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Volumn 136, Issue 5, 1997, Pages 1059-1070

Isoforms of ankyrin-3 that lack the NH2-terminal repeats associate with mouse macrophage lysosomes

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ANKYRIN; ANTIBODY; COMPLEMENTARY DNA; EPITOPE; FLUORESCEIN ISOTHIOCYANATE DEXTRAN; MEMBRANE PROTEIN; RNA; SPECTRIN;

EID: 0030968027     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.136.5.1059     Document Type: Article
Times cited : (67)

References (75)
  • 1
    • 0027993053 scopus 로고
    • Goigi spectrin: Identification of an erythroid β-spectrin homolog associated with the Golgi complex
    • Beck, K.A., J.A. Buchanan, V. Malhotra, and W.J. Nelson. 1994. Goigi spectrin: identification of an erythroid β-spectrin homolog associated with the Golgi complex. J. Cell Biol. 127:707-723.
    • (1994) J. Cell Biol. , vol.127 , pp. 707-723
    • Beck, K.A.1    Buchanan, J.A.2    Malhotra, V.3    Nelson, W.J.4
  • 2
    • 0017853463 scopus 로고
    • Purification of an active proteolytic fragment of the membrane attachment site for human ervthrocyte spectrin
    • Bennett, V. 1978. Purification of an active proteolytic fragment of the membrane attachment site for human ervthrocyte spectrin. J. Biol. Chem. 253:2292-2299.
    • (1978) J. Biol. Chem. , vol.253 , pp. 2292-2299
    • Bennett, V.1
  • 3
    • 0018397366 scopus 로고
    • Identification and partial purification of ankyrin, the high affinity membrane attachment site for human erythrocyte spectrin
    • Bennett, V., and P.J. Stenbuck. 1979. Identification and partial purification of ankyrin, the high affinity membrane attachment site for human erythrocyte spectrin. J. Biol. Chem. 254:2533-2541.
    • (1979) J. Biol. Chem. , vol.254 , pp. 2533-2541
    • Bennett, V.1    Stenbuck, P.J.2
  • 4
    • 0019321291 scopus 로고
    • Association between ankvrin and the cytoplasmic domain of band 3 isolated from human erythrocyte membrane
    • Bennett, V., and P.J. Stenbuck, 1980. Association between ankvrin and the cytoplasmic domain of band 3 isolated from human erythrocyte membrane. J. Biol. Chem. 255:6424-6432.
    • (1980) J. Biol. Chem. , vol.255 , pp. 6424-6432
    • Bennett, V.1    Stenbuck, P.J.2
  • 5
    • 0029079633 scopus 로고
    • Molecular size-fractionation during endocytosis in macrophages
    • Berthiaume, E.P., C. Medina, and J.A. Swanson. 1995. Molecular size-fractionation during endocytosis in macrophages. J. Cell Biol. 129:989-998.
    • (1995) J. Cell Biol. , vol.129 , pp. 989-998
    • Berthiaume, E.P.1    Medina, C.2    Swanson, J.A.3
  • 6
    • 0027155208 scopus 로고
    • Complex patterns of sequence variation and multiple 5′ and 3′ ends are found among transcripts of the erythroid ankyrin gene
    • Birkenmeier, C.S., R.A. While, L.L. Peters, E.J. Hall, S.E. Lux, and J.E. Barker. 1993, Complex patterns of sequence variation and multiple 5′ and 3′ ends are found among transcripts of the erythroid ankyrin gene. J. Biol. Chem. 268:9533-9540.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9533-9540
    • Birkenmeier, C.S.1    While, R.A.2    Peters, L.L.3    Hall, E.J.4    Lux, S.E.5    Barker, J.E.6
  • 7
    • 0026743901 scopus 로고
    • A CD44-like endothelial cell transmembrane glycoprotein (GPH6) interacts with extracellular matrix and ankyrin
    • Bourguignon, L.Y.W., V.B. Lokeshwar, J. He, X. Chen, and G.J. Bourguignon, 1992. A CD44-like endothelial cell transmembrane glycoprotein (GPH6) interacts with extracellular matrix and ankyrin. Mol. Cell Biol. 12:4464-4471.
    • (1992) Mol. Cell Biol. , vol.12 , pp. 4464-4471
    • Bourguignon, L.Y.W.1    Lokeshwar, V.B.2    He, J.3    Chen, X.4    Bourguignon, G.J.5
  • 8
    • 0027729564 scopus 로고
    • B: Structure of the major developmentally regulated domain and selective localization in unmyelinated axons
    • B: structure of the major developmentally regulated domain and selective localization in unmyelinated axons. J. Cell Biol. 123:1463-1473.
    • (1993) J. Cell Biol. , vol.123 , pp. 1463-1473
    • Chan, W.1    Kordeli, E.2    Bennett, V.3
  • 10
    • 0022258568 scopus 로고
    • Lysosome-associated membrane proteins: Characterization of LAMP-1 of macrophage P388 and mouse embryo 3T3 cultured cells
    • Chen, J.W., W. Pan, M.P. D'Souza, and J.T. August. 1985. Lysosome-associated membrane proteins: characterization of LAMP-1 of macrophage P388 and mouse embryo 3T3 cultured cells. Arch. Biochem. Biophys. 239:574-586.
    • (1985) Arch. Biochem. Biophys. , vol.239 , pp. 574-586
    • Chen, J.W.1    Pan, W.2    D'Souza, M.P.3    August, J.T.4
  • 12
    • 0021689392 scopus 로고
    • Brain ankyrin. A membrane-associated protein with binding sites for spectrin, tubulin, and the cytoplasmic domain of the erythrocytc anion channel
    • Davis, J.Q., and V. Bennett. 1984. Brain ankyrin. A membrane-associated protein with binding sites for spectrin, tubulin, and the cytoplasmic domain of the erythrocytc anion channel. J. Biol. Chem. 259:13550-13559.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13550-13559
    • Davis, J.Q.1    Bennett, V.2
  • 13
    • 0025314265 scopus 로고
    • Mapping the binding sites of human erythrocyte ankyrin for the anion exchanger and spectrin
    • Davis, L.H., and V. Bennett. 1990. Mapping the binding sites of human erythrocyte ankyrin for the anion exchanger and spectrin. J. Biol. Chem. 265:10589-10596.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10589-10596
    • Davis, L.H.1    Bennett, V.2
  • 14
    • 0026722207 scopus 로고
    • Ankyrin regulation: An alter-natively spliced segment of the regulatory domain functions as an intramolecular modulator
    • Davis, L.H., J.Q. Davis, and V. Bennett. 1992. Ankyrin regulation: an alter-natively spliced segment of the regulatory domain functions as an intramolecular modulator. J. Biol. Chem. 267:18966-18972.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18966-18972
    • Davis, L.H.1    Davis, J.Q.2    Bennett, V.3
  • 15
    • 0024657748 scopus 로고
    • The CTAB-DNA precipitation method: A common mini-scale preparation of template DNA from phagemids, phages or plasmids suitable for sequencing
    • Del Sal, G., G. Manfioletti, and C. Schneider. 1989. The CTAB-DNA precipitation method: a common mini-scale preparation of template DNA from phagemids, phages or plasmids suitable for sequencing. Biotechniques. 7:514-520.
    • (1989) Biotechniques , vol.7 , pp. 514-520
    • Del Sal, G.1    Manfioletti, G.2    Schneider, C.3
  • 16
    • 0024410410 scopus 로고
    • Functional sorting of actin isoformsin microvascular pericytes
    • DeNofrio, D., T.C. Hoock, and I.M. Herman. 1989. Functional sorting of actin isoformsin microvascular pericytes. J. Cell Biol. 109:191-202.
    • (1989) J. Cell Biol. , vol.109 , pp. 191-202
    • DeNofrio, D.1    Hoock, T.C.2    Herman, I.M.3
  • 17
    • 0026507108 scopus 로고
    • Protein immunolocalization in the spread erythrocyte membrane
    • Derick, L.H., S.C. Liu, A.H. Chishti, and J. Palek. 1992. Protein immunolocalization in the spread erythrocyte membrane. Eur. J. Cell Biol. 57:317-320.
    • (1992) Eur. J. Cell Biol. , vol.57 , pp. 317-320
    • Derick, L.H.1    Liu, S.C.2    Chishti, A.H.3    Palek, J.4
  • 19
    • 0023351697 scopus 로고
    • r 210,000 and 190,000 analogs of erythrocyte ankyrin along the plasma membrane of transporting epithelia, neurons and photoreceptors
    • r 210,000 and 190,000 analogs of erythrocyte ankyrin along the plasma membrane of transporting epithelia, neurons and photoreceptors. Eur. J. Cell Biol. 43:479-486.
    • (1987) Eur. J. Cell Biol. , vol.43 , pp. 479-486
    • Drenckhahn, D.1    Bennett, V.2
  • 20
    • 0022508705 scopus 로고
    • A kinetic analysis of biosynthesis and localization of a lysosomal-associated membrane glycoprotein
    • D'Souza, M.P., and J.T. August. 1986. A kinetic analysis of biosynthesis and localization of a lysosomal-associated membrane glycoprotein. Arch. Biochem. Biophys. 249:522-532.
    • (1986) Arch. Biochem. Biophys. , vol.249 , pp. 522-532
    • D'Souza, M.P.1    August, J.T.2
  • 23
    • 0023915578 scopus 로고
    • Fibroblasts maintain a complete endocytic pathway in the presence of lysosomotropic amines
    • Fritsch, J.E., M.J. Buckmaster, and B. Storrie. 1988. Fibroblasts maintain a complete endocytic pathway in the presence of lysosomotropic amines. Exp. Cell Res. 175:277-285.
    • (1988) Exp. Cell Res. , vol.175 , pp. 277-285
    • Fritsch, J.E.1    Buckmaster, M.J.2    Storrie, B.3
  • 24
    • 0019513926 scopus 로고
    • Temporal changes of lysosome and phagosome pH during phagolysosome formation in macrophages: Studies by fluorescence spectroscopy
    • Geisow, M.J., P. D'Arcy Hart, and M.R. Young. 1981. Temporal changes of lysosome and phagosome pH during phagolysosome formation in macrophages: studies by fluorescence spectroscopy. J. Cell Biol. 89:645-652.
    • (1981) J. Cell Biol. , vol.89 , pp. 645-652
    • Geisow, M.J.1    D'Arcy Hart, P.2    Young, M.R.3
  • 25
    • 0024241414 scopus 로고
    • Sorting of mannose 6-phosphate receptors and lysosomal membrane proteins in endocytic vesicles
    • Geuze, H.J., W. Stoorvogel, G.J. Strous, J.W. Slot, J.E. Bleekemolen, and I. Mellman. 1988. Sorting of mannose 6-phosphate receptors and lysosomal membrane proteins in endocytic vesicles. J. Cell Biol. 107:2491-2501.
    • (1988) J. Cell Biol. , vol.107 , pp. 2491-2501
    • Geuze, H.J.1    Stoorvogel, W.2    Strous, G.J.3    Slot, J.W.4    Bleekemolen, J.E.5    Mellman, I.6
  • 26
    • 0026085673 scopus 로고
    • Apical polarity of Na,K-ATPase in retinal pigment epithelium is linked to a reversal of the ankyrin-fodrin submcmbrane cytoskeluton
    • Gundersen, D., J. Orlowski, and E. Rodriguez-Boulan. 1991. Apical polarity of Na,K-ATPase in retinal pigment epithelium is linked to a reversal of the ankyrin-fodrin submcmbrane cytoskeluton. J. Cell Biol. 112:863-872.
    • (1991) J. Cell Biol. , vol.112 , pp. 863-872
    • Gundersen, D.1    Orlowski, J.2    Rodriguez-Boulan, E.3
  • 27
    • 0022001080 scopus 로고
    • Mechanism of cytoskeletal regulation (I): Functional differences correlate with antigenic dissimilarity in human brain and erythrocyte spectrin
    • Harris, A.S., L.A.D. Green, K.J. Ainger, and J.S. Morrow. 1985. Mechanism of cytoskeletal regulation (I): functional differences correlate with antigenic dissimilarity in human brain and erythrocyte spectrin. Biochem. Biophys. Acta. 830:147-158.
    • (1985) Biochem. Biophys. Acta. , vol.830 , pp. 147-158
    • Harris, A.S.1    Green, L.A.D.2    Ainger, K.J.3    Morrow, J.S.4
  • 28
    • 0026058131 scopus 로고
    • Actin and its mRNA are localized at the plasma membrane and the regions of moving cytoplasm during the cellular response to injury
    • Hoock, T.C. P.M. Newcomb, and J.M. Herman. 1991. β-Actin and its mRNA are localized at the plasma membrane and the regions of moving cytoplasm during the cellular response to injury. J. Cell Biol. 112:653-664.
    • (1991) J. Cell Biol. , vol.112 , pp. 653-664
    • Hoock, T.C.1    Newcomb, P.M.2    Herman, J.M.3
  • 29
    • 0028963869 scopus 로고
    • The polarity of the membrane skeleton in retinal pigment epithelial cells of developing chicken embryos and in primary culture
    • Huotari, V., R. Sormunen, V. Lento, and S. Eskelinen. 1995. The polarity of the membrane skeleton in retinal pigment epithelial cells of developing chicken embryos and in primary culture. Differentiation. 58:205-215.
    • (1995) Differentiation , vol.58 , pp. 205-215
    • Huotari, V.1    Sormunen, R.2    Lento, V.3    Eskelinen, S.4
  • 30
    • 0027405150 scopus 로고
    • Uptake and transport of fluorescent derivatives of dolichol in human fibroblasis
    • Jiang, L.W., B.A. Mitchell, J.G. Teodoro, and J.W. Rip. 1993. Uptake and transport of fluorescent derivatives of dolichol in human fibroblasis. Biochem. Biophys. Acta. 1147:205-213.
    • (1993) Biochem. Biophys. Acta. , vol.1147 , pp. 205-213
    • Jiang, L.W.1    Mitchell, B.A.2    Teodoro, J.G.3    Rip, J.W.4
  • 32
    • 0024230490 scopus 로고
    • A 115-kD polypeptide immunolugically related to erythrocyte band 3 is present in Golgi membranes
    • Kellokumpu, S., L. Neff, S. Jasma-Kellokumpu, R. Kopito, and R. Baron. 1988. A 115-kD polypeptide immunolugically related to erythrocyte band 3 is present in Golgi membranes. Science (Wash. DC). 242:1308-1311.
    • (1988) Science (Wash. DC) , vol.242 , pp. 1308-1311
    • Kellokumpu, S.1    Neff, L.2    Jasma-Kellokumpu, S.3    Kopito, R.4    Baron, R.5
  • 33
    • 0025995618 scopus 로고
    • Ankyrin binds to the 15th repetitive unit of erythroid and nonervthroid β-spectrin
    • Kennedy, S.P., S.L. Warren, B.C. Forget, and J.S. Morrow. 1991. Ankyrin binds to the 15th repetitive unit of erythroid and nonervthroid β-spectrin. J. Cell Biol. 115:267-277.
    • (1991) J. Cell Biol. , vol.115 , pp. 267-277
    • Kennedy, S.P.1    Warren, S.L.2    Forget, B.C.3    Morrow, J.S.4
  • 34
    • 0026077783 scopus 로고
    • Distinct ankyrin isoforms at neuron cell bodies and nodes of Ranvier resolved using erylhrocyte ankyrin-deficient mice
    • Kordeli, E., and V. Bennett. 1991. Distinct ankyrin isoforms at neuron cell bodies and nodes of Ranvier resolved using erylhrocyte ankyrin-deficient mice. J. Cell Biol. 114:1243-1259.
    • (1991) J. Cell Biol. , vol.114 , pp. 1243-1259
    • Kordeli, E.1    Bennett, V.2
  • 35
    • 0022512042 scopus 로고
    • Evidence for a polarity in the distribution of proteins from the cytoskeleton in Torpedo marmorata electrocytes
    • Kordeli, E., J. Cartaud, H.O. Nghiem, L.A. Pradel, C. Dubreuil, D. Paulin, and J.P. Changeux. 1986. Evidence for a polarity in the distribution of proteins from the cytoskeleton in Torpedo marmorata electrocytes. J. Cell Biol. 102:748-761.
    • (1986) J. Cell Biol. , vol.102 , pp. 748-761
    • Kordeli, E.1    Cartaud, J.2    Nghiem, H.O.3    Pradel, L.A.4    Dubreuil, C.5    Paulin, D.6    Changeux, J.P.7
  • 36
    • 0025231649 scopus 로고
    • An isoform of ankyrin is localized at nodes of Ranvier in myelinated axons of central and peripheral nerves
    • Kordeli, E., J. Davis, B. Trapp, and V. Bennett. 1990. An isoform of ankyrin is localized at nodes of Ranvier in myelinated axons of central and peripheral nerves. J. Cell Biol. 110:1341-1352.
    • (1990) J. Cell Biol. , vol.110 , pp. 1341-1352
    • Kordeli, E.1    Davis, J.2    Trapp, B.3    Bennett, V.4
  • 37
    • 0028985712 scopus 로고
    • G: A new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier
    • G: a new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier. J. Biol. Chem. 270:2352-2359.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2352-2359
    • Kordeli, E.1    Lambert, S.2    Bennett, V.3
  • 39
    • 0030213227 scopus 로고    scopus 로고
    • Interpreting cDNA sequences: Some insights from studies on translation
    • Kozak, M. 1996. Interpreting cDNA sequences: some insights from studies on translation. Mamm. Genome. 7:563-574.
    • (1996) Mamm. Genome. , vol.7 , pp. 563-574
    • Kozak, M.1
  • 40
    • 0025840276 scopus 로고
    • A new 440-kD isoform is the major ankyrin in neonatal brain
    • Kunimoto, M., E. Otto, and V. Bennett. 1991. A new 440-kD isoform is the major ankyrin in neonatal brain. J. Cell Biol. 115:1319-1331.
    • (1991) J. Cell Biol. , vol.115 , pp. 1319-1331
    • Kunimoto, M.1    Otto, E.2    Bennett, V.3
  • 41
    • 0014949207 scopus 로고
    • Cleavage of the structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of the structural proteins during the assembly of the head of the bacteriophage T4. Nature (Land.) 227:680-685.
    • (1970) Nature (Land.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 43
    • 0019815675 scopus 로고
    • Fodrin: Axonally transported polypeptides associated with the internal periphery of many cells
    • Levine, J., and M. Willard. 1981. Fodrin: axonally transported polypeptides associated with the internal periphery of many cells. J. Cell Biol. 90:631-643.
    • (1981) J. Cell Biol. , vol.90 , pp. 631-643
    • Levine, J.1    Willard, M.2
  • 45
    • 0021008730 scopus 로고
    • Complexes containing actin and spectrin from erythrocyte and brain
    • Lin, D.C., M.D. Flannagan, and S. Lin. 1983. Complexes containing actin and spectrin from erythrocyte and brain. Cell Motil. 3:375-382.
    • (1983) Cell Motil. , vol.3 , pp. 375-382
    • Lin, D.C.1    Flannagan, M.D.2    Lin, S.3
  • 46
    • 0025856071 scopus 로고
    • Uncoupling of the spectrin-based skeleton from the lipid bilayer in sickled red cells
    • Liu, S.C., L.H. Derick, S. Zhai, and J. Palek. 1991. Uncoupling of the spectrin-based skeleton from the lipid bilayer in sickled red cells. Science (Wash. DC). 252:574-576.
    • (1991) Science (Wash. DC) , vol.252 , pp. 574-576
    • Liu, S.C.1    Derick, L.H.2    Zhai, S.3    Palek, J.4
  • 48
    • 0025117790 scopus 로고
    • Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins
    • Lux, S.E., K.M. John, and V. Bennett. 1990. Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins. Nature (Land.) 344:36-42.
    • (1990) Nature (Land.) , vol.344 , pp. 36-42
    • Lux, S.E.1    John, K.M.2    Bennett, V.3
  • 50
    • 0027374511 scopus 로고
    • The membrane-binding domain of ankyrin contains four independently folded subdomains. each comprised of six ankyrin repeats
    • Michaely, P., and V. Bennett. 1993. The membrane-binding domain of ankyrin contains four independently folded subdomains. each comprised of six ankyrin repeats. J. Biol. Chem. 268:22703-22709.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22703-22709
    • Michaely, P.1    Bennett, V.2
  • 51
    • 0029150191 scopus 로고
    • The ANK repeats of erythrocyte ankyrin form two distinct but cooperative binding sites for the erythrocyte anion exchanger
    • Michaely, P., and V. Bennett. 1995. The ANK repeats of erythrocyte ankyrin form two distinct but cooperative binding sites for the erythrocyte anion exchanger. J. Biol. Chem. 270:22050-22057.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22050-22057
    • Michaely, P.1    Bennett, V.2
  • 52
    • 0027323556 scopus 로고
    • Association of the brain anion exchanger. AE3. with the repeal domain of ankyrin
    • Morgans, C.W., and R.R. Kopito, 1993. Association of the brain anion exchanger. AE3. with the repeal domain of ankyrin. J. Cell Sci. 105:1137-1142.
    • (1993) J. Cell Sci. , vol.105 , pp. 1137-1142
    • Morgans, C.W.1    Kopito, R.R.2
  • 53
    • 0020195691 scopus 로고
    • Acridine orange as a fluorescent probe for lysosomal proton pump
    • Moriyama, Y., T. Takano, and S. Okuma. 1982. Acridine orange as a fluorescent probe for lysosomal proton pump. J. Biochem. (Tokyo). 92:1333-1336.
    • (1982) J. Biochem. (Tokyo) , vol.92 , pp. 1333-1336
    • Moriyama, Y.1    Takano, T.2    Okuma, S.3
  • 54
    • 0024571516 scopus 로고
    • Ankyrin links fodrin to the α subunil of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells
    • Morrow, J.S., C.D. Cianci, T. Ardito, A.S. Mann, and M. Kashgarian. 1989. Ankyrin links fodrin to the α subunil of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells. J. Cell Biol. 108:455-465.
    • (1989) J. Cell Biol. , vol.108 , pp. 455-465
    • Morrow, J.S.1    Cianci, C.D.2    Ardito, T.3    Mann, A.S.4    Kashgarian, M.5
  • 55
    • 0025125799 scopus 로고
    • Identification of a membrane-cytoskeletal complex containing the cell adhesion molecule uvomorulin (E-cadherin). ankyrin, and fodrin in MadinDarby canine kidney epithelial cells
    • Nelson, W.J., E.M. Shore, A.Z. Wang, and R.W. Hammerton. 1990. Identification of a membrane-cytoskeletal complex containing the cell adhesion molecule uvomorulin (E-cadherin). ankyrin, and fodrin in MadinDarby canine kidney epithelial cells. J. Cell Biol. 110:349-357.
    • (1990) J. Cell Biol. , vol.110 , pp. 349-357
    • Nelson, W.J.1    Shore, E.M.2    Wang, A.Z.3    Hammerton, R.W.4
  • 56
    • 0002885684 scopus 로고
    • Lysosomes in the physiology and pathology of cells: Contributions of staining methods
    • Lysosomes. A.V.S de Reuck and M.P. Cameron, editors. London Churchill.
    • Novikoff, A. 1963. Lysosomes in the physiology and pathology of cells: contributions of staining methods. In Lysosomes. A.V.S de Reuck and M.P. Cameron, editors. Ciba Foundation Symposium, London Churchill. 36-77.
    • (1963) Ciba Foundation Symposium , pp. 36-77
    • Novikoff, A.1
  • 57
    • 2642714342 scopus 로고
    • Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents
    • Ohkuma, S., and B. Poole. 1978. Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents. Proc. Natl. Acad. Sci. USA. 75:3327-3331.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 3327-3331
    • Ohkuma, S.1    Poole, A.B.2
  • 58
    • 0025874185 scopus 로고
    • Isolation and characterization of cDNAs encoding human brain ankyrins reveal a family of alternatively spliced genes
    • Otto, E., M. Kunimoto, T. McLaughlin, and V. Bennett. 1991. Isolation and characterization of cDNAs encoding human brain ankyrins reveal a family of alternatively spliced genes. J. Cell Biol. 114:241-253.
    • (1991) J. Cell Biol. , vol.114 , pp. 241-253
    • Otto, E.1    Kunimoto, M.2    McLaughlin, T.3    Bennett, V.4
  • 60
    • 0029047129 scopus 로고
    • Ank3 (epithelial ankyrin). A widely distributed new member of the ankyrin gene family and the major ankyrin in kidney, is expressed in alternatively spliced forms, including forms that lack the repeat domain
    • Peters, L.L., K.M. John, P.M. Lu, E.M. Eicher, A. Higgins, M. Yialamas, L.C. Turtzo, A.J. Otsuka, and S.E. Lux. 1995. Ank3 (epithelial ankyrin). a widely distributed new member of the ankyrin gene family and the major ankyrin in kidney, is expressed in alternatively spliced forms, including forms that lack the repeat domain. J. Cell Biol. 130:313-330.
    • (1995) J. Cell Biol. , vol.130 , pp. 313-330
    • Peters, L.L.1    John, K.M.2    Lu, P.M.3    Eicher, E.M.4    Higgins, A.5    Yialamas, M.6    Turtzo, L.C.7    Otsuka, A.J.8    Lux, S.E.9
  • 62
    • 0027362056 scopus 로고
    • A highly conserved region of human erythrocyte ankyrin contains the capacity to bind spcctrin
    • Platt, O.S., S.E. Lux, and J.F. Falcone. 1993. A highly conserved region of human erythrocyte ankyrin contains the capacity to bind spcctrin. J. Biol. Chem. 268:24421-24426.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24421-24426
    • Platt, O.S.1    Lux, S.E.2    Falcone, J.F.3
  • 63
    • 0021705094 scopus 로고
    • Purification of a high molecular weight actin filament gelation protein from Acanthamoeba that shares antigenic determinants with vertebrate spectrins
    • Pollard, T.D. 1984. Purification of a high molecular weight actin filament gelation protein from Acanthamoeba that shares antigenic determinants with vertebrate spectrins. J. Cell Biol. 99:1970-1980.
    • (1984) J. Cell Biol. , vol.99 , pp. 1970-1980
    • Pollard, T.D.1
  • 66
    • 0027490813 scopus 로고
    • Combined spectrin and ankyrin deficiency is common in autosomal dominant hereditary spherocytosis
    • Savvides, P., O. Shalev, K.M. John, and S.E. Lux. 1993. Combined spectrin and ankyrin deficiency is common in autosomal dominant hereditary spherocytosis. Blood. 82:2953-2960.
    • (1993) Blood , vol.82 , pp. 2953-2960
    • Savvides, P.1    Shalev, O.2    John, K.M.3    Lux, S.E.4
  • 68
    • 0017233794 scopus 로고
    • Membrane flow during pinocytosis. A stereologic analysis
    • Steinman, R.M., S.E. Brodie, and Z.A. Cohn. 1976, Membrane flow during pinocytosis. A stereologic analysis. J. Cell Biol. 68:665-687.
    • (1976) J. Cell Biol. , vol.68 , pp. 665-687
    • Steinman, R.M.1    Brodie, S.E.2    Cohn, Z.A.3
  • 69
    • 0346981810 scopus 로고
    • Comparative observations on lysosomes and phagosomes in kidney and liver of rats after administration of horseradish peroxidase
    • Lysosomes. A.V.S. de Rcuck and M.P. Cameron, editors, London Churchill
    • Straus, W. 1963. Comparative observations on lysosomes and phagosomes in kidney and liver of rats after administration of horseradish peroxidase. In Lysosomes. A.V.S. de Rcuck and M.P. Cameron, editors, Ciba Foundation Symposium. London Churchill. 151-175.
    • (1963) Ciba Foundation Symposium , pp. 151-175
    • Straus, W.1
  • 70
    • 0024431785 scopus 로고
    • Phorhat esters stimulate macropinocytosis and solute flow through macrophages
    • Swanson, J.A. 1989. Phorhat esters stimulate macropinocytosis and solute flow through macrophages. J. Cell Sci. 94:135-142.
    • (1989) J. Cell Sci. , vol.94 , pp. 135-142
    • Swanson, J.A.1
  • 71
    • 0024525180 scopus 로고
    • Fluorescent labeling of endocytic compartments
    • Swanson, J. 1989. Fluorescent labeling of endocytic compartments. Methods Cell Biol. 29:137-151.
    • (1989) Methods Cell Biol. , vol.29 , pp. 137-151
    • Swanson, J.1
  • 72
    • 0021923854 scopus 로고
    • Phorbol esters and horseradish peroxidase stimulate pinocytosis and redirect the flow of pi. nocytosed fluid in macrophages
    • Swanson, J.A., B.D. Yirinec, and S.C. Silverstein. 1985. Phorbol esters and horseradish peroxidase stimulate pinocytosis and redirect the flow of pi. nocytosed fluid in macrophages. J. Cell Biol. 100:851-859.
    • (1985) J. Cell Biol. , vol.100 , pp. 851-859
    • Swanson, J.A.1    Yirinec, B.D.2    Silverstein, S.C.3
  • 73
    • 0023244896 scopus 로고
    • Differential and sequential delivery of fluorescent lysosomal probes into phagolysosomes in mouse peritoneal macrophages
    • Wang, Y.L., and M.B. Goren. 1987. Differential and sequential delivery of fluorescent lysosomal probes into phagolysosomes in mouse peritoneal macrophages. J. Cell Biol. 104:1749-1754.
    • (1987) J. Cell Biol. , vol.104 , pp. 1749-1754
    • Wang, Y.L.1    Goren, M.B.2
  • 74
    • 0021274123 scopus 로고
    • The structural basis of ankyrin function. II. Identification of two functional domains
    • Weaver, D.C., G.R. Pasternack, and V.T. Marchesi. 1984. The structural basis of ankyrin function. II. Identification of two functional domains. J. Biol. Chem. 259:6170-6175.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6170-6175
    • Weaver, D.C.1    Pasternack, G.R.2    Marchesi, V.T.3
  • 75
    • 0025260754 scopus 로고
    • Ankyrin and the hemolytic anemia mutation, nb. map to mouse chromosome 8: Presence of thu nb allele is associated with a truncated erythrocyte ankyrin
    • White, R.A., C.S. Birkenmeier, S.E. Lux, and J.E. Barker. 1990. Ankyrin and the hemolytic anemia mutation, nb. map to mouse chromosome 8: presence of thu nb allele is associated with a truncated erythrocyte ankyrin. Proc. Natl. Acad. Sci. USA. 87:3117-3121.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3117-3121
    • White, R.A.1    Birkenmeier, C.S.2    Lux, S.E.3    Barker, J.E.4


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