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Volumn 48, Issue 7, 2009, Pages 1636-1643

Cell cycle-dependent phosphorylation of MAN1

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ASSAYS; CELL CYCLES; EGG CELLS; IN-VITRO; MITOTIC PHOSPHORYLATIONS; MS/MS SEQUENCING; N TERMINALS; NUCLEAR MEMBRANES; PHOSPHORYLATION SITES; XENOPUS;

EID: 61749084978     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802060v     Document Type: Article
Times cited : (14)

References (52)
  • 2
    • 28444472419 scopus 로고    scopus 로고
    • Pushing the envelope: Structure, function, and dynamics of the nuclear periphery
    • Hetzer, M. W., Walther, T. C., and Mattaj, I. W. (2005) Pushing the envelope: Structure, function, and dynamics of the nuclear periphery. Annu. Rev. Cell Deu. Biol. 21, 347-380.
    • (2005) Annu. Rev. Cell Deu. Biol , vol.21 , pp. 347-380
    • Hetzer, M.W.1    Walther, T.C.2    Mattaj, I.W.3
  • 3
    • 30844455364 scopus 로고    scopus 로고
    • The nuclear envelope: Form and reformation
    • Prunuske, A. J., and Ullman, K. S. (2006) The nuclear envelope: Form and reformation. Curr. Opin. Cell Biol. 18, 108-116.
    • (2006) Curr. Opin. Cell Biol , vol.18 , pp. 108-116
    • Prunuske, A.J.1    Ullman, K.S.2
  • 4
    • 25144491496 scopus 로고    scopus 로고
    • The nuclear membrane proteome: Extending the envelope
    • Schirmer, E. C., and Gerace, L. (2005) The nuclear membrane proteome: Extending the envelope. Trends Biochem. Sci. 30, 551-558.
    • (2005) Trends Biochem. Sci , vol.30 , pp. 551-558
    • Schirmer, E.C.1    Gerace, L.2
  • 5
    • 0042691509 scopus 로고    scopus 로고
    • Nuclear membrane proteins with potential disease links found by subtractive proteomics
    • Schirmer, E. C., Florens, L., Guan, T. L., Yates, J. R., and Gerace, L. (2003) Nuclear membrane proteins with potential disease links found by subtractive proteomics. Science 301, 1380-1382.
    • (2003) Science , vol.301 , pp. 1380-1382
    • Schirmer, E.C.1    Florens, L.2    Guan, T.L.3    Yates, J.R.4    Gerace, L.5
  • 7
    • 0027985787 scopus 로고
    • Identification of a Novel X-Linked Gene Responsible for Emery-Dreifuss Muscular-Dystrophy
    • Bione, S., Maestrini, E., Rivella, S., Mancini, M., Regis, S., Romeo, G., and Toniolo, D. (1994) Identification of a Novel X-Linked Gene Responsible for Emery-Dreifuss Muscular-Dystrophy. Nat. Genet. 8, 323-327.
    • (1994) Nat. Genet , vol.8 , pp. 323-327
    • Bione, S.1    Maestrini, E.2    Rivella, S.3    Mancini, M.4    Regis, S.5    Romeo, G.6    Toniolo, D.7
  • 10
    • 33749003191 scopus 로고    scopus 로고
    • SUN-domain proteins: 'Velcro' that links the nucleoskeleton to the cytoskeleton
    • Tzur, Y. B., Wilson, K. L., and Gruenbaum, Y. (2006) SUN-domain proteins: 'Velcro' that links the nucleoskeleton to the cytoskeleton. Nat. Rev. Mol. Cell Biol. 7, 782-788.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 782-788
    • Tzur, Y.B.1    Wilson, K.L.2    Gruenbaum, Y.3
  • 11
    • 0030461544 scopus 로고    scopus 로고
    • Targeting of membranes to sea urchin sperm chromatin is mediated by a lamin B receptor-like integral membrane protein
    • Collas, P., Courvalin, J. C., and Poccia, D. (1996) Targeting of membranes to sea urchin sperm chromatin is mediated by a lamin B receptor-like integral membrane protein. J. Cell Biol. 135, 1715-1725.
    • (1996) J. Cell Biol , vol.135 , pp. 1715-1725
    • Collas, P.1    Courvalin, J.C.2    Poccia, D.3
  • 12
    • 0030480104 scopus 로고    scopus 로고
    • The lamin B receptor (LBR) provides essential chromatin docking sites at the nuclear envelope
    • Pyrpasopoulou, A., Meier, J., Maison, C., Simos, G., and Georgatos, S. D. (1996) The lamin B receptor (LBR) provides essential chromatin docking sites at the nuclear envelope. EMBO J. 15, 7108-7119.
    • (1996) EMBO J , vol.15 , pp. 7108-7119
    • Pyrpasopoulou, A.1    Meier, J.2    Maison, C.3    Simos, G.4    Georgatos, S.D.5
  • 13
    • 34247532724 scopus 로고    scopus 로고
    • Nuclear envelope precursor vesicle targeting to chromatin is stimulated by protein phosphatase 1 in Xenopus egg extracts
    • Ito, H., Koyama, Y., Takano, M., Ishii, K., Maeno, M., Furukawa, K., and Horigome, T. (2007) Nuclear envelope precursor vesicle targeting to chromatin is stimulated by protein phosphatase 1 in Xenopus egg extracts. Exp. Cell Res. 313, 1897-1910.
    • (2007) Exp. Cell Res , vol.313 , pp. 1897-1910
    • Ito, H.1    Koyama, Y.2    Takano, M.3    Ishii, K.4    Maeno, M.5    Furukawa, K.6    Horigome, T.7
  • 14
    • 0027276759 scopus 로고
    • Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation
    • Foisner, R., and Gerace, L. (1993) Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation. Cell 73, 1267-1279.
    • (1993) Cell , vol.73 , pp. 1267-1279
    • Foisner, R.1    Gerace, L.2
  • 17
    • 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., and Hiraoka, Y. (2008) Live cell imaging and electron microscopy reveal dynamic processes of BAF-directed nuclear envelope assembly. J. Cell Sci. 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
  • 18
    • 0032778974 scopus 로고    scopus 로고
    • LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction
    • Furukawa, K. (1999) LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction. J. Cell Sci. 112, 2485-2492.
    • (1999) J. Cell Sci , vol.112 , pp. 2485-2492
    • Furukawa, K.1
  • 19
    • 0035694820 scopus 로고    scopus 로고
    • Distinct functional domains in emerin bind lamin A and DNA-bridging protein
    • Lee, K. K., Haraguchi, T., Lee, R. S., Koujin, T., Hiraoka, Y., and Wilson, K. L. (2001) Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF. J. Cell Sci. 114, 4567-4573.
    • (2001) BAF. 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
  • 20
    • 0035794643 scopus 로고    scopus 로고
    • LAP2 binds to BAF-DNA complexes: Requirement for the LEM domain and modulation by variable regions
    • Shumaker, D. K, Lee, K. K, Tanhehco, Y. C., Craigie, R., and Wilson, K. L. (2001) LAP2 binds to BAF-DNA complexes: Requirement for the LEM domain and modulation by variable regions. EMBO J. 20, 1754-1764.
    • (2001) EMBO J , vol.20 , pp. 1754-1764
    • Shumaker, D.K.1    Lee, K.K.2    Tanhehco, Y.C.3    Craigie, R.4    Wilson, K.L.5
  • 21
    • 17144380019 scopus 로고    scopus 로고
    • Nuclear membrane protein MAN1: Direct binding to emerin in vitro and two modes of binding to BAF
    • Mansharamani, M., and Wilson, K. L. (2005) Nuclear membrane protein MAN1: Direct binding to emerin in vitro and two modes of binding to BAF. J. Biol. Chem. 280, 13863-13870.
    • (2005) J. Biol. Chem , vol.280 , pp. 13863-13870
    • Mansharamani, M.1    Wilson, K.L.2
  • 22
    • 28844449551 scopus 로고    scopus 로고
    • Dissociation of emerin from barrier-to-autointegration factor is regulated through mitotic phosphorylation of emerin in a Xenopus egg cell-free system
    • Hirano, Y., Segawa, M., Ouchi, F. S., Yamakawa, Y., Furukawa, K, Takeyasu, K, and Horigome, T. (2005) Dissociation of emerin from barrier-to-autointegration factor is regulated through mitotic phosphorylation of emerin in a Xenopus egg cell-free system. J. Biol. Chem. 280, 39925-39933.
    • (2005) J. Biol. Chem , vol.280 , pp. 39925-39933
    • Hirano, Y.1    Segawa, M.2    Ouchi, F.S.3    Yamakawa, Y.4    Furukawa, K.5    Takeyasu, K.6    Horigome, T.7
  • 23
    • 33644864100 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor phosphorylation on Ser-4 regulates emerin binding to lamin A in vitro and emerin localization in vivo
    • Bengtsson, L., and Wilson, K. L. (2006) Barrier-to-autointegration factor phosphorylation on Ser-4 regulates emerin binding to lamin A in vitro and emerin localization in vivo. Mol. Biol. Cell 17, 1154-1163.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1154-1163
    • Bengtsson, L.1    Wilson, K.L.2
  • 24
    • 33846195879 scopus 로고    scopus 로고
    • Caenorhabditis elegans BAF-1 and its kinase VRK-1 participate directly in postmitotic nuclear envelope assembly
    • Gorjanacz, M., Klerkx, E. P., Galy, V., Santarella, R., Lopez-Iglesias, C., Askjaer, P., and Mattaj, I. W. (2007) Caenorhabditis elegans BAF-1 and its kinase VRK-1 participate directly in postmitotic nuclear envelope assembly. EMBO J. 26, 132-143.
    • (2007) EMBO J , vol.26 , pp. 132-143
    • Gorjanacz, M.1    Klerkx, E.P.2    Galy, V.3    Santarella, R.4    Lopez-Iglesias, C.5    Askjaer, P.6    Mattaj, I.W.7
  • 25
    • 33745450085 scopus 로고    scopus 로고
    • The vaccinia-related kinases phosphorylate the N′ terminus of BAF, regulating its interaction with DNA and its retention in the nucleus
    • Nichols, R. J., Wiebe, M. S., and Traktman, P. (2006) The vaccinia-related kinases phosphorylate the N′ terminus of BAF, regulating its interaction with DNA and its retention in the nucleus. Mol. Biol. Cell 17, 2451-2464.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2451-2464
    • Nichols, R.J.1    Wiebe, M.S.2    Traktman, P.3
  • 26
    • 0037446880 scopus 로고    scopus 로고
    • MAN1 and emerin have overlapping function(s) essential for chromosome segregation and cell division in Caenorhabditis elegans
    • Liu, J., Lee, K K, Segura-Totten, M., Neufeld, E., Wilson, K. L., and Gruenbaum, Y. (2003) MAN1 and emerin have overlapping function(s) essential for chromosome segregation and cell division in Caenorhabditis elegans. Proc. Natl. Acad. Sci. U.S.A. 100, 4598-4603.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 4598-4603
    • Liu, J.1    Lee, K.K.2    Segura-Totten, M.3    Neufeld, E.4    Wilson, K.L.5    Gruenbaum, Y.6
  • 27
    • 0036538599 scopus 로고    scopus 로고
    • Intracellular trafficking of MAN1, an integral protein of the nuclear envelope inner membrane
    • Wu, W., Lin, F., and Worman, H. J. (2002) Intracellular trafficking of MAN1, an integral protein of the nuclear envelope inner membrane. J. Cell Sci. 115, 1361-1371.
    • (2002) J. Cell Sci , vol.115 , pp. 1361-1371
    • Wu, W.1    Lin, F.2    Worman, H.J.3
  • 28
    • 0030029383 scopus 로고    scopus 로고
    • The MAN antigens are non-lamin constituents of the nuclear lamina in vertebrate cells
    • PaulinLevasseur, M., Blake, D. L., Julien, M., and Rouleau, L. (1996) The MAN antigens are non-lamin constituents of the nuclear lamina in vertebrate cells. Chromosoma 104, 367-379.
    • (1996) Chromosoma , vol.104 , pp. 367-379
    • PaulinLevasseur, M.1    Blake, D.L.2    Julien, M.3    Rouleau, L.4
  • 29
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen, J. V., Blagoev, B., Gnad, F., Macek, B., Kumar, C., Mortensen, P., and Mann, M. (2006) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127, 635-648.
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 32
    • 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-β superfamily of cytokines
    • Pan, D., Estevez-Salmeron, L. D., Stroschein, S. L., Zhu, X., He, J., Zhou, S., and Luo, K. (2005) The integral inner nuclear membrane protein MAN1 physically interacts with the R-Smad proteins to repress signaling by the transforming growth factor-β superfamily of cytokines. J. Biol. Chem. 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
  • 33
    • 0027186606 scopus 로고
    • Cellular substrates of p34(cdc2) and its companion cyclin-dependent kinases
    • Nigg, E. A. (1993) Cellular substrates of p34(cdc2) and its companion cyclin-dependent kinases. Trends Cell Biol. 3, 296-301.
    • (1993) Trends Cell Biol , vol.3 , pp. 296-301
    • Nigg, E.A.1
  • 34
    • 0030942845 scopus 로고    scopus 로고
    • Mitotic phosphorylation of the lamin B receptor by a serine/arginine kinase and p34(cdc2)
    • Nikolakaki, E., Meier, J., Simos, G., Georgatos, S. D., and Giannakouros, T. (1997) Mitotic phosphorylation of the lamin B receptor by a serine/arginine kinase and p34(cdc2). J. Biol. Chem. 272, 6208-6213.
    • (1997) J. Biol. Chem , vol.272 , pp. 6208-6213
    • Nikolakaki, E.1    Meier, J.2    Simos, G.3    Georgatos, S.D.4    Giannakouros, T.5
  • 35
    • 1842529177 scopus 로고    scopus 로고
    • Regulation of binding of lamin B receptor to chromatin by SR protein kinase and cdc2 kinase in Xenopus egg extracts
    • Takano, M., Koyama, Y., Ito, H., Hoshino, S., Onogi, H., Hagiwara, M., Furukawa, K, and Horigome, T. (2004) Regulation of binding of lamin B receptor to chromatin by SR protein kinase and cdc2 kinase in Xenopus egg extracts. J. Biol. Chem. 279, 13265-13271.
    • (2004) J. Biol. Chem , vol.279 , pp. 13265-13271
    • Takano, M.1    Koyama, Y.2    Ito, H.3    Hoshino, S.4    Onogi, H.5    Hagiwara, M.6    Furukawa, K.7    Horigome, T.8
  • 36
    • 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., and Gerace, L. (1995) Cloning of a cDNA for lamina-associated polypeptide 2 (LAP2) and identification of regions that specify targeting to the nuclear envelope. EMBO J. 14, 1626-1636.
    • (1995) EMBO J , vol.14 , pp. 1626-1636
    • Furukawa, K.1    Pante, N.2    Aebi, U.3    Gerace, L.4
  • 37
    • 0018840796 scopus 로고
    • The nuclear envelope lamina is reversibly depolymerized during mitosis
    • Gerace, L., and Blobel, G. (1980) The nuclear envelope lamina is reversibly depolymerized during mitosis. Cell 19, 277-287.
    • (1980) Cell , vol.19 , pp. 277-287
    • Gerace, L.1    Blobel, G.2
  • 38
    • 0025352896 scopus 로고
    • Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis
    • Heald, R., and McKeon, F. (1990) Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis. Cell 61, 579-589.
    • (1990) Cell , vol.61 , pp. 579-589
    • Heald, R.1    McKeon, F.2
  • 39
    • 0025370462 scopus 로고
    • In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase
    • Peter, M., Nakagawa, J., Doree, M., Labbe, J. C., and Nigg, E. A. (1990) In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase. Cell 61, 591-602.
    • (1990) Cell , vol.61 , pp. 591-602
    • Peter, M.1    Nakagawa, J.2    Doree, M.3    Labbe, J.C.4    Nigg, E.A.5
  • 40
    • 0028853451 scopus 로고
    • Differential mitotic phosphorylation of proteins of the nuclear pore complex
    • Macaulay, C., Meier, E., and Forbes, D. J. (1995) Differential mitotic phosphorylation of proteins of the nuclear pore complex. J. Biol. Chem. 270, 254-262.
    • (1995) J. Biol. Chem , vol.270 , pp. 254-262
    • Macaulay, C.1    Meier, E.2    Forbes, D.J.3
  • 41
    • 2942564430 scopus 로고    scopus 로고
    • Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence
    • Blom, N, Sicheritz-Ponten, T, Gupta, R., Gammeltoft, S., and Brunak, S. (2004) Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence. Proteomics 4, 1633-1649.
    • (2004) Proteomics , vol.4 , pp. 1633-1649
    • Blom, N.1    Sicheritz-Ponten, T.2    Gupta, R.3    Gammeltoft, S.4    Brunak, S.5
  • 42
    • 33745450085 scopus 로고    scopus 로고
    • The vaccinia-related kinases phosphorylate the N′ terminus of BAF, regulating its interaction with DNA and its retention in the nucleus
    • Nichols, R. J., Wiebe, M. S., and Traktman, P. (2006) The vaccinia-related kinases phosphorylate the N′ terminus of BAF, regulating its interaction with DNA and its retention in the nucleus. Mol. Biol. Cell 17, 2451-2464.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2451-2464
    • Nichols, R.J.1    Wiebe, M.S.2    Traktman, P.3
  • 43
    • 33846195879 scopus 로고    scopus 로고
    • Caenorhabditis elegans BAF-1 and its kinase VRK-1 participate directly in postmitotic nuclear envelope assembly
    • Gorjanacz, M., Klerkx, E. P. F., Galy, V., Santarella, R., Lopez-Iglesias, C., Askjaer, P., and Mattaj, I. W. (2007) Caenorhabditis elegans BAF-1 and its kinase VRK-1 participate directly in postmitotic nuclear envelope assembly. EMBO J. 26, 132-143.
    • (2007) EMBO J , vol.26 , pp. 132-143
    • Gorjanacz, M.1    Klerkx, E.P.F.2    Galy, V.3    Santarella, R.4    Lopez-Iglesias, C.5    Askjaer, P.6    Mattaj, I.W.7
  • 44
    • 4143103828 scopus 로고    scopus 로고
    • A phosphorylation cluster in the chromatin-binding region regulates chromosome association of LAP2a
    • Gajewski, A., Csaszar, E., and Foisner, R. (2004) A phosphorylation cluster in the chromatin-binding region regulates chromosome association of LAP2a. J. Biol. Chem. 279, 35813-35821.
    • (2004) J. Biol. Chem , vol.279 , pp. 35813-35821
    • Gajewski, A.1    Csaszar, E.2    Foisner, R.3
  • 47
    • 0037959860 scopus 로고    scopus 로고
    • XMAN1, an inner nuclear membrane protein, antagonizes BMP signaling by interacting with Smad1 in Xenopus embryos
    • Osada, S. I., Ohmori, S., and Taira, M. (2003) XMAN1, an inner nuclear membrane protein, antagonizes BMP signaling by interacting with Smad1 in Xenopus embryos. Development 130, 1783-1794.
    • (2003) Development , vol.130 , pp. 1783-1794
    • Osada, S.I.1    Ohmori, S.2    Taira, M.3
  • 48
    • 13544264752 scopus 로고    scopus 로고
    • MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-β signaling
    • Lin, F., Morrison, J. M., Wu, W., and Worman, H. J. (2005) MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-β signaling. Hum. Mol. Genet. 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
  • 49
    • 33746942748 scopus 로고    scopus 로고
    • Inner nuclear membrane and regulation of Smad-mediated signaling
    • Worman, H. J. (2006) Inner nuclear membrane and regulation of Smad-mediated signaling. Biochim. Biophys. Acta 1761, 626-631.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 626-631
    • Worman, H.J.1
  • 50
    • 0036330001 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor: Major roles in chromatin decondensation and nuclear assembly
    • Segura-Totten, M., Kowalski, A. K, Craigie, R., and Wilson, K. L. (2002) Barrier-to-autointegration factor: Major roles in chromatin decondensation and nuclear assembly. J. Cell Biol. 158, 475-485.
    • (2002) J. Cell Biol , vol.158 , pp. 475-485
    • Segura-Totten, M.1    Kowalski, A.K.2    Craigie, R.3    Wilson, K.L.4
  • 52
    • 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-β superfamily of cytokines
    • Pan, D., Estevez-Salmeron, L. D., Stroschein, S. L., Zhu, X. L., He, J., Zhou, S. L., and Luo, K X. (2005) The integral inner nuclear membrane protein MAN1 physically interacts with the R-Smad proteins to repress signaling by the transforming growth factor-β superfamily of cytokines. J. Biol. Chem. 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.L.4    He, J.5    Zhou, S.L.6    Luo, K.X.7


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