메뉴 건너뛰기




Volumn 141, Issue 1, 1998, Pages 85-99

Dynamin-mediated internalization of caveolae

Author keywords

[No Author keywords available]

Indexed keywords

DYNAMIN;

EID: 0032489879     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.141.1.85     Document Type: Article
Times cited : (646)

References (95)
  • 1
    • 0027443234 scopus 로고
    • Caveolae: Where incoming and outgoing messengers meet
    • Anderson, R.G.W. 1993a. Caveolae: where incoming and outgoing messengers meet. Proc. Natl. Acad. Sci. USA. 90:10909-10913.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10909-10913
    • Anderson, R.G.W.1
  • 2
    • 0027639941 scopus 로고
    • Plasmalemmal caveolae and GPI-anchored membrane proteins
    • Anderson, R.G.W. 1993b. Plasmalemmal caveolae and GPI-anchored membrane proteins. Curr. Opin. Cell Biol. 5:647-652.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 647-652
    • Anderson, R.G.W.1
  • 3
    • 0027415690 scopus 로고
    • Potocytosis of small molecules and ions by caveolae
    • Anderson, R.G.W. 1993c. 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
  • 4
    • 0017334127 scopus 로고
    • Role of the coated endocytic vesicle in the uptake of receptor bound low density lipoprotein in human fibroblasts
    • Anderson, R.G.W., M.S. Brown, and J.L. Goldstein. 1977. Role of the coated endocytic vesicle in the uptake of receptor bound low density lipoprotein in human fibroblasts. Cell. 10:351-364.
    • (1977) Cell , vol.10 , pp. 351-364
    • Anderson, R.G.W.1    Brown, M.S.2    Goldstein, J.L.3
  • 5
    • 0026545612 scopus 로고
    • Potocytosis: Sequestration and transport of small molecules by caveolae
    • Anderson, R.G.W., B.A. Kamen, K.G. Rothberg, and S.W. Lacey. 1992. Potocytosis: sequestration and transport of small molecules by caveolae. Science. 255:410-411.
    • (1992) Science , vol.255 , pp. 410-411
    • Anderson, R.G.W.1    Kamen, B.A.2    Rothberg, K.G.3    Lacey, S.W.4
  • 7
    • 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. 68:533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 8
    • 0041110797 scopus 로고
    • Endothelial plasmalemmal vesicles as elements in a system of branching invaginations from the cell surface
    • Bundgaard, M., J. Frøkjaer-Jensen, and C. Crone. 1979. Endothelial plasmalemmal vesicles as elements in a system of branching invaginations from the cell surface. Proc. Natl. Acad. Sci. USA. 76:6439-6442.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 6439-6442
    • Bundgaard, M.1    Frøkjaer-Jensen, J.2    Crone, C.3
  • 9
    • 0027498027 scopus 로고
    • Multiple GTP-binding proteins participate in clathrin-coated vesicle-mediated endocytosis
    • Carter, L.L., T.E. Redelmeier, L.A. Woollenweber, and S.L. Schmid. 1993. Multiple GTP-binding proteins participate in clathrin-coated vesicle-mediated endocytosis. J. Cell Biol. 120:37-45.
    • (1993) J. Cell Biol. , vol.120 , pp. 37-45
    • Carter, L.L.1    Redelmeier, T.E.2    Woollenweber, L.A.3    Schmid, S.L.4
  • 11
    • 0028137796 scopus 로고
    • Identification of dynamin 2, an isoform ubiquitously expressed in rat tissues
    • Cook, T.A., R. Urrutia, and M.A. McNiven. 1994. Identification of dynamin 2, an isoform ubiquitously expressed in rat tissues. Proc. Natl. Acad. Sci. USA. 91:644-648.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 644-648
    • Cook, T.A.1    Urrutia, R.2    McNiven, M.A.3
  • 12
    • 0029799506 scopus 로고    scopus 로고
    • Three dynamin-encoding genes are differentially expressed in developing rat brain
    • Cook, T., K. Mesa, and R. Urrutia. 1996. Three dynamin-encoding genes are differentially expressed in developing rat brain. J. Neurochem. 67:927-931.
    • (1996) J. Neurochem. , vol.67 , pp. 927-931
    • Cook, T.1    Mesa, K.2    Urrutia, R.3
  • 13
    • 0020482987 scopus 로고
    • Characterization of the cholera toxin receptor on BALB/c 3T3 cells as a ganglioside similar to, or identical with, ganglioside GM1. No evidence for galactoproteins with receptor activity
    • Critchley, D.R., C.H. Streuli, S. Kellie, and B. Patel. 1982. Characterization of the cholera toxin receptor on BALB/c 3T3 cells as a ganglioside similar to, or identical with, ganglioside GM1. No evidence for galactoproteins with receptor activity. Biochem. J. 204:209-219.
    • (1982) Biochem. J. , vol.204 , pp. 209-219
    • Critchley, D.R.1    Streuli, C.H.2    Kellie, S.3    Patel, B.4
  • 14
    • 0028036513 scopus 로고
    • Induction of mutant dynamin specifically blocks endocytic coated vesicle formation
    • Damke, H., T. Baba, D.E. Warnock, and S.L. Schmid. 1994. Induction of mutant dynamin specifically blocks endocytic coated vesicle formation. J. Cell Biol. 127:915-934.
    • (1994) J. Cell Biol. , vol.127 , pp. 915-934
    • Damke, H.1    Baba, T.2    Warnock, D.E.3    Schmid, S.L.4
  • 15
    • 0029134736 scopus 로고
    • Clathrin-independent pinocytosis is induced in cells overexpressing a temperature-sensitive mutant of dynamin
    • Damke, H., T. Baba, A.M. van der Bliek, and S.L. Schmid. 1995. Clathrin-independent pinocytosis is induced in cells overexpressing a temperature-sensitive mutant of dynamin. J. Cell Biol. 131:69-80.
    • (1995) J. Cell Biol. , vol.131 , pp. 69-80
    • Damke, H.1    Baba, T.2    Van Der Bliek, A.M.3    Schmid, S.L.4
  • 18
    • 0027257099 scopus 로고
    • Glycosphingolipid-enriched detergent-insoluble complexes in protein sorting in epithelial cells
    • Fiedler, K., T. Kobayashi, T.V. Kurzchalia, and K. Simons. 1993. Glycosphingolipid-enriched detergent-insoluble complexes in protein sorting in epithelial cells. Biochemistry. 32:6365-6373.
    • (1993) Biochemistry , vol.32 , pp. 6365-6373
    • Fiedler, K.1    Kobayashi, T.2    Kurzchalia, T.V.3    Simons, K.4
  • 19
    • 0019936616 scopus 로고
    • Internalization and degradation of cholera toxin by cultured cells: Relationship to toxin action
    • Fishman, P.H. 1982a. Internalization and degradation of cholera toxin by cultured cells: relationship to toxin action. J. Cell Biol. 93:860-865.
    • (1982) J. Cell Biol. , vol.93 , pp. 860-865
    • Fishman, P.H.1
  • 20
    • 0019986152 scopus 로고
    • Role of membrane gangliosides in the binding and action of bacterial toxins
    • Fishman, P.H. 1982b. Role of membrane gangliosides in the binding and action of bacterial toxins. J. Membr. Biol. 69:85-97.
    • (1982) J. Membr. Biol. , vol.69 , pp. 85-97
    • Fishman, P.H.1
  • 21
    • 0029086362 scopus 로고
    • De novo formation of caveolae in lymphocytes by expression of VIP21-caveolin
    • Fra, A.M., E. Williamson, K. Simons, and R.G. Parton. 1995. De novo formation of caveolae in lymphocytes by expression of VIP21-caveolin. Proc. Natl. Acad. Sci. USA. 92:8655-8659.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8655-8659
    • Fra, A.M.1    Williamson, E.2    Simons, K.3    Parton, R.G.4
  • 22
    • 0024097293 scopus 로고
    • Three-dimensional organization of the plasmalemmal vesicular system in directly frozen capillaries of the rete mirabile in the swim bladder of the eel
    • Frøkjaer-Jensen, J., R.C. Wagner, S.B. Andrews, P. Hagman, and T.S. Reese. 1988. Three-dimensional organization of the plasmalemmal vesicular system in directly frozen capillaries of the rete mirabile in the swim bladder of the eel. Cell Tissue Res. 254:17-24.
    • (1988) Cell Tissue Res. , vol.254 , pp. 17-24
    • Frøkjaer-Jensen, J.1    Wagner, R.C.2    Andrews, S.B.3    Hagman, P.4    Reese, T.S.5
  • 23
    • 0027452708 scopus 로고
    • Calcium pump of the plasma membrane is localized in caveolae
    • Fujimoto, T. 1993. Calcium pump of the plasma membrane is localized in caveolae. J. Cell Biol. 120:1147-1157.
    • (1993) J. Cell Biol. , vol.120 , pp. 1147-1157
    • Fujimoto, T.1
  • 24
    • 0024382542 scopus 로고
    • Novel tyrosine kinase substructures from Rous sarcoma virus-transformed cells are present in the membrane skeleton
    • Glenney, J.R., and L. Zokas. 1989. Novel tyrosine kinase substructures 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
  • 25
    • 0026454933 scopus 로고
    • Sequence and expression of caveolin, a protein component of caveolae plasma membrane domains phosphorylated on tyrosine in Rous sarcoma virus-transformed fibroblasts
    • Glenney, J.R., and D. Soppet. 1992. Sequence and expression of caveolin, a protein component of caveolae plasma membrane domains phosphorylated on tyrosine in Rous sarcoma virus-transformed fibroblasts. Proc. Natl. Acad. Sci. USA. 89:10517-10521.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10517-10521
    • Glenney, J.R.1    Soppet, D.2
  • 26
    • 0018746767 scopus 로고
    • Coated pits, coated vesicles and receptor mediated endocytosis
    • Goldstein, J.L., R.G.W. Anderson, and M.S. Brown. 1979. Coated pits, coated vesicles and receptor mediated endocytosis. Nature. 297:678-685.
    • (1979) Nature , vol.297 , pp. 678-685
    • Goldstein, J.L.1    Anderson, R.G.W.2    Brown, M.S.3
  • 28
    • 0015934086 scopus 로고
    • Temperature-sensitive mutations in Drosophila melanogaster XV: A selection of immobile adults
    • Grigliatti, T.A., L. Hall, R. Rosenbluth, and D.T. Suzuki, 1973. Temperature-sensitive mutations in Drosophila melanogaster XV: a selection of immobile adults. Mol. Gen. Genet. 120:107-114.
    • (1973) Mol. Gen. Genet. , vol.120 , pp. 107-114
    • Grigliatti, T.A.1    Hall, L.2    Rosenbluth, R.3    Suzuki, D.T.4
  • 29
    • 0029942238 scopus 로고    scopus 로고
    • Association of a dynamin-like protein with the Golgi apparatus in mammalian cells
    • Henley, J.R., and M.A. McNiven. 1996. Association of a dynamin-like protein with the Golgi apparatus in mammalian cells. J. Cell Biol. 133:761-775.
    • (1996) J. Cell Biol. , vol.133 , pp. 761-775
    • Henley, J.R.1    McNiven, M.A.2
  • 31
    • 0020601856 scopus 로고
    • Internalization and processing of transferrin and the transferrin receptor in human carcinoma A431 cells
    • Hopkins, C.R., and I.S. Trowbridge. 1983. Internalization and processing of transferrin and the transferrin receptor in human carcinoma A431 cells. J. Cell Biol. 97:508-521.
    • (1983) J. Cell Biol. , vol.97 , pp. 508-521
    • Hopkins, C.R.1    Trowbridge, I.S.2
  • 32
    • 0024387980 scopus 로고
    • Immunoisolation using magnetic solid supports: Subcellular fractionation for cell-free functional studies
    • A.M. Tartakoff, editor. Academic Press, San Diego, CA
    • Howell, K.E., R. Schmid, J. Ugelstad, and J. Gruenberg. 1989. Immunoisolation using magnetic solid supports: subcellular fractionation for cell-free functional studies. In Methods in Cell Biology. A.M. Tartakoff, editor. Academic Press, San Diego, CA. 265-292.
    • (1989) Methods in Cell Biology , pp. 265-292
    • Howell, K.E.1    Schmid, R.2    Ugelstad, J.3    Gruenberg, J.4
  • 33
    • 0018951216 scopus 로고
    • The antibody-induced clustering and endocytosis of HLA antigens on cultured human fibroblasts
    • Huet, C., J.F. Ash, and S.J. Singer. 1980. The antibody-induced clustering and endocytosis of HLA antigens on cultured human fibroblasts. Cell. 21:429-438.
    • (1980) Cell , vol.21 , pp. 429-438
    • Huet, C.1    Ash, J.F.2    Singer, S.J.3
  • 34
    • 0015069740 scopus 로고
    • Ruthenium labeling of micropinocytotic activity in the rat visceral yolk-sac placenta
    • Jollie, W.P., and T.J. Triche. 1971. Ruthenium labeling of micropinocytotic activity in the rat visceral yolk-sac placenta. J. Ultrastruct. Res. 35:541-553.
    • (1971) J. Ultrastruct. Res. , vol.35 , pp. 541-553
    • Jollie, W.P.1    Triche, T.J.2
  • 35
    • 0032559342 scopus 로고    scopus 로고
    • Role of dynamin in the formation of transport vesicles from the trans-Golgi network
    • Jones, S.M., K.E. Howell, J.R. Henley, H. Cao, and M.A. McNiven. 1998. Role of dynamin in the formation of transport vesicles from the trans-Golgi network. Science. 279:573-577.
    • (1998) Science , vol.279 , pp. 573-577
    • Jones, S.M.1    Howell, K.E.2    Henley, J.R.3    Cao, H.4    McNiven, M.A.5
  • 36
    • 0018743649 scopus 로고
    • Endocytosis of cholera toxin in GERL-like structures of murine neuroblastoma cells pretreated with GM1 ganglioside
    • Joseph, K.C., A. Stieber, and N.K. Gonatas. 1979. Endocytosis of cholera toxin in GERL-like structures of murine neuroblastoma cells pretreated with GM1 ganglioside. J. Cell Biol. 81:543-554.
    • (1979) J. Cell Biol. , vol.81 , pp. 543-554
    • Joseph, K.C.1    Stieber, A.2    Gonatas, N.K.3
  • 37
    • 0024844490 scopus 로고
    • Endocytosis of simian virus 40 into the endoplasmic reticulum
    • Kartenbeck, J., H. Stukenbrok, and A. Helenius. 1989. Endocytosis of simian virus 40 into the endoplasmic reticulum. J. Cell Biol. 109:2721-2729.
    • (1989) J. Cell Biol. , vol.109 , pp. 2721-2729
    • Kartenbeck, J.1    Stukenbrok, H.2    Helenius, A.3
  • 38
    • 4243054380 scopus 로고
    • Membranous intermediates in endocytosis are labile, as shown in a temperature-sensitive mutant
    • Kessell, I., B.D. Holst, and T.F. Roth. 1989. Membranous intermediates in endocytosis are labile, as shown in a temperature-sensitive mutant. Proc. Natl. Acad. Sci. USA. 86:4968-4972.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4968-4972
    • Kessell, I.1    Holst, B.D.2    Roth, T.F.3
  • 39
    • 0024368508 scopus 로고
    • Disappearance and reformation of synaptic vesicle membrane upon transmitter release observed under reversible blockage of membrane retrieval
    • Koenig, J.H., and K. Ikeda. 1989. Disappearance and reformation of synaptic vesicle membrane upon transmitter release observed under reversible blockage of membrane retrieval. J. Neurosci. 9:3844-3860.
    • (1989) J. Neurosci. , vol.9 , pp. 3844-3860
    • Koenig, J.H.1    Ikeda, K.2
  • 40
    • 0025115712 scopus 로고
    • Transformational process of the endosomal compartment in nephrocytes of Drosophila melanogaster
    • Koenig, J.H., and K. Ikeda. 1990. Transformational process of the endosomal compartment in nephrocytes of Drosophila melanogaster. Cell Tissue Res. 262:233-244.
    • (1990) Cell Tissue Res. , vol.262 , pp. 233-244
    • Koenig, J.H.1    Ikeda, K.2
  • 41
    • 0020603664 scopus 로고
    • Possible temperature-dependent blockage of synaptic vesicle recycling induced by a single gene mutation in Drosophila
    • Kosaka, T., and K. Ikeda. 1983a. Possible temperature-dependent blockage of synaptic vesicle recycling induced by a single gene mutation in Drosophila. J. Neurobiol. 14:207-225.
    • (1983) J. Neurobiol. , vol.14 , pp. 207-225
    • Kosaka, T.1    Ikeda, K.2
  • 43
    • 0026640940 scopus 로고
    • VIP21, a 21-kD membrane protein is an integral component of trans-Golgi network-derived transport vesicles
    • Kurzchalia, T.V., P. Dupree, R.G. Parton, R. Kellner, H. Virta, M. Lehnert, and K. Simons. 1992. VIP21, a 21-kD membrane protein is an integral component of trans-Golgi network-derived transport vesicles. J. Cell Biol. 118: 1003-1014.
    • (1992) J. Cell Biol. , vol.118 , pp. 1003-1014
    • Kurzchalia, T.V.1    Dupree, P.2    Parton, R.G.3    Kellner, R.4    Virta, H.5    Lehnert, M.6    Simons, K.7
  • 45
    • 0020626609 scopus 로고
    • Depletion of intracellular potassium arrests coated pit formation and receptor-mediated endocytosis in fibroblasts
    • Larkin, J.M., M.S. Brown, J.L. Goldstein, and R.G. Anderson. 1983. Depletion of intracellular potassium arrests coated pit formation and receptor-mediated endocytosis in fibroblasts. Cell. 33:273-285.
    • (1983) Cell , vol.33 , pp. 273-285
    • Larkin, J.M.1    Brown, M.S.2    Goldstein, J.L.3    Anderson, R.G.4
  • 46
    • 0022401444 scopus 로고
    • Modulation of intracellular potassium and ATP: Effects on coated pit function in fibroblasts and hepatocytes
    • Larkin, J.M., W.C. Donzell, and R.G. Anderson. 1985. Modulation of intracellular potassium and ATP: effects on coated pit function in fibroblasts and hepatocytes. J. Cell. Physiol. 124:372-378.
    • (1985) J. Cell. Physiol. , vol.124 , pp. 372-378
    • Larkin, J.M.1    Donzell, W.C.2    Anderson, R.G.3
  • 47
    • 0029117498 scopus 로고
    • The emergence of clathrin-independent pinocytic pathways
    • Lamaze, C., and S.L. Schmid. 1995. The emergence of clathrin-independent pinocytic pathways. Curr. Opin. Cell Biol. 7:573-580.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 573-580
    • Lamaze, C.1    Schmid, S.L.2
  • 48
    • 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 Cell Biol. 4:231-235.
    • (1994) Trends Cell Biol. , vol.4 , pp. 231-235
    • Lisanti, M.P.1    Scherer, P.E.2    Tang, Z.-L.3    Sargiacomo, M.4
  • 49
    • 0019994630 scopus 로고
    • Non-coated membrane invaginations are involved in binding and internalization of cholera and tetanus toxins
    • Montesano, R., J. Roth, A. Robert, and L. Orci. 1982. Non-coated membrane invaginations are involved in binding and internalization of cholera and tetanus toxins. Nature. 296:651-653.
    • (1982) Nature , vol.296 , pp. 651-653
    • Montesano, R.1    Roth, J.2    Robert, A.3    Orci, L.4
  • 50
    • 0026094996 scopus 로고
    • Predominant and developmentally regulated expression of dynamin in neurons
    • Nakata, T., A. Iwamoto, Y. Noda, R. Takemura, H. Yoshikura, and N. Hirokawa. 1991. Predominant and developmentally regulated expression of dynamin in neurons. Neuron. 7:461-469.
    • (1991) Neuron , vol.7 , pp. 461-469
    • Nakata, T.1    Iwamoto, A.2    Noda, Y.3    Takemura, R.4    Yoshikura, H.5    Hirokawa, N.6
  • 51
    • 0027155543 scopus 로고
    • A novel member of the dynamin family of GTP-binding proteins is expressed specifically in the testis
    • Nakata, T., R. Takemura, and N. Hirokawa. 1993. A novel member of the dynamin family of GTP-binding proteins is expressed specifically in the testis. J. Cell Sci. 105:1-5.
    • (1993) J. Cell Sci. , vol.105 , pp. 1-5
    • Nakata, T.1    Takemura, R.2    Hirokawa, N.3
  • 52
    • 0025006964 scopus 로고
    • Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins
    • Obar, R.A., C.A. Collins, J.A. Hammarback, H.S. Shpetner, and R.B. Vallee. 1990. Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins. Nature. 347:256-261.
    • (1990) Nature , vol.347 , pp. 256-261
    • Obar, R.A.1    Collins, C.A.2    Hammarback, J.A.3    Shpetner, H.S.4    Vallee, R.B.5
  • 53
    • 0032489880 scopus 로고    scopus 로고
    • Dynamin at the neck caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium
    • Oh, P., D.P. McIntosh, and J.E. Schnitzer. 1998. Dynamin at the neck caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium. J. Cell Biol. 141:101-114.
    • (1998) J. Cell Biol. , vol.141 , pp. 101-114
    • Oh, P.1    McIntosh, D.P.2    Schnitzer, J.E.3
  • 54
    • 0014301569 scopus 로고
    • Structural modulation of plasmalemmal vesicles
    • Palade, G.E., and R.R. Bruns. 1968. Structural modulation of plasmalemmal vesicles. J. Cell Biol. 37:633-649.
    • (1968) J. Cell Biol. , vol.37 , pp. 633-649
    • Palade, G.E.1    Bruns, R.R.2
  • 56
  • 57
    • 0029147426 scopus 로고
    • Digging into caveolae
    • Parton, R.G., and K. Simons. 1995. Digging into caveolae. Science. 269:1398-1399.
    • (1995) Science , vol.269 , pp. 1398-1399
    • Parton, R.G.1    Simons, K.2
  • 58
    • 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
  • 59
    • 0018075954 scopus 로고
    • Transformed cell lines susceptible or resistant to in vivo surveillance against tumorigenesis
    • Patek, P.Q., J.L. Collins, and M. Cohn. 1978. Transformed cell lines susceptible or resistant to in vivo surveillance against tumorigenesis. Nature. 276:510-511.
    • (1978) Nature , vol.276 , pp. 510-511
    • Patek, P.Q.1    Collins, J.L.2    Cohn, M.3
  • 61
    • 0022364832 scopus 로고
    • Endothelial plasmalemmal vesicles have a characteristic striped bipolar surface structure
    • Peters, K.-R., W. Carley, and G.E. Palade. 1985. Endothelial plasmalemmal vesicles have a characteristic striped bipolar surface structure. J. Cell Biol. 101:2233-2238.
    • (1985) J. Cell Biol. , vol.101 , pp. 2233-2238
    • Peters, K.-R.1    Carley, W.2    Palade, G.E.3
  • 62
    • 0018332644 scopus 로고
    • Reversible alteration in the neuromuscular junctions of Drosophila melanogaster bearing a temperature-sensitive mutation, shibire
    • Poodry, C.A., and L. Edgar. 1979. Reversible alteration in the neuromuscular junctions of Drosophila melanogaster bearing a temperature-sensitive mutation, shibire. J. Cell Biol. 81:520-527.
    • (1979) J. Cell Biol. , vol.81 , pp. 520-527
    • Poodry, C.A.1    Edgar, L.2
  • 63
    • 0028294852 scopus 로고
    • Transcytosis in the continuous endothelium of the myocardial microvasculature is inhibited by N-ethylmaleimide
    • Predescu, D., R. Horvat, S. Predescu, and G.E. Palade. 1994. Transcytosis in the continuous endothelium of the myocardial microvasculature is inhibited by N-ethylmaleimide. Proc. Natl. Acad. Sci. USA. 91:3014-3018.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3014-3018
    • Predescu, D.1    Horvat, R.2    Predescu, S.3    Palade, G.E.4
  • 64
    • 33750849530 scopus 로고    scopus 로고
    • Plasmalemmal vesicles function as transcytotic carriers for small proteins in the continuous endothelium
    • Predescu, S.A, D.N. Predescu, and G.E. Palade. 1997. Plasmalemmal vesicles function as transcytotic carriers for small proteins in the continuous endothelium. Am. J. Physiol. 41:937-949.
    • (1997) Am. J. Physiol. , vol.41 , pp. 937-949
    • Predescu, S.A.1    Predescu, D.N.2    Palade, G.E.3
  • 65
    • 0028026793 scopus 로고
    • The role of clathrin, adaptors and dynamin in endocytosis
    • Robinson, M.S. 1994. The role of clathrin, adaptors and dynamin in endocytosis. Curr. Opin. Cell Biol. 6:538-544.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 538-544
    • Robinson, M.S.1
  • 68
    • 0021676864 scopus 로고
    • Analysis of transferrin recycling in mitotic and interphase HeLa cells by quantitative fluorescence microscopy
    • Sager, P.R., P.A. Brown, and R.D. Berlin. 1984. Analysis of transferrin recycling in mitotic and interphase HeLa cells by quantitative fluorescence microscopy. Cell. 39:275-282.
    • (1984) Cell , vol.39 , pp. 275-282
    • Sager, P.R.1    Brown, P.A.2    Berlin, R.D.3
  • 69
    • 0028352977 scopus 로고
    • Retrograde transport from the Golgi complex to the ER of both Shiga toxin and the nontoxic Shiga B-fragment is regulated by butyric acid and cAMP
    • Sandvig, K., M. Ryd, O. Garred, E. Schweda, P.K. Holm, and B. van Deurs. 1994. Retrograde transport from the Golgi complex to the ER of both Shiga toxin and the nontoxic Shiga B-fragment is regulated by butyric acid and cAMP. J. Cell Biol. 126:53-64.
    • (1994) J. Cell Biol. , vol.126 , pp. 53-64
    • Sandvig, K.1    Ryd, M.2    Garred, O.3    Schweda, E.4    Holm, P.K.5    Van Deurs, B.6
  • 70
  • 71
    • 0029861240 scopus 로고    scopus 로고
    • Thapsigargin-induced transport of cholera toxin to the endoplasmic reticulum
    • Sandvig, K., O. Garred, and B. van Deurs. 1996. Thapsigargin-induced transport of cholera toxin to the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA. 93:12339-12343.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12339-12343
    • Sandvig, K.1    Garred, O.2    Van Deurs, B.3
  • 72
    • 0025605785 scopus 로고
    • Biochemical and immunochemical analysis of rat brain dynamin interaction with microtubules and organelles in vivo and in vitro
    • Scaife, R., and R.L. Margolis. 1990. Biochemical and immunochemical analysis of rat brain dynamin interaction with microtubules and organelles in vivo and in vitro. J. Cell Biol. 111:3023-3033.
    • (1990) J. Cell Biol. , vol.111 , pp. 3023-3033
    • Scaife, R.1    Margolis, R.L.2
  • 73
    • 0027997787 scopus 로고
    • Filipin-sensitive caveolae-mediated transport in endothelium: Reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules
    • Schnitzer, J.E., P. Oh, E. Pinney, and J. Allard. 1994. Filipin-sensitive caveolae-mediated transport in endothelium: reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules. J. Cell Biol. 127: 1217-1232.
    • (1994) J. Cell Biol. , vol.127 , pp. 1217-1232
    • Schnitzer, J.E.1    Oh, P.2    Pinney, E.3    Allard, J.4
  • 74
    • 0029082412 scopus 로고
    • Separation of caveolae from associated microdomains of GPI-anchored proteins
    • Schnitzer, J.E., D.P. McIntosh, A.M. Dvorak, J. Liu, and P. Oh. 1995a. Separation of caveolae from associated microdomains of GPI-anchored proteins. Science. 269:1435-1439.
    • (1995) Science , vol.269 , pp. 1435-1439
    • Schnitzer, J.E.1    McIntosh, D.P.2    Dvorak, A.M.3    Liu, J.4    Oh, P.5
  • 75
    • 0028925762 scopus 로고
    • Caveolae from luminal plasmalemma of rat lung endothelium: Microdomains enriched in caveolin, Ca (2+)-ATPase, and inositol trisphosphate receptor
    • Schnitzer, J.E., P. Oh, B.S. Jacobson, and A.M. Dvorak. 1995b. Caveolae from luminal plasmalemma of rat lung endothelium: microdomains enriched in caveolin, Ca (2+)-ATPase, and inositol trisphosphate receptor. Proc. Natl. Acad. Sci. USA. 92:1759-1763.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1759-1763
    • Schnitzer, J.E.1    Oh, P.2    Jacobson, B.S.3    Dvorak, A.M.4
  • 76
    • 0029809310 scopus 로고    scopus 로고
    • Role of GTP hydrolysis in fission of caveolae directly from plasma membranes
    • Schnitzer, J.E., P. Oh, and D.P. McIntosh. 1996. Role of GTP hydrolysis in fission of caveolae directly from plasma membranes. Science. 274:239-242.
    • (1996) Science , vol.274 , pp. 239-242
    • Schnitzer, J.E.1    Oh, P.2    McIntosh, D.P.3
  • 77
    • 0024047352 scopus 로고
    • Caveolae: Static inpocketings of the plasma membrane, dynamic vesicles or plain artifact?
    • Severs, N.J. 1988. Caveolae: static inpocketings of the plasma membrane, dynamic vesicles or plain artifact? J. Cell Sci. 90:341-348.
    • (1988) J. Cell Sci. , vol.90 , pp. 341-348
    • Severs, N.J.1
  • 78
    • 0024342278 scopus 로고
    • Identification of dynamin, a novel mechanochemical enzyme that mediates interactions between microtubules
    • Shpetner, H.S., and R.B. Vallee. 1989. Identification of dynamin, a novel mechanochemical enzyme that mediates interactions between microtubules. Cell. 59:421-432.
    • (1989) Cell , vol.59 , pp. 421-432
    • Shpetner, H.S.1    Vallee, R.B.2
  • 80
    • 0024339819 scopus 로고
    • Antisera specific for the alpha 1, alpha 2, alpha 3, and beta subunits of the Na,K-ATPase: Differential expression of alpha and beta subunits in rat tissue membranes
    • Shyjan, A.W., and R. Levenson. 1989. Antisera specific for the alpha 1, alpha 2, alpha 3, and beta subunits of the Na,K-ATPase: differential expression of alpha and beta subunits in rat tissue membranes. Biochemistry. 28:4531-4335.
    • (1989) Biochemistry , vol.28 , pp. 4531-14335
    • Shyjan, A.W.1    Levenson, R.2
  • 81
    • 0027952583 scopus 로고
    • Protein kinase C activators inhibit receptor-mediated potocytosis by preventing internalization of caveolae
    • Smart, E.J., D.C. Foster, Y.-S. Ying, B.A. Kamen, and R.G.W. Anderson. 1994. Protein kinase C activators inhibit receptor-mediated potocytosis by preventing internalization of caveolae. J. Cell Biol. 124:307-313.
    • (1994) J. Cell Biol. , vol.124 , pp. 307-313
    • Smart, E.J.1    Foster, D.C.2    Ying, Y.-S.3    Kamen, B.A.4    Anderson, R.G.W.5
  • 82
    • 0028889719 scopus 로고
    • Hormonal regulation of caveolae internalization
    • Smart, E.J., Y.-S. Ying, and R.G.W. Anderson. 1995. Hormonal regulation of caveolae internalization. J. Cell Biol. 131:929-938.
    • (1995) J. Cell Biol. , vol.131 , pp. 929-938
    • Smart, E.J.1    Ying, Y.-S.2    Anderson, R.G.W.3
  • 84
    • 0030745673 scopus 로고    scopus 로고
    • Major histocompatibility complex class I molecules mediate association of SV40 with caveolae
    • Stang, E., J. Kartenbeck, and R.G. Parton. 1997. Major histocompatibility complex class I molecules mediate association of SV40 with caveolae. Mol. Biol. Cell. 8:47-57.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 47-57
    • Stang, E.1    Kartenbeck, J.2    Parton, R.G.3
  • 85
    • 0028923349 scopus 로고
    • Tubular membrane invaginations coated by dynamin rings are induced by GTP-γS in nerve terminals
    • Takei, K., P.S. McPherson, S.L. Schmid, and P. De Camilli. 1995. Tubular membrane invaginations coated by dynamin rings are induced by GTP-γS in nerve terminals. Nature. 374:186-190.
    • (1995) Nature , vol.374 , pp. 186-190
    • Takei, K.1    McPherson, P.S.2    Schmid, S.L.3    De Camilli, P.4
  • 86
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Nalt. Acad. Sci. USA. 76:4350-4354.
    • (1979) Proc. Nalt. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 87
    • 0023449563 scopus 로고
    • Ligands internalized through coated or noncoated invaginations follow a common intracellular pathway
    • Tran, D., J.L. Carpentier, F. Sawano, P. Gorden, and L. Orci. 1987. Ligands internalized through coated or noncoated invaginations follow a common intracellular pathway. Proc. Natl. Acad. Scid. USA. 84:7957-7961.
    • (1987) Proc. Natl. Acad. Scid. USA , vol.84 , pp. 7957-7961
    • Tran, D.1    Carpentier, J.L.2    Sawano, F.3    Gorden, P.4    Orci, L.5
  • 88
    • 0031026631 scopus 로고    scopus 로고
    • The dynamins: Redundant or distinct functions for an expanding family of related GTP-ases?
    • Urrutia R., J.R. Henley, T. Cook, and M.A. McNiven. 1997. The dynamins: Redundant or distinct functions for an expanding family of related GTP-ases? Proc. Natl. Acad. Sci. USA. 94:377-384.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 377-384
    • Urrutia, R.1    Henley, J.R.2    Cook, T.3    McNiven, M.A.4
  • 89
    • 0022385727 scopus 로고
    • Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
    • Vale, R.D., T.S. Reese, and M.P. Sheetz. 1985. Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility. Cell. 42: 39-50.
    • (1985) Cell , vol.42 , pp. 39-50
    • Vale, R.D.1    Reese, T.S.2    Sheetz, M.P.3
  • 90
    • 0025810110 scopus 로고
    • Dynamin-like protein encoded by the Drosophila shibire gene associated with vesicular traffic
    • van der Bliek, A.M., and E.M. Meyerowitz. 1991. Dynamin-like protein encoded by the Drosophila shibire gene associated with vesicular traffic. Nature. 351:411-414.
    • (1991) Nature , vol.351 , pp. 411-414
    • Van Der Bliek, A.M.1    Meyerowitz, E.M.2
  • 93
    • 0030298146 scopus 로고    scopus 로고
    • Dynamin GTPase, a force-generating molecular switch
    • Warnock, D.E., and S.L. Schmid. 1996. Dynamin GTPase, a force-generating molecular switch. BioEssays. 18:885-893.
    • (1996) BioEssays , vol.18 , pp. 885-893
    • Warnock, D.E.1    Schmid, S.L.2
  • 94
    • 0026786340 scopus 로고
    • Endocytosis: What goes in and how
    • Watts, C., and M. Marsh. 1992. Endocytosis: what goes in and how. J. Cell Sci. 103:1-8.
    • (1992) J. Cell Sci. , vol.103 , pp. 1-8
    • Watts, C.1    Marsh, M.2
  • 95
    • 77049234363 scopus 로고
    • The fine structure of the gall bladder epithelium of the mouse
    • Yamada, E. 1955. The fine structure of the gall bladder epithelium of the mouse. J. Biophys. Biochem. Cytol. 1:445-458.
    • (1955) J. Biophys. Biochem. Cytol. , vol.1 , pp. 445-458
    • Yamada, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.