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Volumn 177, Issue 1, 2012, Pages 113-118

Filaments assembly of ectopically expressed Caenorhabditis elegans lamin within Xenopus oocytes

Author keywords

Caenorhabditis elegans lamin; Cryo electron tomography; Intermediate filaments; Nuclear lamina; Protofilaments

Indexed keywords

HELMINTH PROTEIN; LAMIN;

EID: 84855855189     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2011.11.002     Document Type: Article
Times cited : (31)

References (38)
  • 1
    • 0022519369 scopus 로고
    • The nuclear lamina is a meshwork of intermediate-type filaments
    • Aebi U., Cohn J., Buhle L., Gerace L. The nuclear lamina is a meshwork of intermediate-type filaments. Nature 1986, 323:560-564.
    • (1986) Nature , vol.323 , pp. 560-564
    • Aebi, U.1    Cohn, J.2    Buhle, L.3    Gerace, L.4
  • 2
    • 79961049347 scopus 로고    scopus 로고
    • A laminopathic mutation disrupting lamin filament assembly causes disease-like phenotypes in Caenorhabditis elegans
    • Bank E.M., Ben-Harush K., Medalia O.Y G. A laminopathic mutation disrupting lamin filament assembly causes disease-like phenotypes in Caenorhabditis elegans. Mol. Biol. Cell 2011, 22:2716-2728.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 2716-2728
    • Bank, E.M.1    Ben-Harush, K.2    Medalia, O.Y.G.3
  • 3
    • 72449161758 scopus 로고    scopus 로고
    • Visualizing cellular processes at the molecular level by cryo-electron tomography
    • Ben-Harush K., Maimon T., Patla I., Villa E., Medalia O. Visualizing cellular processes at the molecular level by cryo-electron tomography. J. Cell Sci. 2010, 123:7-12.
    • (2010) J. Cell Sci. , vol.123 , pp. 7-12
    • Ben-Harush, K.1    Maimon, T.2    Patla, I.3    Villa, E.4    Medalia, O.5
  • 5
    • 0025130161 scopus 로고
    • Structural features in the heptad substructure and longer range repeats of two-stranded alpha-fibrous proteins
    • Conway J.F., Parry D.A. Structural features in the heptad substructure and longer range repeats of two-stranded alpha-fibrous proteins. Int. J. Biol. Macromol. 1990, 12:328-334.
    • (1990) Int. J. Biol. Macromol. , vol.12 , pp. 328-334
    • Conway, J.F.1    Parry, D.A.2
  • 6
    • 4544228141 scopus 로고    scopus 로고
    • The nuclear envelope lamina network has elasticity and a compressibility limit suggestive of a molecular shock absorber
    • Dahl K.N., Kahn S.M., Wilson K.L., Discher D.E. The nuclear envelope lamina network has elasticity and a compressibility limit suggestive of a molecular shock absorber. J. Cell Sci. 2004, 117:4779-4786.
    • (2004) J. Cell Sci. , vol.117 , pp. 4779-4786
    • Dahl, K.N.1    Kahn, S.M.2    Wilson, K.L.3    Discher, D.E.4
  • 7
    • 33745904741 scopus 로고    scopus 로고
    • Distinct structural and mechanical properties of the nuclear lamina in Hutchinson-Gilford progeria syndrome
    • Dahl K.N., Scaffidi P., Islam M.F., Yodh A.G., Wilson K.L., Misteli T. Distinct structural and mechanical properties of the nuclear lamina in Hutchinson-Gilford progeria syndrome. Proc. Natl. Acad. Sci. USA 2006, 103:10271-10276.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 10271-10276
    • Dahl, K.N.1    Scaffidi, P.2    Islam, M.F.3    Yodh, A.G.4    Wilson, K.L.5    Misteli, T.6
  • 10
    • 0036968863 scopus 로고    scopus 로고
    • Domain-specific antibodies reveal multiple-site topology of Nup153 within the nuclear pore complex
    • Fahrenkrog B., Maco B., Fager A.M., Koser J., Sauder U., Ullman K.S., Aebi U. Domain-specific antibodies reveal multiple-site topology of Nup153 within the nuclear pore complex. J. Struct. Biol. 2002, 140:254-267.
    • (2002) J. Struct. Biol. , vol.140 , pp. 254-267
    • Fahrenkrog, B.1    Maco, B.2    Fager, A.M.3    Koser, J.4    Sauder, U.5    Ullman, K.S.6    Aebi, U.7
  • 12
    • 38949154474 scopus 로고    scopus 로고
    • Filaments made from A- and B-type lamins differ in structure and organization
    • Goldberg M.W., Huttenlauch I., Hutchison C.J., Stick R. Filaments made from A- and B-type lamins differ in structure and organization. J. Cell Sci. 2008, 121:215-225.
    • (2008) J. Cell Sci. , vol.121 , pp. 215-225
    • Goldberg, M.W.1    Huttenlauch, I.2    Hutchison, C.J.3    Stick, R.4
  • 14
    • 18244401885 scopus 로고    scopus 로고
    • Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex
    • Hawryluk-Gara L.A., Shibuya E.K., Wozniak R.W. Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex. Mol. Biol. Cell 2005, 16:2382-2394.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2382-2394
    • Hawryluk-Gara, L.A.1    Shibuya, E.K.2    Wozniak, R.W.3
  • 15
    • 0029879294 scopus 로고    scopus 로고
    • The EM program package: a platform for image processing in biological electron microscopy
    • Hegerl R. The EM program package: a platform for image processing in biological electron microscopy. J. Struct. Biol. 1996, 116:30-34.
    • (1996) J. Struct. Biol. , vol.116 , pp. 30-34
    • Hegerl, R.1
  • 16
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular Scaffolds
    • Herrmann H., Aebi U. Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular Scaffolds. Annu. Rev. Biochem. 2004, 73:749-789.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 17
    • 0028923173 scopus 로고
    • Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells
    • Hozak P., Sasseville A.M., Raymond Y., Cook P.R. Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells. J. Cell Sci. 1995, 108(Pt 2):635-644.
    • (1995) J. Cell Sci. , vol.108 , Issue.PART 2 , pp. 635-644
    • Hozak, P.1    Sasseville, A.M.2    Raymond, Y.3    Cook, P.R.4
  • 18
    • 41649116913 scopus 로고    scopus 로고
    • Tensile properties of single desmin intermediate filaments
    • Kreplak L., Herrmann H., Aebi U. Tensile properties of single desmin intermediate filaments. Biophys. J. 2008, 94:2790-2799.
    • (2008) Biophys. J. , vol.94 , pp. 2790-2799
    • Kreplak, L.1    Herrmann, H.2    Aebi, U.3
  • 21
    • 14844330221 scopus 로고    scopus 로고
    • Structural studies by electron tomography: from cells to molecules
    • Lucic V., Forster F., Baumeister W. Structural studies by electron tomography: from cells to molecules. Annu. Rev. Biochem. 2005, 74:833-865.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 833-865
    • Lucic, V.1    Forster, F.2    Baumeister, W.3
  • 23
    • 77957252774 scopus 로고    scopus 로고
    • Cryoelectron tomography of eukaryotic cells
    • Mader A., Elad N., Medalia O. Cryoelectron tomography of eukaryotic cells. Methods Enzymol. 2010, 483:245-265.
    • (2010) Methods Enzymol. , vol.483 , pp. 245-265
    • Mader, A.1    Elad, N.2    Medalia, O.3
  • 26
    • 0022546016 scopus 로고
    • Structural studies on lamin. Similarities and differences between lamin and intermediate-filament proteins
    • Parry D.A., Conway J.F., Steinert P.M. Structural studies on lamin. Similarities and differences between lamin and intermediate-filament proteins. Biochem. J. 1986, 238:305-308.
    • (1986) Biochem. J. , vol.238 , pp. 305-308
    • Parry, D.A.1    Conway, J.F.2    Steinert, P.M.3
  • 28
    • 33748296316 scopus 로고    scopus 로고
    • The laminopathies: a clinical review
    • Rankin J., Ellard S. The laminopathies: a clinical review. Clin. Genet. 2006, 70:261-274.
    • (2006) Clin. Genet. , vol.70 , pp. 261-274
    • Rankin, J.1    Ellard, S.2
  • 29
    • 0034254413 scopus 로고    scopus 로고
    • Incorporation of the nuclear pore basket protein nup153 into nuclear pore structures is dependent upon lamina assembly: evidence from cell-free extracts of Xenopus eggs
    • Smythe C., Jenkins H.E., Hutchison C.J. Incorporation of the nuclear pore basket protein nup153 into nuclear pore structures is dependent upon lamina assembly: evidence from cell-free extracts of Xenopus eggs. EMBO J. 2000, 19:3918-3931.
    • (2000) EMBO J. , vol.19 , pp. 3918-3931
    • Smythe, C.1    Jenkins, H.E.2    Hutchison, C.J.3
  • 30
    • 0027936303 scopus 로고
    • The gene structure of B-type nuclear lamins of Xenopus laevis: implications for the evolution of the vertebrate lamin family
    • Stick R. The gene structure of B-type nuclear lamins of Xenopus laevis: implications for the evolution of the vertebrate lamin family. Chromosome Res. 1994, 2:376-382.
    • (1994) Chromosome Res. , vol.2 , pp. 376-382
    • Stick, R.1
  • 31
    • 77951879537 scopus 로고    scopus 로고
    • Oocytes as an experimental system to analyze the ultrastructure of endogenous and ectopically expressed nuclear envelope components by field-emission scanning electron microscopy
    • Stick R., Goldberg M.W. Oocytes as an experimental system to analyze the ultrastructure of endogenous and ectopically expressed nuclear envelope components by field-emission scanning electron microscopy. Methods 2010, 51:170-176.
    • (2010) Methods , vol.51 , pp. 170-176
    • Stick, R.1    Goldberg, M.W.2
  • 32
    • 0031686054 scopus 로고    scopus 로고
    • Nuclear lamins: their structure, assembly, and interactions
    • Stuurman N., Heins S., Aebi U. Nuclear lamins: their structure, assembly, and interactions. J. Struct. Biol. 1998, 122:42-66.
    • (1998) J. Struct. Biol. , vol.122 , pp. 42-66
    • Stuurman, N.1    Heins, S.2    Aebi, U.3
  • 34
    • 34247485356 scopus 로고    scopus 로고
    • A-type lamin networks in light of laminopathic diseases
    • Vlcek S., Foisner R. A-type lamin networks in light of laminopathic diseases. Biochim. Biophys. Acta 2007, 1773:661-674.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 661-674
    • Vlcek, S.1    Foisner, R.2
  • 38
    • 80053563027 scopus 로고    scopus 로고
    • Cryo-electron tomography: gaining insight into cellular processes by structural approaches
    • Yahav T., Maimon T., Grossman E., Dahan I., Medalia O. Cryo-electron tomography: gaining insight into cellular processes by structural approaches. Curr. Opin. Struct. Biol. 2011, 21:670-677.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 670-677
    • Yahav, T.1    Maimon, T.2    Grossman, E.3    Dahan, I.4    Medalia, O.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.