메뉴 건너뛰기




Volumn 137, Issue 6, 1997, Pages 1355-1367

Amphiphysin II (SH3p9; BIN1), a member of the amphiphysin/Rvs family, is concentrated in the cortical cytomatrix of axon initial segments and nodes of ranvier in brain and around T tubules in skeletal muscle

Author keywords

[No Author keywords available]

Indexed keywords

BRAIN PROTEIN; MUSCLE PROTEIN;

EID: 0030905586     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.137.6.1355     Document Type: Article
Times cited : (227)

References (64)
  • 1
    • 0028928199 scopus 로고
    • Defining protein interactions with yeast actin in vivo
    • Amberg, D.C., E. Basart, and D. Botstein. 1995. Defining protein interactions with yeast actin in vivo. Nat. Struct. Biol. 2:28-35.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 28-35
    • Amberg, D.C.1    Basart, E.2    Botstein, D.3
  • 2
    • 0027219273 scopus 로고
    • Alteration of a yeast SH3 protein leads to conditional viability with defects in cytoskeletal and budding patterns
    • Bauer, F., M. Urdaci, M. Aigle, and M. Crouzet. 1993. Alteration of a yeast SH3 protein leads to conditional viability with defects in cytoskeletal and budding patterns. Mol. Cell. Biol. 13:5070-5084.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5070-5084
    • Bauer, F.1    Urdaci, M.2    Aigle, M.3    Crouzet, M.4
  • 3
    • 0028275807 scopus 로고
    • Identification of Hox genes in newborn lung and effects of gestational age and retinoic acid on their expression
    • Bogue, C.W., I. Gross, H. Vasavada, D.W. Dynia, C.M. Wilson, and H.D. Jacobs. 1994. Identification of Hox genes in newborn lung and effects of gestational age and retinoic acid on their expression. Am. J. Physiol. 266:L448-454.
    • (1994) Am. J. Physiol. , vol.266
    • Bogue, C.W.1    Gross, I.2    Vasavada, H.3    Dynia, D.W.4    Wilson, C.M.5    Jacobs, H.D.6
  • 4
    • 0022369827 scopus 로고
    • Clathrin structure characterized with monoclonal antibodies. I. Analysis of multiple antigenic sites
    • Brodsky, F.M. 1985. Clathrin structure characterized with monoclonal antibodies. I. Analysis of multiple antigenic sites. J. Cell Biol. 101:2047-2054.
    • (1985) J. Cell Biol. , vol.101 , pp. 2047-2054
    • Brodsky, F.M.1
  • 5
    • 0014377043 scopus 로고
    • Ultrastructural analysis of individual layers in the lateral geniculate body of the monkey
    • Campos-Ortega, J.A., P. Glees, and V. Neuhoff. 1968. Ultrastructural analysis of individual layers in the lateral geniculate body of the monkey. Z. Zellforsch. Mikrosk. Anat. 87:82-100.
    • (1968) Z. Zellforsch. Mikrosk. Anat. , vol.87 , pp. 82-100
    • Campos-Ortega, J.A.1    Glees, P.2    Neuhoff, V.3
  • 6
    • 0023879477 scopus 로고
    • Characterization of the proteins purified with monoclonal antibodies to glutamic acid decarboxylase
    • Chang, Y.C., and D.I. Gottlieb. 1988. Characterization of the proteins purified with monoclonal antibodies to glutamic acid decarboxylase. J. Neurosci. 8: 2123-2130.
    • (1988) J. Neurosci. , vol.8 , pp. 2123-2130
    • Chang, Y.C.1    Gottlieb, D.I.2
  • 7
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen, C., and H. Okayama. 1987. High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7:2745-2752.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 8
    • 0014651488 scopus 로고
    • Observations on the ultrastructure of the axon hillock and initial axon segment of lumbosacral motoneurons in the cat
    • Conradi, S. 1969. Observations on the ultrastructure of the axon hillock and initial axon segment of lumbosacral motoneurons in the cat. Acta. Physiol. Scand. Suppl. 332:65-84.
    • (1969) Acta. Physiol. Scand. Suppl. , vol.332 , pp. 65-84
    • Conradi, S.1
  • 9
    • 0025989149 scopus 로고
    • Yeast mutant affected for viability upon nutrient starvation: Characterization and cloning of the RVS161 gene
    • Crouzet, M., M. Urdaci, L. Dulau, and M. Aigle. 1991. Yeast mutant affected for viability upon nutrient starvation: characterization and cloning of the RVS161 gene. Yeast. 7:727-743.
    • (1991) Yeast , vol.7 , pp. 727-743
    • Crouzet, M.1    Urdaci, M.2    Dulau, L.3    Aigle, M.4
  • 10
    • 0028169904 scopus 로고
    • Autoimmunity in stiff-Man syndrome with breast cancer is targeted to the C-terminal region of human amphiphysin, a protein similar to the yeast proteins, Rvs167 and Rvs161
    • David, C., M. Solimena, and P. De Camilli. 1994. Autoimmunity in stiff-Man syndrome with breast cancer is targeted to the C-terminal region of human amphiphysin, a protein similar to the yeast proteins, Rvs167 and Rvs161. FEBS (Fed. Eur. Biochem. Soc.) Letts. 351:73-79.
    • (1994) FEBS (Fed. Eur. Biochem. Soc.) Letts. , vol.351 , pp. 73-79
    • David, C.1    Solimena, M.2    De Camilli, P.3
  • 11
    • 0030060326 scopus 로고    scopus 로고
    • A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals
    • David, C., P.S. McPherson, O. Mundigl, and P. De Camilli. 1996. A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals. Proc. Natl. Acad. Sci. USA. 93:331-335.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 331-335
    • David, C.1    McPherson, P.S.2    Mundigl, O.3    De Camilli, P.4
  • 12
    • 0020961646 scopus 로고
    • Synapsin I (protein I), a nerve terminal-specific phosphoprotein. I. Its general distribution in synapses of the central and peripheral nervous system demonstrated by immunofluorescence in frozen and plastic sections
    • De Camilli, P., R. Cameron, and P. Greengard. 1983. Synapsin I (protein I), a nerve terminal-specific phosphoprotein. I. Its general distribution in synapses of the central and peripheral nervous system demonstrated by immunofluorescence in frozen and plastic sections. J. Cell Biol. 96:1337-1354.
    • (1983) J. Cell Biol. , vol.96 , pp. 1337-1354
    • De Camilli, P.1    Cameron, R.2    Greengard, P.3
  • 13
    • 0021270292 scopus 로고
    • Distribution of microtubule-associated protein 2 in the nervous system of the rat studied by immunofluorescence
    • De Camilli, P., P.E. Miller, F. Navone, W.E. Theurkauf, and R.B. Vallee. 1984. Distribution of microtubule-associated protein 2 in the nervous system of the rat studied by immunofluorescence. Neuroscience. 11:817-846.
    • (1984) Neuroscience , vol.11 , pp. 817-846
    • De Camilli, P.1    Miller, P.E.2    Navone, F.3    Theurkauf, W.E.4    Vallee, R.B.5
  • 15
    • 0029898290 scopus 로고    scopus 로고
    • Identification of a small cytoplasmic ankyrin (AnkG119) in the kidney and muscle that binds β Ι σ spectrin and associates with the Golgi apparatus
    • Devarajan, P., P.R. Stabach, A.S. Mann, T. Ardito, M. Kashgarian, and J.S. Morrow. 1996. Identification of a small cytoplasmic ankyrin (AnkG119) in the kidney and muscle that binds β Ι σ spectrin and associates with the Golgi apparatus. J. Cell Biol. 133:819-830.
    • (1996) J. Cell Biol. , vol.133 , pp. 819-830
    • Devarajan, P.1    Stabach, P.R.2    Mann, A.S.3    Ardito, T.4    Kashgarian, M.5    Morrow, J.S.6
  • 16
    • 0025161331 scopus 로고
    • Localization of the α1 and α2 subunits of the dihydropyridine receptor and ankyrin in skeletal muscle triads
    • Flucher, B.E., M.E. Morton, S.C. Froehner, and M.P. Daniels. 1990. Localization of the α1 and α2 subunits of the dihydropyridine receptor and ankyrin in skeletal muscle triads. Neuron. 5:339-351.
    • (1990) Neuron. , vol.5 , pp. 339-351
    • Flucher, B.E.1    Morton, M.E.2    Froehner, S.C.3    Daniels, M.P.4
  • 18
    • 0029832206 scopus 로고    scopus 로고
    • The carboxyl terminus of GLUT4 contains a serine-leucine-leucine sequence that functions as a potent internalization motif in Chinese hamster ovary cells
    • Garippa, R.J., A. Johnson, J. Park, R.L. Petrush, and T.E. McGraw. 1996. The carboxyl terminus of GLUT4 contains a serine-leucine-leucine sequence that functions as a potent internalization motif in Chinese hamster ovary cells. J. Biol. Chem. 271:20660-20668.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20660-20668
    • Garippa, R.J.1    Johnson, A.2    Park, J.3    Petrush, R.L.4    McGraw, T.E.5
  • 20
    • 0029744106 scopus 로고    scopus 로고
    • The junction-assodated protein, zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cell-cell contacts
    • Gottardi, C.J., M. Arpin, A.S. Fanning, and D. Louvard. 1996. The junction-assodated protein, zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cell-cell contacts. Proc. Natl. Acad. Sci. USA. 93:10779-10784.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10779-10784
    • Gottardi, C.J.1    Arpin, M.2    Fanning, A.S.3    Louvard, D.4
  • 21
    • 0031000481 scopus 로고    scopus 로고
    • The SH3 domain of amphiphysin binds the proline rich domain of dynamin at a single site which defines a new SH3 binding consensus sequence
    • Grabs, D, V. Slepnev, Z. Songyang, C. David, M. Lynch, L.C. Cantley, and P. De Camilli. 1997. The SH3 domain of amphiphysin binds the proline rich domain of dynamin at a single site which defines a new SH3 binding consensus sequence. J. Biol. Chem. 272:13419-13425.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13419-13425
    • Grabs, D.1    Slepnev, V.2    Songyang, Z.3    David, C.4    Lynch, M.5    Cantley, L.C.6    De Camilli, P.7
  • 22
    • 0028051807 scopus 로고
    • Characterization and ultrastructural localization of a novel 90-kDa protein unique to skeletal muscle junctional sarcoplasmic reticulum
    • Guo, W., A.O. Jorgensen, and K.P. Campbell. 1994. Characterization and ultrastructural localization of a novel 90-kDa protein unique to skeletal muscle junctional sarcoplasmic reticulum. J. Biol. Chem. 269:28359-28365.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28359-28365
    • Guo, W.1    Jorgensen, A.O.2    Campbell, K.P.3
  • 23
    • 0028978034 scopus 로고
    • Chromosomal localization of the ankyrinG gene (ANK3/ Ank3) to human 10q21 and mouse 10
    • Kapfhamer, D., D.E. Miller, S. Lambert, V. Bennett, T.W. Glover, and M. Burmeister. 1995. Chromosomal localization of the ankyrinG gene (ANK3/ Ank3) to human 10q21 and mouse 10. Genomics. 27:189-191.
    • (1995) Genomics , vol.27 , pp. 189-191
    • Kapfhamer, D.1    Miller, D.E.2    Lambert, S.3    Bennett, V.4    Glover, T.W.5    Burmeister, M.6
  • 24
    • 0014041872 scopus 로고
    • Three-dimensional studies of neurons in the lateral geniculate nucleus of the rat. III. Specialized neuronal contacts in the neuropile
    • Karlsson, U.L. 1967. Three-dimensional studies of neurons in the lateral geniculate nucleus of the rat. III. Specialized neuronal contacts in the neuropile. J. Utrastruct. Res. 17:137-157.
    • (1967) J. Utrastruct. Res. , vol.17 , pp. 137-157
    • Karlsson, U.L.1
  • 25
    • 0025614726 scopus 로고
    • Localization of anti-clathrin antibody in the sarcomere and sensitivity of myofibril structure to chloroquine suggest a role for clathrin in myofibril assembly
    • Kaufman, S.J., D. Bielser, and R.F. Foster. 1990. Localization of anti-clathrin antibody in the sarcomere and sensitivity of myofibril structure to chloroquine suggest a role for clathrin in myofibril assembly. Exp. Cell Res. 191: 227-238.
    • (1990) Exp. Cell Res. , vol.191 , pp. 227-238
    • Kaufman, S.J.1    Bielser, D.2    Foster, R.F.3
  • 26
    • 0029971383 scopus 로고    scopus 로고
    • Characterization of a second human clathrin heavy chain polypeptide gene (CLH-22) from chromosome 22q11
    • Kedra, C., M. Peyrard, I. Fransson, J.E. Collins, I. Dunham, B.A. Roe, and J.P. Dumanski. 1996. Characterization of a second human clathrin heavy chain polypeptide gene (CLH-22) from chromosome 22q11. Hum. Mol. Genet. 5: 625-631.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 625-631
    • Kedra, C.1    Peyrard, M.2    Fransson, I.3    Collins, J.E.4    Dunham, I.5    Roe, B.A.6    Dumanski, J.P.7
  • 27
    • 0021225796 scopus 로고
    • An improved procedure for immunoelectron microscopy: Ultrathin plastic embedding of immunolabeled ultrathin frozen sections
    • Keller, G.A., K.T. Tokuyasu, A.H. Dutton, and S.J. Singer. 1984. An improved procedure for immunoelectron microscopy: ultrathin plastic embedding of immunolabeled ultrathin frozen sections. Proc. Natl. Acad. Sci. USA. 81: 5744-5747.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 5744-5747
    • Keller, G.A.1    Tokuyasu, K.T.2    Dutton, A.H.3    Singer, S.J.4
  • 28
    • 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
  • 29
    • 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
  • 30
    • 0020603664 scopus 로고
    • Possible temperature-dependent blockage of synaptic vesicle recycling induced by a single gene mutation in Drosophila
    • Kosaka, T., and K. Ikeda. 1983. 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
  • 31
    • 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
  • 32
    • 0018726948 scopus 로고
    • Ouabain binding and coupling sodium, potassium and chloride transport in isolated transverse tubules from skeletal muscle
    • Lau, H.Y., A.H. Caswell, H. Garcia, and L. Letelier. 1979. Ouabain binding and coupling sodium, potassium and chloride transport in isolated transverse tubules from skeletal muscle. J. Gen. Physiol. 74:335-349.
    • (1979) J. Gen. Physiol. , vol.74 , pp. 335-349
    • Lau, H.Y.1    Caswell, A.H.2    Garcia, H.3    Letelier, L.4
  • 34
    • 0029968116 scopus 로고    scopus 로고
    • A transcription map in the CATCH22 critical region: Identification, mapping, and ordering of four novel transcripts expressed in heart
    • Lindsay, E.A., P. Rizzu, R. Antonacci, V. Jurecic, J. Delmas-Mata, C.C. Lee, U.J. Kim, P.J. Scambler, and A. Baldini. 1996. A transcription map in the CATCH22 critical region: identification, mapping, and ordering of four novel transcripts expressed in heart. Genomics. 32:104-112.
    • (1996) Genomics , vol.32 , pp. 104-112
    • Lindsay, E.A.1    Rizzu, P.2    Antonacci, R.3    Jurecic, V.4    Delmas-Mata, J.5    Lee, C.C.6    Kim, U.J.7    Scambler, P.J.8    Baldini, A.9
  • 35
    • 0030004228 scopus 로고    scopus 로고
    • Prediction and analysis of coiled-coil structures
    • Lupas, A. 1996. Prediction and analysis of coiled-coil structures. Methods Enzymol. 266:513-525.
    • (1996) Methods Enzymol. , vol.266 , pp. 513-525
    • Lupas, A.1
  • 36
    • 0028073746 scopus 로고
    • p145, a major Grb2-binding protein in brain, is co-localized with dynamin in nerve terminals where it undergoes activity-dependent dephosphorylation
    • McPherson, P.S., K. Takei, S.L. Schmid, and P. De Camilli. 1994. p145, a major Grb2-binding protein in brain, is co-localized with dynamin in nerve terminals where it undergoes activity-dependent dephosphorylation. J. Biol. Chem. 269:30132-30139.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30132-30139
    • McPherson, P.S.1    Takei, K.2    Schmid, S.L.3    De Camilli, P.4
  • 38
    • 0000026363 scopus 로고
    • An atlas of the distribution of GABAnergic neurons and terminals in the rat CNS as revealed by GAD immunocytochemistry
    • A. Bjorklund and T. Hokfelt, editors. Elsevier Science Publishers, Amsterdam, The Netherlands
    • Mugnaini, E., and W.H. Oertel. 1985. An atlas of the distribution of GABAnergic neurons and terminals in the rat CNS as revealed by GAD immunocytochemistry. In Handbook of Chemical Neuroanatomy. Vol 4: GABA and Neuropeptides in the CNS. A. Bjorklund and T. Hokfelt, editors. Elsevier Science Publishers, Amsterdam, The Netherlands. 436-608.
    • (1985) Handbook of Chemical Neuroanatomy. Vol 4: GABA and Neuropeptides in the CNS , vol.4 , pp. 436-608
    • Mugnaini, E.1    Oertel, W.H.2
  • 39
    • 0027997975 scopus 로고
    • Endocytosis is required for the growth of vacuolar H(+)-ATPase-defective yeast: Identification of six new END genes
    • Munn, A.L., and H. Riezman. 1994. Endocytosis is required for the growth of vacuolar H(+)-ATPase-defective yeast: identification of six new END genes. J. Cell Biol. 127:373-386.
    • (1994) J. Cell Biol. , vol.127 , pp. 373-386
    • Munn, A.L.1    Riezman, H.2
  • 40
    • 0028856410 scopus 로고
    • end5, end6, and end7: Mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae
    • Munn, A.L., B.J. Stevenson, M.I. Geli, and H. Riezman. 1995. end5, end6, and end7: mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae. Mol. Biol. Cell. 6:1721-1742.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 1721-1742
    • Munn, A.L.1    Stevenson, B.J.2    Geli, M.I.3    Riezman, H.4
  • 41
    • 0029562270 scopus 로고
    • The T-tubule is a cell-surface target for insulin-regulated recycling of membrane proteins in skeletal muscle
    • Muñoz, P., M. Rosemblatt, X. Testar, M. Palacin, G. Thoidis, P.F. Pilch, and A. Zorzano. 1995a. The T-tubule is a cell-surface target for insulin-regulated recycling of membrane proteins in skeletal muscle. Biochem. J. 307:393-400.
    • (1995) Biochem. J. , vol.307 , pp. 393-400
    • Muñoz, P.1    Rosemblatt, M.2    Testar, X.3    Palacin, M.4    Thoidis, G.5    Pilch, P.F.6    Zorzano, A.7
  • 42
    • 0028903251 scopus 로고
    • Isolation and characterization of distinct domains of sarcolemma and T-tubules from rat skeletal muscle
    • Muñoz, P., M. Rosemblatt, X. Testar, M. Palacin, and A. Zorzano. 1995b. Isolation and characterization of distinct domains of sarcolemma and T-tubules from rat skeletal muscle. Biochem. J. 307:273-280.
    • (1995) Biochem. J. , vol.307 , pp. 273-280
    • Muñoz, P.1    Rosemblatt, M.2    Testar, X.3    Palacin, M.4    Zorzano, A.5
  • 43
    • 0023262074 scopus 로고
    • Ankyrin binding to Na+ + K+ATPase and implications for the organization of membrane domains in polarized cells
    • Nelson, W.J., and P.J. Veshnock. 1987. Ankyrin binding to (Na+ + K+(ATPase and implications for the organization of membrane domains in polarized cells. Nature (Lond.). 328:533-536.
    • (1987) Nature (Lond.) , vol.328 , pp. 533-536
    • Nelson, W.J.1    Veshnock, P.J.2
  • 45
    • 0344081527 scopus 로고
    • The axon
    • A. Peters, S.L. Palay, and H. Webster, editors. Oxford University Press, New York
    • Peters, A., S. Palay, and H. Webster. 1991. The axon. In The Fine Structure of the Nervous System. A. Peters, S.L. Palay, and H. Webster, editors. Oxford University Press, New York. 101-137.
    • (1991) The Fine Structure of the Nervous System , pp. 101-137
    • Peters, A.1    Palay, S.2    Webster, H.3
  • 46
    • 0026748769 scopus 로고    scopus 로고
    • Translocation of the glucose transporter (GLUT4) to the cell surface in permeabilized 3T3-L1 adipocytes: Effects of ATP, insulin, and GTP gamma S and localization of GLUT4 to clathrin lattices
    • Robinson, L.J., S. Pang, D.S. Harris, J. Heuser, and D.E. James. 1996. Translocation of the glucose transporter (GLUT4) to the cell surface in permeabilized 3T3-L1 adipocytes: effects of ATP, insulin, and GTP gamma S and localization of GLUT4 to clathrin lattices. J. Cell Biol. 117:1181-1196.
    • (1996) J. Cell Biol. , vol.117 , pp. 1181-1196
    • Robinson, L.J.1    Pang, S.2    Harris, D.S.3    Heuser, J.4    James, D.E.5
  • 48
    • 0029741917 scopus 로고    scopus 로고
    • BIN1 is a novel MYC-interacting protein with features of a tumour suppressor
    • Sakamuro, D., K.J. Elliott, R. Wechsler-Reya, and G.C. Prendergast. 1996. BIN1 is a novel MYC-interacting protein with features of a tumour suppressor. Nat. Gen. 14:69-76.
    • (1996) Nat. Gen. , vol.14 , pp. 69-76
    • Sakamuro, D.1    Elliott, K.J.2    Wechsler-Reya, R.3    Prendergast, G.C.4
  • 49
    • 0026018293 scopus 로고
    • Immunolocalization studies of putative guidance molecules used by axons and growth cones of intersegemental interneurons in the chick embryo spinal cord
    • Shiga, T., and M.W. Oppenheim. 1991. Immunolocalization studies of putative guidance molecules used by axons and growth cones of intersegemental interneurons in the chick embryo spinal cord. J. Comp. Neurol. 310:234-252.
    • (1991) J. Comp. Neurol. , vol.310 , pp. 234-252
    • Shiga, T.1    Oppenheim, M.W.2
  • 50
    • 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
  • 53
    • 0028910268 scopus 로고
    • Actin cytoskeleton and budding pattern are altered in the yeast rvs161 mutant: The Rvs161 protein shares common domains with the brain protein amphiphysin
    • Sivadon, P., F. Bauer, M. Aigle, and M. Crouzet. 1995. Actin cytoskeleton and budding pattern are altered in the yeast rvs161 mutant: The Rvs161 protein shares common domains with the brain protein amphiphysin. Mol. Gen. Genet. 246:485-495.
    • (1995) Mol. Gen. Genet. , vol.246 , pp. 485-495
    • Sivadon, P.1    Bauer, F.2    Aigle, M.3    Crouzet, M.4
  • 55
    • 0029890281 scopus 로고    scopus 로고
    • Cloning of ligand targets: Systemic isolation of SH3 domain-containing proteins
    • Sparks, A.B., N.G. Hoffman, S.J. McConnell, D.M. Fowlkes, and B.K. Kay. 1996. Cloning of ligand targets: systemic isolation of SH3 domain-containing proteins. Nat. Biotechnol. 14:741-744.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 741-744
    • Sparks, A.B.1    Hoffman, N.G.2    McConnell, S.J.3    Fowlkes, D.M.4    Kay, B.K.5
  • 56
    • 0023948543 scopus 로고
    • Ankyrin and spectrin associate with voltage-dependent sodium channels in brain
    • Srinivasan, Y., L. Elmer, J. Davis. V. Bennett, and K. Angelides. 1988. Ankyrin and spectrin associate with voltage-dependent sodium channels in brain. Nature (Lond.). 333:177-180.
    • (1988) Nature (Lond.) , vol.333 , pp. 177-180
    • Srinivasan, Y.1    Elmer, L.2    Davis, J.3    Bennett, V.4    Angelides, K.5
  • 57
    • 0028923349 scopus 로고
    • Tubular membrane invaginations coated by dynamin rings are induced by GTP-γ S 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-γ S in nerve terminals. Nature (Lond.). 374:186-190.
    • (1995) Nature (Lond.) , vol.374 , pp. 186-190
    • Takei, K.1    McPherson, P.S.2    Schmid, S.L.3    De Camilli, P.4
  • 58
    • 0024318954 scopus 로고
    • Use of poly(vinylpyrrolidone) and poly(vinyl alcohol) for cryoultramicrotomy
    • Tokuyasu, K.T. 1989. Use of poly(vinylpyrrolidone) and poly(vinyl alcohol) for cryoultramicrotomy. Histochem. J. 21:163-171.
    • (1989) Histochem. J. , vol.21 , pp. 163-171
    • Tokuyasu, K.T.1
  • 59
    • 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. Natl. Acad. Sci. USA. 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 60
    • 0027380638 scopus 로고
    • Submembranous junctional plaque proteins include potential tumor suppressor molecules
    • Tsukita, S., M. Itoh, A. Nagafuchi, S. Yonemura, and S. Tsukita. 1993. Submembranous junctional plaque proteins include potential tumor suppressor molecules. J. Cell Biol. 123:1049-1053.
    • (1993) J. Cell Biol. , vol.123 , pp. 1049-1053
    • Tsukita, S.1    Itoh, M.2    Nagafuchi, A.3    Yonemura, S.4    Tsukita, S.5
  • 61
    • 0028986797 scopus 로고
    • The appendage domain of α-adaptin is a high affinity binding site for dynamin
    • Wang, L.H., T.C. Südhof, and R.G.W. Anderson. 1995. The appendage domain of α-adaptin is a high affinity binding site for dynamin. J. Biol. Chem. 270: 10079-10083.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10079-10083
    • Wang, L.H.1    Südhof, T.C.2    Anderson, R.G.W.3
  • 62
    • 0029862135 scopus 로고    scopus 로고
    • Insulin unmasks a COOH-terminal glut4 epitope and increases glucose transport across T-tubules in skeletal muscle
    • Wang, W., P.A. Hansen, B.A. Marshall, J.O. Holloszy, and M. Mueckler. 1996. Insulin unmasks a COOH-terminal glut4 epitope and increases glucose transport across T-tubules in skeletal muscle. J. Cell Biol. 135:415-430.
    • (1996) J. Cell Biol. , vol.135 , pp. 415-430
    • Wang, W.1    Hansen, P.A.2    Marshall, B.A.3    Holloszy, J.O.4    Mueckler, M.5
  • 63
    • 0017894289 scopus 로고
    • Intra-axonal ferric ion-ferrocyanaide staining of nodes of Ranvier and initial segments in central myelinated fibers
    • Waxman, S.G., and D.C. Quick. 1978. Intra-axonal ferric ion-ferrocyanaide staining of nodes of Ranvier and initial segments in central myelinated fibers. Brain Res. 144:1-10.
    • (1978) Brain Res. , vol.144 , pp. 1-10
    • Waxman, S.G.1    Quick, D.C.2
  • 64
    • 0027398432 scopus 로고
    • Molecular dissection of the myelinated axon
    • Waxman, S.G., and J.M. Ritchie. 1993. Molecular dissection of the myelinated axon. Ann. Neurol. 33:121-136.
    • (1993) Ann. Neurol. , vol.33 , pp. 121-136
    • Waxman, S.G.1    Ritchie, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.