메뉴 건너뛰기




Volumn 419, Issue , 1997, Pages 355-364

Cell surface dynamics of GPI-anchored proteins

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOSYLATED PROTEIN; GLYCOSYLPHOSPHATIDYLINOSITOL; GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 0030919779     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4419-8632-0_47     Document Type: Conference Paper
Times cited : (56)

References (58)
  • 1
    • 0025203675 scopus 로고
    • Glycolipid anchoring of plasma membrane proteins
    • Cross, G. A. M. 1990. Glycolipid anchoring of plasma membrane proteins. Ann. Rev. Cell Biol., 6:1-34.
    • (1990) Ann. Rev. Cell Biol. , vol.6 , pp. 1-34
    • Cross, G.A.M.1
  • 2
    • 0027294030 scopus 로고
    • The structure and biosynthesis of glycosyl phosphatidylinositol protein anchors
    • Englund, P. T. 1993. The structure and biosynthesis of glycosyl phosphatidylinositol protein anchors. [Review]. Annu Rev Biochem. 62:121-38.
    • (1993) Annu Rev Biochem. , vol.62 , pp. 121-138
    • Englund, P.T.1
  • 3
    • 0023944337 scopus 로고
    • Cell-surface anchoring of proteins via glycosyl phosphatidylinositol structures
    • Ferguson, M. A. J. and A. F. Williams 1988. Cell-surface anchoring of proteins via glycosyl phosphatidylinositol structures. Ann. Rev. Biochem., 57:285-320.
    • (1988) Ann. Rev. Biochem. , vol.57 , pp. 285-320
    • Ferguson, M.A.J.1    Williams, A.F.2
  • 4
    • 0001902665 scopus 로고
    • Glycolipid-anchoring of cell surface proteins
    • Schlesinger, M. J., Schlesinger, M. J.s. CRC Press, Boca Raton Ann Arbour London Tokyo
    • Field, M. C. and A. K. Menon 1992. Glycolipid-anchoring of cell surface proteins. In Lipid modification of proteins. Schlesinger, M. J., Schlesinger, M. J.s. CRC Press, Boca Raton Ann Arbour London Tokyo. 83-134.
    • (1992) Lipid Modification of Proteins , pp. 83-134
    • Field, M.C.1    Menon, A.K.2
  • 5
    • 0024316809 scopus 로고
    • The glycosyl-phosphatidylinositol anchor of membrane proteins
    • Low, M. G. 1989. The glycosyl-phosphatidylinositol anchor of membrane proteins. Biochim. Biophys. Acta, 988:427-454.
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 427-454
    • Low, M.G.1
  • 6
    • 0001210761 scopus 로고
    • Structural analysis of the glycosylinositol phospholipid anchors of membrane proteins
    • Mayor, S. and A. K. Menon 1990. Structural analysis of the glycosylinositol phospholipid anchors of membrane proteins. Methods: A Companion to Methods in Enzymology, 1:297-305.
    • (1990) Methods: A Companion to Methods in Enzymology , vol.1 , pp. 297-305
    • Mayor, S.1    Menon, A.K.2
  • 7
    • 0027257177 scopus 로고
    • The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes
    • McConville, M. J. and M. A. Ferguson 1993. The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes. Biochem. J., 294:30-204.
    • (1993) Biochem. J. , vol.294 , pp. 30-204
    • McConville, M.J.1    Ferguson, M.A.2
  • 8
    • 0027976353 scopus 로고
    • What can GPI do for you
    • Ferguson, M. A. J. 1994. What can GPI do for you. Parasitology Today, 10:48-52.
    • (1994) Parasitology Today , vol.10 , pp. 48-52
    • Ferguson, M.A.J.1
  • 9
    • 0025055080 scopus 로고
    • Glycophospholipid membrane anchoring provides clues to the mechanism of protein sorting in polarized epithelial cells
    • Lisanti, M. P. and E. Rodriguez-Boulan 1990. Glycophospholipid membrane anchoring provides clues to the mechanism of protein sorting in polarized epithelial cells. Trends Biochem. Sci., 15:113-118.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 113-118
    • Lisanti, M.P.1    Rodriguez-Boulan, E.2
  • 10
    • 0025341760 scopus 로고
    • Polarized sorting in epithelia
    • Simons, K. and A. Wandinger-Ness 1990. Polarized sorting in epithelia. [Review]. Cell, 62:207-10.
    • (1990) Cell , vol.62 , pp. 207-210
    • Simons, K.1    Wandinger-Ness, A.2
  • 11
    • 0027269661 scopus 로고
    • The tyrosine kinase connection: How GPI-anchored proteins activate T cells
    • Brown, D. 1993. The tyrosine kinase connection: how GPI-anchored proteins activate T cells. [Review]. Current Opinion in Immunology, 5:349-54.
    • (1993) Current Opinion in Immunology , vol.5 , pp. 349-354
    • Brown, D.1
  • 12
    • 0026013817 scopus 로고
    • Phosphatidylinositol membrane anchors and T-cell activation
    • Robinson, P. J. 1991. Phosphatidylinositol membrane anchors and T-cell activation. Immunol. Today, 12:35-41.
    • (1991) Immunol. Today , vol.12 , pp. 35-41
    • Robinson, P.J.1
  • 13
    • 0027414646 scopus 로고
    • Caveolae and sorting in the trans-Golgi network of epithelial cells
    • Dupree, P., R. G. Parton, G. Raposo, T. V. Kurzchalia and K. Simons 1993. Caveolae and sorting in the trans-Golgi network of epithelial cells. Embo J, 12:1597-605.
    • (1993) Embo J , vol.12 , pp. 1597-1605
    • Dupree, P.1    Parton, R.G.2    Raposo, G.3    Kurzchalia, T.V.4    Simons, K.5
  • 15
    • 0026667338 scopus 로고
    • Interactions between GPI-anchored proteins and membrane lipids
    • Brown, D. 1992. Interactions between GPI-anchored proteins and membrane lipids. Trends in Cell Biology, 2:338-343.
    • (1992) Trends in Cell Biology , vol.2 , pp. 338-343
    • Brown, D.1
  • 16
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown, D. A. and J. K. Rose 1992. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell, 68:533-44.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 17
    • 0024382542 scopus 로고
    • Novel tyrosine kinase substrates from rous sarcoma virus transformed cells are present in the membrane skeleton
    • Glenney, J. R. and L. Zokas 1989. Novel tyrosine kinase substrates from rous sarcoma virus transformed cells are present in the membrane skeleton. J. Cell Biol., 108:2401-2408.
    • (1989) J. Cell Biol. , vol.108 , pp. 2401-2408
    • Glenney, J.R.1    Zokas, L.2
  • 18
    • 0024287104 scopus 로고
    • Ectoenzymes of the kidney microvillar membrane: Differential solubilization by detergents can predict a glycosyl-phosphatidylinositol membrane anchor
    • Hooper, N. M. and A. J. Turner 1988. Ectoenzymes of the kidney microvillar membrane: differential solubilization by detergents can predict a glycosyl-phosphatidylinositol membrane anchor. Biochem. J., 250:865-869.
    • (1988) Biochem. J. , vol.250 , pp. 865-869
    • Hooper, N.M.1    Turner, A.J.2
  • 19
    • 0027363575 scopus 로고
    • Caveolin forms a hetero-oligomeric protein complex that interacts with an apical GPI-linked protein: Implications for the biogenesis of caveolae
    • Lisanti, M. P., Z. L. Tang and M. Sargiacomo 1993. Caveolin forms a hetero-oligomeric protein complex that interacts with an apical GPI-linked protein: implications for the biogenesis of caveolae. Journal of Cell Biology, 123:595-604.
    • (1993) Journal of Cell Biology , vol.123 , pp. 595-604
    • Lisanti, M.P.1    Tang, Z.L.2    Sargiacomo, M.3
  • 21
    • 0028000605 scopus 로고
    • Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking
    • Mayor, S., K. G. Rothberg and F. R. Maxfield 1994. Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking. Science, 264:1948-51.
    • (1994) Science , vol.264 , pp. 1948-1951
    • Mayor, S.1    Rothberg, K.G.2    Maxfield, F.R.3
  • 22
    • 0029044628 scopus 로고
    • Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment
    • Mayor, S. and F. R. Maxfield 1995. Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment. Molecular Biology of the Cell, 6:929-44.
    • (1995) Molecular Biology of the Cell , vol.6 , pp. 929-944
    • Mayor, S.1    Maxfield, F.R.2
  • 23
    • 0028138521 scopus 로고
    • Regulated internalization of caveolae
    • Parton, R. G., B. Joggerst and K. Simons 1994. Regulated internalization of caveolae. J. Cell Biol., 127:1199-1215.
    • (1994) J. Cell Biol. , vol.127 , pp. 1199-1215
    • Parton, R.G.1    Joggerst, B.2    Simons, K.3
  • 24
    • 0026349333 scopus 로고
    • Glycosyl-phosphatidylinositol-anchored membrane proteins can be distinguished from transmembrane polypeptide-anchored proteins by differential solubilization and temperature-induced phase separation in Triton X - 114
    • Hooper, N. M. and A. Bashir 1991. Glycosyl-phosphatidylinositol-anchored membrane proteins can be distinguished from transmembrane polypeptide-anchored proteins by differential solubilization and temperature-induced phase separation in Triton X - 114. Biochem J., 280:745-751.
    • (1991) Biochem J. , vol.280 , pp. 745-751
    • Hooper, N.M.1    Bashir, A.2
  • 25
    • 0027275642 scopus 로고
    • Signal transducing molecules and glycosylphosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells
    • Sargiacomo, M., M. Sudol, Z. Tang and M. P. Lisanti 1993. Signal transducing molecules and glycosylphosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells. Journal of Cell Biology, 122:789-807.
    • (1993) Journal of Cell Biology , vol.122 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.3    Lisanti, M.P.4
  • 27
    • 0027970448 scopus 로고
    • Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae
    • Fra, A. M., E. Williamson, K. Simons and R. G. Parton 1994. Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae. J. Biol. Chem. 269:30745-30748.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30745-30748
    • Fra, A.M.1    Williamson, E.2    Simons, K.3    Parton, R.G.4
  • 29
    • 0028151351 scopus 로고
    • Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior
    • Schroeder, R., E. London and D. A. Brown 1994. Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior. Proc. Natl. Acad. Sci. (USA), 91:12130-12134.
    • (1994) Proc. Natl. Acad. Sci. (USA) , vol.91 , pp. 12130-12134
    • Schroeder, R.1    London, E.2    Brown, D.A.3
  • 30
    • 0027467580 scopus 로고
    • Large, detergent-resistant complexes containing murine antigens Thy-1 and Ly-6 and protein tyrosine kinase p56lck
    • Bohuslav, J., T. Cinek and V. Horejsi 1993. Large, detergent-resistant complexes containing murine antigens Thy-1 and Ly-6 and protein tyrosine kinase p56lck. European Journal of Immunology, 23:825-31.
    • (1993) European Journal of Immunology , vol.23 , pp. 825-831
    • Bohuslav, J.1    Cinek, T.2    Horejsi, V.3
  • 31
    • 0026662674 scopus 로고
    • The nature of large noncovalent complexes containing glycosyl-phosphatidylinositol-anchored membrane glycoproteins and protein tyrosine kinases
    • Cinek, T. and V. Horejsi 1992. The nature of large noncovalent complexes containing glycosyl-phosphatidylinositol-anchored membrane glycoproteins and protein tyrosine kinases. Journal of Immunology, 149:2262-70.
    • (1992) Journal of Immunology , vol.149 , pp. 2262-2270
    • Cinek, T.1    Horejsi, V.2
  • 32
    • 0026352248 scopus 로고
    • GPI-anchored cell-surface molecules complexed to protein tyrosine kinases
    • Stefanova, I., V. Horejsi, I. J. Ansotegui, W. Knapp and H. Stockinger 1991. GPI-anchored cell-surface molecules complexed to protein tyrosine kinases. Science, 254:1016-1019.
    • (1991) Science , vol.254 , pp. 1016-1019
    • Stefanova, I.1    Horejsi, V.2    Ansotegui, I.J.3    Knapp, W.4    Stockinger, H.5
  • 33
    • 0028285191 scopus 로고
    • Caveolae, caveolin and caveolin-rich membrane domains: A signalling hypothesis
    • Lisanti, M. P., P. E. Scherer, Z. L. Tang and M. Sargiacomo 1994. Caveolae, caveolin and caveolin-rich membrane domains: a signalling hypothesis. Trends in Cell Biology, 4:231-235.
    • (1994) Trends in Cell Biology , vol.4 , pp. 231-235
    • Lisanti, M.P.1    Scherer, P.E.2    Tang, Z.L.3    Sargiacomo, M.4
  • 34
    • 0028175989 scopus 로고
    • Cysteine3 of Src family protein tyrosine kinase determines palmitoylation and localization in caveolae
    • Shenoy, S. A., D. J. Dietzen, J. Kwong, D. C. Link and D. M. Lublin 1994. Cysteine3 of Src family protein tyrosine kinase determines palmitoylation and localization in caveolae. Journal of Cell Biology, 126:353-63.
    • (1994) Journal of Cell Biology , vol.126 , pp. 353-363
    • Shenoy, S.A.1    Dietzen, D.J.2    Kwong, J.3    Link, D.C.4    Lublin, D.M.5
  • 35
    • 0015863154 scopus 로고
    • Selective solubilization of proteins and phospholipids from red blood cell membranes by nonionic detergents
    • Yu, J., D. A. Fishman and T. L. Steck 1973. Selective solubilization of proteins and phospholipids from red blood cell membranes by nonionic detergents. J Supramol. Struct., 1:233-248.
    • (1973) J Supramol. Struct. , vol.1 , pp. 233-248
    • Yu, J.1    Fishman, D.A.2    Steck, T.L.3
  • 36
    • 0028273033 scopus 로고
    • TAG-1 can mediate homophilic binding, but neurite outgrowth on TAG-1 requires an L1-like molecule and beta 1 integrins
    • Felsenfeld, D. P., M. A. Hynes, K. M. Skoler, A. J. Furley and T. M. Jessell 1994. TAG-1 can mediate homophilic binding, but neurite outgrowth on TAG-1 requires an L1-like molecule and beta 1 integrins. Neuron, 12:675-90.
    • (1994) Neuron , vol.12 , pp. 675-690
    • Felsenfeld, D.P.1    Hynes, M.A.2    Skoler, K.M.3    Furley, A.J.4    Jessell, T.M.5
  • 37
    • 0025237057 scopus 로고
    • The axonal glycoprotein TAG-1 is an immunoglobulin superfamily member with neurite outgrowth-promoting activity
    • Furley, A. J., S. B. Morton, D. Manalo, D. Karagogeos, J. Dodd and T. M. Jessell 1990. The axonal glycoprotein TAG-1 is an immunoglobulin superfamily member with neurite outgrowth-promoting activity. Cell, 61:157-70.
    • (1990) Cell , vol.61 , pp. 157-170
    • Furley, A.J.1    Morton, S.B.2    Manalo, D.3    Karagogeos, D.4    Dodd, J.5    Jessell, T.M.6
  • 38
    • 0030068772 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator receptor reversibly dissociates from complement receptor type 3 (alpha M beta 2' CD11b/CD18) during neutrophil polarization
    • Kindzelskii, A. L., Z. O. Laska, R. 3. Todd and H. R. Petty 1996. Urokinase-type plasminogen activator receptor reversibly dissociates from complement receptor type 3 (alpha M beta 2' CD11b/CD18) during neutrophil polarization. Journal of Immunology, 156:297-309.
    • (1996) Journal of Immunology , vol.156 , pp. 297-309
    • Kindzelskii, A.L.1    Laska, Z.O.2    Todd III, R.3    Petty, H.R.4
  • 39
    • 0030052464 scopus 로고    scopus 로고
    • LPS induces CD14 association with complement receptor type 3, which is reversed by neutrophil adhesion
    • Zarewych, D. M., A. L. Kindzelskii, R. 3. Todd and H. R. Petty 1996. LPS induces CD14 association with complement receptor type 3, which is reversed by neutrophil adhesion. Journal of Immunology, 156:430-3.
    • (1996) Journal of Immunology , vol.156 , pp. 430-433
    • Zarewych, D.M.1    Kindzelskii, A.L.2    Todd III, R.3    Petty, H.R.4
  • 40
    • 0026775909 scopus 로고
    • Evidence for synthesis of scrapie prion proteins in the endocytic pathway
    • Borchelt, D. R., A. Taraboulos and S. B. Prusiner 1992. Evidence for synthesis of scrapie prion proteins in the endocytic pathway. Journal of Biological Chemistry, 267:16188-99.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 16188-16199
    • Borchelt, D.R.1    Taraboulos, A.2    Prusiner, S.B.3
  • 41
    • 0023683407 scopus 로고
    • Delivery of folates to the cytoplasm of MA104 cells is mediated by a surface membrane receptor that recycles
    • Kamen, B. A., M. T. Wang, A. J. Streckfuss, X. Peryea and R. G. Anderson 1988. Delivery of folates to the cytoplasm of MA104 cells is mediated by a surface membrane receptor that recycles. J Biol Chem, 263:13602-9.
    • (1988) J Biol Chem , vol.263 , pp. 13602-13609
    • Kamen, B.A.1    Wang, M.T.2    Streckfuss, A.J.3    Peryea, X.4    Anderson, R.G.5
  • 42
    • 0026587547 scopus 로고
    • Endocytosis of glycophospholipid-anchored and transmembrane forms of CD4 by different endocytic pathways
    • Keller, G.-A., M. W. Siegel and I. W. Caras 1991. Endocytosis of glycophospholipid-anchored and transmembrane forms of CD4 by different endocytic pathways. EMBO J., 11:863-874.
    • (1991) EMBO J. , vol.11 , pp. 863-874
    • Keller, G.-A.1    Siegel, M.W.2    Caras, I.W.3
  • 43
    • 0025133358 scopus 로고
    • Vectorial apical delivery and slow endocytosis of a glycolipid-anchored fusion protein in transfected MDCK cells_
    • Lisanti, M. P., I. W. Caras, T. Gilbert, D. Hanzel and B. E. Rodriguez 1990. Vectorial apical delivery and slow endocytosis of a glycolipid-anchored fusion protein in transfected MDCK cells_. Proc. Natl. Acad. Sci. USA, 87:7419-7423.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7419-7423
    • Lisanti, M.P.1    Caras, I.W.2    Gilbert, T.3    Hanzel, D.4    Rodriguez, B.E.5
  • 44
    • 0025303751 scopus 로고
    • The glycophospholipid-linked folate receptor internalizes folate without entering the clathrin-coated pit endocytic pathway
    • Rothberg, K. G., Y.-S. Ying, J. F. Kolhousr, B. A. Kamen and R. G. W. Anderson 1990. The glycophospholipid-linked folate receptor internalizes folate without entering the clathrin-coated pit endocytic pathway. J. Cell Biol., 110:637-649.
    • (1990) J. Cell Biol. , vol.110 , pp. 637-649
    • Rothberg, K.G.1    Ying, Y.-S.2    Kolhousr, J.F.3    Kamen, B.A.4    Anderson, R.G.W.5
  • 45
    • 0025373111 scopus 로고
    • Scrapie prion proteins accumulate in the cytoplasm of persistently infected cultured cells
    • Taraboulos, A., D. Serban and S. B. Prusiner 1990. Scrapie prion proteins accumulate in the cytoplasm of persistently infected cultured cells. J. Cell Biol. 110:2117-2132.
    • (1990) J. Cell Biol. , vol.110 , pp. 2117-2132
    • Taraboulos, A.1    Serban, D.2    Prusiner, S.B.3
  • 46
    • 0027415690 scopus 로고
    • Potocytosis of small molecules and ions by caveolae
    • Anderson, R. G. W. 1993. Potocytosis of small molecules and ions by caveolae. Trends Cell Biol., 3:69-72.
    • (1993) Trends Cell Biol. , vol.3 , pp. 69-72
    • Anderson, R.G.W.1
  • 47
    • 0027436790 scopus 로고
    • Endocytosis of folate-protein conjugates: Ultrastructural localization in KB cells
    • Turek, J. J., C. P. Leamon and P. S. Low 1993. Endocytosis of folate-protein conjugates: ultrastructural localization in KB cells. Journal of Cell Science, 106:423-130.
    • (1993) Journal of Cell Science , vol.106 , pp. 423-1130
    • Turek, J.J.1    Leamon, C.P.2    Low, P.S.3
  • 48
    • 0024383781 scopus 로고
    • Lipid recycling between the plasma membrane and intracellular compartments: Transport and metabolism of fluorescent sphingomyclin analogues in cultured fibroblasts
    • Koval, M. and R. E. Pagano 1989. Lipid recycling between the plasma membrane and intracellular compartments: transport and metabolism of fluorescent sphingomyclin analogues in cultured fibroblasts. J. Cell Biol., 108:2169-2181.
    • (1989) J. Cell Biol. , vol.108 , pp. 2169-2181
    • Koval, M.1    Pagano, R.E.2
  • 49
    • 0027243406 scopus 로고
    • Sorting of membrane components from endosomes and subsequent recycling to the cell surface occurs by a bulk flow process
    • Mayor, S., J. P. Presley and F. R. Maxfield 1993. Sorting of membrane components from endosomes and subsequent recycling to the cell surface occurs by a bulk flow process. J. Cell Biol., 121:1257-1269.
    • (1993) J. Cell Biol. , vol.121 , pp. 1257-1269
    • Mayor, S.1    Presley, J.P.2    Maxfield, F.R.3
  • 50
    • 0029117498 scopus 로고
    • The emergence of clathrin-independent pinocytic pathways
    • Lamaze, C. and S. L. Schmid 1995. The emergence of clathrin-independent pinocytic pathways. Current Opinion in Cell Biology, 7:573-580.
    • (1995) Current Opinion in Cell Biology , vol.7 , pp. 573-580
    • Lamaze, C.1    Schmid, S.L.2
  • 51
    • 0027503126 scopus 로고
    • Cell fractionation and electron microscope studies of kidney folate-binding protein
    • Birn, H., J. Selhub and E. I. Christensen 1993. Cell fractionation and electron microscope studies of kidney folate-binding protein. American Journal of Physiology, 264:C302-C310.
    • (1993) American Journal of Physiology , vol.264
    • Birn, H.1    Selhub, J.2    Christensen, E.I.3
  • 53
    • 0028966735 scopus 로고
    • Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform
    • Taraboulos, A., M. Scott, A. Semenov, D. Avraham, L. Laszlo and S. B. Prusiner 1995. Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform. Journal of Cell Biology, 129:121-32.
    • (1995) Journal of Cell Biology , vol.129 , pp. 121-132
    • Taraboulos, A.1    Scott, M.2    Semenov, A.3    Avraham, D.4    Laszlo, L.5    Prusiner, S.B.6
  • 55
    • 0026625261 scopus 로고
    • Lowering cholesterol content of MA104 cells inhibits receptor-mediated transport of folate
    • Chang, W.-J., K. G. Rothberg, B. A. Kamen and R. G. W. Anderson 1992. Lowering cholesterol content of MA104 cells inhibits receptor-mediated transport of folate. J. Cell Biol., 118:63-69.
    • (1992) J. Cell Biol. , vol.118 , pp. 63-69
    • Chang, W.-J.1    Rothberg, K.G.2    Kamen, B.A.3    Anderson, R.G.W.4
  • 56
    • 0025695634 scopus 로고
    • Cholesterol controls the clustering of the glycophospholipid-linked membrane receptor for 5-methyltetrahydrofolate
    • Rothberg, K. G., Y.-S. Ying, B. A. Kamen and R. G. W. Anderson 1990. Cholesterol controls the clustering of the glycophospholipid-linked membrane receptor for 5-methyltetrahydrofolate. J. Cell Biol., 111:2931-2938.
    • (1990) J. Cell Biol. , vol.111 , pp. 2931-2938
    • Rothberg, K.G.1    Ying, Y.-S.2    Kamen, B.A.3    Anderson, R.G.W.4
  • 57
    • 0023883979 scopus 로고
    • Glycosyl-phosphatidylinositol moiety that anchors Trypanosoma brucei variant surface glycoprotein to the membrane
    • Ferguson, M. A. J., S. W. Homans, R. A. Dwek and T. W. Rademacher 1988. Glycosyl-phosphatidylinositol moiety that anchors Trypanosoma brucei variant surface glycoprotein to the membrane. Science, 239:753-759.
    • (1988) Science , vol.239 , pp. 753-759
    • Ferguson, M.A.J.1    Homans, S.W.2    Dwek, R.A.3    Rademacher, T.W.4
  • 58
    • 0026535445 scopus 로고
    • Delivery of ligands from sorting endosomes to late endosomes occurs by maturation of sorting endosomes
    • Dunn, K. W. and F. R. Maxfield 1992. Delivery of ligands from sorting endosomes to late endosomes occurs by maturation of sorting endosomes. J Cell. Biol., 117:301-310.
    • (1992) J Cell. Biol. , vol.117 , pp. 301-310
    • Dunn, K.W.1    Maxfield, F.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.