메뉴 건너뛰기




Volumn 150, Issue 2, 2000, Pages 349-360

HIV-1 Rev depolymerizes microtubules to form stable bilayered rings

Author keywords

Acquired immunodeficiency syndrome; HIV 1 Rev; Kinesin; Microtubules; Tubulin

Indexed keywords

KINESIN; MAGNESIUM ION;

EID: 0034710249     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.150.2.349     Document Type: Article
Times cited : (43)

References (82)
  • 2
    • 0029039801 scopus 로고
    • Interaction of dolastatin 10 with tubulin: Induction of aggregation and hinding and dissociation reactions
    • Bai, R., G.F. Taylor, J.M. Schmidt, M.D. Williams, J.A. Kepler, G.R. Pettit, and E. Hamel. 1995. Interaction of dolastatin 10 with tubulin: induction of aggregation and hinding and dissociation reactions. Mol. Pharmacol. 47:965-976.
    • (1995) Mol. Pharmacol. , vol.47 , pp. 965-976
    • Bai, R.1    Taylor, G.F.2    Schmidt, J.M.3    Williams, M.D.4    Kepler, J.A.5    Pettit, G.R.6    Hamel, E.7
  • 3
    • 0029759374 scopus 로고    scopus 로고
    • Characterization of the interaction of cryptophycin 1 with tuhulin: Binding in the Vinca domain, competitive inhibition of dolastatin 10 binding, and an unusual aggregation reaction
    • Bai, R., R.E. Schwartz, J.A. Kepler, G.R. Pettit, and E. Hamel. 1996. Characterization of the interaction of cryptophycin 1 with tuhulin: binding in the Vinca domain, competitive inhibition of dolastatin 10 binding, and an unusual aggregation reaction. Cancer Res. 56:4398-4406.
    • (1996) Cancer Res. , vol.56 , pp. 4398-4406
    • Bai, R.1    Schwartz, R.E.2    Kepler, J.A.3    Pettit, G.R.4    Hamel, E.5
  • 4
    • 0033607202 scopus 로고    scopus 로고
    • Interactions of the sponge-derived antimitotic tripeptide hemiasterlin with tubulin: Comparison with dolastatin 10 and cryptophycin 1
    • Bai, R., N.A. Durso, D.L. Sackett, and E. Hamel. 1999. Interactions of the sponge-derived antimitotic tripeptide hemiasterlin with tubulin: comparison with dolastatin 10 and cryptophycin 1. Biochemistry. 38:14302-14310.
    • (1999) Biochemistry , vol.38 , pp. 14302-14310
    • Bai, R.1    Durso, N.A.2    Sackett, D.L.3    Hamel, E.4
  • 7
    • 0022385617 scopus 로고
    • Tubulin, hybrid dimers, and tubulin S. Stepwise charge reduction and polymerization
    • Bhattacharyya, B., D.L. Sackett, and J. Wolff. 1985. Tubulin, hybrid dimers, and tubulin S. Stepwise charge reduction and polymerization. J. Biol. Chem. 260:10208-10216.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10208-10216
    • Bhattacharyya, B.1    Sackett, D.L.2    Wolff, J.3
  • 8
    • 0032503245 scopus 로고    scopus 로고
    • Subcellular localization of human immunodeficiency virus type 1 RNAs, Rev. And the splicing factor SC-35
    • Bøe, S.O., B. Bjorndal, B. Røsok, A.M. Szilvay, and K.H. Kalland. 1998. Subcellular localization of human immunodeficiency virus type 1 RNAs, Rev. and the splicing factor SC-35. Virology. 244:473-482.
    • (1998) Virology , vol.244 , pp. 473-482
    • Bøe, S.O.1    Bjorndal, B.2    Røsok, B.3    Szilvay, A.M.4    Kalland, K.H.5
  • 9
    • 0029149833 scopus 로고
    • Identification of a novel cellular co-factor for the Rev/Rex class of retroviral proteins
    • Bogerd, H.P., R.A. Fridell, S. Madore, and B.R. Cullen. 1995. Identification of a novel cellular co-factor for the Rev/Rex class of retroviral proteins. Cell. 82:485-494.
    • (1995) Cell , vol.82 , pp. 485-494
    • Bogerd, H.P.1    Fridell, R.A.2    Madore, S.3    Cullen, B.R.4
  • 10
    • 0030040630 scopus 로고    scopus 로고
    • The capsid architecture of channel catfish virus, an evolutionarily distant herpesvirus, is largely conserved in the absence of discernible sequence homology with herpes simplex virus
    • Booy, P.P., B.L. Trus, A.J. Davison, and A.C. Steven. 1996. The capsid architecture of channel catfish virus, an evolutionarily distant herpesvirus, is largely conserved in the absence of discernible sequence homology with herpes simplex virus. Virology. 215:134-141.
    • (1996) Virology , vol.215 , pp. 134-141
    • Booy, P.P.1    Trus, B.L.2    Davison, A.J.3    Steven, A.C.4
  • 12
    • 0039415382 scopus 로고    scopus 로고
    • Regulation of the export of RNA from the nucleus
    • Cole, C.N., and C. Saavedra. 1997. Regulation of the export of RNA from the nucleus. Semin. Cell Dev. Biol. 8:71-78.
    • (1997) Semin. Cell Dev. Biol. , vol.8 , pp. 71-78
    • Cole, C.N.1    Saavedra, C.2
  • 14
    • 0031954906 scopus 로고    scopus 로고
    • Posttranscriptional regulation by the HIV-1 Rev protein
    • Cullen, B.R. 1998. Posttranscriptional regulation by the HIV-1 Rev protein. Semin. Virol. 8:327-334.
    • (1998) Semin. Virol. , vol.8 , pp. 327-334
    • Cullen, B.R.1
  • 15
    • 0027453986 scopus 로고
    • Biochemical characterization of binding of multiple HIV-1 Rev monomeric proteins to the Rev response element
    • Daly, T.J., R.C. Doten, P. Rennert, M. Auer, H. Jaksche, A. Donner, G. Fisk, and J.R. Rusche. 1993. Biochemical characterization of binding of multiple HIV-1 Rev monomeric proteins to the Rev response element. Biochemistry. 32:10497-10505.
    • (1993) Biochemistry , vol.32 , pp. 10497-10505
    • Daly, T.J.1    Doten, R.C.2    Rennert, P.3    Auer, M.4    Jaksche, H.5    Donner, A.6    Fisk, G.7    Rusche, J.R.8
  • 16
    • 0031585529 scopus 로고    scopus 로고
    • Direct effect of type 1 human immunodeficiency virus (HIV-I) on intestinal epithelial cell differentiation: Relationship to HIV-I enteropathy
    • Delezay, O., N. Yahi, C. Tamalet, S. Baghdiguian, J.A. Boudier, and J. Fantini. 1997. Direct effect of type 1 human immunodeficiency virus (HIV-I) on intestinal epithelial cell differentiation: relationship to HIV-I enteropathy. Virology. 238:231-242.
    • (1997) Virology , vol.238 , pp. 231-242
    • Delezay, O.1    Yahi, N.2    Tamalet, C.3    Baghdiguian, S.4    Boudier, J.A.5    Fantini, J.6
  • 17
    • 0033534575 scopus 로고    scopus 로고
    • Kin 1 kinesins are microtubule-destabilizing enzymes
    • Desai, A., S. Verma, T. Mitchison, and C.E. Walczak. 1999. Kin 1 kinesins are microtubule-destabilizing enzymes. Cell. 96:69-78.
    • (1999) Cell , vol.96 , pp. 69-78
    • Desai, A.1    Verma, S.2    Mitchison, T.3    Walczak, C.E.4
  • 18
    • 0028291130 scopus 로고
    • Solution structure of GDP-tubulin double rings to 3 nm resolution and comparison with microtubules
    • Diaz, J.F., E. Pantos, J. Bordas, and J.M. Andreu. 1994. Solution structure of GDP-tubulin double rings to 3 nm resolution and comparison with microtubules. J. Mol. Biol. 238:214-223.
    • (1994) J. Mol. Biol. , vol.238 , pp. 214-223
    • Diaz, J.F.1    Pantos, E.2    Bordas, J.3    Andreu, J.M.4
  • 20
    • 0030852135 scopus 로고    scopus 로고
    • Association of human immunodeficiency virus Nef protein with actin is myristoylation dependent and influences its subcellular localization
    • Fackler, O.T., N. Kienzle, E. Kremmer, A. Boese, B. Schramm, T. Klimkait, C. Kucherer, and N. Mueller-Lantzsch. 1997. Association of human immunodeficiency virus Nef protein with actin is myristoylation dependent and influences its subcellular localization. Eur. J. Biochem. 247:843-851.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 843-851
    • Fackler, O.T.1    Kienzle, N.2    Kremmer, E.3    Boese, A.4    Schramm, B.5    Klimkait, T.6    Kucherer, C.7    Mueller-Lantzsch, N.8
  • 21
    • 0033546316 scopus 로고    scopus 로고
    • A new nucleoporin-like protein interacts with both HIV-1 Rev nuclear export signal and CRM-1
    • Farjot, G., A. Sergeant, and I. Mikaelian. 1999. A new nucleoporin-like protein interacts with both HIV-1 Rev nuclear export signal and CRM-1. J. Biol. Chem. 274:17309-17317.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17309-17317
    • Farjot, G.1    Sergeant, A.2    Mikaelian, I.3
  • 22
    • 0029130169 scopus 로고
    • The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs
    • Fisher, U., J. Huber, W.C. Boelens, I.W. Mattaj, and R. Lührman. 1995. The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell. 82:475-483.
    • (1995) Cell , vol.82 , pp. 475-483
    • Fisher, U.1    Huber, J.2    Boelens, W.C.3    Mattaj, I.W.4    Lührman, R.5
  • 23
    • 0030836217 scopus 로고    scopus 로고
    • Site-specific phosphorylation of the human immunodeficiency virus type-1 Rev protein accelerates formation of an efficient RNA-binding conformation
    • Fouls, D.E., H.L. True, K.A. Cengel, and D.W. Celander. 1997. Site-specific phosphorylation of the human immunodeficiency virus type-1 Rev protein accelerates formation of an efficient RNA-binding conformation. Biochemistry. 36:13256-13262.
    • (1997) Biochemistry , vol.36 , pp. 13256-13262
    • Fouls, D.E.1    True, H.L.2    Cengel, K.A.3    Celander, D.W.4
  • 25
    • 0016792383 scopus 로고
    • Magnesium-induced self-association of calf brain tubulin. I. Stoichiometry
    • Frigon, R.P., and S.N. Timasheff. 1975. Magnesium-induced self-association of calf brain tubulin. I. Stoichiometry. Biochemistry. 14:4559-4566.
    • (1975) Biochemistry , vol.14 , pp. 4559-4566
    • Frigon, R.P.1    Timasheff, S.N.2
  • 26
    • 0030198504 scopus 로고    scopus 로고
    • HIV Rev uses a conserved cellular protein export pathway for the nucleocytoplasmic transport of viral RNAs
    • Fritz, C.C., and M.R. Green. 1996. HIV Rev uses a conserved cellular protein export pathway for the nucleocytoplasmic transport of viral RNAs. Curr. Biol. 6:848-854.
    • (1996) Curr. Biol. , vol.6 , pp. 848-854
    • Fritz, C.C.1    Green, M.R.2
  • 28
    • 0023442001 scopus 로고
    • Microtubule assembly in cytoplasmic extracts of Xenopus oocytes and eggs
    • Gard, D.L., and M.W. Kirschner. 1987. Microtubule assembly in cytoplasmic extracts of Xenopus oocytes and eggs. J. Cell Biol 105:2191-2201.
    • (1987) J. Cell Biol , vol.105 , pp. 2191-2201
    • Gard, D.L.1    Kirschner, M.W.2
  • 29
    • 0031009808 scopus 로고    scopus 로고
    • Small heat shock protein suppression of Vpr-induced cytoskeletal defects in budding yeast
    • Gu, J.R., M. Emerman, and S. Sandmeyer. 1997. Small heat shock protein suppression of Vpr-induced cytoskeletal defects in budding yeast. Mol. Cell Biol. 17:4033-4042.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 4033-4042
    • Gu, J.R.1    Emerman, M.2    Sandmeyer, S.3
  • 30
    • 0002233957 scopus 로고
    • Regulation of retroviral RNA export
    • Hammarskjold, M.L. 1977. Regulation of retroviral RNA export. Semin. Cell Dev. Biol. 8:83-90.
    • (1977) Semin. Cell Dev. Biol. , vol.8 , pp. 83-90
    • Hammarskjold, M.L.1
  • 31
    • 0033595814 scopus 로고    scopus 로고
    • Microtubule disassembly by ATP-dependent oligomerization of the AAA enzyme katanin
    • Hartman, J.J., and R.D. Vale. 1999. Microtubule disassembly by ATP-dependent oligomerization of the AAA enzyme katanin. Science. 286:782-785.
    • (1999) Science , vol.286 , pp. 782-785
    • Hartman, J.J.1    Vale, R.D.2
  • 32
    • 0025882673 scopus 로고
    • Human immunodeficiency virus type 1 regulator of virion expression. Rev, forms nucleo-protein filaments after binding to a purine-rich "bubble" located within the revresponse region of viral RNA
    • Heaphy, S., J.T. Finch, M.J. Gait, J. Karn, and M. Singh. 1991. Human immunodeficiency virus type 1 regulator of virion expression. Rev, forms nucleo-protein filaments after binding to a purine-rich "bubble" located within the revresponse region of viral RNA. Proc. Natl. Acad. Sci. USA. 88:7366-7370.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7366-7370
    • Heaphy, S.1    Finch, J.T.2    Gait, M.J.3    Karn, J.4    Singh, M.5
  • 33
    • 0031578895 scopus 로고    scopus 로고
    • Interactions between HIV Rev and nuclear import and export factors: The Rev nuclear localisation signal mediates specific binding to human importin-beta
    • Henderson, B.R., and P. Percipalle. 1997. Interactions between HIV Rev and nuclear import and export factors: the Rev nuclear localisation signal mediates specific binding to human importin-beta. J. Mol. Biol. 274:693-707.
    • (1997) J. Mol. Biol. , vol.274 , pp. 693-707
    • Henderson, B.R.1    Percipalle, P.2
  • 34
    • 0032923913 scopus 로고    scopus 로고
    • Dissociation of the tubulin-sequestering and microtubule catastrophe-promoting activities of oncoprotein 18/stathmin
    • Howell, B., N. Larsson, M. Gullberg, and L. Cassimeris. 1999. Dissociation of the tubulin-sequestering and microtubule catastrophe-promoting activities of oncoprotein 18/stathmin. Mol. Biol. Cell. 10:105-118.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 105-118
    • Howell, B.1    Larsson, N.2    Gullberg, M.3    Cassimeris, L.4
  • 35
    • 0031954020 scopus 로고    scopus 로고
    • Transport of macromolecules between the nucleus and the cytoplasm
    • Izaurralde, E., and S. Adam. 1998. Transport of macromolecules between the nucleus and the cytoplasm. RNA. 4:351-364.
    • (1998) RNA , vol.4 , pp. 351-364
    • Izaurralde, E.1    Adam, S.2
  • 36
    • 0027973040 scopus 로고
    • The human immunodeficiency virus type I Rev protein shuttles between the cytoplasm and nuclear compartments
    • Kalland, K.H., A.M. Szilvay, K.A. Brokstad, W. Sætrevik, and G. Haukenes. 1994. The human immunodeficiency virus type I Rev protein shuttles between the cytoplasm and nuclear compartments. Mol. Cell Biol. 14:7436-7444.
    • (1994) Mol. Cell Biol. , vol.14 , pp. 7436-7444
    • Kalland, K.H.1    Szilvay, A.M.2    Brokstad, K.A.3    Sætrevik, W.4    Haukenes, G.5
  • 37
    • 0028018287 scopus 로고
    • Cellular-distribution of HIV type-1 Nef protein: Identification of domains in Nef required for association with membrane and detergent-insoluble cellular matrix
    • Kaminchik, J., R. Margalit, S. Yaish, H. Drummer, B. Amit, N. Sarver, M. Gorecki, and A. Panel. 1994. Cellular-distribution of HIV type-1 Nef protein: identification of domains in Nef required for association with membrane and detergent-insoluble cellular matrix. AIDS Res. Hum. Retroviruses. 10:1003-1010.
    • (1994) AIDS Res. Hum. Retroviruses , vol.10 , pp. 1003-1010
    • Kaminchik, J.1    Margalit, R.2    Yaish, S.3    Drummer, H.4    Amit, B.5    Sarver, N.6    Gorecki, M.7    Panel, A.8
  • 38
    • 0029655893 scopus 로고    scopus 로고
    • Cytoskeleton association and virion incorporation of the human immunodeficiency virus type 1 Vif protein
    • Karczewski, M.K., and K. Strebel. 1996. Cytoskeleton association and virion incorporation of the human immunodeficiency virus type 1 Vif protein. J. Virol. 70:494-507.
    • (1996) J. Virol. , vol.70 , pp. 494-507
    • Karczewski, M.K.1    Strebel, K.2
  • 39
    • 0034695259 scopus 로고    scopus 로고
    • 15 Angstrom resolution model of the monomeric kinesin motor, KIF1A
    • Kikkawa, M., Y. Okada, and N. Hirokawa. 2000. 15 angstrom resolution model of the monomeric kinesin motor, KIF1A. Cell. 100:241-252.
    • (2000) Cell , vol.100 , pp. 241-252
    • Kikkawa, M.1    Okada, Y.2    Hirokawa, N.3
  • 40
    • 0032961471 scopus 로고    scopus 로고
    • Preparation and properties of pure tubulin S
    • Knipling, L., J. Hwang, and J. Wolff. 1999. Preparation and properties of pure tubulin S. Cell Motil. Cytoskel. 43:63-71.
    • (1999) Cell Motil. Cytoskel. , vol.43 , pp. 63-71
    • Knipling, L.1    Hwang, J.2    Wolff, J.3
  • 41
    • 0029360470 scopus 로고
    • Improved methods for determination of rotational symmetries in macromolecules
    • Kocsis, E., M.E. Cerritelli, B.L. Trus, N. Cheng, and A.C. Steven. 1995. Improved methods for determination of rotational symmetries in macromolecules. Ultramicroscopy. 60:219-228.
    • (1995) Ultramicroscopy , vol.60 , pp. 219-228
    • Kocsis, E.1    Cerritelli, M.E.2    Trus, B.L.3    Cheng, N.4    Steven, A.C.5
  • 42
    • 0027276264 scopus 로고
    • Multiple sites for subtilisin cleavage of tubulin: Effects of divalent-cations
    • Lobert, S., B.S. Hennington, and J.J. Correia. 1993. Multiple sites for subtilisin cleavage of tubulin: effects of divalent-cations. Cell Motil. Cytoskel. 25:282-297.
    • (1993) Cell Motil. Cytoskel. , vol.25 , pp. 282-297
    • Lobert, S.1    Hennington, B.S.2    Correia, J.J.3
  • 43
    • 0020622592 scopus 로고
    • Formation in vitro of sperm pronuclei and mitotic chromosomes induced hy amphibian ooplasmic components
    • Lohka, M., and Y. Masui. 1983. Formation in vitro of sperm pronuclei and mitotic chromosomes induced hy amphibian ooplasmic components. Science. 220:719-721.
    • (1983) Science , vol.220 , pp. 719-721
    • Lohka, M.1    Masui, Y.2
  • 44
    • 0028944633 scopus 로고
    • A domain of human immunodeficiency virus type-1 Vpr containing repeated H(S/F)RIG amino-acid motifs causes cell-growth arrest and structural defects
    • Macreadie, I.G., L.A. Castelli, D.R. Hewish, A. Kirkpatrick, A.C. Ward, and A.A. Azad. 1995. A domain of human immunodeficiency virus type-1 Vpr containing repeated H(S/F)RIG amino-acid motifs causes cell-growth arrest and structural defects. Proc. Natl. Acad. Sci. USA. 92:2770-2774.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2770-2774
    • Macreadie, I.G.1    Castelli, L.A.2    Hewish, D.R.3    Kirkpatrick, A.4    Ward, A.C.5    Azad, A.A.6
  • 46
    • 0032966626 scopus 로고    scopus 로고
    • Structures of kinesin and kinesin-microtubule interactions
    • Mandelkow, E., and A. Hoenger. 1999. Structures of kinesin and kinesin-microtubule interactions. Curr. Opin. Cell Biol. 11:34-14.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 34-114
    • Mandelkow, E.1    Hoenger, A.2
  • 47
    • 0025868445 scopus 로고
    • Microtubule dynamics and microtubule caps - A time-resolved cryoelectron microscopy study
    • Mandelkow, K.M., K. Mandelkow, and R.A. Milligan. 1991. Microtubule dynamics and microtubule caps - a time-resolved cryoelectron microscopy study. J. Cell Biol. 114:977-991.
    • (1991) J. Cell Biol. , vol.114 , pp. 977-991
    • Mandelkow, K.M.1    Mandelkow, K.2    Milligan, R.A.3
  • 48
    • 0031707505 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: The soluble phase
    • Mattaj, I.W., and L. Englmeier. 1998. Nucleocytoplasmic transport: the soluble phase. Annu. Rev. Biochem. 67:265-306.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 265-306
    • Mattaj, I.W.1    Englmeier, L.2
  • 50
    • 0024425928 scopus 로고
    • Cold depolymerization of microtubules to double rings: Geometric stabilisation of assemblies
    • Melki, R., M.F. Carlier, D. Pantaloni, and S.N. Timasheff. 1989. Cold depolymerization of microtubules to double rings: geometric stabilisation of assemblies. Biochemistry. 28:9143-9152.
    • (1989) Biochemistry , vol.28 , pp. 9143-9152
    • Melki, R.1    Carlier, M.F.2    Pantaloni, D.3    Timasheff, S.N.4
  • 51
    • 0039940808 scopus 로고    scopus 로고
    • Control of the structural stability of the tubulin dimer by one high affinity hound magnesium ion at nucleotide N-site
    • Menendez, M., G. Rivas, J.F. Diaz, and J.M. Andreu. 1998. Control of the structural stability of the tubulin dimer by one high affinity hound magnesium ion at nucleotide N-site. J. Biol. Chem. 273:167-176.
    • (1998) J. Biol. Chem. , vol.273 , pp. 167-176
    • Menendez, M.1    Rivas, G.2    Diaz, J.F.3    Andreu, J.M.4
  • 52
    • 0030962705 scopus 로고    scopus 로고
    • Diffraction by helical structures with seams: Microtubules
    • Metoz, F., and R.H. Wade. 1997. Diffraction by helical structures with seams: microtubules. J. Struct. Biol. 118:128-139.
    • (1997) J. Struct. Biol. , vol.118 , pp. 128-139
    • Metoz, F.1    Wade, R.H.2
  • 54
    • 0021710353 scopus 로고
    • Interactions of tubulin with chromatin proteins: H1 and core histories
    • Mithieux, G., C. Alquier, B. Roux, and B. Rousset. 1984. Interactions of tubulin with chromatin proteins: H1 and core histories. J. Biol. Chem. 259:15523-15531.
    • (1984) J. Biol. Chem. , vol.259 , pp. 15523-15531
    • Mithieux, G.1    Alquier, C.2    Roux, B.3    Rousset, B.4
  • 55
    • 0029080215 scopus 로고
    • The cytotoxicity of human immunodeficiency virus type 1 Rev: Implications for its interaction with the nucleolar protein B23
    • Miyazaki, Y., T. Takamatsu, T. Nosaka, S. Fujita, T.E. Martin, and M. Hatanaka. 1995. The cytotoxicity of human immunodeficiency virus type 1 Rev: implications for its interaction with the nucleolar protein B23. Exp. Cell Res. 219:93-101.
    • (1995) Exp. Cell Res. , vol.219 , pp. 93-101
    • Miyazaki, Y.1    Takamatsu, T.2    Nosaka, T.3    Fujita, S.4    Martin, T.E.5    Hatanaka, M.6
  • 56
    • 0033040630 scopus 로고    scopus 로고
    • In vitro approaches to study actin and microtubule dependent cell processes
    • Moreau, V., and M. Way. 1999. In vitro approaches to study actin and microtubule dependent cell processes. Curr. Opin. Cell Biol. 11:152-158.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 152-158
    • Moreau, V.1    Way, M.2
  • 57
    • 0026478027 scopus 로고
    • Stabilization of sea urchin flagellar microtubules by histone H1
    • Multigner, L., J. Gagnon, A. Van Dorsselaer, and D. Job. 1992. Stabilization of sea urchin flagellar microtubules by histone H1. Nature. 360:33-39.
    • (1992) Nature , vol.360 , pp. 33-39
    • Multigner, L.1    Gagnon, J.2    Van Dorsselaer, A.3    Job, D.4
  • 58
    • 0026266161 scopus 로고
    • Cell-cycle extracts
    • Murray, A.W. 1991. Cell-cycle extracts. Methods Cell Biol. 36:581-605.
    • (1991) Methods Cell Biol. , vol.36 , pp. 581-605
    • Murray, A.W.1
  • 60
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha beta tubulin dimer by electron crystallography
    • Nogales, E., S.G. Wolf, and K.H. Downing. 1998. Structure of the alpha beta tubulin dimer by electron crystallography. Nature. 391:199-203.
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 63
    • 0029190887 scopus 로고
    • Structure and function in the tubulin dimer and the role of the acidic carboxyl terminus
    • Sackett, D.L. 1995a. Structure and function in the tubulin dimer and the role of the acidic carboxyl terminus. Subcell. Biochem. 24:255-302.
    • (1995) Subcell. Biochem. , vol.24 , pp. 255-302
    • Sackett, D.L.1
  • 64
    • 0029069324 scopus 로고
    • Vinca site agents induce structural changes in tubulin different from and antagonistic to changes induced by colchicine site agents
    • Sackett, D.L. 1995b. Vinca site agents induce structural changes in tubulin different from and antagonistic to changes induced by colchicine site agents. Biochemistry. 34:7010-7019.
    • (1995) Biochemistry , vol.34 , pp. 7010-7019
    • Sackett, D.L.1
  • 65
    • 0023025012 scopus 로고
    • Proteolysis of tubulin and the substructure of the tubulin dimer
    • Sackett, D.L., and J. Wolff. 1986. Proteolysis of tubulin and the substructure of the tubulin dimer. J. Biol. Chem. 261:9070-9076.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9070-9076
    • Sackett, D.L.1    Wolff, J.2
  • 66
    • 0026231651 scopus 로고
    • Isolation of microtubule protein from mammalian brain frozen for extended periods of time
    • Sackett, D.L., L. Knipling, and J. Wolff. 1991. Isolation of microtubule protein from mammalian brain frozen for extended periods of time. Prot. Expr. Purif. 2:390-393.
    • (1991) Prot. Expr. Purif. , vol.2 , pp. 390-393
    • Sackett, D.L.1    Knipling, L.2    Wolff, J.3
  • 68
    • 0029122732 scopus 로고
    • Identification of a novel nuclear pore-associated protein as a functional target of the HIV-1 Rev protein in yeast
    • Stutz, F., M. Neville, and M. Rosbash. 1995. Identification of a novel nuclear pore-associated protein as a functional target of the HIV-1 Rev protein in yeast. Cell. 82:495-506.
    • (1995) Cell , vol.82 , pp. 495-506
    • Stutz, F.1    Neville, M.2    Rosbash, M.3
  • 69
    • 0029066104 scopus 로고
    • Nuclear export of the human immunodeficiency virus type I nucleocytoplasmic shuttle protein Rev is mediated by its activation domain and is blocked by transdominant negative mutants
    • Szilvay, A.M., K.A. Brokstad, R. Kopperud, G. Haukenes, and K.H. Kalland. 1995. Nuclear export of the human immunodeficiency virus type I nucleocytoplasmic shuttle protein Rev is mediated by its activation domain and is blocked by transdominant negative mutants. J. Virol. 69:3315-3323.
    • (1995) J. Virol. , vol.69 , pp. 3315-3323
    • Szilvay, A.M.1    Brokstad, K.A.2    Kopperud, R.3    Haukenes, G.4    Kalland, K.H.5
  • 70
    • 0028136474 scopus 로고
    • Mass analysis of biological macromolecular complexes by STEM
    • Thomas, D., P. Schultz, A.C. Steven, and J.S. Wall. 1994. Mass analysis of biological macromolecular complexes by STEM. Biol. Cell. 80:181-192.
    • (1994) Biol. Cell , vol.80 , pp. 181-192
    • Thomas, D.1    Schultz, P.2    Steven, A.C.3    Wall, J.S.4
  • 71
    • 0031047864 scopus 로고    scopus 로고
    • Probing the structure of the HIV-1 tirans activator protein by functional analysis
    • Thomas, S., J. Hauber, and G. Casari. 1997. Probing the structure of the HIV-1 tIrans activator protein by functional analysis. Prot. Eng. 10:103-107.
    • (1997) Prot. Eng. , vol.10 , pp. 103-107
    • Thomas, S.1    Hauber, J.2    Casari, G.3
  • 74
    • 0029975086 scopus 로고    scopus 로고
    • Digital image processing of electron micrographs: The PIC system-III
    • Trus, B.L., E. Kocsis, J.F. Conway, and A.C. Steven. 1996. Digital image processing of electron micrographs: the PIC system-III. J. Struct. Biol. 116:61-67.
    • (1996) J. Struct. Biol. , vol.116 , pp. 61-67
    • Trus, B.L.1    Kocsis, E.2    Conway, J.F.3    Steven, A.C.4
  • 75
    • 0018557470 scopus 로고
    • Tubulin rings: Curved filaments with limited flexibility and two modes of association
    • Voter, W.A., and H.P. Erickson. 1979. Tubulin rings: curved filaments with limited flexibility and two modes of association. J. Supramol. Struct. 10:419-431.
    • (1979) J. Supramol. Struct. , vol.10 , pp. 419-431
    • Voter, W.A.1    Erickson, H.P.2
  • 76
    • 0031972530 scopus 로고    scopus 로고
    • Scanning transmission electron microscopy of nuclear structures
    • Wall, J.S., J.F. Hainfeld, and M.N. Simon. 1998. Scanning transmission electron microscopy of nuclear structures. Methods Cell Biol. 53:139-164.
    • (1998) Methods Cell Biol. , vol.53 , pp. 139-164
    • Wall, J.S.1    Hainfeld, J.F.2    Simon, M.N.3
  • 79
    • 0025871993 scopus 로고
    • HIV-1 Rev expressed in recombinant Escherichia coli: Purification, polymerization, and conformational properties
    • Wingfield, P.T., S.J. Stahl, M.A. Payton, S. Venkatesan, M. Misra, and A.C. Steven. 1991. HIV-1 Rev expressed in recombinant Escherichia coli: purification, polymerization, and conformational properties. Biochemistry. 30: 7527-7534.
    • (1991) Biochemistry , vol.30 , pp. 7527-7534
    • Wingfield, P.T.1    Stahl, S.J.2    Payton, M.A.3    Venkatesan, S.4    Misra, M.5    Steven, A.C.6
  • 80
    • 0029989734 scopus 로고
    • Charge-shielding and the "paradoxical" stimulation of tubulin polymerization by guanidine hydrochloride
    • Wolff, J., L. Knipling, and D.L. Sackett. 1995. Charge-shielding and the "paradoxical" stimulation of tubulin polymerization by guanidine hydrochloride. Biochemistry. 35:5910-5920.
    • (1995) Biochemistry , vol.35 , pp. 5910-5920
    • Wolff, J.1    Knipling, L.2    Sackett, D.L.3
  • 81
    • 0029955450 scopus 로고    scopus 로고
    • Cation selective promotion of tubulin polymerization by alkali metal chlorides
    • Wolff, J., D.L. Sackett, and L. Knipling. 1996. Cation selective promotion of tubulin polymerization by alkali metal chlorides. Prot. Sci. 5:2020-2028.
    • (1996) Prot. Sci. , vol.5 , pp. 2020-2028
    • Wolff, J.1    Sackett, D.L.2    Knipling, L.3
  • 82
    • 0029933537 scopus 로고    scopus 로고
    • Flexible regions of RNA structure facilitate co-operative Rev assembly on the Rev-response element
    • Zemmel, R.W., A.C. Kelley, J. Karn, and P.J.G. Butler. 1996. Flexible regions of RNA structure facilitate co-operative Rev assembly on the Rev-response element. J. Mol. Biol. 258:763-777.
    • (1996) J. Mol. Biol. , vol.258 , pp. 763-777
    • Zemmel, R.W.1    Kelley, A.C.2    Karn, J.3    Butler, P.J.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.