메뉴 건너뛰기




Volumn 87, Issue 23, 2013, Pages 12756-12765

Prohibitin interacts with envelope proteins of white spot syndrome virus and prevents infection in the red swamp crayfish, Procambarus clarkii

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; PROHIBITIN; PROHIBITIN 1; PROTEIN VP24; PROTEIN VP26; PROTEIN VP28; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN;

EID: 84886806366     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02198-13     Document Type: Article
Times cited : (48)

References (55)
  • 1
    • 0001590871 scopus 로고    scopus 로고
    • The SPFH domain: implicated in regulating targeted protein turnover in stomatins and other membrane-associated proteins
    • Tavernarakis N, Driscoll M, Kyrpides NC. 1999. The SPFH domain: implicated in regulating targeted protein turnover in stomatins and other membrane-associated proteins. Trends Biochem. Sci. 24:425-427.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 425-427
    • Tavernarakis, N.1    Driscoll, M.2    Kyrpides, N.C.3
  • 2
    • 77953284896 scopus 로고    scopus 로고
    • Prohibitins:mitochondrial partners in development and stress response
    • Van Aken O, Whelan J, Van Breusegem F. 2010. Prohibitins:mitochondrial partners in development and stress response. Trends Plant Sci. 15: 275-282.
    • (2010) Trends Plant Sci. , vol.15 , pp. 275-282
    • Van Aken, O.1    Whelan, J.2    Van Breusegem, F.3
  • 4
    • 0029801945 scopus 로고    scopus 로고
    • Prohibitin in breast cancer cell lines:loss of antiproliferative activity is linked to 3= untranslated region mutations
    • Jupe ER, Liu XT, Kiehlbauch JL, McClung JK, Dell'Orco RT. 1996. Prohibitin in breast cancer cell lines:loss of antiproliferative activity is linked to 3= untranslated region mutations. Cell Growth Differ. 7:871-878.
    • (1996) Cell Growth Differ. , vol.7 , pp. 871-878
    • Jupe, E.R.1    Liu, X.T.2    Kiehlbauch, J.L.3    McClung, J.K.4    Dell'Orco, R.T.5
  • 5
    • 57349146677 scopus 로고    scopus 로고
    • MicroRNA-27a functions as an oncogene in gastric adenocarcinoma by targeting prohibitin
    • Liu T, Tang H, Lang Y, Liu M, Li X. 2009. MicroRNA-27a functions as an oncogene in gastric adenocarcinoma by targeting prohibitin. Cancer Lett. 273:233-242.
    • (2009) Cancer Lett. , vol.273 , pp. 233-242
    • Liu, T.1    Tang, H.2    Lang, Y.3    Liu, M.4    Li, X.5
  • 6
    • 33747196977 scopus 로고    scopus 로고
    • The prohibitins:emerging roles in diverse functions
    • Mishra S, Murphy LC, Murphy LJ. 2006. The prohibitins:emerging roles in diverse functions. J. Cell. Mol. Med. 10:353-363.
    • (2006) J. Cell. Mol. Med. , vol.10 , pp. 353-363
    • Mishra, S.1    Murphy, L.C.2    Murphy, L.J.3
  • 7
    • 56349102165 scopus 로고    scopus 로고
    • Prohibitin function within mitochondria: essential roles for cell proliferation and cristae morphogenesis
    • Merkwirth C, Langer T. 2009. Prohibitin function within mitochondria: essential roles for cell proliferation and cristae morphogenesis. Biochim. Biophys. Acta 1793:27-32.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 27-32
    • Merkwirth, C.1    Langer, T.2
  • 8
    • 6044254763 scopus 로고    scopus 로고
    • Differential immunization identifies PHB1/PHB2 as blood-borne tumor antigens
    • Mengwasser J, Piau A, Schlag P, Sleeman JP. 2004. Differential immunization identifies PHB1/PHB2 as blood-borne tumor antigens. Oncogene 23:7430-7435.
    • (2004) Oncogene , vol.23 , pp. 7430-7435
    • Mengwasser, J.1    Piau, A.2    Schlag, P.3    Sleeman, J.P.4
  • 9
    • 77956632914 scopus 로고    scopus 로고
    • The role of prohibitin in cell signaling
    • Mishra S, Ande SR, Nyomba BL. 2010. The role of prohibitin in cell signaling. FEBS J. 277:3937-3946.
    • (2010) FEBS J. , vol.277 , pp. 3937-3946
    • Mishra, S.1    Ande, S.R.2    Nyomba, B.L.3
  • 11
    • 67651097640 scopus 로고    scopus 로고
    • Insulin induced phosphorylation of prohibitin at tyrosine 114 recruits Shp1
    • Ande SR, Gu Y, Nyomba BL, Mishra S. 2009. Insulin induced phosphorylation of prohibitin at tyrosine 114 recruits Shp1. Biochim. Biophys. Acta 1793:1372-1378.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 1372-1378
    • Ande, S.R.1    Gu, Y.2    Nyomba, B.L.3    Mishra, S.4
  • 12
    • 70449705816 scopus 로고    scopus 로고
    • Prohibitin interacts with phosphatidylinositol 3,4,5-triphosphate (PIP3) and modulates insulin signaling
    • Ande SR, Mishra S. 2009. Prohibitin interacts with phosphatidylinositol 3,4,5-triphosphate (PIP3) and modulates insulin signaling. Biochem. Biophys. Res. Commun. 390:1023-1028.
    • (2009) Biochem. Biophys. Res. Commun. , vol.390 , pp. 1023-1028
    • Ande, S.R.1    Mishra, S.2
  • 14
    • 33749017960 scopus 로고    scopus 로고
    • Prohibitin and cofilin are intracellular effectors of transforming growth factor beta signaling in human prostate cancer cells
    • Zhu B, Fukada K, Zhu H, Kyprianou N. 2006. Prohibitin and cofilin are intracellular effectors of transforming growth factor beta signaling in human prostate cancer cells. Cancer Res. 66:8640-8647.
    • (2006) Cancer Res. , vol.66 , pp. 8640-8647
    • Zhu, B.1    Fukada, K.2    Zhu, H.3    Kyprianou, N.4
  • 15
    • 77956173389 scopus 로고    scopus 로고
    • Identification and characterization of prohibitin as a receptor protein mediating DENV-2 entry into insect cells
    • Kuadkitkan A, Wikan N, Fongsaran C, Smith DR. 2010. Identification and characterization of prohibitin as a receptor protein mediating DENV-2 entry into insect cells. Virology 406:149-161.
    • (2010) Virology , vol.406 , pp. 149-161
    • Kuadkitkan, A.1    Wikan, N.2    Fongsaran, C.3    Smith, D.R.4
  • 16
    • 34250808501 scopus 로고    scopus 로고
    • The leucine-rich repeat (LRR) protein, CaLRR1, interacts with the hypersensitive induced reaction (HIR) protein, CaHIR1, and suppresses cell death induced by the CaHIR1 protein
    • Jung HW, Hwang BK. 2007. The leucine-rich repeat (LRR) protein, CaLRR1, interacts with the hypersensitive induced reaction (HIR) protein, CaHIR1, and suppresses cell death induced by the CaHIR1 protein. Mol. Plant Pathol. 8:503-514.
    • (2007) Mol. Plant Pathol. , vol.8 , pp. 503-514
    • Jung, H.W.1    Hwang, B.K.2
  • 17
    • 40949117085 scopus 로고    scopus 로고
    • Distinct roles of the pepper hypersensitive induced reaction protein gene CaHIR1 in disease and osmotic stress, as determined by comparative transcriptome and proteome analyses
    • Jung HW, Lim CW, Lee SC, Choi HW, Hwang CH, Hwang BK. 2008. Distinct roles of the pepper hypersensitive induced reaction protein gene CaHIR1 in disease and osmotic stress, as determined by comparative transcriptome and proteome analyses. Planta 227:409-425.
    • (2008) Planta , vol.227 , pp. 409-425
    • Jung, H.W.1    Lim, C.W.2    Lee, S.C.3    Choi, H.W.4    Hwang, C.H.5    Hwang, B.K.6
  • 18
    • 33751100626 scopus 로고    scopus 로고
    • The plant immune system
    • Jones JD, Dangl JL. 2006. The plant immune system. Nature 444:323-329.
    • (2006) Nature , vol.444 , pp. 323-329
    • Jones, J.D.1    Dangl, J.L.2
  • 19
    • 68149172458 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the translationally controlled tumor protein from Fenneropenaeus chinensis
    • Wang S, Zhao XF, Wang JX. 2009. Molecular cloning and characterization of the translationally controlled tumor protein from Fenneropenaeus chinensis. Mol. Biol. Rep. 36:1683-1693.
    • (2009) Mol. Biol. Rep. , vol.36 , pp. 1683-1693
    • Wang, S.1    Zhao, X.F.2    Wang, J.X.3
  • 20
    • 77951126524 scopus 로고    scopus 로고
    • Three Kazal-type serine proteinase inhibitors from the red swamp crayfish Procambarus clarkii and the characterization, function analysis of hcPcSPI2
    • Li XC, Zhang RR, Sun RR, Lan JF, Zhao XF, Wang JX. 2010. Three Kazal-type serine proteinase inhibitors from the red swamp crayfish Procambarus clarkii and the characterization, function analysis of hcPcSPI2. Fish Shellfish Immunol. 28:942-951.
    • (2010) Fish Shellfish Immunol. , vol.28 , pp. 942-951
    • Li, X.C.1    Zhang, R.R.2    Sun, R.R.3    Lan, J.F.4    Zhao, X.F.5    Wang, J.X.6
  • 21
    • 54849440103 scopus 로고    scopus 로고
    • Molecular cloning and expression analysis of chymotrypsin-like serine protease from the Chinese shrimp, Fenneropenaeus chinensis
    • Shi XZ, Zhao XF, Wang JX. 2008. Molecular cloning and expression analysis of chymotrypsin-like serine protease from the Chinese shrimp, Fenneropenaeus chinensis. Fish Shellfish Immunol. 25:589-597.
    • (2008) Fish Shellfish Immunol. , vol.25 , pp. 589-597
    • Shi, X.Z.1    Zhao, X.F.2    Wang, J.X.3
  • 22
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method
    • Livak KJ, Schmittgen TD. 2001. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 25:402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 23
    • 33644539486 scopus 로고    scopus 로고
    • Identification and molecular characterization of a peritrophin-like protein from fleshy prawn (Fenneropenaeus chinensis)
    • Du XJ, Wang JX, Liu N, Zhao XF, Li FH, Xiang JH. 2006. Identification and molecular characterization of a peritrophin-like protein from fleshy prawn (Fenneropenaeus chinensis). Mol. Immunol. 43:1633-1644.
    • (2006) Mol. Immunol. , vol.43 , pp. 1633-1644
    • Du, X.J.1    Wang, J.X.2    Liu, N.3    Zhao, X.F.4    Li, F.H.5    Xiang, J.H.6
  • 24
    • 33748761934 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a lipopolysaccharide and beta-1,3-glucan binding protein from fleshy prawn (Fenneropenaeus chinensis)
    • Du XJ, Zhao XF, Wang JX. 2007. Molecular cloning and characterization of a lipopolysaccharide and beta-1,3-glucan binding protein from fleshy prawn (Fenneropenaeus chinensis). Mol. Immunol. 44:1085-1094.
    • (2007) Mol. Immunol. , vol.44 , pp. 1085-1094
    • Du, X.J.1    Zhao, X.F.2    Wang, J.X.3
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 66949167063 scopus 로고    scopus 로고
    • TRBP homolog interacts with eukaryotic initiation factor 6 (eIF6) in Fenneropenaeus chinensis
    • Wang S, Liu N, Chen AJ, Zhao XF, Wang JX. 2009. TRBP homolog interacts with eukaryotic initiation factor 6 (eIF6) in Fenneropenaeus chinensis. J. Immunol. 182:5250-5258.
    • (2009) J. Immunol. , vol.182 , pp. 5250-5258
    • Wang, S.1    Liu, N.2    Chen, A.J.3    Zhao, X.F.4    Wang, J.X.5
  • 28
    • 77449152144 scopus 로고    scopus 로고
    • Conjugation of colloidal gold to proteins
    • Oliver C. 2010. Conjugation of colloidal gold to proteins. Methods Mol. Biol. 588:369-373.
    • (2010) Methods Mol. Biol. , vol.588 , pp. 369-373
    • Oliver, C.1
  • 29
    • 12844271179 scopus 로고    scopus 로고
    • A simple and efficient method for purification of intact white spot syndrome virus (WSSV) viral particles
    • Xie X, Li H, Xu L, Yang F. 2005. A simple and efficient method for purification of intact white spot syndrome virus (WSSV) viral particles. Virus Res. 108:63-67.
    • (2005) Virus Res. , vol.108 , pp. 63-67
    • Xie, X.1    Li, H.2    Xu, L.3    Yang, F.4
  • 30
    • 80455162309 scopus 로고    scopus 로고
    • A vector that expresses VP28 of WSSV can protect red swamp crayfish from white spot disease
    • Mu Y, Lan JF, Zhang XW, Wang XW, Zhao XF, Wang JX. 2012. A vector that expresses VP28 of WSSV can protect red swamp crayfish from white spot disease. Dev. Comp. Immunol. 36:442-449.
    • (2012) Dev. Comp. Immunol. , vol.36 , pp. 442-449
    • Mu, Y.1    Lan, J.F.2    Zhang, X.W.3    Wang, X.W.4    Zhao, X.F.5    Wang, J.X.6
  • 32
    • 84872000931 scopus 로고    scopus 로고
    • SUMOconjugating enzyme E2 UBC9 mediates viral immediate-early protein SUMOylation in crayfish to facilitate reproduction of white spot syndrome virus
    • Chen AJ, Gao L, Wang XW, Zhao XF, Wang JX. 2013. SUMOconjugating enzyme E2 UBC9 mediates viral immediate-early protein SUMOylation in crayfish to facilitate reproduction of white spot syndrome virus. J. Virol. 87:636-647.
    • (2013) J. Virol. , vol.87 , pp. 636-647
    • Chen, A.J.1    Gao, L.2    Wang, X.W.3    Zhao, X.F.4    Wang, J.X.5
  • 33
    • 33747840389 scopus 로고    scopus 로고
    • GRAMM-X public web server for protein-protein docking
    • Tovchigrechko A, Vakser IA. 2006. GRAMM-X public web server for protein-protein docking. Nucleic Acids Res. 34:W310-W314.
    • (2006) Nucleic Acids Res. , vol.34
    • Tovchigrechko, A.1    Vakser, I.A.2
  • 34
    • 0038526303 scopus 로고    scopus 로고
    • ZDOCK:an initial-stage protein-docking algorithm
    • Chen R, Li L, Weng Z. 2003. ZDOCK:an initial-stage protein-docking algorithm. Proteins 52:80-87.
    • (2003) Proteins , vol.52 , pp. 80-87
    • Chen, R.1    Li, L.2    Weng, Z.3
  • 36
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • doi:10.1186/1471-2105-9-40
    • Zhang Y. 2008. I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9:40. doi:10.1186/1471-2105-9-40.
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1
  • 37
    • 33646854930 scopus 로고    scopus 로고
    • Proteomics of Rac GTPase signaling reveals its predominant role in elicitor-induced defense response of cultured rice cells
    • Fujiwara M, Umemura K, Kawasaki T, Shimamoto K. 2006. Proteomics of Rac GTPase signaling reveals its predominant role in elicitor-induced defense response of cultured rice cells. Plant Physiol. 140:734-745.
    • (2006) Plant Physiol. , vol.140 , pp. 734-745
    • Fujiwara, M.1    Umemura, K.2    Kawasaki, T.3    Shimamoto, K.4
  • 40
    • 41949089066 scopus 로고    scopus 로고
    • The PHB1/2 phosphocomplex is required for mitochondrial homeostasis and survival of human T cells
    • Ross JA, Nagy ZS, Kirken RA. 2008. The PHB1/2 phosphocomplex is required for mitochondrial homeostasis and survival of human T cells. J. Biol. Chem. 283:4699-4713.
    • (2008) J. Biol. Chem. , vol.283 , pp. 4699-4713
    • Ross, J.A.1    Nagy, Z.S.2    Kirken, R.A.3
  • 41
    • 73949150062 scopus 로고    scopus 로고
    • Identification of the cellular prohibitin 1/prohibitin 2 heterodimer as an interaction partner of the C-terminal cytoplasmic domain of the HIV-1 glycoprotein
    • Emerson V, Holtkotte D, Pfeiffer T, Wang IH, Schnolzer M, Kempf T, Bosch V. 2010. Identification of the cellular prohibitin 1/prohibitin 2 heterodimer as an interaction partner of the C-terminal cytoplasmic domain of the HIV-1 glycoprotein. J. Virol. 84:1355-1365.
    • (2010) J. Virol. , vol.84 , pp. 1355-1365
    • Emerson, V.1    Holtkotte, D.2    Pfeiffer, T.3    Wang, I.H.4    Schnolzer, M.5    Kempf, T.6    Bosch, V.7
  • 42
    • 69949122935 scopus 로고    scopus 로고
    • Endogenous HIV-1 Vpr-mediated apoptosis and proteome alteration of human T-cell leukemia virus-1 transformed C8166 cells
    • He F, Zeng Y, Wu X, Ji Y, He X, Andrus T, Zhu T, Wang T. 2009. Endogenous HIV-1 Vpr-mediated apoptosis and proteome alteration of human T-cell leukemia virus-1 transformed C8166 cells. Apoptosis 14: 1212-1226.
    • (2009) Apoptosis , vol.14 , pp. 1212-1226
    • He, F.1    Zeng, Y.2    Wu, X.3    Ji, Y.4    He, X.5    Andrus, T.6    Zhu, T.7    Wang, T.8
  • 43
    • 14844282115 scopus 로고    scopus 로고
    • A novel C-type immulectin-3 from Manduca sexta is translocated from hemolymph into the cytoplasm of hemocytes
    • Yu XQ, Tracy ME, Ling E, Scholz FR, Trenczek T. 2005. A novel C-type immulectin-3 from Manduca sexta is translocated from hemolymph into the cytoplasm of hemocytes. Insect Biochem. Mol. Biol. 35:285-295.
    • (2005) Insect Biochem. Mol. Biol. , vol.35 , pp. 285-295
    • Yu, X.Q.1    Tracy, M.E.2    Ling, E.3    Scholz, F.R.4    Trenczek, T.5
  • 44
    • 79961199685 scopus 로고    scopus 로고
    • Enzyme E2 from Chinese white shrimp inhibits replication of white spot syndrome virus and ubiquitinates its RING domain proteins
    • Chen AJ, Wang S, Zhao XF, Yu XQ, Wang JX. 2011. Enzyme E2 from Chinese white shrimp inhibits replication of white spot syndrome virus and ubiquitinates its RING domain proteins. J. Virol. 85:8069-8079.
    • (2011) J. Virol. , vol.85 , pp. 8069-8079
    • Chen, A.J.1    Wang, S.2    Zhao, X.F.3    Yu, X.Q.4    Wang, J.X.5
  • 45
    • 34848914211 scopus 로고    scopus 로고
    • Prohibitin binds to C3 and enhances complement activation
    • Mishra S, Moulik S, Murphy LJ. 2007. Prohibitin binds to C3 and enhances complement activation. Mol. Immunol. 44:1897-1902.
    • (2007) Mol. Immunol. , vol.44 , pp. 1897-1902
    • Mishra, S.1    Moulik, S.2    Murphy, L.J.3
  • 46
    • 0035811840 scopus 로고    scopus 로고
    • White spot syndrome virus envelope protein VP28 is involved in the systemic infection of shrimp
    • van Hulten MC, Witteveldt J, Snippe M, Vlak JM. 2001. White spot syndrome virus envelope protein VP28 is involved in the systemic infection of shrimp. Virology 285:228-233.
    • (2001) Virology , vol.285 , pp. 228-233
    • van Hulten, M.C.1    Witteveldt, J.2    Snippe, M.3    Vlak, J.M.4
  • 47
    • 66149142139 scopus 로고    scopus 로고
    • Four major envelope proteins of white spot syndrome virus bind to form a complex
    • Zhou Q, Xu L, Li H, Qi YP, Yang F. 2009. Four major envelope proteins of white spot syndrome virus bind to form a complex. J. Virol. 83:4709-4712.
    • (2009) J. Virol. , vol.83 , pp. 4709-4712
    • Zhou, Q.1    Xu, L.2    Li, H.3    Qi, Y.P.4    Yang, F.5
  • 48
    • 13544250708 scopus 로고    scopus 로고
    • Vp28 of shrimp white spot syndrome virus is involved in the attachment and penetration into shrimp cells
    • Yi G, Wang Z, Qi Y, Yao L, Qian J, Hu L. 2004. Vp28 of shrimp white spot syndrome virus is involved in the attachment and penetration into shrimp cells. J. Biochem. Mol. Biol. 37:726-734.
    • (2004) J. Biochem. Mol. Biol. , vol.37 , pp. 726-734
    • Yi, G.1    Wang, Z.2    Qi, Y.3    Yao, L.4    Qian, J.5    Hu, L.6
  • 49
    • 0033799648 scopus 로고    scopus 로고
    • Three functionally diverged major structural proteins of white spot syndrome virus evolved by gene duplication
    • van Hulten MC, Goldbach RW, Vlak JM. 2000. Three functionally diverged major structural proteins of white spot syndrome virus evolved by gene duplication. J. Gen. Virol. 81:2525-2529.
    • (2000) J. Gen. Virol. , vol.81 , pp. 2525-2529
    • van Hulten, M.C.1    Goldbach, R.W.2    Vlak, J.M.3
  • 50
    • 34249944303 scopus 로고    scopus 로고
    • Crystal structures of major envelope proteins VP26 and VP28 from white spot syndrome virus shed light on their evolutionary relationship
    • Tang X, Wu J, Sivaraman J, Hew CL. 2007. Crystal structures of major envelope proteins VP26 and VP28 from white spot syndrome virus shed light on their evolutionary relationship. J. Virol. 81:6709-6717.
    • (2007) J. Virol. , vol.81 , pp. 6709-6717
    • Tang, X.1    Wu, J.2    Sivaraman, J.3    Hew, C.L.4
  • 51
    • 33750330669 scopus 로고    scopus 로고
    • Proteomic analysis of the major envelope and nucleocapsid proteins of white spot syndrome virus
    • Xie X, Xu L, Yang F. 2006. Proteomic analysis of the major envelope and nucleocapsid proteins of white spot syndrome virus. J. Virol. 80:10615-10623.
    • (2006) J. Virol. , vol.80 , pp. 10615-10623
    • Xie, X.1    Xu, L.2    Yang, F.3
  • 52
    • 0038314400 scopus 로고    scopus 로고
    • Virus entry, assembly, budding, and membrane rafts
    • Chazal N, Gerlier D. 2003. Virus entry, assembly, budding, and membrane rafts. Microbiol. Mol. Biol. Rev. 67:226-237.
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 226-237
    • Chazal, N.1    Gerlier, D.2
  • 55
    • 33745621561 scopus 로고    scopus 로고
    • White spot syndrome virus VP24 interacts with VP28 and is involved in virus infection
    • Xie X, Yang F. 2006. White spot syndrome virus VP24 interacts with VP28 and is involved in virus infection. J. Gen. Virol. 87:1903-1908.
    • (2006) J. Gen. Virol. , vol.87 , pp. 1903-1908
    • Xie, X.1    Yang, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.