메뉴 건너뛰기




Volumn 77, Issue 1, 1999, Pages 241-247

Conformational changes of the in situ nuclear pore complex

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CARRIER PROTEIN; NUCLEAR PROTEIN; SODIUM CHLORIDE;

EID: 0033014673     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)76885-2     Document Type: Article
Times cited : (79)

References (29)
  • 2
    • 0025180782 scopus 로고
    • Visualization of transport-related configurations of the nuclear pore transporter
    • Akey, C. W. 1990. Visualization of transport-related configurations of the nuclear pore transporter. Biophys. J. 58:341-355.
    • (1990) Biophys. J. , vol.58 , pp. 341-355
    • Akey, C.W.1
  • 3
    • 0027287349 scopus 로고
    • Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy
    • Akey, C. W., and M. Radermacher. 1993. Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy. J. Cell Biol. 122:1-19.
    • (1993) J. Cell Biol. , vol.122 , pp. 1-19
    • Akey, C.W.1    Radermacher, M.2
  • 4
    • 0025371353 scopus 로고
    • The permeability of the nuclear envelope in dividing and nondividing cell cultures
    • Feldherr, C. M., and D. Akin. 1990. The permeability of the nuclear envelope in dividing and nondividing cell cultures. J. Cell Biol. 111:1-8.
    • (1990) J. Cell Biol. , vol.111 , pp. 1-8
    • Feldherr, C.M.1    Akin, D.2
  • 5
    • 0029786355 scopus 로고    scopus 로고
    • Aldosterone activates the nuclear pore transporter in cultured kidney cells imaged with atomic force microscopy
    • Folprecht, G., S. Schneider, and H. Oberleithner. 1996. Aldosterone activates the nuclear pore transporter in cultured kidney cells imaged with atomic force microscopy. Pfluegers Arch. 432:831-838.
    • (1996) Pfluegers Arch. , vol.432 , pp. 831-838
    • Folprecht, G.1    Schneider, S.2    Oberleithner, H.3
  • 6
    • 0026676877 scopus 로고
    • Structure and function of the nuclear pore
    • Forbes, D. J. 1992. Structure and function of the nuclear pore. Annu. Rev. Cell Biol. 8:495-527.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 495-527
    • Forbes, D.J.1
  • 7
    • 0024147084 scopus 로고
    • Functional organization of the nuclear envelope
    • Gerace, L., and B. Burke. 1988. Functional organization of the nuclear envelope. Annu. Rev. Cell Biol. 4:335-374.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 335-374
    • Gerace, L.1    Burke, B.2
  • 8
    • 0029015891 scopus 로고
    • Structural and functional organization of the nuclear envelope
    • Goldberg, M. W., and T. D. Allen. 1995. Structural and functional organization of the nuclear envelope. Curr. Opin. Cell Biol. 7:301-309.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 301-309
    • Goldberg, M.W.1    Allen, T.D.2
  • 9
    • 0026500909 scopus 로고
    • Nuclear import protein is inhibited by an antibody to a lumenal epitope of a nuclear pore complex glycoprotein
    • Greber, U. F., and L. Gerace. 1992. Nuclear import protein is inhibited by an antibody to a lumenal epitope of a nuclear pore complex glycoprotein. J. Cell. Biol. 116:15-30.
    • (1992) J. Cell. Biol. , vol.116 , pp. 15-30
    • Greber, U.F.1    Gerace, L.2
  • 10
    • 0028851245 scopus 로고
    • Depletion of calcium from the lumen of endoplasmic reticulum reversible inhibits passive diffusion and signal-mediated transport into the nucleus
    • Greber, U. F., and L. Gerace. 1995. Depletion of calcium from the lumen of endoplasmic reticulum reversible inhibits passive diffusion and signal-mediated transport into the nucleus. J. Cell. Biol. 128:5-25.
    • (1995) J. Cell. Biol. , vol.128 , pp. 5-25
    • Greber, U.F.1    Gerace, L.2
  • 11
    • 0025253486 scopus 로고
    • A major glycoprotein of the nuclear pore complex is a membrane-spanning polypeptide with a large lumenal domain and a small cytoplasmic tail
    • Greber, U. F., A. Senior, and L. Gerace. 1990. A major glycoprotein of the nuclear pore complex is a membrane-spanning polypeptide with a large lumenal domain and a small cytoplasmic tail. EMBO J. 9:1495-1502.
    • (1990) EMBO J. , vol.9 , pp. 1495-1502
    • Greber, U.F.1    Senior, A.2    Gerace, L.3
  • 13
    • 0026539008 scopus 로고
    • The nuclear pore: At the crossroads
    • Hanover, J. A. 1992. The nuclear pore: at the crossroads. FASEB J. 6:2288-2295.
    • (1992) FASEB J. , vol.6 , pp. 2288-2295
    • Hanover, J.A.1
  • 14
    • 0026776959 scopus 로고
    • Architecture and design of the nuclear pore complex
    • Hinshaw, J. E., B. O. Carragher, and R. A. Milligan. 1992. Architecture and design of the nuclear pore complex. Cell. 69:1133-1141.
    • (1992) Cell , vol.69 , pp. 1133-1141
    • Hinshaw, J.E.1    Carragher, B.O.2    Milligan, R.A.3
  • 15
    • 0026323478 scopus 로고
    • Toward a more complete 3-D structure of the nuclear pore complex
    • Jarnik, M., and U. Aebi. 1991. Toward a more complete 3-D structure of the nuclear pore complex. J. Struct. Biol. 107:291-308.
    • (1991) J. Struct. Biol. , vol.107 , pp. 291-308
    • Jarnik, M.1    Aebi, U.2
  • 16
    • 0023878349 scopus 로고
    • Nuclear transport in 3T3 fibroblasts: Effects of growth factors, transformation, and cell shape
    • Jiang, L. W., and M. Schindler. 1988. Nuclear transport in 3T3 fibroblasts: effects of growth factors, transformation, and cell shape. J. Cell Biol. 106:13-19.
    • (1988) J. Cell Biol. , vol.106 , pp. 13-19
    • Jiang, L.W.1    Schindler, M.2
  • 17
    • 0028131997 scopus 로고
    • Spatiotemporal distribution of protein kinase and phosphatase activities
    • Inagaki, N., M. Ito, T. Nakano, and M. Inagaki. 1994. Spatiotemporal distribution of protein kinase and phosphatase activities. Trends Biochem. Sci. 19:448-452.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 448-452
    • Inagaki, N.1    Ito, M.2    Nakano, T.3    Inagaki, M.4
  • 18
    • 85023086213 scopus 로고
    • Molecular mechanisms of intracellular calcium release in Xenopus laevis oocytes
    • Lechleiter, J., and D. E. Clapham. 1992. Molecular mechanisms of intracellular calcium release in Xenopus laevis oocytes. Cell. 69:1-20.
    • (1992) Cell , vol.69 , pp. 1-20
    • Lechleiter, J.1    Clapham, D.E.2
  • 19
    • 0028030252 scopus 로고
    • Single-channel inositol 1,4,5-trisphosphate receptor currents revealed by patch clamp of isolated Xenopus oocyte nuclei
    • Mak, D. O., and J. K. Foskett. 1994. Single-channel inositol 1,4,5-trisphosphate receptor currents revealed by patch clamp of isolated Xenopus oocyte nuclei. J. Biol. Chem. 269:29375-29378.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29375-29378
    • Mak, D.O.1    Foskett, J.K.2
  • 20
    • 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
  • 21
    • 0345529797 scopus 로고
    • Toward the molecular details of the nuclear pore complex at the molecular level
    • Pante, N., and U. Aebi. 1994. Toward the molecular details of the nuclear pore complex at the molecular level. J. Struct. Biol. 3:178-189.
    • (1994) J. Struct. Biol. , vol.3 , pp. 178-189
    • Pante, N.1    Aebi, U.2
  • 22
    • 0031239585 scopus 로고    scopus 로고
    • Nuclear calcium and the regulation of the nuclear pore complex
    • Perez-Terzic, C. M., M. Jaconi, and D. E Clapham. 1997. Nuclear calcium and the regulation of the nuclear pore complex. Bioessays. 19:787-792.
    • (1997) Bioessays , vol.19 , pp. 787-792
    • Perez-Terzic, C.M.1    Jaconi, M.2    Clapham, D.E.3
  • 23
    • 0029744799 scopus 로고    scopus 로고
    • Conformational states of the nuclear pore complex induced by depletion of nuclear calcium stores
    • Perez-Terzic, C., J. Pyle, M. Jaconi, L. Stehno-Bittel, and D. E. Clapham. 1996. Conformational states of the nuclear pore complex induced by depletion of nuclear calcium stores. Science. 273:1875-1877.
    • (1996) Science , vol.273 , pp. 1875-1877
    • Perez-Terzic, C.1    Pyle, J.2    Jaconi, M.3    Stehno-Bittel, L.4    Clapham, D.E.5
  • 24
    • 0026014878 scopus 로고
    • Human cyclins A and B1 are differentially located in the cell and undergo cell cycle-dependent nuclear transport
    • Pines, J., and T. Hunter. 1991. Human cyclins A and B1 are differentially located in the cell and undergo cell cycle-dependent nuclear transport. J. Cell Biol. 115:1-17.
    • (1991) J. Cell Biol. , vol.115 , pp. 1-17
    • Pines, J.1    Hunter, T.2
  • 25
    • 0032523832 scopus 로고    scopus 로고
    • ATP-induced shape change of nuclear pores visualized with the atomic force microscope
    • Rakowska, A., T. Danker, S. W. Schneider, and H. Oberleithner. 1998. ATP-induced shape change of nuclear pores visualized with the atomic force microscope. J. Membr. Biol. 163:129-136.
    • (1998) J. Membr. Biol. , vol.163 , pp. 129-136
    • Rakowska, A.1    Danker, T.2    Schneider, S.W.3    Oberleithner, H.4
  • 29
    • 0028301412 scopus 로고
    • Nuclear phosphatidylinositols decrease during S-phase of the cell cycle in HeLa cells
    • York, J. D., and P. W. Majerus. 1994. Nuclear phosphatidylinositols decrease during S-phase of the cell cycle in HeLa cells. J. Biol. Chem. 269:7847-7850.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7847-7850
    • York, J.D.1    Majerus, P.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.