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Volumn 7, Issue , 2006, Pages

Nuclear envelope transmembrane proteins (NETs) that are up-regulated during myogenesis

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; MEMBRANE PROTEIN;

EID: 33750943167     PISSN: 14712121     EISSN: 14712121     Source Type: Journal    
DOI: 10.1186/1471-2121-7-38     Document Type: Article
Times cited : (70)

References (63)
  • 1
    • 0024147084 scopus 로고
    • Functional organization of the nuclear envelope
    • Gerace L, Burke B: Functional organization of the nuclear envelope. Annu Rev Cell Biol 1988, 4:335-374.
    • (1988) Annu Rev Cell Biol , vol.4 , pp. 335-374
    • Gerace, L.1    Burke, B.2
  • 3
    • 28444472419 scopus 로고    scopus 로고
    • Pushing the envelope: Structure, function, and dynamics of the nuclear periphery
    • Hetzer MW, Walther TC, Mattaj IW: Pushing the envelope: structure, function, and dynamics of the nuclear periphery. Annu Rev Cell Dev Biol 2005, 21:347-380.
    • (2005) Annu Rev Cell Dev Biol , vol.21 , pp. 347-380
    • Hetzer, M.W.1    Walther, T.C.2    Mattaj, I.W.3
  • 4
    • 33744967486 scopus 로고    scopus 로고
    • Dynamic nuclear pore complexes: Life on the edge
    • Tran EJ, Wente SR: Dynamic nuclear pore complexes: life on the edge. Cell 2006, 125:1041-1053.
    • (2006) Cell , vol.125 , pp. 1041-1053
    • Tran, E.J.1    Wente, S.R.2
  • 5
    • 1842813943 scopus 로고    scopus 로고
    • The nuclear pore complex: A jack of all trades?
    • Fahrenkrog B, Koser J, Aebi U: The nuclear pore complex: a jack of all trades? Trends Biochem Sci 2004, 29:175-182.
    • (2004) Trends Biochem Sci , vol.29 , pp. 175-182
    • Fahrenkrog, B.1    Koser, J.2    Aebi, U.3
  • 6
    • 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
  • 8
    • 0036843975 scopus 로고    scopus 로고
    • Lamins: Building blocks or regulators of gene expression?
    • Hutchison CJ: Lamins: building blocks or regulators of gene expression? Nat Rev Mol Cell Biol 2002, 3:848-858.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 848-858
    • Hutchison, C.J.1
  • 10
    • 0037439661 scopus 로고    scopus 로고
    • ANChors away: An actin based mechanism of nuclear positioning
    • Starr DA, Han M: ANChors away: an actin based mechanism of nuclear positioning. J Cell Sci 2003, 116:211-216.
    • (2003) J Cell Sci , vol.116 , pp. 211-216
    • Starr, D.A.1    Han, M.2
  • 11
    • 32644479020 scopus 로고    scopus 로고
    • Here come the SUNs: A nucleocytoskeletal missing link
    • Worman HJ, Gundersen GG: Here come the SUNs: a nucleocytoskeletal missing link. Trends Cell Biol 2006, 16:67-69.
    • (2006) Trends Cell Biol , vol.16 , pp. 67-69
    • Worman, H.J.1    Gundersen, G.G.2
  • 12
    • 25144515509 scopus 로고    scopus 로고
    • Nuclear envelope, nuclear lamina, and inherited disease
    • Worman HJ, Courvalin JC: Nuclear envelope, nuclear lamina, and inherited disease. Int Rev Cytol 2005, 246:231-279.
    • (2005) Int Rev Cytol , vol.246 , pp. 231-279
    • Worman, H.J.1    Courvalin, J.C.2
  • 13
    • 16544362438 scopus 로고    scopus 로고
    • Structural organization and functions of the nucleus in development, aging, and disease
    • Mounkes L, Stewart CL: Structural organization and functions of the nucleus in development, aging, and disease. Curr Top Dev Biol 2004, 61:191-228.
    • (2004) Curr Top Dev Biol , vol.61 , pp. 191-228
    • Mounkes, L.1    Stewart, C.L.2
  • 14
    • 7944219648 scopus 로고    scopus 로고
    • A-type lamins: Guardians of the soma?
    • Hutchison CJ, Worman HJ: A-type lamins: guardians of the soma? Nat Cell Biol 2004, 6:1062-1067.
    • (2004) Nat Cell Biol , vol.6 , pp. 1062-1067
    • Hutchison, C.J.1    Worman, H.J.2
  • 15
    • 17544383469 scopus 로고    scopus 로고
    • Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1
    • Ye Q, Worman HJ: Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1. J Biol Chem 1996, 271:14653-14656.
    • (1996) J Biol Chem , vol.271 , pp. 14653-14656
    • Ye, Q.1    Worman, H.J.2
  • 17
    • 33746942748 scopus 로고    scopus 로고
    • Inner nuclear membrane and regulation of Smad-mediated signaling
    • Worman HJ: Inner nuclear membrane and regulation of Smad-mediated signaling. Biochim Biophys Acta 2006.
    • (2006) Biochim Biophys Acta
    • Worman, H.J.1
  • 18
    • 30444450095 scopus 로고    scopus 로고
    • KASH 'n Karry: The KASH domain family of cargo-specific cytoskeletal adaptor proteins
    • Starr DA, Fischer JA: KASH 'n Karry: the KASH domain family of cargo-specific cytoskeletal adaptor proteins. Bioessays 2005, 27:1136-1146.
    • (2005) Bioessays , vol.27 , pp. 1136-1146
    • Starr, D.A.1    Fischer, J.A.2
  • 21
    • 33646555082 scopus 로고    scopus 로고
    • SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton
    • Haque F, Lloyd DJ, Smallwood DT, Dent CL, Shanahan CM, Fry AM, Trembath RC, Shackleton S: SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton. Mol Cell Biol 2006, 26:3738-3751.
    • (2006) Mol Cell Biol , vol.26 , pp. 3738-3751
    • Haque, F.1    Lloyd, D.J.2    Smallwood, D.T.3    Dent, C.L.4    Shanahan, C.M.5    Fry, A.M.6    Trembath, R.C.7    Shackleton, S.8
  • 22
    • 0042691509 scopus 로고    scopus 로고
    • Nuclear membrane proteins with potential disease links found by subtractive proteomics
    • Schirmer EC, Florens L, Guan T, Yates JR, Gerace L: Nuclear membrane proteins with potential disease links found by subtractive proteomics. Science 2003, 301:1380-1382.
    • (2003) Science , vol.301 , pp. 1380-1382
    • Schirmer, E.C.1    Florens, L.2    Guan, T.3    Yates, J.R.4    Gerace, L.5
  • 23
    • 0347989458 scopus 로고    scopus 로고
    • Cellular and molecular regulation of muscle regeneration
    • Charge SB, Rudnicki MA: Cellular and molecular regulation of muscle regeneration. Physiol Rev 2004, 84:209-238.
    • (2004) Physiol Rev , vol.84 , pp. 209-238
    • Charge, S.B.1    Rudnicki, M.A.2
  • 24
    • 0021672811 scopus 로고
    • Cardiac actin is the major actin gene product in skeletal muscle cell differentiation in vitro
    • Bains W, Ponte P, Blau H, Kedes L: Cardiac actin is the major actin gene product in skeletal muscle cell differentiation in vitro. Mol Cell Biol 1984, 4:1449-1453.
    • (1984) Mol Cell Biol , vol.4 , pp. 1449-1453
    • Bains, W.1    Ponte, P.2    Blau, H.3    Kedes, L.4
  • 25
    • 0031969222 scopus 로고    scopus 로고
    • Cell heterogeneity upon myogenic differentiation: Down-regulation of MyoD and Myf-5 generates 'reserve cells'
    • Yoshida N, Yoshida S, Koishi K, Masuda K, Nabeshima Y: Cell heterogeneity upon myogenic differentiation: down-regulation of MyoD and Myf-5 generates 'reserve cells'. J Cell Sci 1998, III ( Pt 6):769-779.
    • (1998) J Cell Sci , vol.3 , Issue.PART 6 , pp. 769-779
    • Yoshida, N.1    Yoshida, S.2    Koishi, K.3    Masuda, K.4    Nabeshima, Y.5
  • 28
    • 3142587059 scopus 로고    scopus 로고
    • Protein folding and quality control in the endoplasmic reticulum
    • Kleizen B, Braakman I: Protein folding and quality control in the endoplasmic reticulum. Curr Opin Cell Biol 2004, 16:343-349.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 343-349
    • Kleizen, B.1    Braakman, I.2
  • 29
    • 0016377705 scopus 로고
    • Isolation of rough and smooth microsomes - General
    • Dallner G: Isolation of rough and smooth microsomes - general. Methods Enzymol 1974, 31:191-201.
    • (1974) Methods Enzymol , vol.31 , pp. 191-201
    • Dallner, G.1
  • 30
    • 16244368745 scopus 로고    scopus 로고
    • Identification of novel integral membrane proteins of the nuclear envelope with potential disease links using subtractive proteomics
    • discussion 76-80, 227-30
    • Schirmer EC, Florens L, Guan T, Yates JR, Gerace L: Identification of novel integral membrane proteins of the nuclear envelope with potential disease links using subtractive proteomics. Novartis Found Symp 2005, 264:63-76; discussion 76-80, 227-30.
    • (2005) Novartis Found Symp , vol.264 , pp. 63-76
    • Schirmer, E.C.1    Florens, L.2    Guan, T.3    Yates, J.R.4    Gerace, L.5
  • 31
    • 0035197416 scopus 로고    scopus 로고
    • Inner nuclear membrane proteins: Functions and targeting
    • Holmer L, Worman HJ: Inner nuclear membrane proteins: functions and targeting. Cell Mol Life Sci 2001, 58:1741-1747.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 1741-1747
    • Holmer, L.1    Worman, H.J.2
  • 34
    • 15444374750 scopus 로고    scopus 로고
    • The AAA+ protein torsinA interacts with a conserved domain present in LAP1 and a novel ER protein
    • Goodchild RE, Dauer WT: The AAA+ protein torsinA interacts with a conserved domain present in LAP1 and a novel ER protein. J Cell Biol 2005, 168:855-862.
    • (2005) J Cell Biol , vol.168 , pp. 855-862
    • Goodchild, R.E.1    Dauer, W.T.2
  • 35
    • 30544449477 scopus 로고    scopus 로고
    • LEM2 is a novel MAN1-related inner nuclear membrane protein associated with A-type lamins
    • Brachner A, Reipert S, Foisner R, Gotzmann J: LEM2 is a novel MAN1-related inner nuclear membrane protein associated with A-type lamins. J Cell Sci 2005, 118:5797-5810.
    • (2005) J Cell Sci , vol.118 , pp. 5797-5810
    • Brachner, A.1    Reipert, S.2    Foisner, R.3    Gotzmann, J.4
  • 37
    • 0347927630 scopus 로고    scopus 로고
    • SANE, a novel LEM domain protein, regulates bone morphogenetic protein signaling through interaction with Smad1
    • Raju GP, Dimova N, Klein PS, Huang HC: SANE, a novel LEM domain protein, regulates bone morphogenetic protein signaling through interaction with Smad1. J Biol Chem 2003, 278:428-437.
    • (2003) J Biol Chem , vol.278 , pp. 428-437
    • Raju, G.P.1    Dimova, N.2    Klein, P.S.3    Huang, H.C.4
  • 38
    • 0037959860 scopus 로고    scopus 로고
    • XMAN1, an inner nuclear membrane protein, antagonizes BMP signaling by interacting with Smad1 in Xenopus embryos
    • Osada S, Ohmori SY, Taira M: XMAN1, an inner nuclear membrane protein, antagonizes BMP signaling by interacting with Smad1 in Xenopus embryos. Development 2003, 130:1783-1794.
    • (2003) Development , vol.130 , pp. 1783-1794
    • Osada, S.1    Ohmori, S.Y.2    Taira, M.3
  • 39
    • 13544264752 scopus 로고    scopus 로고
    • MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-beta signaling
    • Lin F, Morrison JM, Wu W, Worman HJ: MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-beta signaling. Hum Mol Genet 2005, 14:437-445.
    • (2005) Hum Mol Genet , vol.14 , pp. 437-445
    • Lin, F.1    Morrison, J.M.2    Wu, W.3    Worman, H.J.4
  • 40
    • 18144411595 scopus 로고    scopus 로고
    • The integral inner nuclear membrane protein MAN1 physically interacts with the R-Smad proteins to repress signaling by the transforming growth factor-{beta} superfamily of cytokines
    • Pan D, Estevez-Salmeron LD, Stroschein SL, Zhu X, He J, Zhou S, Luo K: The integral inner nuclear membrane protein MAN1 physically interacts with the R-Smad proteins to repress signaling by the transforming growth factor-{beta} superfamily of cytokines. J Biol Chem 2005, 280:15992-16001.
    • (2005) J Biol Chem , vol.280 , pp. 15992-16001
    • Pan, D.1    Estevez-Salmeron, L.D.2    Stroschein, S.L.3    Zhu, X.4    He, J.5    Zhou, S.6    Luo, K.7
  • 41
    • 27144543784 scopus 로고    scopus 로고
    • Scaffolding microdomains and beyond: The function of reggie/flotillin proteins
    • Langhorst MF, Reuter A, Stuermer CA: Scaffolding microdomains and beyond: the function of reggie/flotillin proteins. Cell Mol Life Sci 2005, 62:2228-2240.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2228-2240
    • Langhorst, M.F.1    Reuter, A.2    Stuermer, C.A.3
  • 42
    • 23844462163 scopus 로고    scopus 로고
    • Flotillins and the PHB domain protein family: Rafts, worms and anaesthetics
    • Morrow IC, Parton RG: Flotillins and the PHB domain protein family: rafts, worms and anaesthetics. Traffic 2005, 6:725-740.
    • (2005) Traffic , vol.6 , pp. 725-740
    • Morrow, I.C.1    Parton, R.G.2
  • 43
    • 12344260000 scopus 로고    scopus 로고
    • Polarized sorting in epithelial cells: Raft clustering and the biogenesis of the apical membrane
    • Schuck S, Simons K: Polarized sorting in epithelial cells: raft clustering and the biogenesis of the apical membrane. J Cell Sci 2004, 117:5955-5964.
    • (2004) J Cell Sci , vol.117 , pp. 5955-5964
    • Schuck, S.1    Simons, K.2
  • 44
    • 0242268532 scopus 로고    scopus 로고
    • Lipid rafts and caveolae as portals for endocytosis: New insights and common mechanisms
    • Parton RG, Richards AA: Lipid rafts and caveolae as portals for endocytosis: new insights and common mechanisms. Traffic 2003, 4:724-738.
    • (2003) Traffic , vol.4 , pp. 724-738
    • Parton, R.G.1    Richards, A.A.2
  • 45
    • 29144483525 scopus 로고    scopus 로고
    • Toward understanding the dynamics of membrane-raft-based molecular interactions
    • Kusumi A, Suzuki K: Toward understanding the dynamics of membrane-raft-based molecular interactions. Biochim Biophys Acta 2005, 1746:234-251.
    • (2005) Biochim Biophys Acta , vol.1746 , pp. 234-251
    • Kusumi, A.1    Suzuki, K.2
  • 46
    • 0029013986 scopus 로고
    • Induced and spontaneous neuritogenesis are associated with enhanced expression of ganglioside GM1 in the nuclear membrane
    • Wu G, Lu ZH, Ledeen RW: Induced and spontaneous neuritogenesis are associated with enhanced expression of ganglioside GM1 in the nuclear membrane. J Neurosci 1995, 15:3739-3746.
    • (1995) J Neurosci , vol.15 , pp. 3739-3746
    • Wu, G.1    Lu, Z.H.2    Ledeen, R.W.3
  • 48
    • 0028987552 scopus 로고
    • Neutral sphingomyelinase: Localization in rat liver nuclei and involvement in regeneration/proliferation
    • Alessenko A, Chatterjee S: Neutral sphingomyelinase: localization in rat liver nuclei and involvement in regeneration/proliferation. Mol Cell Biochem 1995, 143:169-174.
    • (1995) Mol Cell Biochem , vol.143 , pp. 169-174
    • Alessenko, A.1    Chatterjee, S.2
  • 49
    • 33644874204 scopus 로고    scopus 로고
    • The hexosamine signaling pathway: Deciphering the "O-GlcNAc code"
    • Love DC, Hanover JA: The hexosamine signaling pathway: deciphering the "O-GlcNAc code". Sci STKE 2005, 2005:re13.
    • (2005) Sci STKE 2005 , vol.re13
    • Love, D.C.1    Hanover, J.A.2
  • 50
    • 3042613480 scopus 로고    scopus 로고
    • O-GlcNAc a sensor of cellular state: The role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress
    • Zachara NE, Hart GW: O-GlcNAc a sensor of cellular state: the role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress. Biochim Biophys Acta 2004, 1673:13-28.
    • (2004) Biochim Biophys Acta , vol.1673 , pp. 13-28
    • Zachara, N.E.1    Hart, G.W.2
  • 51
    • 3543085572 scopus 로고    scopus 로고
    • Ganglioside/glycosphingolipid turnover: New concepts
    • Tettamanti G: Ganglioside/glycosphingolipid turnover: new concepts. Glycoconj J 2004, 20:301-317.
    • (2004) Glycoconj J , vol.20 , pp. 301-317
    • Tettamanti, G.1
  • 52
    • 0037135626 scopus 로고    scopus 로고
    • The Ceramide-centric universe of lipid-mediated cell regulation: Stress encounters of the lipid kind
    • Hannun YA, Obeid LM: The Ceramide-centric universe of lipid-mediated cell regulation: stress encounters of the lipid kind. J Biol Chem 2002, 277:25847-25850.
    • (2002) J Biol Chem , vol.277 , pp. 25847-25850
    • Hannun, Y.A.1    Obeid, L.M.2
  • 53
    • 3543114272 scopus 로고    scopus 로고
    • Biologically active sphingolipids in cancer pathogenesis and treatment
    • Ogretmen B, Hannun YA: Biologically active sphingolipids in cancer pathogenesis and treatment. Nat Rev Cancer 2004, 4:604-616.
    • (2004) Nat Rev Cancer , vol.4 , pp. 604-616
    • Ogretmen, B.1    Hannun, Y.A.2
  • 54
    • 17744367455 scopus 로고    scopus 로고
    • Integral membrane lipid phosphatases/phosphotransferases: Common structure and diverse functions
    • Sigal YJ, McDermott MI, Morris AJ: Integral membrane lipid phosphatases/ phosphotransferases: common structure and diverse functions. Biochem J 2005, 387:281-293.
    • (2005) Biochem J , vol.387 , pp. 281-293
    • Sigal, Y.J.1    McDermott, M.I.2    Morris, A.J.3
  • 55
    • 28844452498 scopus 로고    scopus 로고
    • Lipid phosphate phosphatases and lipid phosphate signalling
    • Pyne S, Long JS, Ktistakis NT, Pyne NJ: Lipid phosphate phosphatases and lipid phosphate signalling. Biochem Soc Trans 2005, 33:1370-1374.
    • (2005) Biochem Soc Trans , vol.33 , pp. 1370-1374
    • Pyne, S.1    Long, J.S.2    Ktistakis, N.T.3    Pyne, N.J.4
  • 56
    • 0042887042 scopus 로고    scopus 로고
    • The emerging role of lysophosphatidic acid in cancer
    • Mills GB, Moolenaar WH: The emerging role of lysophosphatidic acid in cancer. Nat Rev Cancer 2003, 3:582-591.
    • (2003) Nat Rev Cancer , vol.3 , pp. 582-591
    • Mills, G.B.1    Moolenaar, W.H.2
  • 57
    • 0022981355 scopus 로고
    • Developmental progression of myosin gene expression in cultured muscle cells
    • Silberstein L, Webster SG, Travis M, Blau HM: Developmental progression of myosin gene expression in cultured muscle cells. Cell 1986, 46:1075-1081.
    • (1986) Cell , vol.46 , pp. 1075-1081
    • Silberstein, L.1    Webster, S.G.2    Travis, M.3    Blau, H.M.4
  • 58
    • 84872275435 scopus 로고    scopus 로고
    • [http://www.scripps.edu/researchservices/dna_array/]
  • 59
    • 23844551199 scopus 로고    scopus 로고
    • Stochastic models inspired by hybridization theory for short oligonucleotide arrays
    • Wu Z, Irizarry RA: Stochastic models inspired by hybridization theory for short oligonucleotide arrays. J Comput Biol 2005, 12:882-893.
    • (2005) J Comput Biol , vol.12 , pp. 882-893
    • Wu, Z.1    Irizarry, R.A.2
  • 60
    • 0034948896 scopus 로고    scopus 로고
    • A Bayesian framework for the analysis of microarray expression data: Regularized t -test and statistical inferences of gene changes
    • Baldi P, Long AD: A Bayesian framework for the analysis of microarray expression data: regularized t -test and statistical inferences of gene changes. Bioinformatics 2001, 17:509-519.
    • (2001) Bioinformatics , vol.17 , pp. 509-519
    • Baldi, P.1    Long, A.D.2
  • 61
    • 0023257987 scopus 로고
    • Monoclonal antibodies identify a group of nuclear pore complex glycoproteins
    • Snow CM, Senior A, Gerace L: Monoclonal antibodies identify a group of nuclear pore complex glycoproteins. J Cell Biol 1987, 104:1143-1156.
    • (1987) J Cell Biol , vol.104 , pp. 1143-1156
    • Snow, C.M.1    Senior, A.2    Gerace, L.3
  • 62
    • 0019304939 scopus 로고
    • Colorimetric determination of phospholipids with ammonium ferrothiocyanate
    • Stewart JC: Colorimetric determination of phospholipids with ammonium ferrothiocyanate. Anal Biochem 1980, 104:10-14.
    • (1980) Anal Biochem , vol.104 , pp. 10-14
    • Stewart, J.C.1
  • 63
    • 84872269676 scopus 로고    scopus 로고
    • [http://ellerbruch.nmu.edu/cs255/jnord/boxplot].


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