메뉴 건너뛰기




Volumn 133, Issue 4, 1996, Pages 819-830

Identification of a small cytoplasmic ankyrin (AnkG19) in the kidney and muscle that binds βI∑* spectrin and associates with the golgi apparatus

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; SPECTRIN;

EID: 0029898290     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.133.4.819     Document Type: Article
Times cited : (162)

References (60)
  • 2
    • 0027993053 scopus 로고
    • Golgi spectrin: Identification of an erythroid beta-spectrin homolog associated with the Golgi complex
    • Beck, K.A., J.A. Buchanan, V. Malhotra, and W.J. Nelson. 1994. Golgi spectrin: identification of an erythroid beta-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
  • 3
    • 0026806912 scopus 로고
    • Ankyrins. Adaptors between diverse plasma membrane proteins and the cytoplasm
    • Bennett, V. 1992. Ankyrins. Adaptors between diverse plasma membrane proteins and the cytoplasm. J. Biol. Chem. 267:8703-8706.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8703-8706
    • Bennett, V.1
  • 4
    • 0027333413 scopus 로고
    • The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane
    • Bennett, V., and D.M. Gilligan. 1993. The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane. Annu. Rev. Cell Biol. 9:27-66.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 27-66
    • Bennett, V.1    Gilligan, D.M.2
  • 5
    • 0017277818 scopus 로고
    • Assay of proteins in the presence of interfering materials
    • Bensadoun, A., and D. Weinstein. 1976. Assay of proteins in the presence of interfering materials. Anal. Biochem. 70:241-250.
    • (1976) Anal. Biochem. , vol.70 , pp. 241-250
    • Bensadoun, A.1    Weinstein, D.2
  • 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. White, 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    White, R.A.2    Peters, L.L.3    Hall, E.J.4    Lux, S.E.5    Barker, J.E.6
  • 7
    • 0027333330 scopus 로고
    • Hundreds of ankyrin-like repeats in functionally diverse proteins: Mobile modules that cross phyla horizontally?
    • Bork, P. 1993. Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally? Proteins. 17:363-374.
    • (1993) Proteins. , vol.17 , pp. 363-374
    • Bork, P.1
  • 8
    • 0022484218 scopus 로고
    • A lymphoma plasma membrane-associated protein with ankyrin-like properties
    • Bourguignon, L.Y., G. Walker, S.J. Suchard, and K. Balazovich. 1986. A lymphoma plasma membrane-associated protein with ankyrin-like properties. J. Cell Biol. 102:2115-2124.
    • (1986) J. Cell Biol. , vol.102 , pp. 2115-2124
    • Bourguignon, L.Y.1    Walker, G.2    Suchard, S.J.3    Balazovich, K.4
  • 9
    • 0027729564 scopus 로고
    • 440-kD ankyrinB: Structure of the major developmentally regulated domain and selective localization in unmyelinated axons
    • Chan, W., E. Kordeli, and V. Bennett. 1993. 440-kD ankyrinB: 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
    • 0023277545 scopus 로고
    • Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P., and N. Sacchi. 1987. Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 11
    • 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
  • 12
    • 0025115664 scopus 로고
    • +) -ATPase interact with distinct sites on ankyrin in in vitro assays
    • +) (-ATPase interact with distinct sites on ankyrin in in vitro assays. J. Biol. Chem. 265:17252-17256.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17252-17256
    • Davis, J.Q.1    Bennett, V.2
  • 13
    • 0024515166 scopus 로고
    • Diversity of membrane binding sites of ankyrins
    • Davis, J., L. Davis, and V. Bennett. 1989. Diversity of membrane binding sites of ankyrins. J. Biol. Chem. 264:6417-6426.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6417-6426
    • Davis, J.1    Davis, L.2    Bennett, V.3
  • 14
    • 0025859717 scopus 로고
    • Specific 33-residue repeat(s) of erythrocyte ankyrin associate with the anion exchanger
    • Davis, L.H., E. Otto, and V. Bennett. 1991. Specific 33-residue repeat(s) of erythrocyte ankyrin associate with the anion exchanger. J. Biol. Chem. 266:11163-11169.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11163-11169
    • Davis, L.H.1    Otto, E.2    Bennett, V.3
  • 16
    • 0028262115 scopus 로고
    • Ankyrin binds to two distinct cytoplasmic domains of Na,K-ATPase a subunit
    • Devarajan, P., D.A. Scaramuzzino, and J.S. Morrow. 1994. Ankyrin binds to two distinct cytoplasmic domains of Na,K-ATPase a subunit. Proc. Natl. Acad. Sci. USA. 91:2965-2969.
    • (1994) Proc. Natl. Acad. Sci. USA. , vol.91 , pp. 2965-2969
    • Devarajan, P.1    Scaramuzzino, D.A.2    Morrow, J.S.3
  • 17
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 18
    • 0028293148 scopus 로고
    • Cytosolic interaction between deltex and Notch ankyrin repeats implicates dellex in the Notch signaling pathway
    • Diederich, R.J., K. Matsuno, H. Hing, and T.S. Artavanis. 1994. Cytosolic interaction between deltex and Notch ankyrin repeats implicates dellex in the Notch signaling pathway. Development (Cumb.). 120:473-481.
    • (1994) Development (Cumb.). , vol.120 , pp. 473-481
    • Diederich, R.J.1    Matsuno, K.2    Hing, H.3    Artavanis, T.S.4
  • 19
    • 0028173073 scopus 로고
    • Ankyrin and beta-spectrin accumulate independently of alpha-spectrin in Drosophila
    • Dubreuil, R.R., and J. Yu. 1994. Ankyrin and beta-spectrin accumulate independently of alpha-spectrin in Drosophila. Proc. Natl. Acad. Sci. USA. 91:10285-10289.
    • (1994) Proc. Natl. Acad. Sci. USA. , vol.91 , pp. 10285-10289
    • Dubreuil, R.R.1    Yu, J.2
  • 20
    • 0027027666 scopus 로고
    • Large numbers of alternatively spliced isoforms of the regulatory region of human erythrocyte ankyrin
    • Gallagher, P.G., W.T. Tse, A.L. Scarpa, S.E. Lux, and E.G. Forget. 1992. Large numbers of alternatively spliced isoforms of the regulatory region of human erythrocyte ankyrin. Trans. Assoc. Am. Phys. 105:268-277.
    • (1992) Trans. Assoc. Am. Phys. , vol.105 , pp. 268-277
    • Gallagher, P.G.1    Tse, W.T.2    Scarpa, A.L.3    Lux, S.E.4    Forget, E.G.5
  • 21
    • 0028984235 scopus 로고
    • Immunocytochemical localization of beta-COP to the ER-Golgi boundary and the TGN
    • Griffiths, G., R. Pepperkok, J.K. Locker, and T.E. Kreis. 1995. Immunocytochemical localization of beta-COP to the ER-Golgi boundary and the TGN. J. Cell Sci. 108:2839-2856.
    • (1995) J. Cell Sci. , vol.108 , pp. 2839-2856
    • Griffiths, G.1    Pepperkok, R.2    Locker, J.K.3    Kreis, T.E.4
  • 22
    • 0022645389 scopus 로고
    • Mechanisms of cytoskeletal regulation: Functional and antigenic diversity in human erythrocyte and brain beta spectrin
    • Harris, A.S., J.P. Anderson, P.D. Yurchenco, L.A.D. Green, K.J. Ainger, and J.S. Morrow. 1986. Mechanisms of cytoskeletal regulation: functional and antigenic diversity in human erythrocyte and brain beta spectrin. J. Cell. Biochem. 30:51-70.
    • (1986) J. Cell. Biochem. , vol.30 , pp. 51-70
    • Harris, A.S.1    Anderson, J.P.2    Yurchenco, P.D.3    Green, L.A.D.4    Ainger, K.J.5    Morrow, J.S.6
  • 23
    • 0024326027 scopus 로고
    • Calmodulin regulates fodrin susceptibility to cleavage by calcium-dependent protease 1
    • Harris, A.S., D.E. Croall, and J.S. Morrow. 1989. Calmodulin regulates fodrin susceptibility to cleavage by calcium-dependent protease 1. J. Biol. Chem. 264:17401-17408.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17401-17408
    • Harris, A.S.1    Croall, D.E.2    Morrow, J.S.3
  • 25
    • 0026202069 scopus 로고
    • Secretory granule and synaptic vesicle formation
    • Kelly, R.B. 1991. Secretory granule and synaptic vesicle formation. Curr. Opin. Cell Biol. 3:654-660.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 654-660
    • Kelly, R.B.1
  • 26
    • 0028245275 scopus 로고
    • A partial structural repeat forms the heterodimer self-association site of all β-spectrins
    • Kennedy, S.P., S.A. Weed, B.G. Forget, and J.S. Morrow. 1994. A partial structural repeat forms the heterodimer self-association site of all β-spectrins. J. Biol. Chem. 269:11400-11408.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11400-11408
    • Kennedy, S.P.1    Weed, S.A.2    Forget, B.G.3    Morrow, J.S.4
  • 28
    • 0026077783 scopus 로고
    • Distinct ankyrin isoforms at neuron cell bodies and nodes of Ranvier resolved usinn erythrocyte ankyrin-deficient mice
    • Kordeli, E., and V. Bennett. 1991. Distinct ankyrin isoforms at neuron cell bodies and nodes of Ranvier resolved usinn erythrocyte ankyrin-deficient mice. J. Cell Biol. 114:1243-1259.
    • (1991) J. Cell Biol. , vol.114 , pp. 1243-1259
    • Kordeli, E.1    Bennett, V.2
  • 29
    • 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
  • 30
    • 0028985712 scopus 로고
    • AnkyrinG. A new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier
    • Kordeli, E., S. Lambert, and V. Bennett. 1995. AnkyrinG. 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
  • 31
    • 0028068272 scopus 로고
    • Coat proteins in intracellular membrane transport
    • Kreis, T.E., and R. Pepperkok. 1994. Coat proteins in intracellular membrane transport. Curr. Opin. Cell Biol. 6:533-537.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 533-537
    • Kreis, T.E.1    Pepperkok, R.2
  • 32
    • 0025840276 scopus 로고
    • A new 440-kD isoform is the major ankyrin in neonatal rat brain
    • Kunimoto, M., E. Otto, and V. Bennett. 1991. A new 440-kD isoform is the major ankyrin in neonatal rat 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
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.). 227:680-685.
    • (1970) Nature (Lond.). , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0026497661 scopus 로고
    • Cytoskeleton-plasma membrane interactions
    • Luna, E.J., and A.L. Hitt. 1992. Cytoskeleton-plasma membrane interactions. Science (Wash. DC). 258:955-964.
    • (1992) Science (Wash. DC). , vol.258 , pp. 955-964
    • Luna, E.J.1    Hitt, A.L.2
  • 36
    • 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. 1990a. Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins. Nature (Lond.). 344:36-42.
    • (1990) Nature (Lond.). , vol.344 , pp. 36-42
    • Lux, S.E.1    John, K.M.2    Bennett, V.3
  • 38
    • 0028068273 scopus 로고
    • Mechanisms of cell polarity: Sorting and transport in epithelial cells
    • Matter, K., and I. Mellman. 1994. Mechanisms of cell polarity: sorting and transport in epithelial cells. Curr. Opin. Cell Biol. 6:545-554.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 545-554
    • Matter, K.1    Mellman, I.2
  • 39
    • 0029166488 scopus 로고
    • Hierarchy of mechanisms involved in generating Na/K-ATPase polarity in MDCK epithelial cells
    • Mays, R.W., K.A. Siemers, B.A. Fritz, A.W. Lowe, G. van Meer, and W.J. Nelson. 1995. Hierarchy of mechanisms involved in generating Na/K-ATPase polarity in MDCK epithelial cells. J. Cell Biol. 130:1105-1115.
    • (1995) J. Cell Biol. , vol.130 , pp. 1105-1115
    • Mays, R.W.1    Siemers, K.A.2    Fritz, B.A.3    Lowe, A.W.4    Van Meer, G.5    Nelson, W.J.6
  • 40
    • 0016335085 scopus 로고
    • Periodate-lysine paraformaldehyde fixative. A new fixative for immunoelectron microscopy
    • McLean, I.W., and P.K. Nakane. 1974. Periodate-lysine paraformaldehyde fixative. A new fixative for immunoelectron microscopy. J. Histochem. Cytochem. 22:1077-1083.
    • (1974) J. Histochem. Cytochem. , vol.22 , pp. 1077-1083
    • McLean, I.W.1    Nakane, P.K.2
  • 41
    • 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
  • 43
    • 0019522402 scopus 로고
    • Self-assembly of spectrin oligomers in vitro: A basis for a dynamic cytskeleton
    • Morrow, J.S., and V.T. Marchesi. 1981. Self-assembly of spectrin oligomers in vitro: a basis for a dynamic cytskeleton. J. Cell Biol. 88:463-468.
    • (1981) J. Cell Biol. , vol.88 , pp. 463-468
    • Morrow, J.S.1    Marchesi, V.T.2
  • 44
    • 0024571516 scopus 로고
    • Ankyrin links fodrin to alpha Na/K ATPase in Madin-Darby canine kidney cells and in renal tubule cells
    • Morrow, J.S., C. Cianci, T. Ardito, A. Mann, and M.T. Kashgarian. 1989. Ankyrin links fodrin to alpha Na/K ATPase in Madin-Darby canine kidney cells and in renal tubule cells. J. Cell Biol. 108:455-465.
    • (1989) J. Cell Biol. , vol.108 , pp. 455-465
    • Morrow, J.S.1    Cianci, C.2    Ardito, T.3    Mann, A.4    Kashgarian, M.T.5
  • 45
    • 0004791869 scopus 로고
    • Polarized assembly of spectrin and ankyrin in epithelial cells
    • M.S. Mooseker and J.S. Morrow, editors. Academic Press. New York
    • Morrow, J.S., C.D. Cianci, S.P. Kennedy, and S.L. Warren. 1991. Polarized assembly of spectrin and ankyrin in epithelial cells. In Ordering the Membrane Cytoskeleton Trilayer, M.S. Mooseker and J.S. Morrow, editors. Academic Press. New York. 227-244.
    • (1991) Ordering the Membrane Cytoskeleton Trilayer , pp. 227-244
    • Morrow, J.S.1    Cianci, C.D.2    Kennedy, S.P.3    Warren, S.L.4
  • 46
    • 0000589008 scopus 로고    scopus 로고
    • Of membrane stability and mosaics: The spectrin cytoskeleton
    • J. Hoffman and J. Jamieson. editors. Oxford Press, London. In press
    • Morrow, J.S., D.L. Rimm, S.P. Kennedy, C.D. Cianci, J.H. Sinard, and S.A. Weed. 1996. Of membrane stability and mosaics: the spectrin cytoskeleton. In Handbook of Physiology. J. Hoffman and J. Jamieson. editors. Oxford Press, London. In press.
    • (1996) Handbook of Physiology
    • Morrow, J.S.1    Rimm, D.L.2    Kennedy, S.P.3    Cianci, C.D.4    Sinard, J.H.5    Weed, S.A.6
  • 47
    • 0023001826 scopus 로고
    • Dynamics of membrane-skeleton (fodrin) organization during development of polarity in Madin-Darby canine kidney epithelial cells
    • Nelson, W.J., and P.J. Veshnock. 1986. Dynamics of membrane-skeleton (fodrin) organization during development of polarity in Madin-Darby canine kidney epithelial cells. J. Cell Biol. 103:1751-1765.
    • (1986) J. Cell Biol. , vol.103 , pp. 1751-1765
    • Nelson, W.J.1    Veshnock, P.J.2
  • 48
    • 0025874185 scopus 로고
    • Isolation and characterizatoin 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 characterizatoin 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
  • 49
    • 0027220591 scopus 로고
    • Beta-COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo
    • Pepperkok, R., J. Scheel, H. Horstmann, H.P. Hauri, G. Griffiths, and T.E. Kreis. 1993. Beta-COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo. Cell. 74:71-82.
    • (1993) Cell. , vol.74 , pp. 71-82
    • Pepperkok, R.1    Scheel, J.2    Horstmann, H.3    Hauri, H.P.4    Griffiths, G.5    Kreis, T.E.6
  • 50
    • 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 repeal 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 repeal 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
  • 52
    • 0027362056 scopus 로고
    • A highly conserved region of human erythrocyte ankyrin contains the capacity to bind spectrin
    • Platt, O.S., S.E. Lux, and J.F. Falcone. 1993. A highly conserved region of human erythrocyte ankyrin contains the capacity to bind spectrin. 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
  • 53
    • 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
  • 55
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D.B., and K.S. Johnson. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene (Amst.). 67:31-40.
    • (1988) Gene (Amst.). , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 56
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedures and some applications
    • Towbin, M., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedures and some applications. Proc. Natl. Acad. Sci. USA. 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA. , vol.76 , pp. 4350-4354
    • Towbin, M.1    Staehelin, T.2    Gordon, J.3
  • 58
    • 0021247689 scopus 로고
    • The structural basis of ankyrin function. I. Identification of two structural domains
    • Weaver, D.C., and V.T. Marchesi. 1984. The structural basis of ankyrin function. I. Identification of two structural domains. J. Biol. Chem. 259:6165-6169.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6165-6169
    • Weaver, D.C.1    Marchesi, V.T.2
  • 59
    • 0021274123 scopus 로고
    • The structural basis of ankyrin function II. Identification of Iwo functional domains
    • Weaver, D.C., G.R. Pasternack, and V.T. Marchesi. 1984. The structural basis of ankyrin function II. Identification of Iwo 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
  • 60
    • 0028875216 scopus 로고
    • Cytoplasmic coat proteins involved in endosome function
    • Whitney, J.A., M. Gomez., D. Sheff, T.E. Kreis, and I. Mellman. 1995. Cytoplasmic coat proteins involved in endosome function. Cell. 83:703-713.
    • (1995) Cell. , vol.83 , pp. 703-713
    • Whitney, J.A.1    Gomez, M.2    Sheff, D.3    Kreis, T.E.4    Mellman, I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.