메뉴 건너뛰기




Volumn 7, Issue 11, 2012, Pages

ERMO3/MVP1/GOLD36 Is Involved in a Cell Type-Specific Mechanism for Maintaining ER Morphology in Arabidopsis thaliana

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS PROTEIN; PROTEIN ERMO3; PROTEIN PYK10; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR NAI1; UNCLASSIFIED DRUG;

EID: 84869101190     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0049103     Document Type: Article
Times cited : (22)

References (43)
  • 1
    • 77951052587 scopus 로고    scopus 로고
    • Myosin-dependent endoplasmic reticulum motility and F-actin organization in plant cells
    • Ueda H, Yokota E, Kutsuna N, Shimada T, Tamura K, et al. (2010) Myosin-dependent endoplasmic reticulum motility and F-actin organization in plant cells. Proc Natl Acad Sci U S A 107: 6894-6899.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 6894-6899
    • Ueda, H.1    Yokota, E.2    Kutsuna, N.3    Shimada, T.4    Tamura, K.5
  • 2
    • 0034610998 scopus 로고    scopus 로고
    • In vitro formation of the endoplasmic reticulum occurs independently of microtubules by a controlled fusion reaction
    • Dreier L, Rapoport TA, (2000) In vitro formation of the endoplasmic reticulum occurs independently of microtubules by a controlled fusion reaction. J Cell Biol 148: 883-898.
    • (2000) J Cell Biol , vol.148 , pp. 883-898
    • Dreier, L.1    Rapoport, T.A.2
  • 3
    • 0034618102 scopus 로고    scopus 로고
    • Mutants affecting the structure of the cortical endoplasmic reticulum in Saccharomyces cerevisiae
    • Prinz WA, Grzyb L, Veenhuis M, Kahana JA, Silver PA, et al. (2000) Mutants affecting the structure of the cortical endoplasmic reticulum in Saccharomyces cerevisiae. J Cell Biol 150: 461-474.
    • (2000) J Cell Biol , vol.150 , pp. 461-474
    • Prinz, W.A.1    Grzyb, L.2    Veenhuis, M.3    Kahana, J.A.4    Silver, P.A.5
  • 4
    • 32044445021 scopus 로고    scopus 로고
    • A class of membrane proteins shaping the tubular endoplasmic reticulum
    • Voeltz GK, Prinz WA, Shibata Y, Rist JM, Rapoport TA, (2006) A class of membrane proteins shaping the tubular endoplasmic reticulum. Cell 124: 573-586.
    • (2006) Cell , vol.124 , pp. 573-586
    • Voeltz, G.K.1    Prinz, W.A.2    Shibata, Y.3    Rist, J.M.4    Rapoport, T.A.5
  • 5
    • 40049085592 scopus 로고    scopus 로고
    • Membrane proteins of the endoplasmic reticulum induce high-curvature tubules
    • Hu J, Shibata Y, Voss C, Shemesh T, Li Z, et al. (2008) Membrane proteins of the endoplasmic reticulum induce high-curvature tubules. Science 319: 1247-1250.
    • (2008) Science , vol.319 , pp. 1247-1250
    • Hu, J.1    Shibata, Y.2    Voss, C.3    Shemesh, T.4    Li, Z.5
  • 6
    • 49649084487 scopus 로고    scopus 로고
    • The reticulon and DP1/Yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum
    • Shibata Y, Voss C, Rist JM, Hu J, Rapoport TA, et al. (2008) The reticulon and DP1/Yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum. J Biol Chem 283: 18892-18904.
    • (2008) J Biol Chem , vol.283 , pp. 18892-18904
    • Shibata, Y.1    Voss, C.2    Rist, J.M.3    Hu, J.4    Rapoport, T.A.5
  • 8
    • 68049096310 scopus 로고    scopus 로고
    • A class of dynamin-like GTPases involved in the generation of the tubular ER network
    • Hu J, Shibata Y, Zhu PP, Voss C, Rismanchi N, et al. (2009) A class of dynamin-like GTPases involved in the generation of the tubular ER network. Cell 138: 549-561.
    • (2009) Cell , vol.138 , pp. 549-561
    • Hu, J.1    Shibata, Y.2    Zhu, P.P.3    Voss, C.4    Rismanchi, N.5
  • 9
    • 79251471434 scopus 로고    scopus 로고
    • Mechanisms determining the morphology of the peripheral ER
    • Shibata Y, Shemesh T, Prinz WA, Palazzo AF, Kozlov MM, et al. (2010) Mechanisms determining the morphology of the peripheral ER. Cell 143: 774-788.
    • (2010) Cell , vol.143 , pp. 774-788
    • Shibata, Y.1    Shemesh, T.2    Prinz, W.A.3    Palazzo, A.F.4    Kozlov, M.M.5
  • 10
    • 34447269976 scopus 로고    scopus 로고
    • Reticulon-like proteins in Arabidopsis thaliana: structural organization and ER localization
    • Nziengui H, Bouhidel K, Pillon D, Der C, Marty F, et al. (2007) Reticulon-like proteins in Arabidopsis thaliana: structural organization and ER localization. FEBS Lett 581: 3356-3362.
    • (2007) FEBS Lett , vol.581 , pp. 3356-3362
    • Nziengui, H.1    Bouhidel, K.2    Pillon, D.3    Der, C.4    Marty, F.5
  • 11
    • 77953177103 scopus 로고    scopus 로고
    • Five Arabidopsis reticulon isoforms share endoplasmic reticulum location, topology, and membrane-shaping properties
    • Sparkes I, Tolley N, Aller I, Svozil J, Osterrieder A, et al. (2010) Five Arabidopsis reticulon isoforms share endoplasmic reticulum location, topology, and membrane-shaping properties. Plant Cell 22: 1333-1343.
    • (2010) Plant Cell , vol.22 , pp. 1333-1343
    • Sparkes, I.1    Tolley, N.2    Aller, I.3    Svozil, J.4    Osterrieder, A.5
  • 12
    • 60149110302 scopus 로고    scopus 로고
    • Functions of reticulons in plants: What we can learn from animals and yeasts
    • Nziengui H, Schoefs B, (2009) Functions of reticulons in plants: What we can learn from animals and yeasts. Cell Mol Life Sci 66: 584-595.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 584-595
    • Nziengui, H.1    Schoefs, B.2
  • 13
    • 37249073837 scopus 로고    scopus 로고
    • Overexpression of a plant reticulon remodels the lumen of the cortical endoplasmic reticulum but does not perturb protein transport
    • Tolley N, Sparkes IA, Hunter PR, Craddock CP, Nuttall J, et al. (2008) Overexpression of a plant reticulon remodels the lumen of the cortical endoplasmic reticulum but does not perturb protein transport. Traffic 9: 94-102.
    • (2008) Traffic , vol.9 , pp. 94-102
    • Tolley, N.1    Sparkes, I.A.2    Hunter, P.R.3    Craddock, C.P.4    Nuttall, J.5
  • 14
    • 77954218288 scopus 로고    scopus 로고
    • Further assembly required: construction and dynamics of the endoplasmic reticulum network
    • Park SH, Blackstone C, (2010) Further assembly required: construction and dynamics of the endoplasmic reticulum network. EMBO Rep 11: 515-521.
    • (2010) EMBO Rep , vol.11 , pp. 515-521
    • Park, S.H.1    Blackstone, C.2
  • 15
    • 79960322829 scopus 로고    scopus 로고
    • Arabidopsis RHD3 mediates the generation of the tubular ER network and is required for Golgi distribution and motility in plant cells
    • Chen J, Stefano G, Brandizzi F, Zheng H, (2011) Arabidopsis RHD3 mediates the generation of the tubular ER network and is required for Golgi distribution and motility in plant cells. J Cell Sci 124: 2241-2252.
    • (2011) J Cell Sci , vol.124 , pp. 2241-2252
    • Chen, J.1    Stefano, G.2    Brandizzi, F.3    Zheng, H.4
  • 16
    • 84859164539 scopus 로고    scopus 로고
    • In Arabidopsis, the spatial and dynamic organization of the endoplasmic reticulum and Golgi apparatus is influenced by the integrity of the C-terminal domain of RHD3, a non-essential GTPase
    • Stefano G, Renna L, Moss T, McNew JA, Brandizzi F, (2012) In Arabidopsis, the spatial and dynamic organization of the endoplasmic reticulum and Golgi apparatus is influenced by the integrity of the C-terminal domain of RHD3, a non-essential GTPase. Plant J 69: 957-66.
    • (2012) Plant J , vol.69 , pp. 957-966
    • Stefano, G.1    Renna, L.2    Moss, T.3    McNew, J.A.4    Brandizzi, F.5
  • 17
    • 26844533346 scopus 로고    scopus 로고
    • KATAMARI1/MURUS3 Is a novel golgi membrane protein that is required for endomembrane organization in Arabidopsis
    • Tamura K, Shimada T, Kondo M, Nishimura M, Hara-Nishimura I, (2005) KATAMARI1/MURUS3 Is a novel golgi membrane protein that is required for endomembrane organization in Arabidopsis. Plant Cell 17: 1764-1776.
    • (2005) Plant Cell , vol.17 , pp. 1764-1776
    • Tamura, K.1    Shimada, T.2    Kondo, M.3    Nishimura, M.4    Hara-Nishimura, I.5
  • 18
    • 48949107700 scopus 로고    scopus 로고
    • Myosin XI-K Is required for rapid trafficking of Golgi stacks, peroxisomes, and mitochondria in leaf cells of Nicotiana benthamiana
    • Avisar D, Prokhnevsky AI, Makarova KS, Koonin EV, Dolja VV, (2008) Myosin XI-K Is required for rapid trafficking of Golgi stacks, peroxisomes, and mitochondria in leaf cells of Nicotiana benthamiana. Plant Physiol 146: 1098-1108.
    • (2008) Plant Physiol , vol.146 , pp. 1098-1108
    • Avisar, D.1    Prokhnevsky, A.I.2    Makarova, K.S.3    Koonin, E.V.4    Dolja, V.V.5
  • 19
    • 75649083805 scopus 로고    scopus 로고
    • Movement and Remodeling of the Endoplasmic Reticulum in Nondividing Cells of Tobacco Leaves
    • Sparkes I, Runions J, Hawes C, Griffing L, (2009) Movement and Remodeling of the Endoplasmic Reticulum in Nondividing Cells of Tobacco Leaves. Plant Cell 21: 3937-3949.
    • (2009) Plant Cell , vol.21 , pp. 3937-3949
    • Sparkes, I.1    Runions, J.2    Hawes, C.3    Griffing, L.4
  • 20
    • 73249134584 scopus 로고    scopus 로고
    • GNOM-LIKE1/ERMO1 and SEC24a/ERMO2 are required for maintenance of endoplasmic reticulum morphology in Arabidopsis thaliana
    • Nakano RT, Matsushima R, Ueda H, Tamura K, Shimada T, et al. (2009) GNOM-LIKE1/ERMO1 and SEC24a/ERMO2 are required for maintenance of endoplasmic reticulum morphology in Arabidopsis thaliana. Plant Cell 21: 3672-3685.
    • (2009) Plant Cell , vol.21 , pp. 3672-3685
    • Nakano, R.T.1    Matsushima, R.2    Ueda, H.3    Tamura, K.4    Shimada, T.5
  • 21
    • 73249134381 scopus 로고    scopus 로고
    • A missense mutation in the Arabidopsis COPII coat protein Sec24A induces the formation of clusters of the endoplasmic reticulum and Golgi apparatus
    • Faso C, Chen YN, Tamura K, Held M, Zemelis S, et al. (2009) A missense mutation in the Arabidopsis COPII coat protein Sec24A induces the formation of clusters of the endoplasmic reticulum and Golgi apparatus. Plant Cell 21: 3655-3671.
    • (2009) Plant Cell , vol.21 , pp. 3655-3671
    • Faso, C.1    Chen, Y.N.2    Tamura, K.3    Held, M.4    Zemelis, S.5
  • 22
    • 0034797989 scopus 로고    scopus 로고
    • A proteinase-storing body that prepares for cell death or stresses in the epidermal cells of Arabidopsis
    • Hayashi Y, Yamada K, Shimada T, Matsushima R, Nishizawa NK, et al. (2001) A proteinase-storing body that prepares for cell death or stresses in the epidermal cells of Arabidopsis. Plant Cell Physiol 42: 894-899.
    • (2001) Plant Cell Physiol , vol.42 , pp. 894-899
    • Hayashi, Y.1    Yamada, K.2    Shimada, T.3    Matsushima, R.4    Nishizawa, N.K.5
  • 23
    • 0346037065 scopus 로고    scopus 로고
    • An endoplasmic reticulum-derived structure that is induced under stress conditions in Arabidopsis
    • Matsushima R, Hayashi Y, Kondo M, Shimada T, Nishimura M, et al. (2002) An endoplasmic reticulum-derived structure that is induced under stress conditions in Arabidopsis. Plant Physiol 130: 1807-1814.
    • (2002) Plant Physiol , vol.130 , pp. 1807-1814
    • Matsushima, R.1    Hayashi, Y.2    Kondo, M.3    Shimada, T.4    Nishimura, M.5
  • 24
    • 63049105704 scopus 로고    scopus 로고
    • Constitutive and inducible ER bodies of Arabidopsis thaliana accumulate distinct beta-glucosidases
    • Ogasawara K, Yamada K, Christeller JT, Kondo M, Hatsugai N, et al. (2009) Constitutive and inducible ER bodies of Arabidopsis thaliana accumulate distinct beta-glucosidases. Plant Cell Physiol 50: 480-488.
    • (2009) Plant Cell Physiol , vol.50 , pp. 480-488
    • Ogasawara, K.1    Yamada, K.2    Christeller, J.T.3    Kondo, M.4    Hatsugai, N.5
  • 25
    • 0344100119 scopus 로고    scopus 로고
    • A wound-inducible organelle derived from endoplasmic reticulum: a plant strategy against environmental stresses?
    • Hara-Nishimura I, Matsushima R, (2003) A wound-inducible organelle derived from endoplasmic reticulum: a plant strategy against environmental stresses? Curr Opin Plant Biol 6: 583-588.
    • (2003) Curr Opin Plant Biol , vol.6 , pp. 583-588
    • Hara-Nishimura, I.1    Matsushima, R.2
  • 26
    • 48849112921 scopus 로고    scopus 로고
    • Antagonistic jacalin-related lectins regulate the size of ER body-type beta-glucosidase complexes in Arabidopsis thaliana
    • Nagano AJ, Fukao Y, Fujiwara M, Nishimura M, Hara-Nishimura I, (2008) Antagonistic jacalin-related lectins regulate the size of ER body-type beta-glucosidase complexes in Arabidopsis thaliana. Plant Cell Physiol 49: 969-980.
    • (2008) Plant Cell Physiol , vol.49 , pp. 969-980
    • Nagano, A.J.1    Fukao, Y.2    Fujiwara, M.3    Nishimura, M.4    Hara-Nishimura, I.5
  • 28
    • 73249121280 scopus 로고    scopus 로고
    • MODIFIED VACUOLE PHENOTYPE1 is an Arabidopsis myrosinase-associated protein involved in endomembrane protein trafficking
    • Agee AE, Surpin M, Sohn EJ, Girke T, Rosado A, et al. (2010) MODIFIED VACUOLE PHENOTYPE1 is an Arabidopsis myrosinase-associated protein involved in endomembrane protein trafficking. Plant Physiol 152: 120-132.
    • (2010) Plant Physiol , vol.152 , pp. 120-132
    • Agee, A.E.1    Surpin, M.2    Sohn, E.J.3    Girke, T.4    Rosado, A.5
  • 29
    • 77956804277 scopus 로고    scopus 로고
    • A missense mutation in the vacuolar protein GOLD36 causes organizational defects in the ER and aberrant protein trafficking in the plant secretory pathway
    • Marti L, Stefano G, Tamura K, Hawes C, Renna L, et al. (2010) A missense mutation in the vacuolar protein GOLD36 causes organizational defects in the ER and aberrant protein trafficking in the plant secretory pathway. Plant J 63: 901-913.
    • (2010) Plant J , vol.63 , pp. 901-913
    • Marti, L.1    Stefano, G.2    Tamura, K.3    Hawes, C.4    Renna, L.5
  • 30
    • 0026604647 scopus 로고
    • Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum
    • Lewis MJ, Pelham HR, (1992) Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum. Cell 68: 353-364.
    • (1992) Cell , vol.68 , pp. 353-364
    • Lewis, M.J.1    Pelham, H.R.2
  • 31
    • 0026752711 scopus 로고
    • Immunological evidence that plants use both HDEL and KDEL for targeting proteins to the endoplasmic reticulum
    • Napier RM, Fowke LC, Hawes C, Lewis M, Pelham HR, (1992) Immunological evidence that plants use both HDEL and KDEL for targeting proteins to the endoplasmic reticulum. J Cell Sci 102 (Pt 2) (): 261-271.
    • (1992) J Cell Sci , vol.102 , Issue.Pt 2 , pp. 261-271
    • Napier, R.M.1    Fowke, L.C.2    Hawes, C.3    Lewis, M.4    Pelham, H.R.5
  • 32
    • 2942677348 scopus 로고    scopus 로고
    • NAI1 gene encodes a basic-helix-loop-helix-type putative transcription factor that regulates the formation of an endoplasmic reticulum-derived structure, the ER body
    • Matsushima R, Fukao Y, Nishimura M, Hara-Nishimura I, (2004) NAI1 gene encodes a basic-helix-loop-helix-type putative transcription factor that regulates the formation of an endoplasmic reticulum-derived structure, the ER body. Plant Cell 16: 1536-1549.
    • (2004) Plant Cell , vol.16 , pp. 1536-1549
    • Matsushima, R.1    Fukao, Y.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 33
    • 0242515793 scopus 로고    scopus 로고
    • A novel ER-derived compartment, the ER body, selectively accumulates a beta-glucosidase with an ER-retention signal in Arabidopsis
    • Matsushima R, Kondo M, Nishimura M, Hara-Nishimura I, (2003) A novel ER-derived compartment, the ER body, selectively accumulates a beta-glucosidase with an ER-retention signal in Arabidopsis. Plant J 33: 493-502.
    • (2003) Plant J , vol.33 , pp. 493-502
    • Matsushima, R.1    Kondo, M.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 34
    • 34249821366 scopus 로고    scopus 로고
    • Arabidopsis KAM2/GRV2 is required for proper endosome formation and functions in vacuolar sorting and determination of the embryo growth axis
    • Tamura K, Takahashi H, Kunieda T, Fuji K, Shimada T, et al. (2007) Arabidopsis KAM2/GRV2 is required for proper endosome formation and functions in vacuolar sorting and determination of the embryo growth axis. Plant Cell 19: 320-332.
    • (2007) Plant Cell , vol.19 , pp. 320-332
    • Tamura, K.1    Takahashi, H.2    Kunieda, T.3    Fuji, K.4    Shimada, T.5
  • 35
    • 0031080071 scopus 로고    scopus 로고
    • The C-terminal HDEL sequence is sufficient for retention of secretory proteins in the endoplasmic reticulum (ER) but promotes vacuolar targeting of proteins that escape the ER
    • Gomord V, Denmat LA, Fitchette-Lainé AC, Satiat-Jeunemaitre B, Hawes C, et al. (1997) The C-terminal HDEL sequence is sufficient for retention of secretory proteins in the endoplasmic reticulum (ER) but promotes vacuolar targeting of proteins that escape the ER. Plant J 11: 313-325.
    • (1997) Plant J , vol.11 , pp. 313-325
    • Gomord, V.1    Denmat, L.A.2    Fitchette-Lainé, A.C.3    Satiat-Jeunemaitre, B.4    Hawes, C.5
  • 36
    • 33745464631 scopus 로고    scopus 로고
    • The gene controlling the quantitative trait locus EPITHIOSPECIFIER MODIFIER1 alters glucosinolate hydrolysis and insect resistance in Arabidopsis
    • Zhang Z, Ober JA, Kliebenstein DJ, (2006) The gene controlling the quantitative trait locus EPITHIOSPECIFIER MODIFIER1 alters glucosinolate hydrolysis and insect resistance in Arabidopsis. Plant Cell 18: 1524-1536.
    • (2006) Plant Cell , vol.18 , pp. 1524-1536
    • Zhang, Z.1    Ober, J.A.2    Kliebenstein, D.J.3
  • 37
    • 74449084030 scopus 로고    scopus 로고
    • Stomagen positively regulates stomatal density in Arabidopsis
    • Sugano SS, Shimada T, Imai Y, Okawa K, Tamai A, et al. (2010) Stomagen positively regulates stomatal density in Arabidopsis. Nature 463: 241-244.
    • (2010) Nature , vol.463 , pp. 241-244
    • Sugano, S.S.1    Shimada, T.2    Imai, Y.3    Okawa, K.4    Tamai, A.5
  • 38
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough SJ, Bent AF, (1998) Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J 16: 735-743.
    • (1998) Plant J , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 39
    • 0042357049 scopus 로고    scopus 로고
    • Vacuolar processing enzymes are essential for proper processing of seed storage proteins in Arabidopsis thaliana
    • Shimada T, Yamada K, Kataoka M, Nakaune S, Koumoto Y, et al. (2003) Vacuolar processing enzymes are essential for proper processing of seed storage proteins in Arabidopsis thaliana. J Biol Chem 278: 32292-32299.
    • (2003) J Biol Chem , vol.278 , pp. 32292-32299
    • Shimada, T.1    Yamada, K.2    Kataoka, M.3    Nakaune, S.4    Koumoto, Y.5
  • 40
    • 57749091765 scopus 로고    scopus 로고
    • NAI2 is an endoplasmic reticulum body component that enables ER body formation in Arabidopsis thaliana
    • Yamada K, Nagano AJ, Nishina M, Hara-Nishimura I, Nishimura M, (2008) NAI2 is an endoplasmic reticulum body component that enables ER body formation in Arabidopsis thaliana. Plant Cell 20: 2529-2540.
    • (2008) Plant Cell , vol.20 , pp. 2529-2540
    • Yamada, K.1    Nagano, A.J.2    Nishina, M.3    Hara-Nishimura, I.4    Nishimura, M.5
  • 41
    • 25444452649 scopus 로고    scopus 로고
    • Activation of an ER-body-localized beta-glucosidase via a cytosolic binding partner in damaged tissues of Arabidopsis thaliana
    • Nagano AJ, Matsushima R, Hara-Nishimura I, (2005) Activation of an ER-body-localized beta-glucosidase via a cytosolic binding partner in damaged tissues of Arabidopsis thaliana. Plant Cell Physiol 46: 1140-1148.
    • (2005) Plant Cell Physiol , vol.46 , pp. 1140-1148
    • Nagano, A.J.1    Matsushima, R.2    Hara-Nishimura, I.3
  • 42
    • 0031106374 scopus 로고    scopus 로고
    • A rapid increase in the level of binding protein (BiP) is accompanied by synthesis and degradation of storage proteins in pumpkin cotyledons
    • Hatano K, Shimada T, Hiraiwa N, Nishimura M, Hara-Nishimura I, (1997) A rapid increase in the level of binding protein (BiP) is accompanied by synthesis and degradation of storage proteins in pumpkin cotyledons. Plant Cell Physiol 38: 344-351.
    • (1997) Plant Cell Physiol , vol.38 , pp. 344-351
    • Hatano, K.1    Shimada, T.2    Hiraiwa, N.3    Nishimura, M.4    Hara-Nishimura, I.5
  • 43
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJC, Creasy DM, Cottrell JS, (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. ELECTROPHORESIS 20: 3551-3567.
    • (1999) ELECTROPHORESIS , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.