메뉴 건너뛰기




Volumn 34, Issue , 2015, Pages 135-141

Establishment of NE asymmetry-targeting of membrane proteins to the inner nuclear membrane

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H4; LAMIN A; LAMIN B; LAMIN C; MEMBRANE PROTEIN;

EID: 84944680459     PISSN: 09550674     EISSN: 18790410     Source Type: Journal    
DOI: 10.1016/j.ceb.2015.04.005     Document Type: Review
Times cited : (60)

References (58)
  • 2
    • 84871929542 scopus 로고    scopus 로고
    • Outfits for different occasions: tissue-specific roles of nuclear envelope proteins
    • Gomez-Cavazos J.S., Hetzer M.W. Outfits for different occasions: tissue-specific roles of nuclear envelope proteins. Curr Opin Cell Biol 2012, 24:775-783.
    • (2012) Curr Opin Cell Biol , vol.24 , pp. 775-783
    • Gomez-Cavazos, J.S.1    Hetzer, M.W.2
  • 3
    • 84901505712 scopus 로고    scopus 로고
    • NET gains and losses: the role of changing nuclear envelope proteomes in genome regulation
    • Wong X., Luperchio T.R., Reddy K.L. NET gains and losses: the role of changing nuclear envelope proteomes in genome regulation. Curr Opin Cell Biol 2014, 28C:105-120.
    • (2014) Curr Opin Cell Biol , vol.28 C , pp. 105-120
    • Wong, X.1    Luperchio, T.R.2    Reddy, K.L.3
  • 4
    • 84899567326 scopus 로고    scopus 로고
    • Breaching the nuclear envelope in development and disease
    • Hatch E., Hetzer M. Breaching the nuclear envelope in development and disease. J Cell Biol 2014, 205:133-141.
    • (2014) J Cell Biol , vol.205 , pp. 133-141
    • Hatch, E.1    Hetzer, M.2
  • 5
    • 84897036591 scopus 로고    scopus 로고
    • Mechanisms and dynamics of nuclear lamina-genome interactions
    • Amendola M., van Steensel B. Mechanisms and dynamics of nuclear lamina-genome interactions. Curr Opin Cell Biol 2014, 28:61-68.
    • (2014) Curr Opin Cell Biol , vol.28 , pp. 61-68
    • Amendola, M.1    van Steensel, B.2
  • 6
    • 84902465522 scopus 로고    scopus 로고
    • Functional architecture of the cell's nucleus in development, aging, and disease
    • Burke B., Stewart C.L. Functional architecture of the cell's nucleus in development, aging, and disease. Curr Top Dev Biol 2014, 109:1-52.
    • (2014) Curr Top Dev Biol , vol.109 , pp. 1-52
    • Burke, B.1    Stewart, C.L.2
  • 7
    • 0025666495 scopus 로고
    • Internuclear exchange of an inner nuclear membrane protein (p55) in heterokaryons: in vivo evidence for the interaction of p55 with the nuclear lamina
    • Powell L., Burke B. Internuclear exchange of an inner nuclear membrane protein (p55) in heterokaryons: in vivo evidence for the interaction of p55 with the nuclear lamina. J Cell Biol 1990, 111:2225-2234.
    • (1990) J Cell Biol , vol.111 , pp. 2225-2234
    • Powell, L.1    Burke, B.2
  • 8
    • 0027500249 scopus 로고
    • The amino-terminal domain of the lamin B receptor is a nuclear envelope targeting signal
    • Soullam B., Worman H.J. The amino-terminal domain of the lamin B receptor is a nuclear envelope targeting signal. J Cell Biol 1993, 120:1093-1100.
    • (1993) J Cell Biol , vol.120 , pp. 1093-1100
    • Soullam, B.1    Worman, H.J.2
  • 9
    • 0029069183 scopus 로고
    • Signals and structural features involved in integral membrane protein targeting to the inner nuclear membrane
    • Soullam B., Worman H.J. Signals and structural features involved in integral membrane protein targeting to the inner nuclear membrane. J Cell Biol 1995, 130:15-27.
    • (1995) J Cell Biol , vol.130 , pp. 15-27
    • Soullam, B.1    Worman, H.J.2
  • 10
    • 0030763228 scopus 로고    scopus 로고
    • Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosis
    • Ellenberg J., Siggia E.D., Moreira J.E., Smith C.L., Presley J.F., Worman H.J., Lippincott-Schwartz J. Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosis. J Cell Biol 1997, 138:1193-1206.
    • (1997) J Cell Biol , vol.138 , pp. 1193-1206
    • Ellenberg, J.1    Siggia, E.D.2    Moreira, J.E.3    Smith, C.L.4    Presley, J.F.5    Worman, H.J.6    Lippincott-Schwartz, J.7
  • 11
    • 32244448250 scopus 로고    scopus 로고
    • Dependence of diffusional mobility of integral inner nuclear membrane proteins on A-type lamins
    • Ostlund C., Sullivan T., Stewart C.L., Worman H.J. Dependence of diffusional mobility of integral inner nuclear membrane proteins on A-type lamins. Biochemistry 2006, 45:1374-1382.
    • (2006) Biochemistry , vol.45 , pp. 1374-1382
    • Ostlund, C.1    Sullivan, T.2    Stewart, C.L.3    Worman, H.J.4
  • 13
    • 70849084351 scopus 로고    scopus 로고
    • Dynamics and molecular interactions of linker of nucleoskeleton and cytoskeleton (LINC) complex proteins
    • Ostlund C., Folker E.S., Choi J.C., Gomes E.R., Gundersen G.G., Worman H.J. Dynamics and molecular interactions of linker of nucleoskeleton and cytoskeleton (LINC) complex proteins. J Cell Sci 2009, 122:4099-4108.
    • (2009) J Cell Sci , vol.122 , pp. 4099-4108
    • Ostlund, C.1    Folker, E.S.2    Choi, J.C.3    Gomes, E.R.4    Gundersen, G.G.5    Worman, H.J.6
  • 14
    • 11244316478 scopus 로고    scopus 로고
    • Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore
    • Ohba T., Schirmer E.C., Nishimoto T., Gerace L. Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore. J Cell Biol 2004, 167:1051-1062.
    • (2004) J Cell Biol , vol.167 , pp. 1051-1062
    • Ohba, T.1    Schirmer, E.C.2    Nishimoto, T.3    Gerace, L.4
  • 15
    • 33748310680 scopus 로고    scopus 로고
    • Karyopherin-mediated import of integral inner nuclear membrane proteins
    • King M.C., Lusk C.P., Blobel G. Karyopherin-mediated import of integral inner nuclear membrane proteins. Nature 2006, 442:1003-1007.
    • (2006) Nature , vol.442 , pp. 1003-1007
    • King, M.C.1    Lusk, C.P.2    Blobel, G.3
  • 16
    • 84942142223 scopus 로고    scopus 로고
    • Live imaging and modeling of inner nuclear membrane targeting reveals its molecular requirements in mammalian cells
    • Boni A., Ploliti A.Z., Strnad P., Xiang W., Hossain M.J., Ellenberg J. Live imaging and modeling of inner nuclear membrane targeting reveals its molecular requirements in mammalian cells. J Cell Biol 2015, 209:705-720.
    • (2015) J Cell Biol , vol.209 , pp. 705-720
    • Boni, A.1    Ploliti, A.Z.2    Strnad, P.3    Xiang, W.4    Hossain, M.J.5    Ellenberg, J.6
  • 17
    • 84942142224 scopus 로고    scopus 로고
    • Diffusion and retention are major determinants of protein targeting to the inner nuclear membrane
    • Ungricht R., Klann M., Horvath P., Kutay U. Diffusion and retention are major determinants of protein targeting to the inner nuclear membrane. J Cell Biol 2015, 209:687-704.
    • (2015) J Cell Biol , vol.209 , pp. 687-704
    • Ungricht, R.1    Klann, M.2    Horvath, P.3    Kutay, U.4
  • 18
    • 0036538599 scopus 로고    scopus 로고
    • Intracellular trafficking of MAN1, an integral protein of the nuclear envelope inner membrane
    • Wu W., Lin F., Worman H.J. Intracellular trafficking of MAN1, an integral protein of the nuclear envelope inner membrane. J Cell Sci 2002, 115:1361-1371.
    • (2002) J Cell Sci , vol.115 , pp. 1361-1371
    • Wu, W.1    Lin, F.2    Worman, H.J.3
  • 19
    • 81855217987 scopus 로고    scopus 로고
    • Evolvement of LEM proteins as chromatin tethers at the nuclear periphery
    • Brachner A., Foisner R. Evolvement of LEM proteins as chromatin tethers at the nuclear periphery. Biochem Soc Trans 2011, 39:1735-1741.
    • (2011) Biochem Soc Trans , vol.39 , pp. 1735-1741
    • Brachner, A.1    Foisner, R.2
  • 20
    • 0033083786 scopus 로고    scopus 로고
    • Distinct regions specify the nuclear membrane targeting of emerin, the responsible protein for Emery-Dreifuss muscular dystrophy
    • Tsuchiya Y., Hase A., Ogawa M., Yorifuji H., Arahata K. Distinct regions specify the nuclear membrane targeting of emerin, the responsible protein for Emery-Dreifuss muscular dystrophy. Eur J Biochem 1999, 259:859-865.
    • (1999) Eur J Biochem , vol.259 , pp. 859-865
    • Tsuchiya, Y.1    Hase, A.2    Ogawa, M.3    Yorifuji, H.4    Arahata, K.5
  • 21
    • 0028989340 scopus 로고
    • Cloning of a cDNA for lamina-associated polypeptide 2 (LAP2) and identification of regions that specify targeting to the nuclear envelope
    • Furukawa K., Pante N., Aebi U., Gerace L. Cloning of a cDNA for lamina-associated polypeptide 2 (LAP2) and identification of regions that specify targeting to the nuclear envelope. EMBO J 1995, 14:1626-1636.
    • (1995) EMBO J , vol.14 , pp. 1626-1636
    • Furukawa, K.1    Pante, N.2    Aebi, U.3    Gerace, L.4
  • 22
    • 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
  • 24
    • 0035694820 scopus 로고    scopus 로고
    • Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF
    • Lee K.K., Haraguchi T., Lee R.S., Koujin T., Hiraoka Y., Wilson K.L. Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF. J Cell Sci 2001, 114:4567-4573.
    • (2001) J Cell Sci , vol.114 , pp. 4567-4573
    • Lee, K.K.1    Haraguchi, T.2    Lee, R.S.3    Koujin, T.4    Hiraoka, Y.5    Wilson, K.L.6
  • 25
    • 50249107835 scopus 로고    scopus 로고
    • Live cell imaging and electron microscopy reveal dynamic processes of BAF-directed nuclear envelope assembly
    • Haraguchi T., Kojidani T., Koujin T., Shimi T., Osakada H., Mori C., Yamamoto A., Hiraoka Y. Live cell imaging and electron microscopy reveal dynamic processes of BAF-directed nuclear envelope assembly. J Cell Sci 2008, 121:2540-2554.
    • (2008) J Cell Sci , vol.121 , pp. 2540-2554
    • Haraguchi, T.1    Kojidani, T.2    Koujin, T.3    Shimi, T.4    Osakada, H.5    Mori, C.6    Yamamoto, A.7    Hiraoka, Y.8
  • 26
    • 33751012099 scopus 로고    scopus 로고
    • The inner nuclear membrane protein Lem2 is critical for normal nuclear envelope morphology
    • Ulbert S., Antonin W., Platani M., Mattaj I.W. The inner nuclear membrane protein Lem2 is critical for normal nuclear envelope morphology. FEBS Lett 2006, 580:6435-6441.
    • (2006) FEBS Lett , vol.580 , pp. 6435-6441
    • Ulbert, S.1    Antonin, W.2    Platani, M.3    Mattaj, I.W.4
  • 28
    • 0037470050 scopus 로고    scopus 로고
    • Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro
    • Holaska J.M., Lee K.K., Kowalski A.K., Wilson K.L. Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro. J Biol Chem 2003, 278:6969-6975.
    • (2003) J Biol Chem , vol.278 , pp. 6969-6975
    • Holaska, J.M.1    Lee, K.K.2    Kowalski, A.K.3    Wilson, K.L.4
  • 29
    • 0032512832 scopus 로고    scopus 로고
    • The major nuclear envelope targeting domain of LAP2 coincides with its lamin binding region but is distinct from its chromatin interaction domain
    • Furukawa K., Fritze C.E., Gerace L. The major nuclear envelope targeting domain of LAP2 coincides with its lamin binding region but is distinct from its chromatin interaction domain. J Biol Chem 1998, 273:4213-4219.
    • (1998) J Biol Chem , vol.273 , pp. 4213-4219
    • Furukawa, K.1    Fritze, C.E.2    Gerace, L.3
  • 30
    • 0027276759 scopus 로고
    • Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation
    • Foisner R., Gerace L. Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation. Cell 1993, 73:1267-1279.
    • (1993) Cell , vol.73 , pp. 1267-1279
    • Foisner, R.1    Gerace, L.2
  • 31
    • 84861543038 scopus 로고    scopus 로고
    • LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins
    • Sosa B.A., Rothballer A., Kutay U., Schwartz T.U. LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins. Cell 2012, 149:1035-1047.
    • (2012) Cell , vol.149 , pp. 1035-1047
    • Sosa, B.A.1    Rothballer, A.2    Kutay, U.3    Schwartz, T.U.4
  • 32
    • 77954886484 scopus 로고    scopus 로고
    • A classical NLS and the SUN domain contribute to the targeting of SUN2 to the inner nuclear membrane
    • Turgay Y., Ungricht R., Rothballer A., Kiss A., Csucs G., Horvath P., Kutay U. A classical NLS and the SUN domain contribute to the targeting of SUN2 to the inner nuclear membrane. EMBO J 2010, 29:2262-2275.
    • (2010) EMBO J , vol.29 , pp. 2262-2275
    • Turgay, Y.1    Ungricht, R.2    Rothballer, A.3    Kiss, A.4    Csucs, G.5    Horvath, P.6    Kutay, U.7
  • 33
    • 79955966597 scopus 로고    scopus 로고
    • Multiple mechanisms actively target the SUN protein UNC-84 to the inner nuclear membrane
    • Tapley E.C., Ly N., Starr D.A. Multiple mechanisms actively target the SUN protein UNC-84 to the inner nuclear membrane. Mol Biol Cell 2011, 22:1739-1752.
    • (2011) Mol Biol Cell , vol.22 , pp. 1739-1752
    • Tapley, E.C.1    Ly, N.2    Starr, D.A.3
  • 34
    • 0027386803 scopus 로고
    • The first membrane spanning region of the lamin B receptor is sufficient for sorting to the inner nuclear membrane
    • Smith S., Blobel G. The first membrane spanning region of the lamin B receptor is sufficient for sorting to the inner nuclear membrane. J Cell Biol 1993, 120:631-637.
    • (1993) J Cell Biol , vol.120 , pp. 631-637
    • Smith, S.1    Blobel, G.2
  • 36
    • 84871112046 scopus 로고    scopus 로고
    • Lamin B receptor recognizes specific modifications of histone H4 in heterochromatin formation
    • Hirano Y., Hizume K., Kimura H., Takeyasu K., Haraguchi T., Hiraoka Y. Lamin B receptor recognizes specific modifications of histone H4 in heterochromatin formation. J Biol Chem 2012, 287:42654-42663.
    • (2012) J Biol Chem , vol.287 , pp. 42654-42663
    • Hirano, Y.1    Hizume, K.2    Kimura, H.3    Takeyasu, K.4    Haraguchi, T.5    Hiraoka, Y.6
  • 38
    • 0028363978 scopus 로고
    • Primary structure analysis and lamin B and DNA binding of human LBR, an integral protein of the nuclear envelope inner membrane
    • Ye Q., Worman H.J. Primary structure analysis and lamin B and DNA binding of human LBR, an integral protein of the nuclear envelope inner membrane. J Biol Chem 1994, 269:11306-11311.
    • (1994) J Biol Chem , vol.269 , pp. 11306-11311
    • Ye, Q.1    Worman, H.J.2
  • 39
    • 0030987777 scopus 로고    scopus 로고
    • Domain-specific interactions of human HP1-type chromodomain proteins and inner nuclear membrane protein LBR
    • Ye Q., Callebaut I., Pezhman A., Courvalin J.C., Worman H.J. Domain-specific interactions of human HP1-type chromodomain proteins and inner nuclear membrane protein LBR. J Biol Chem 1997, 272:14983-14989.
    • (1997) J Biol Chem , vol.272 , pp. 14983-14989
    • Ye, Q.1    Callebaut, I.2    Pezhman, A.3    Courvalin, J.C.4    Worman, H.J.5
  • 42
    • 67349231939 scopus 로고    scopus 로고
    • Interaction between the inner nuclear membrane lamin B receptor and the heterochromatic methyl binding protein, MeCP2
    • Guarda A., Bolognese F., Bonapace I.M., Badaracco G. Interaction between the inner nuclear membrane lamin B receptor and the heterochromatic methyl binding protein, MeCP2. Exp Cell Res 2009, 315:1895-1903.
    • (2009) Exp Cell Res , vol.315 , pp. 1895-1903
    • Guarda, A.1    Bolognese, F.2    Bonapace, I.M.3    Badaracco, G.4
  • 43
    • 33847367253 scopus 로고    scopus 로고
    • Lamin B receptor plays a role in stimulating nuclear envelope production and targeting membrane vesicles to chromatin during nuclear envelope assembly through direct interaction with importin beta
    • Ma Y., Cai S., Lv Q., Jiang Q., Zhang Q., Sodmergen, Zhai Z., Zhang C. Lamin B receptor plays a role in stimulating nuclear envelope production and targeting membrane vesicles to chromatin during nuclear envelope assembly through direct interaction with importin beta. J Cell Sci 2007, 120:520-530.
    • (2007) J Cell Sci , vol.120 , pp. 520-530
    • Ma, Y.1    Cai, S.2    Lv, Q.3    Jiang, Q.4    Zhang, Q.5    Sodmergen Zhai, Z.6    Zhang, C.7
  • 44
    • 77954388089 scopus 로고    scopus 로고
    • The nucleoporin Nup188 controls passage of membrane proteins across the nuclear pore complex
    • Theerthagiri G., Eisenhardt N., Schwarz H., Antonin W. The nucleoporin Nup188 controls passage of membrane proteins across the nuclear pore complex. J Cell Biol 2010, 189:1129-1142.
    • (2010) J Cell Biol , vol.189 , pp. 1129-1142
    • Theerthagiri, G.1    Eisenhardt, N.2    Schwarz, H.3    Antonin, W.4
  • 45
    • 79953323939 scopus 로고    scopus 로고
    • Traversing the NPC along the pore membrane: targeting of membrane proteins to the INM
    • Antonin W., Ungricht R., Kutay U. Traversing the NPC along the pore membrane: targeting of membrane proteins to the INM. Nucleus 2011, 2:87-91.
    • (2011) Nucleus , vol.2 , pp. 87-91
    • Antonin, W.1    Ungricht, R.2    Kutay, U.3
  • 46
    • 34948891095 scopus 로고    scopus 로고
    • Snapshots of nuclear pore complexes in action captured by cryo-electron tomography
    • Beck M., Lucic V., Forster F., Baumeister W., Medalia O. Snapshots of nuclear pore complexes in action captured by cryo-electron tomography. Nature 2007, 449:611-615.
    • (2007) Nature , vol.449 , pp. 611-615
    • Beck, M.1    Lucic, V.2    Forster, F.3    Baumeister, W.4    Medalia, O.5
  • 47
    • 84861966443 scopus 로고    scopus 로고
    • The human nuclear pore complex as revealed by cryo-electron tomography
    • Maimon T., Elad N., Dahan I., Medalia O. The human nuclear pore complex as revealed by cryo-electron tomography. Structure 2012, 20:998-1006.
    • (2012) Structure , vol.20 , pp. 998-1006
    • Maimon, T.1    Elad, N.2    Dahan, I.3    Medalia, O.4
  • 48
    • 84876124126 scopus 로고    scopus 로고
    • Quantitative analysis of membrane protein transport across the nuclear pore complex
    • Meinema A.C., Poolman B., Veenhoff L.M. Quantitative analysis of membrane protein transport across the nuclear pore complex. Traffic 2013, 14:487-501.
    • (2013) Traffic , vol.14 , pp. 487-501
    • Meinema, A.C.1    Poolman, B.2    Veenhoff, L.M.3
  • 51
    • 33750349837 scopus 로고    scopus 로고
    • Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase
    • Deng M., Hochstrasser M. Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase. Nature 2006, 443:827-831.
    • (2006) Nature , vol.443 , pp. 827-831
    • Deng, M.1    Hochstrasser, M.2
  • 52
    • 84887022716 scopus 로고    scopus 로고
    • The human protein PRR14 tethers heterochromatin to the nuclear lamina during interphase and mitotic exit
    • Poleshko A., Mansfield K.M., Burlingame C.C., Andrake M.D., Shah N.R., Katz R.A. The human protein PRR14 tethers heterochromatin to the nuclear lamina during interphase and mitotic exit. Cell Rep 2013, 5:292-301.
    • (2013) Cell Rep , vol.5 , pp. 292-301
    • Poleshko, A.1    Mansfield, K.M.2    Burlingame, C.C.3    Andrake, M.D.4    Shah, N.R.5    Katz, R.A.6
  • 55
    • 84862689455 scopus 로고    scopus 로고
    • The nuclear envelope protein emerin binds directly to histone deacetylase 3 (HDAC3) and activates HDAC3 activity
    • Demmerle J., Koch A.J., Holaska J.M. The nuclear envelope protein emerin binds directly to histone deacetylase 3 (HDAC3) and activates HDAC3 activity. J Biol Chem 2012, 287:22080-22088.
    • (2012) J Biol Chem , vol.287 , pp. 22080-22088
    • Demmerle, J.1    Koch, A.J.2    Holaska, J.M.3
  • 56
    • 26444589253 scopus 로고    scopus 로고
    • The nuclear-envelope protein and transcriptional repressor LAP2beta interacts with HDAC3 at the nuclear periphery, and induces histone H4 deacetylation
    • Somech R., Shaklai S., Geller O., Amariglio N., Simon A.J., Rechavi G., Gal-Yam E.N. The nuclear-envelope protein and transcriptional repressor LAP2beta interacts with HDAC3 at the nuclear periphery, and induces histone H4 deacetylation. J Cell Sci 2005, 118:4017-4025.
    • (2005) J Cell Sci , vol.118 , pp. 4017-4025
    • Somech, R.1    Shaklai, S.2    Geller, O.3    Amariglio, N.4    Simon, A.J.5    Rechavi, G.6    Gal-Yam, E.N.7
  • 58
    • 84881140677 scopus 로고    scopus 로고
    • The nuclear envelope LEM-domain protein emerin
    • Berk J.M., Tifft K.E., Wilson K.L. The nuclear envelope LEM-domain protein emerin. Nucleus 2013, 4:298-314.
    • (2013) Nucleus , vol.4 , pp. 298-314
    • Berk, J.M.1    Tifft, K.E.2    Wilson, K.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.