메뉴 건너뛰기




Volumn 208, Issue 6, 2015, Pages 671-681

The nucleoporin gp210/Nup210 controls muscle differentiation by regulating nuclear envelope/ER homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

CALNEXIN; CASPASE 12; CASPASE 3; GP210 PROTEIN; NUCLEOPORIN; NUP210 PROTEIN; SHORT HAIRPIN RNA; UNCLASSIFIED DRUG; CASPASE; NUP210 PROTEIN, MOUSE;

EID: 84925355181     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201410047     Document Type: Article
Times cited : (50)

References (43)
  • 1
    • 34250777112 scopus 로고    scopus 로고
    • The nuclear envelope and transcriptional control
    • Akhtar, A., and S.M. Gasser. 2007. The nuclear envelope and transcriptional control. Nat. Rev. Genet. 8:507-517. http://dx.doi.org/10.1038/nrg2122.
    • (2007) Nat. Rev. Genet , vol.8 , pp. 507-517
    • Akhtar, A.1    Gasser, S.M.2
  • 2
    • 0035800787 scopus 로고    scopus 로고
    • Proteomic analysis of nucleoporin interacting proteins
    • Allen, N.P., L. Huang, A. Burlingame, and M. Rexach. 2001. Proteomic analysis of nucleoporin interacting proteins. J. Biol. Chem. 276:29268-29274. http://dx.doi.org/10.1074/jbc.M102629200.
    • (2001) J. Biol. Chem , vol.276 , pp. 29268-29274
    • Allen, N.P.1    Huang, L.2    Burlingame, A.3    Rexach, M.4
  • 3
    • 84855272573 scopus 로고    scopus 로고
    • Stress-induced C/EBP homology protein (CHOP) represses MyoD transcription to delay myoblast differentiation
    • Alter, J., and E. Bengal. 2011. Stress-induced C/EBP homology protein (CHOP) represses MyoD transcription to delay myoblast differentiation. PLoS ONE. 6:e29498. http://dx.doi.org/10.1371/journal.pone.0029498.
    • (2011) PLoS ONE , vol.6
    • Alter, J.1    Bengal, E.2
  • 4
    • 70350417325 scopus 로고    scopus 로고
    • Bile acids: regulation of apoptosis by ursodeoxycholic acid
    • Amaral, J.D., R.J. Viana, R.M. Ramalho, C.J. Steer, and C.M. Rodrigues. 2009. Bile acids: regulation of apoptosis by ursodeoxycholic acid. J. Lipid Res. 50:1721-1734. http://dx.doi.org/10.1194/jlr.R900011-JLR200.
    • (2009) J. Lipid Res , vol.50 , pp. 1721-1734
    • Amaral, J.D.1    Viana, R.J.2    Ramalho, R.M.3    Steer, C.J.4    Rodrigues, C.M.5
  • 5
    • 34047262162 scopus 로고    scopus 로고
    • Transcriptional regulation at the nuclear pore complex
    • Brown, C.R., and P.A. Silver. 2007. Transcriptional regulation at the nuclear pore complex. Curr. Opin. Genet. Dev. 17:100-106. http://dx.doi.org/10.1016/j.gde.2007.02.005.
    • (2007) Curr. Opin. Genet. Dev , vol.17 , pp. 100-106
    • Brown, C.R.1    Silver, P.A.2
  • 6
    • 75749103380 scopus 로고    scopus 로고
    • Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes
    • Capelson, M., Y. Liang, R. Schulte, W. Mair, U. Wagner, and M.W. Hetzer. 2010. Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes. Cell. 140:372-383. http://dx.doi.org/10.1016/j.cell.2009.12.054.
    • (2010) Cell , vol.140 , pp. 372-383
    • Capelson, M.1    Liang, Y.2    Schulte, R.3    Mair, W.4    Wagner, U.5    Hetzer, M.W.6
  • 7
    • 0037008997 scopus 로고    scopus 로고
    • Proteomic analysis of the mammalian nuclear pore complex
    • Cronshaw, J.M., A.N. Krutchinsky, W. Zhang, B.T. Chait, and M.J. Matunis. 2002. Proteomic analysis of the mammalian nuclear pore complex. J. Cell Biol. 158:915-927. http://dx.doi.org/10.1083/jcb.200206106.
    • (2002) J. Cell Biol , vol.158 , pp. 915-927
    • Cronshaw, J.M.1    Krutchinsky, A.N.2    Zhang, W.3    Chait, B.T.4    Matunis, M.J.5
  • 8
    • 84857031394 scopus 로고    scopus 로고
    • A change in nuclear pore complex composition regulates cell differentiation
    • D'Angelo, M.A., J.S. Gomez-Cavazos, A. Mei, D.H. Lackner, and M.W. Hetzer. 2012. A change in nuclear pore complex composition regulates cell differentiation. Dev. Cell. 22:446-458. http://dx.doi.org/10.1016/j.devcel.2011.11.021.
    • (2012) Dev. Cell , vol.22 , pp. 446-458
    • D'Angelo, M.A.1    Gomez-Cavazos, J.S.2    Mei, A.3    Lackner, D.H.4    Hetzer, M.W.5
  • 9
    • 84875604713 scopus 로고    scopus 로고
    • Cancer biology and the nuclear envelope: a convoluted relationship
    • de las Heras, J.I., D.G. Batrakou, and E.C. Schirmer. 2013. Cancer biology and the nuclear envelope: a convoluted relationship. Semin. Cancer Biol. 23:125-137. http://dx.doi.org/10.1016/j.semcancer.2012.01.008.
    • (2013) Semin. Cancer Biol , vol.23 , pp. 125-137
    • de las Heras, J.I.1    Batrakou, D.G.2    Schirmer, E.C.3
  • 10
    • 84855217862 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in skeletal muscle: origin and metabolic consequences
    • Deldicque, L., P. Hespel, and M. Francaux. 2012. Endoplasmic reticulum stress in skeletal muscle: origin and metabolic consequences. Exerc. Sport Sci. Rev. 40:43-49. http://dx.doi.org/10.1097/JES.0b013e3182355e8c.
    • (2012) Exerc. Sport Sci. Rev , vol.40 , pp. 43-49
    • Deldicque, L.1    Hespel, P.2    Francaux, M.3
  • 11
    • 4143137715 scopus 로고    scopus 로고
    • Dynamic properties of nuclear pore complex proteins in gp210 deficient cells
    • Eriksson, C., C. Rustum, and E. Hallberg. 2004. Dynamic properties of nuclear pore complex proteins in gp210 deficient cells. FEBS Lett. 572:261-265. http://dx.doi.org/10.1016/j.febslet.2004.07.044.
    • (2004) FEBS Lett , vol.572 , pp. 261-265
    • Eriksson, C.1    Rustum, C.2    Hallberg, E.3
  • 12
    • 0020399177 scopus 로고
    • Identification of a major polypeptide of the nuclear pore complex
    • Gerace, L., Y. Ottaviano, and C. Kondor-Koch. 1982. Identification of a major polypeptide of the nuclear pore complex. J. Cell Biol. 95:826-837. http://dx.doi.org/10.1083/jcb.95.3.826.
    • (1982) J. Cell Biol , vol.95 , pp. 826-837
    • Gerace, L.1    Ottaviano, Y.2    Kondor-Koch, C.3
  • 13
    • 84871929542 scopus 로고    scopus 로고
    • Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins
    • Gomez-Cavazos, J.S., and M.W. Hetzer. 2012. Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins. Curr. Opin. Cell Biol. 24:775-783. http://dx.doi.org/10.1016/j.ceb.2012.08.008.
    • (2012) Curr. Opin. Cell Biol , vol.24 , pp. 775-783
    • Gomez-Cavazos, J.S.1    Hetzer, M.W.2
  • 14
    • 0028851245 scopus 로고
    • Depletion of calcium from the lumen of endoplasmic reticulum reversibly inhibits passive diffusion and signalmediated transport into the nucleus
    • Greber, U.F., and L. Gerace. 1995. Depletion of calcium from the lumen of endoplasmic reticulum reversibly inhibits passive diffusion and signalmediated transport into the nucleus. J. Cell Biol. 128:5-14. http://dx.doi.org/10.1083/jcb.128.1.5.
    • (1995) J. Cell Biol , vol.128 , pp. 5-14
    • Greber, U.F.1    Gerace, L.2
  • 15
    • 0036223543 scopus 로고    scopus 로고
    • Nup98 is a mobile nucleoporin with transcription-dependent dynamics
    • Griffis, E.R., N. Altan, J. Lippincott-Schwartz, and M.A. Powers. 2002. Nup98 is a mobile nucleoporin with transcription-dependent dynamics. Mol. Biol. Cell. 13:1282-1297. http://dx.doi.org/10.1091/mbc.01-11-0538.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1282-1297
    • Griffis, E.R.1    Altan, N.2    Lippincott-Schwartz, J.3    Powers, M.A.4
  • 16
    • 79959423595 scopus 로고    scopus 로고
    • The structure of the nuclear pore complex
    • Hoelz, A., E.W. Debler, and G. Blobel. 2011. The structure of the nuclear pore complex. Annu. Rev. Biochem. 80:613-643. http://dx.doi.org/10.1146/annurev-biochem-060109-151030.
    • (2011) Annu. Rev. Biochem , vol.80 , pp. 613-643
    • Hoelz, A.1    Debler, E.W.2    Blobel, G.3
  • 17
    • 70350524986 scopus 로고    scopus 로고
    • Overlapping functions of nuclear envelope proteins NET25 (Lem2) and emerin in regulation of extracellular signal-regulated kinase signaling in myoblast differentiation
    • Huber, M.D., T. Guan, and L. Gerace. 2009. Overlapping functions of nuclear envelope proteins NET25 (Lem2) and emerin in regulation of extracellular signal-regulated kinase signaling in myoblast differentiation. Mol. Cell. Biol. 29:5718-5728. http://dx.doi.org/10.1128/MCB.00270-09.
    • (2009) Mol. Cell. Biol , vol.29 , pp. 5718-5728
    • Huber, M.D.1    Guan, T.2    Gerace, L.3
  • 18
    • 0035028511 scopus 로고    scopus 로고
    • Apoptosis and syncytial fusion in human placental trophoblast and skeletal muscle
    • Huppertz, B., D.S. Tews, and P. Kaufmann. 2001. Apoptosis and syncytial fusion in human placental trophoblast and skeletal muscle. Int. Rev. Cytol. 205:215-253. http://dx.doi.org/10.1016/S0074-7696(01)05005-7.
    • (2001) Int. Rev. Cytol , vol.205 , pp. 215-253
    • Huppertz, B.1    Tews, D.S.2    Kaufmann, P.3
  • 19
    • 79951555476 scopus 로고    scopus 로고
    • Functional interactions between nucleoporins and chromatin
    • Liang, Y., and M.W. Hetzer. 2011. Functional interactions between nucleoporins and chromatin. Curr. Opin. Cell Biol. 23:65-70. http://dx.doi.org/10.1016/j.ceb.2010.09.008.
    • (2011) Curr. Opin. Cell Biol , vol.23 , pp. 65-70
    • Liang, Y.1    Hetzer, M.W.2
  • 20
    • 44449129923 scopus 로고    scopus 로고
    • Nuclear pore composition regulates neural stem/progenitor cell differentiation in the mouse embryo
    • Lupu, F., A. Alves, K. Anderson, V. Doye, and E. Lacy. 2008. Nuclear pore composition regulates neural stem/progenitor cell differentiation in the mouse embryo. Dev. Cell. 14:831-842. http://dx.doi.org/10.1016/j.devcel.2008.03.011.
    • (2008) Dev. Cell , vol.14 , pp. 831-842
    • Lupu, F.1    Alves, A.2    Anderson, K.3    Doye, V.4    Lacy, E.5
  • 21
    • 17144404877 scopus 로고    scopus 로고
    • Comparative genomics, evolution and origins of the nuclear envelope and nuclear pore complex
    • Mans, B.J., V. Anantharaman, L. Aravind, and E.V. Koonin. 2004. Comparative genomics, evolution and origins of the nuclear envelope and nuclear pore complex. Cell Cycle. 3:1612-1637. http://dx.doi.org/10.4161/cc.3.12.1316.
    • (2004) Cell Cycle , vol.3 , pp. 1612-1637
    • Mans, B.J.1    Anantharaman, V.2    Aravind, L.3    Koonin, E.V.4
  • 22
    • 0037072937 scopus 로고    scopus 로고
    • An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12
    • Morishima, N., K. Nakanishi, H. Takenouchi, T. Shibata, and Y. Yasuhiko. 2002. An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12. J. Biol. Chem. 277:34287-34294. http://dx.doi.org/10.1074/jbc.M204973200.
    • (2002) J. Biol. Chem , vol.277 , pp. 34287-34294
    • Morishima, N.1    Nakanishi, K.2    Takenouchi, H.3    Shibata, T.4    Yasuhiko, Y.5
  • 23
    • 80053425920 scopus 로고    scopus 로고
    • Activating transcription factor-6 (ATF6) mediates apoptosis with reduction of myeloid cell leukemia sequence 1 (Mcl-1) protein via induction of WW domain binding protein 1
    • Morishima, N., K. Nakanishi, and A. Nakano. 2011. Activating transcription factor-6 (ATF6) mediates apoptosis with reduction of myeloid cell leukemia sequence 1 (Mcl-1) protein via induction of WW domain binding protein 1. J. Biol. Chem. 286:35227-35235. http://dx.doi.org/10.1074/jbc.M111.233502.
    • (2011) J. Biol. Chem , vol.286 , pp. 35227-35235
    • Morishima, N.1    Nakanishi, K.2    Nakano, A.3
  • 24
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa, T., H. Zhu, N. Morishima, E. Li, J. Xu, B.A. Yankner, and J. Yuan. 2000. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature. 403:98-103. http://dx.doi.org/10.1038/47513.
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 26
    • 22344455409 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress signaling transmitted by ATF6 mediates apoptosis during muscle development
    • Nakanishi, K., T. Sudo, and N. Morishima. 2005. Endoplasmic reticulum stress signaling transmitted by ATF6 mediates apoptosis during muscle development. J. Cell Biol. 169:555-560. http://dx.doi.org/10.1083/jcb.200412024.
    • (2005) J. Cell Biol , vol.169 , pp. 555-560
    • Nakanishi, K.1    Sudo, T.2    Morishima, N.3
  • 27
    • 84932605338 scopus 로고    scopus 로고
    • Transient Ca2+ depletion from the endoplasmic reticulum is critical for skeletal myoblast differentiation
    • Nakanishi, K., K. Kakiguchi, S. Yonemura, A. Nakano, and N. Morishima. 2015. Transient Ca2+ depletion from the endoplasmic reticulum is critical for skeletal myoblast differentiation. FASEB J. 29:1-13.
    • (2015) FASEB J , vol.29 , pp. 1-13
    • Nakanishi, K.1    Kakiguchi, K.2    Yonemura, S.3    Nakano, A.4    Morishima, N.5
  • 28
    • 0032874218 scopus 로고    scopus 로고
    • cDNA cloning and embryonic expression of mouse nuclear pore membrane glycoprotein 210 mRNA
    • Olsson, M., M. Ekblom, L. Fecker, M. Kurkinen, and P. Ekblom. 1999. cDNA cloning and embryonic expression of mouse nuclear pore membrane glycoprotein 210 mRNA. Kidney Int. 56:827-838. http://dx.doi.org/10.1046/j.1523-1755.1999.00618.x.
    • (1999) Kidney Int , vol.56 , pp. 827-838
    • Olsson, M.1    Ekblom, M.2    Fecker, L.3    Kurkinen, M.4    Ekblom, P.5
  • 29
    • 0346992146 scopus 로고    scopus 로고
    • Limited expression of nuclear pore membrane glycoprotein 210 in cell lines and tissues suggests cell-type specific nuclear pores in metazoans
    • Olsson, M., S. Schéele, and P. Ekblom. 2004. Limited expression of nuclear pore membrane glycoprotein 210 in cell lines and tissues suggests cell-type specific nuclear pores in metazoans. Exp. Cell Res. 292:359-370. http://dx.doi.org/10.1016/j.yexcr.2003.09.014.
    • (2004) Exp. Cell Res , vol.292 , pp. 359-370
    • Olsson, M.1    Schéele, S.2    Ekblom, P.3
  • 31
    • 33748069813 scopus 로고    scopus 로고
    • Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes
    • Özcan, U., E. Yilmaz, L. Özcan, M. Furuhashi, E. Vaillancourt, R.O. Smith, C.Z. Görgün, and G.S. Hotamisligil. 2006. Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes. Science. 313:1137-1140. http://dx.doi.org/10.1126/science.1128294.
    • (2006) Science , vol.313 , pp. 1137-1140
    • Özcan, U.1    Yilmaz, E.2    Özcan, L.3    Furuhashi, M.4    Vaillancourt, E.5    Smith, R.O.6    Görgün, C.Z.7    Hotamisligil, G.S.8
  • 32
    • 7944236264 scopus 로고    scopus 로고
    • Mapping the dynamic organization of the nuclear pore complex inside single living cells
    • Rabut, G., V. Doye, and J. Ellenberg. 2004. Mapping the dynamic organization of the nuclear pore complex inside single living cells. Nat. Cell Biol. 6:1114-1121. http://dx.doi.org/10.1038/ncb1184.
    • (2004) Nat. Cell Biol , vol.6 , pp. 1114-1121
    • Rabut, G.1    Doye, V.2    Ellenberg, J.3
  • 33
    • 84867786612 scopus 로고    scopus 로고
    • Nuclear pore complex composition: a new regulator of tissue-specific and developmental functions
    • Raices, M., and M.A. D'Angelo. 2012. Nuclear pore complex composition: a new regulator of tissue-specific and developmental functions. Nat. Rev. Mol. Cell Biol. 13:687-699. http://dx.doi.org/10.1038/nrm3461.
    • (2012) Nat. Rev. Mol. Cell Biol , vol.13 , pp. 687-699
    • Raices, M.1    D'Angelo, M.A.2
  • 35
    • 84892759344 scopus 로고    scopus 로고
    • Apoptosis in differentiating C2C12 muscle cells selectively targets Bcl-2-deficient myotubes
    • Schöneich, C., E. Dremina, N. Galeva, and V. Sharov. 2014. Apoptosis in differentiating C2C12 muscle cells selectively targets Bcl-2-deficient myotubes. Apoptosis. 19:42-57. http://dx.doi.org/10.1007/s10495-013-0922-7.
    • (2014) Apoptosis , vol.19 , pp. 42-57
    • Schöneich, C.1    Dremina, E.2    Galeva, N.3    Sharov, V.4
  • 36
    • 23144440940 scopus 로고    scopus 로고
    • PRALINE: a multiple sequence alignment toolbox that integrates homology-extended and secondary structure information
    • Simossis, V.A., and J. Heringa. 2005. PRALINE: a multiple sequence alignment toolbox that integrates homology-extended and secondary structure information. Nucleic Acids Res. 33(Suppl. 2):W289-W294. http://dx.doi.org/10.1093/nar/gki390.
    • (2005) Nucleic Acids Res , vol.33 , pp. W289-W294
    • Simossis, V.A.1    Heringa, J.2
  • 37
    • 33646808579 scopus 로고    scopus 로고
    • Nuclear pore complex assembly and maintenance in POM121-and gp210-deficient cells
    • Stavru, F., G. Nautrup-Pedersen, V.C. Cordes, and D. Görlich. 2006. Nuclear pore complex assembly and maintenance in POM121-and gp210-deficient cells. J. Cell Biol. 173:477-483. http://dx.doi.org/10.1083/jcb.200601002.
    • (2006) J. Cell Biol , vol.173 , pp. 477-483
    • Stavru, F.1    Nautrup-Pedersen, G.2    Cordes, V.C.3    Görlich, D.4
  • 38
    • 84872720740 scopus 로고    scopus 로고
    • Solution structure of the Big domain from Streptococcus pneumoniae reveals a novel Ca2+-binding module
    • Wang, T., J. Zhang, X. Zhang, C. Xu, and X. Tu. 2013. Solution structure of the Big domain from Streptococcus pneumoniae reveals a novel Ca2+-binding module. Sci Rep. 3:1079. http://dx.doi.org/10.1038/srep01079.
    • (2013) Sci Rep , vol.3 , pp. 1079
    • Wang, T.1    Zhang, J.2    Zhang, X.3    Xu, C.4    Tu, X.5
  • 39
    • 0027043255 scopus 로고
    • The single transmembrane segment of gp210 is sufficient for sorting to the pore membrane domain of the nuclear envelope
    • Wozniak, R.W., and G. Blobel. 1992. The single transmembrane segment of gp210 is sufficient for sorting to the pore membrane domain of the nuclear envelope. J. Cell Biol. 119:1441-1449. http://dx.doi.org/10.1083/jcb.119.6.1441.
    • (1992) J. Cell Biol , vol.119 , pp. 1441-1449
    • Wozniak, R.W.1    Blobel, G.2
  • 40
    • 0024360678 scopus 로고
    • Primary structure analysis of an integral membrane glycoprotein of the nuclear pore
    • Wozniak, R.W., E. Bartnik, and G. Blobel. 1989. Primary structure analysis of an integral membrane glycoprotein of the nuclear pore. J. Cell Biol. 108:2083-2092. http://dx.doi.org/10.1083/jcb.108.6.2083.
    • (1989) J. Cell Biol , vol.108 , pp. 2083-2092
    • Wozniak, R.W.1    Bartnik, E.2    Blobel, G.3
  • 41
    • 0036725164 scopus 로고    scopus 로고
    • Effect of tauroursodeoxycholic acid on endoplasmic reticulum stress-induced caspase-12 activation
    • Xie, Q., V.I. Khaoustov, C.C. Chung, J. Sohn, B. Krishnan, D.E. Lewis, and B. Yoffe. 2002. Effect of tauroursodeoxycholic acid on endoplasmic reticulum stress-induced caspase-12 activation. Hepatology. 36:592-601. http://dx.doi.org/10.1053/jhep.2002.35441.
    • (2002) Hepatology , vol.36 , pp. 592-601
    • Xie, Q.1    Khaoustov, V.I.2    Chung, C.C.3    Sohn, J.4    Krishnan, B.5    Lewis, D.E.6    Yoffe, B.7
  • 42
    • 34548172495 scopus 로고    scopus 로고
    • Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6α and XBP1
    • Yamamoto, K., T. Sato, T. Matsui, M. Sato, T. Okada, H. Yoshida, A. Harada, and K. Mori. 2007. Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6α and XBP1. Dev. Cell. 13:365-376. http://dx.doi.org/10.1016/j.devcel.2007.07.018.
    • (2007) Dev. Cell , vol.13 , pp. 365-376
    • Yamamoto, K.1    Sato, T.2    Matsui, T.3    Sato, M.4    Okada, T.5    Yoshida, H.6    Harada, A.7    Mori, K.8
  • 43
    • 57349179985 scopus 로고    scopus 로고
    • Mutation in nuclear pore component NUP155 leads to atrial fibrillation and early sudden cardiac death
    • Zhang, X., S. Chen, S. Yoo, S. Chakrabarti, T. Zhang, T. Ke, C. Oberti, S.L. Yong, F. Fang, L. Li, et al. 2008. Mutation in nuclear pore component NUP155 leads to atrial fibrillation and early sudden cardiac death. Cell. 135:1017-1027. http://dx.doi.org/10.1016/j.cell.2008.10.022.
    • (2008) Cell , vol.135 , pp. 1017-1027
    • Zhang, X.1    Chen, S.2    Yoo, S.3    Chakrabarti, S.4    Zhang, T.5    Ke, T.6    Oberti, C.7    Yong, S.L.8    Fang, F.9    Li, L.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.