao, P.2    Sarkar, B.3
  • 48
    • 0033597931 scopus 로고    scopus 로고
    • Sphingolipid depletion increases formation of the scrapie prion protein in neuroblastoma cells infected with prions
    • Naslavsky, N., Shmeeda, H., Friedlander, G., Yanai, A., Futerman, A.H., Barenholz, Y., and Taraboulos, A. (1999). Sphingolipid depletion increases formation of the scrapie prion protein in neuroblastoma cells infected with prions. J. Biol. Chem. 274, 20763-20771.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20763-20771
    • Naslavsky, N.1    Shmeeda, H.2    Friedlander, G.3    Yanai, A.4    Futerman, A.H.5    Barenholz, Y.6    Taraboulos, A.7
  • 49
    • 0030894380 scopus 로고    scopus 로고
    • Characterization of detergent-insoluble complex containing the cellular prion protein and its scrapie isoform
    • Naslavsky, N., Stein, R., Yanai, A., Friedlander, G., and Taraboulos, A. (1997). Characterization of detergent-insoluble complex containing the cellular prion protein and its scrapie isoform. J. Biol. Chem. 272, 6324-6331.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6324-6331
    • Naslavsky, N.1    Stein, R.2    Yanai, A.3    Friedlander, G.4    Taraboulos, A.5
  • 50
    • 0025014865 scopus 로고
    • Subcellular distribution of small GTP binding proteins in pancreas: Identification of small GTP binding proteins in the rough endoplasmic reticulum
    • Nigam, S.K. (1990). Subcellular distribution of small GTP binding proteins in pancreas: identification of small GTP binding proteins in the rough endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 87, 1296-1299.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1296-1299
    • Nigam, S.K.1
  • 51
    • 0142169397 scopus 로고    scopus 로고
    • Protein refolding assisted by self-assembled nanogels as novel artificial molecular chaperone
    • Nomura, Y., Ikeda, M., Yamaguchi, N., Aoyama, Y., and Akiyoshi, K. (2003). Protein refolding assisted by self-assembled nanogels as novel artificial molecular chaperone. FEBS Lett. 553, 271-276.
    • (2003) FEBS Lett. , vol.553 , pp. 271-276
    • Nomura, Y.1    Ikeda, M.2    Yamaguchi, N.3    Aoyama, Y.4    Akiyoshi, K.5
  • 52
    • 0035660246 scopus 로고    scopus 로고
    • Sphingolipids in mammalian cell signalling
    • Ohanian, J., and Ohanian, V. (2001). Sphingolipids in mammalian cell signalling. Cell Mol. Life Sci. 58, 2053-2068.
    • (2001) Cell Mol. Life Sci. , vol.58 , pp. 2053-2068
    • Ohanian, J.1    Ohanian, V.2
  • 53
    • 0028057494 scopus 로고
    • Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae
    • Parton, R.G. (1994). Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae. J. Histochem. Cytochem. 42, 155-166.
    • (1994) J. Histochem. Cytochem. , vol.42 , pp. 155-166
    • Parton, R.G.1
  • 54
    • 0038697962 scopus 로고    scopus 로고
    • Chaperones and folding of MHC class I molecules in the endoplasmic reticulum
    • Paulsson, K., and Wang, P. (2003). Chaperones and folding of MHC class I molecules in the endoplasmic reticulum. Biochim. Biophys. Acta 1641, 1-12.
    • (2003) Biochim. Biophys. Acta , vol.1641 , pp. 1-12
    • Paulsson, K.1    Wang, P.2
  • 55
    • 17544366508 scopus 로고    scopus 로고
    • Effect of the D178N mutation and the codon 129 polymorphism on the metabolism of the prion protein
    • Petersen, R.B., Parchi, P., Richardson, S.L., Urig, C.B., and Gambetti, P. (1996). Effect of the D178N mutation and the codon 129 polymorphism on the metabolism of the prion protein. J. Biol. Chem. 271, 12661-12668.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12661-12668
    • Petersen, R.B.1    Parchi, P.2    Richardson, S.L.3    Urig, C.B.4    Gambetti, P.5
  • 56
    • 17344386598 scopus 로고    scopus 로고
    • An antibody raised against a conserved sequence of the prion protein recognizes pathological isoforms in human and animal prion diseases, including Creutzfeldt-Jakob disease and bovine spongiform encephalopathy
    • Piccardo, P. et al. (1998). An antibody raised against a conserved sequence of the prion protein recognizes pathological isoforms in human and animal prion diseases, including Creutzfeldt-Jakob disease and bovine spongiform encephalopathy. Am. J. Pathol. 152, 1415-1420.
    • (1998) Am. J. Pathol. , vol.152 , pp. 1415-1420
    • Piccardo, P.1
  • 58
    • 0032496218 scopus 로고    scopus 로고
    • Abnormal properties of prion protein with insertional mutations in different cell types
    • Priola, S.A., and Chesebro, B. (1998). Abnormal properties of prion protein with insertional mutations in different cell types. J. Biol. Chem. 273, 11980-11985.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11980-11985
    • Priola, S.A.1    Chesebro, B.2
  • 59
    • 0026779146 scopus 로고
    • Effects of brefeldin A on endocytosis, transcytosis and transport to the Golgi complex in polarized MDCK cells
    • Prydz, K., Hansen, S.H., Sandvig, K., and van Deurs, B. (1992). Effects of brefeldin A on endocytosis, transcytosis and transport to the Golgi complex in polarized MDCK cells. J. Cell Biol. 119, 259-272.
    • (1992) J. Cell Biol. , vol.119 , pp. 259-272
    • Prydz, K.1    Hansen, S.H.2    Sandvig, K.3    Van Deurs, B.4
  • 61
    • 0026570788 scopus 로고
    • Perturbation of the morphology of the trans-Golgi network following Brefeldin A treatment: Redistribution of a TGN-specific integral membrane protein, TGN38
    • Reaves, B., and Banting, G. (1992). Perturbation of the morphology of the trans-Golgi network following Brefeldin A treatment: redistribution of a TGN-specific integral membrane protein, TGN38. J. Cell Biol. 116, 85-94.
    • (1992) J. Cell Biol. , vol.116 , pp. 85-94
    • Reaves, B.1    Banting, G.2
  • 62
    • 0033915741 scopus 로고    scopus 로고
    • Misfolding of membrane proteins in health and disease: The lady or the tiger?
    • Sanders, C.R., and Nagy, J.K. (2000). Misfolding of membrane proteins in health and disease: the lady or the tiger? Curr. Opin. Struct. Biol. 10, 438-442.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 438-442
    • Sanders, C.R.1    Nagy, J.K.2
  • 63
    • 0037762571 scopus 로고    scopus 로고
    • Biosynthesis and degradation of mammalian glycosphingolipids
    • Sandhoff, K., and Kolter, T. (2003). Biosynthesis and degradation of mammalian glycosphingolipids. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 358, 847-861.
    • (2003) Philos. Trans. R. Soc. Lond. B. Biol. Sci. , vol.358 , pp. 847-861
    • Sandhoff, K.1    Kolter, T.2
  • 64
    • 0036306046 scopus 로고    scopus 로고
    • Binding of prion protein to lipid membranes and implication for prion replication
    • Sanghera, N., and Pinheiro, T.J. (2002). Binding of prion protein to lipid membranes and implication for prion replication. J. Mol. Biol. 315, 1241-1256.
    • (2002) J. Mol. Biol. , vol.315 , pp. 1241-1256
    • Sanghera, N.1    Pinheiro, T.J.2
  • 67
    • 0033229897 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-anchor intermediates associate with triton-insoluble membranes in subcellular compartments that include the endoplasmic reticulum
    • Sevlever, D., Pickett, S., Mann, K.J., Sambamurti, K., Medof, M.E., and Rosenberry, T.L. (1999). Glycosylphosphatidylinositol-anchor intermediates associate with triton-insoluble membranes in subcellular compartments that include the endoplasmic reticulum. Biochem. J. 343, 627-635.
    • (1999) Biochem. J. , vol.343 , pp. 627-635
    • Sevlever, D.1    Pickett, S.2    Mann, K.J.3    Sambamurti, K.4    Medof, M.E.5    Rosenberry, T.L.6
  • 68
    • 0028305135 scopus 로고
    • A glycolipid-anchored prion protein is endocytosed via clathrin-coated pits
    • Shyng, S-L., Heuser, J.E., and Harris, D.A. (1994). A glycolipid-anchored prion protein is endocytosed via clathrin-coated pits. J. Cell Biol. 125, 1239-1250.
    • (1994) J. Cell Biol. , vol.125 , pp. 1239-1250
    • Shyng, S.-L.1    Heuser, J.E.2    Harris, D.A.3
  • 69
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membrane
    • Simons, K., and Ikonen, E. (1997). Functional rafts in cell membrane. Nature 387, 569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 70
    • 0030665269 scopus 로고    scopus 로고
    • Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast
    • Sutterlin, C., Doering, T.L., Schimmoller, F., Schroder, S., and Riezman, H. (1997). Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast. J. Cell Sci. 110(Pt 21), 2703-2714.
    • (1997) J. Cell Sci. , vol.110 , Issue.PART 21 , pp. 2703-2714
    • Sutterlin, C.1    Doering, T.L.2    Schimmoller, F.3    Schroder, S.4    Riezman, H.5
  • 71
    • 0037956030 scopus 로고    scopus 로고
    • Biochemical sub-fractionation of the Mammalian Golgi apparatus
    • Taguchi, T., Pypaert, M., and Warren, G. (2003). Biochemical sub-fractionation of the Mammalian Golgi apparatus. Traffic 4, 344-352.
    • (2003) Traffic , vol.4 , pp. 344-352
    • Taguchi, T.1    Pypaert, M.2    Warren, G.3
  • 73
    • 0028966735 scopus 로고
    • Cholesterol depletion and modification of COOH terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform
    • Taraboulos, A., Scott, M.R.D., Semenov, A., Avraham, D., Laszlo, L., and Prusiner, S.B. (1995). Cholesterol depletion and modification of COOH terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform. J. Cell Biol. 129, 121-132.
    • (1995) J. Cell Biol. , vol.129 , pp. 121-132
    • Taraboulos, A.1    Scott, M.R.D.2    Semenov, A.3    Avraham, D.4    Laszlo, L.5    Prusiner, S.B.6
  • 74
    • 0028882424 scopus 로고
    • Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
    • Telling, G.C., Scott, M., Mastrianni, J., Gabizon, R., Torchia, M., Cohen, F.E., DeArmond, S.J., and Prusiner, S.B. (1995). Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83, 79-90.
    • (1995) Cell , vol.83 , pp. 79-90
    • Telling, G.C.1    Scott, M.2    Mastrianni, J.3    Gabizon, R.4    Torchia, M.5    Cohen, F.E.6    DeArmond, S.J.7    Prusiner, S.B.8
  • 75
    • 0023161210 scopus 로고
    • Enzymatic deglycosylation of glycoproteins
    • Thotakura, N.R., and Bahl, O.P. (1987). Enzymatic deglycosylation of glycoproteins. Methods Enzymol. 138, 350-359.
    • (1987) Methods Enzymol. , vol.138 , pp. 350-359
    • Thotakura, N.R.1    Bahl, O.P.2
  • 76
    • 0028360654 scopus 로고
    • The mode of anchorage to the cell surface determines both the function and the membrane location of Thy-1 glycoprotein
    • Tiveron, M.C., Nosten-Bertrand, M., Jani, H., Garnett, D., Hirst, E.M., Grosveld, F., and Morris, R.J. (1994). The mode of anchorage to the cell surface determines both the function and the membrane location of Thy-1 glycoprotein. J. Cell Sci. 107, 1783-1796.
    • (1994) J. Cell Sci. , vol.107 , pp. 1783-1796
    • Tiveron, M.C.1    Nosten-Bertrand, M.2    Jani, H.3    Garnett, D.4    Hirst, E.M.5    Grosveld, F.6    Morris, R.J.7
  • 77
    • 0035028838 scopus 로고    scopus 로고
    • Rafts membrane domains: From a liquid-ordered membrane phase to a site of pathogen attack
    • van der Goot, F.G., and Harder, T. (2001). Rafts membrane domains: from a liquid-ordered membrane phase to a site of pathogen attack. Semin. Immunol. 13, 89-97.
    • (2001) Semin. Immunol. , vol.13 , pp. 89-97
    • Van Der Goot, F.G.1    Harder, T.2
  • 79
    • 0028301797 scopus 로고
    • Brefeldin A causes structural and functional alterations of the trans-Golgi network of MDCK cells
    • Wagner, M., Rajasekanaran, A.K., Hanzel, D.K., Mayor, S., and Rodriguez-Boulan, E. (1994). Brefeldin A causes structural and functional alterations of the trans-Golgi network of MDCK cells. J. Cell Sci. 107, 933-943.
    • (1994) J. Cell Sci. , vol.107 , pp. 933-943
    • Wagner, M.1    Rajasekanaran, A.K.2    Hanzel, D.K.3    Mayor, S.4    Rodriguez-Boulan, E.5
  • 80
    • 0141844613 scopus 로고    scopus 로고
    • The N-terminal region of the prion protein ectodomain contains a lipid raft targeting determinant
    • Walmsley, A.R., Zeng, F., and Hooper, N.M. (2003). The N-terminal region of the prion protein ectodomain contains a lipid raft targeting determinant. J. Biol. Chem. 278, 37241-37248.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37241-37248
    • Walmsley, A.R.1    Zeng, F.2    Hooper, N.M.3
  • 81
    • 0037665405 scopus 로고    scopus 로고
    • Determinants of the in vivo folding of the prion protein. A bipartite function of helix 1 in folding and aggregation
    • Winklhofer, F., Heske, J., Heller, U., Reintjes, A., Muranyi, W., Moarefi, I., and Tatzelt, J. (2003). Determinants of the in vivo folding of the prion protein. A bipartite function of helix 1 in folding and aggregation. J. Biol. Chem. 278, 14961-14970.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14961-14970
    • Winklhofer, F.1    Heske, J.2    Heller, U.3    Reintjes, A.4    Muranyi, W.5    Moarefi, I.6    Tatzelt, J.7
  • 83
    • 0033730407 scopus 로고    scopus 로고
    • The p58-positive pre-golgi intermediates consist of distinct subpopulations of particles that show differential binding of COPI and COPII coats and contain vacuolar H(+)-ATPase
    • Ying, M., Flatmark, T., and Saraste, J. (2000). The p58-positive pre-golgi intermediates consist of distinct subpopulations of particles that show differential binding of COPI and COPII coats and contain vacuolar H(+)-ATPase. J. Cell Sci. 11(Pt 20), 3623-3638.
    • (2000) J. Cell Sci. , vol.11 , Issue.PART 20 , pp. 3623-3638
    • Ying, M.1    Flatmark, T.2    Saraste, J.3
  • 84
    • 0027315413 scopus 로고
    • Glycosylphosphatidylinositol-anchored proteins are preferentially targeted to the basolateral surface in Fischer rat thyroid epithelial cells
    • Zurzolo, C., Lisanti, M.P., Caras, I.W., Nitsch, L., and Rodriguez-Boulan, E. (1993). Glycosylphosphatidylinositol-anchored proteins are preferentially targeted to the basolateral surface in Fischer rat thyroid epithelial cells. J. Cell Biol. 121, 1031-1039.
    • (1993) J. Cell Biol. , vol.121 , pp. 1031-1039
    • Zurzolo, C.1    Lisanti, M.P.2    Caras, I.W.3    Nitsch, L.4    Rodriguez-Boulan, E.5
  • 85
    • 0028032064 scopus 로고
    • VIP21/caveolin, glycosphingolipid clusters and the sorting of glycosylphosphatidylinositol-anchored proteins in epithelial cells
    • Zurzolo, C., van't Hof, W., Van Meer, G., and Rodriguez-Boulan, E. (1994). VIP21/caveolin, glycosphingolipid clusters and the sorting of glycosylphosphatidylinositol-anchored proteins in epithelial cells. EMBO J. 13, 42-53.
    • (1994) EMBO J. , vol.13 , pp. 42-53
    • Zurzolo, C.1    Van't Hof, W.2    Van Meer, G.3    Rodriguez-Boulan, E.4


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