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Volumn 10, Issue , 2013, Pages 58-68

Apolipophorins and insects immune response

Author keywords

Apolipophorin III; Galleria mellonella; Insect immunity; Lipophorin

Indexed keywords


EID: 84890426667     PISSN: None     EISSN: 1824307X     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (72)

References (102)
  • 1
    • 41149127811 scopus 로고    scopus 로고
    • Competition between immune function and lipid transport for the protein apolipophorin III leads to stress-induced immunosuppression in crickets
    • Adamo SA, Roberts JL, Easy RH, Ross NW. Competition between immune function and lipid transport for the protein apolipophorin III leads to stress-induced immunosuppression in crickets. J. Exp. Biol. 211: 531-538, 2008.
    • (2008) J. Exp. Biol. , vol.211 , pp. 531-538
    • Adamo, S.A.1    Roberts, J.L.2    Easy, R.H.3    Ross, N.W.4
  • 2
    • 0023937366 scopus 로고
    • Human apolipoprotein E3 in aqueous solution II. Properties of the amino- carboxyl-terminal domains
    • Aggerbeck LP, Wetterau KH, Weisgraber KH, Wu C-SC, Lindergren FT. Human apolipoprotein E3 in aqueous solution II. Properties of the amino- carboxyl-terminal domains. J. Biol. Chem. 263: 6249-6258, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6249-6258
    • Aggerbeck, L.P.1    Wetterau, K.H.2    Weisgraber, K.H.3    Wu, C.-S.C.4    Lindergren, F.T.5
  • 3
    • 34247114978 scopus 로고    scopus 로고
    • Preliminary characterization of hemolymph coagulation in Anopheles gambiae larvae
    • Agianian B, Lesch C, Loseva O, Dushay MS. Preliminary characterization of hemolymph coagulation in Anopheles gambiae larvae. Dev. Comp. Immunol. 31: 879-888, 2007.
    • (2007) Dev. Comp. Immunol. , vol.31 , pp. 879-888
    • Agianian, B.1    Lesch, C.2    Loseva, O.3    Dushay, M.S.4
  • 4
    • 53149116721 scopus 로고    scopus 로고
    • Host-derived extracellular nucleic acids enhance innate immune responses, induce coagulation, and prolong survival upon infection in insects
    • Altincicek B, Stötzel S, Wygrecka M, Preissner KT, Vilcinskas A. Host-derived extracellular nucleic acids enhance innate immune responses, induce coagulation, and prolong survival upon infection in insects. J Immunol. 181: 2705-2712, 2008.
    • (2008) J Immunol. , vol.181 , pp. 2705-2712
    • Altincicek, B.1    Stötzel, S.2    Wygrecka, M.3    Preissner, K.T.4    Vilcinskas, A.5
  • 5
    • 15944373508 scopus 로고    scopus 로고
    • Apolipophorin III is a substrate for protease IV from Pseudomonas aeruginosa
    • Andrejko M, Cytryńska M, Jakubowicz T. Apolipophorin III is a substrate for protease IV from Pseudomonas aeruginosa. FEMS Microbiol. Lett. 243: 331-337, 2005.
    • (2005) FEMS Microbiol. Lett. , vol.243 , pp. 331-337
    • Andrejko, M.1    Cytryńska, M.2    Jakubowicz, T.3
  • 6
    • 84874099183 scopus 로고    scopus 로고
    • Effect of Pseudomonas aeruginosa elastase B on level and activity of immune proteins/peptides of Galleria mellonella hemolymph
    • Andrejko M, Mizerska-Dudka M. Effect of Pseudomonas aeruginosa elastase B on level and activity of immune proteins/peptides of Galleria mellonella hemolymph. J. Insect. Sci. 12: 88, 2012.
    • (2012) J. Insect. Sci. , vol.12 , pp. 88
    • Andrejko, M.1    Mizerska-Dudka, M.2
  • 7
    • 36849047229 scopus 로고    scopus 로고
    • Changes in Galleria mellonella apolipophorin III level during Pseudomonas aeruginosa infection
    • Andrejko M, Mizerska-Dudka M, Jakubowicz T. Changes in Galleria mellonella apolipophorin III level during Pseudomonas aeruginosa infection. J. Invertebr. Pathol. 97: 14-19, 2008.
    • (2008) J. Invertebr. Pathol. , vol.97 , pp. 14-19
    • Andrejko, M.1    Mizerska-Dudka, M.2    Jakubowicz, T.3
  • 8
    • 84877622232 scopus 로고    scopus 로고
    • Diverse susceptibility of Galleria mellonella humoral immune response factors to the exoproteinase activity of entomopathogenic and clinical strains of Pseudomonas aeruginosa
    • Andrejko M, Zdybicka-Barabas A, Wawrzoszek M, Cytryńska M. Diverse susceptibility of Galleria mellonella humoral immune response factors to the exoproteinase activity of entomopathogenic and clinical strains of Pseudomonas aeruginosa. Zool. Sci. 30: 345-351, 2013.
    • (2013) Zool. Sci. , vol.30 , pp. 345-351
    • Andrejko, M.1    Zdybicka-Barabas, A.2    Wawrzoszek, M.3    Cytryńska, M.4
  • 11
    • 0032941090 scopus 로고    scopus 로고
    • Apolipoprotein E knock-out mice are highly susceptible to endotoxemia and Klebsiella pneumoniae infection
    • Bont N, Netea MG, Demacker PNM, Verschueren I, Kullberg BJ, Van Dijk KW, et al. Apolipoprotein E knock-out mice are highly susceptible to endotoxemia and Klebsiella pneumoniae infection. J. Lipid Res. 40: 680-685, 1999.
    • (1999) J. Lipid Res. , vol.40 , pp. 680-685
    • Bont, N.1    Netea, M.G.2    Demacker, P.N.M.3    Verschueren, I.4    Kullberg, B.J.5    Van Dijk, K.W.6
  • 13
    • 77954083148 scopus 로고    scopus 로고
    • A pathogenic parasite interferes with phagocytosis of insect immunocompetent cells
    • Brivio MF, Mastore M, Nappi AJ. A pathogenic parasite interferes with phagocytosis of insect immunocompetent cells. Dev. Comp. Immunol. 34: 991-998, 2010.
    • (2010) Dev. Comp. Immunol. , vol.34 , pp. 991-998
    • Brivio, M.F.1    Mastore, M.2    Nappi, A.J.3
  • 14
    • 33645421838 scopus 로고    scopus 로고
    • Parasite-host relationship: A lesson from a professional killer
    • Brivio MF, Mastore M, Pagani M. Parasite-host relationship: a lesson from a professional killer. Inv. Surv. J. 2: 41-53, 2005.
    • (2005) Inv. Surv. J. , vol.2 , pp. 41-53
    • Brivio, M.F.1    Mastore, M.2    Pagani, M.3
  • 15
    • 0021765682 scopus 로고
    • Structural studies of apolipoprotein A-I/phosphatidylcholine recombinants by high-field proton NMR, nondenaturing gradient gel electrophoresis, and electron microscopy
    • Brouillette CG, Jones JL, Ng TC, Kercret H, Chung BH, Segrest J. P. Structural studies of apolipoprotein A-I/phosphatidylcholine recombinants by high-field proton NMR, nondenaturing gradient gel electrophoresis, and electron microscopy. Biochemistry 23: 359-367, 1984.
    • (1984) Biochemistry , vol.23 , pp. 359-367
    • Brouillette, C.G.1    Jones, J.L.2    Ng, T.C.3    Kercret, H.4    Chung, B.H.5    Segrest, J.P.6
  • 16
    • 38249008493 scopus 로고
    • Characteristic of apolipophorin-III of the southwestern corn borer, Diatraea grandiosella
    • Burks CS, Shelby KS, Chippendale GM. Characteristic of apolipophorin-III of the southwestern corn borer, Diatraea grandiosella. Insect Biochem. Mol. Biol. 22: 905-915, 1992.
    • (1992) Insect Biochem. Mol. Biol. , vol.22 , pp. 905-915
    • Burks, C.S.1    Shelby, K.S.2    Chippendale, G.M.3
  • 17
    • 0022501235 scopus 로고
    • Apolipophorin III In locust: Purification and characterization
    • Chino H, Yazawa M. Apolipophorin III In locust: purification and characterization. J. Lipid Res. 27: 377-385, 1986.
    • (1986) J. Lipid Res. , vol.27 , pp. 377-385
    • Chino, H.1    Yazawa, M.2
  • 18
    • 70349501783 scopus 로고    scopus 로고
    • Apolipophorin III interaction with model membranes composed of phosphatidylcholine and sphingomyelin using differential scanning calorimetry
    • Chiu MH, Wan Ch-P, Weers PMM, Prenner EJ. Apolipophorin III interaction with model membranes composed of phosphatidylcholine and sphingomyelin using differential scanning calorimetry. Biochim. Biophys. Acta 1788: 2160-2168, 2009.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 2160-2168
    • Chiu, M.H.1    Wan, C.-P.2    Weers, P.M.M.3    Prenner, E.J.4
  • 19
    • 0035988708 scopus 로고    scopus 로고
    • Purification and characterization of apolipophorin III from immune hemolymph of Heliothis virescens pupae
    • Chung KT, Ourth DD. Purification and characterization of apolipophorin III from immune hemolymph of Heliothis virescens pupae. Comp. Biochem. Physiol. 132B: 505-514, 2002.
    • (2002) Comp. Biochem. Physiol. , vol.132 B , pp. 505-514
    • Chung, K.T.1    Ourth, D.D.2
  • 20
    • 34547927446 scopus 로고    scopus 로고
    • The structure of apolipoprotein A-I in high density lipoproteins
    • Davidson WS, Thompson TB. The structure of apolipoprotein A-I in high density lipoproteins. J. Biol. Chem. 282: 22249-22253, 2007.
    • (2007) J. Biol. Chem. , vol.282 , pp. 22249-22253
    • Davidson, W.S.1    Thompson, T.B.2
  • 22
    • 0035009726 scopus 로고    scopus 로고
    • Localization of injected apolipophorin III in vivo-new insights into the immune activation process directed by this protein
    • Dettloff M, Kaiser B, Wiesner A. Localization of injected apolipophorin III in vivo-new insights into the immune activation process directed by this protein. J. Insect Physiol. 47: 789-797, 2001a.
    • (2001) J. Insect Physiol. , vol.47 , pp. 789-797
    • Dettloff, M.1    Kaiser, B.2    Wiesner, A.3
  • 23
    • 0035213499 scopus 로고    scopus 로고
    • Lipophorin of a lower density is formed during immune responses in the lepidopteran insect Galleria mellonella
    • Dettloff M, Wittwer D, Weise C, Wiesner A. Lipophorin of a lower density is formed during immune responses in the lepidopteran insect Galleria mellonella. Cell Tissue Res. 306: 449-458, 2001b.
    • (2001) Cell Tissue Res. , vol.306 , pp. 449-458
    • Dettloff, M.1    Wittwer, D.2    Weise, C.3    Wiesner, A.4
  • 24
    • 0031252949 scopus 로고    scopus 로고
    • Haemolymph proteins of larvae of Galleria mellonella detoxify endotoxins of the insect pathogenic bacteria Xenorhabdus nematophilus (Enterobacteriaceae)
    • Dunphy G, Halwani A. Haemolymph proteins of larvae of Galleria mellonella detoxify endotoxins of the insect pathogenic bacteria Xenorhabdus nematophilus (Enterobacteriaceae). J. Insect Physiol. 43: 1023-1029, 1997.
    • (1997) J. Insect Physiol. , vol.43 , pp. 1023-1029
    • Dunphy, G.1    Halwani, A.2
  • 25
    • 68549133224 scopus 로고    scopus 로고
    • Insect hemolymph clotting
    • Dushay MS. Insect hemolymph clotting. Cell. Mol. Life Sci. 66: 2643-2650, 2009.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 2643-2650
    • Dushay, M.S.1
  • 26
    • 0032407614 scopus 로고    scopus 로고
    • Two major proteins from locust plasma are involved in coagulation and are specifically precipitated by laminarin, a beta-1, 3-glucan
    • Duvic B, Brehélin M. Two major proteins from locust plasma are involved in coagulation and are specifically precipitated by laminarin, a beta-1, 3-glucan. Insect Biochem. Mol. Biol. 28: 959-967, 1998.
    • (1998) Insect Biochem. Mol. Biol. , vol.28 , pp. 959-967
    • Duvic, B.1    Brehélin, M.2
  • 27
    • 0038418381 scopus 로고    scopus 로고
    • NMR solution structure and dynamics of an exchangeable apolipoprotein, Locusta migratoria apolipophorin III
    • Fan D, Zheng Y, Yang D, Wang J. NMR solution structure and dynamics of an exchangeable apolipoprotein, Locusta migratoria apolipophorin III. J. Biol. Chem. 278: 21212-21220, 2003.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21212-21220
    • Fan, D.1    Zheng, Y.2    Yang, D.3    Wang, J.4
  • 28
    • 0037205467 scopus 로고    scopus 로고
    • Structure of apolipophorin III in discoidal lipoproteins. Interhelical distances in the lipid-bound state and conformational change upon binding to lipid
    • Garda HA, Arrese EL, Soulages JL. Structure of apolipophorin III in discoidal lipoproteins. Interhelical distances in the lipid-bound state and conformational change upon binding to lipid. J. Biol. Chem. 277: 19773-19782, 2002.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19773-19782
    • Garda, H.A.1    Arrese, E.L.2    Soulages, J.L.3
  • 29
    • 78149477892 scopus 로고    scopus 로고
    • Apolipophorin-III mediates antiplasmodial epithelial responses in Anopheles gambiae (G3) mosquitoes
    • Gupta L, Noh JY, Jo YH, Oh SH, Kumar S, Noh MY, et al. Apolipophorin-III mediates antiplasmodial epithelial responses in Anopheles gambiae (G3) mosquitoes. PLoS ONE 5: e15410. doi:10. 1371/journal. pone. 0015410, 2010.
    • (2010) PLoS ONE , vol.5
    • Gupta, L.1    Noh, J.Y.2    Jo, Y.H.3    Oh, S.H.4    Kumar, S.5    Noh, M.Y.6
  • 30
    • 0032754032 scopus 로고    scopus 로고
    • Apolipophorin III in Galleria mellonella potentiates hemolymph lytic activity
    • Halwani AE, Dunphy GB. Apolipophorin III in Galleria mellonella potentiates hemolymph lytic activity. Dev. Comp. Immunol. 23: 563-570, 1999.
    • (1999) Dev. Comp. Immunol. , vol.23 , pp. 563-570
    • Halwani, A.E.1    Dunphy, G.B.2
  • 31
    • 0034521485 scopus 로고    scopus 로고
    • Apolipophorin-III and the interactions of lipoteichoic acids with the immediate immune responses of Galleria mellonella
    • Halwani AE, Niven DF, Dunphy GB. Apolipophorin-III and the interactions of lipoteichoic acids with the immediate immune responses of Galleria mellonella. J. Invertebr. Pathol. 76: 233-241, 2000.
    • (2000) J. Invertebr. Pathol. , vol.76 , pp. 233-241
    • Halwani, A.E.1    Niven, D.F.2    Dunphy, G.B.3
  • 32
    • 80655144740 scopus 로고    scopus 로고
    • Silkworm apolipophorin protein inhibits Staphylococcus aureus virulence
    • Hanada Y, Sekimizu K, Kaito C. Silkworm apolipophorin protein inhibits Staphylococcus aureus virulence. J. Biol. Chem. 286: 39360-39369, 2011.
    • (2011) J. Biol. Chem. , vol.286 , pp. 39360-39369
    • Hanada, Y.1    Sekimizu, K.2    Kaito, C.3
  • 34
    • 0028010474 scopus 로고
    • Clearance of lipopolysaccharide in hemolymph of the silkworm Bombyx mori: Its role in the termination of cecropin mRNA induction
    • Kato Y, Motoi Y, Taniai K, Kadono-Okuda K, Hiramatsu M, Yamakawa M. Clearance of lipopolysaccharide in hemolymph of the silkworm Bombyx mori: its role in the termination of cecropin mRNA induction. Insect Biochem. Mol. Biol. 24: 539-545, 1994a.
    • (1994) Insect Biochem. Mol. Biol. , vol.24 , pp. 539-545
    • Kato, Y.1    Motoi, Y.2    Taniai, K.3    Kadono-Okuda, K.4    Hiramatsu, M.5    Yamakawa, M.6
  • 35
    • 0028448281 scopus 로고
    • Lipopolysaccharide-lipophorin complex formation in insect hemolymph: A common pathway of lipopolysaccharide detoxification both in insects and in mammals
    • Kato Y, Motoi Y, Taniai K, Kadono-Okuda K, Yamamoto M, Higashino Y, et al. Lipopolysaccharide-lipophorin complex formation in insect hemolymph: a common pathway of lipopolysaccharide detoxification both in insects and in mammals. Insect Biochem. Mol. Biol. 24: 547-555, 1994b.
    • (1994) Insect Biochem. Mol. Biol. , vol.24 , pp. 547-555
    • Kato, Y.1    Motoi, Y.2    Taniai, K.3    Kadono-Okuda, K.4    Yamamoto, M.5    Higashino, Y.6
  • 38
    • 0032253174 scopus 로고    scopus 로고
    • Cloning and expression of apolipophorin III from the common cutworm, Spodoptera litura
    • Kim E, Kim SH, Choi CS, Park YI, Kim HR. Cloning and expression of apolipophorin III from the common cutworm, Spodoptera litura. Arch. Insect Biochem. Physiol. 39: 166-173, 1998.
    • (1998) Arch. Insect Biochem. Physiol. , vol.39 , pp. 166-173
    • Kim, E.1    Kim, S.H.2    Choi, C.S.3    Park, Y.I.4    Kim, H.R.5
  • 39
    • 4744367572 scopus 로고    scopus 로고
    • Immune activation of apolipophorin-III and distribution in hemocytes from Hyphantria cunea
    • Kim HJ, Je HJ, Park SY, Lee IH, Jin BR, Yun HK, et al. Immune activation of apolipophorin-III and distribution in hemocytes from Hyphantria cunea. Insect Biochem. Mol. Biol. 34: 1011-1023, 2004.
    • (2004) Insect Biochem. Mol. Biol. , vol.34 , pp. 1011-1023
    • Kim, H.J.1    Je, H.J.2    Park, S.Y.3    Lee, I.H.4    Jin, B.R.5    Yun, H.K.6
  • 41
    • 33746309850 scopus 로고    scopus 로고
    • Tyrosine fluorescence analysis of apolipophorin III - lipopolysaccharide interaction
    • Leon LJ, Pratt CC, Vasquez LJ, Weers PMM. Tyrosine fluorescence analysis of apolipophorin III - lipopolysaccharide interaction. Archiv. Biochem. Biophys. 452: 38-45, 2006b.
    • (2006) Archiv. Biochem. Biophys. , vol.452 , pp. 38-45
    • Leon, L.J.1    Pratt, C.C.2    Vasquez, L.J.3    Weers, P.M.M.4
  • 42
    • 33645400827 scopus 로고    scopus 로고
    • Recognition and inactivation of LPS by lipophorin particles
    • Ma G, Hay D, Li D, Asgari S, Schmidt O. Recognition and inactivation of LPS by lipophorin particles. Dev. Comp. Immunol. 30: 619-626, 2006.
    • (2006) Dev. Comp. Immunol. , vol.30 , pp. 619-626
    • Ma, G.1    Hay, D.2    Li, D.3    Asgari, S.4    Schmidt, O.5
  • 43
    • 33744721801 scopus 로고    scopus 로고
    • Structure and expression of the lipophorin-encoding gene of the malaria vector, Anopheles gambiae
    • Marinotti O, Capurro ML, Nirmala X, Calvo E, James AA. Structure and expression of the lipophorin-encoding gene of the malaria vector, Anopheles gambiae. Comp. Biochem. Physiol. 144B: 101-109, 2006.
    • (2006) Comp. Biochem. Physiol. , vol.144 B , pp. 101-109
    • Marinotti, O.1    Capurro, M.L.2    Nirmala, X.3    Calvo, E.4    James, A.A.5
  • 45
    • 0033551071 scopus 로고    scopus 로고
    • A molecular trigger of lipid-binding induced opening of a helix bundle exchangeable apolipoprotein
    • Narayanaswami V, Wang J, Schieve D, Kay CM, Ryan RO. A molecular trigger of lipid-binding induced opening of a helix bundle exchangeable apolipoprotein. Proc. Natl. Acad. Sci. USA 96: 4366-4371, 1999.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4366-4371
    • Narayanaswami, V.1    Wang, J.2    Schieve, D.3    Kay, C.M.4    Ryan, R.O.5
  • 46
    • 0029967954 scopus 로고    scopus 로고
    • Disulfide bond engineering to monitor conformational opening of apolipophorin III during lipid binding
    • Narayanaswami V, Wang J, Kay CM, Scraba DG, Ryan RO. Disulfide bond engineering to monitor conformational opening of apolipophorin III during lipid binding. J. Biol. Chem. 271: 26855-26862, 1996
    • (1996) J. Biol. Chem. , vol.271 , pp. 26855-26862
    • Narayanaswami, V.1    Wang, J.2    Kay, C.M.3    Scraba, D.G.4    Ryan, R.O.5
  • 47
    • 0035949656 scopus 로고    scopus 로고
    • Insect immune activation by apolipophorin III is correlated with the lipid-binding properties of this protein
    • Niere M, Dettloff M, Maier T, Ziegler M, Wiesner A. Insect immune activation by apolipophorin III is correlated with the lipid-binding properties of this protein. Biochemistry 40: 11502-11508, 2001.
    • (2001) Biochemistry , vol.40 , pp. 11502-11508
    • Niere, M.1    Dettloff, M.2    Maier, T.3    Ziegler, M.4    Wiesner, A.5
  • 49
    • 84864710516 scopus 로고    scopus 로고
    • Characterization of the apoLp-III/LPS complex: Insight into the mode of binding interaction
    • Oztug M, Martinon D, Weers PMM. Characterization of the apoLp-III/LPS complex: insight into the mode of binding interaction. Biochemistry 51: 6220-6227, 2012.
    • (2012) Biochemistry , vol.51 , pp. 6220-6227
    • Oztug, M.1    Martinon, D.2    Weers, P.M.M.3
  • 51
    • 4344699934 scopus 로고    scopus 로고
    • Effects of two hemolymph proteins on humoral defense reactions in the wax moth, Galleria mellonella
    • Park SY, Kim CH, Jeong WH, Lee JH, Seo SJ, Han YS, et al. Effects of two hemolymph proteins on humoral defense reactions in the wax moth, Galleria mellonella. Dev. Comp. Immunol. 29: 43-51, 2005.
    • (2005) Dev. Comp. Immunol. , vol.29 , pp. 43-51
    • Park, S.Y.1    Kim, C.H.2    Jeong, W.H.3    Lee, J.H.4    Seo, S.J.5    Han, Y.S.6
  • 52
    • 10044286925 scopus 로고    scopus 로고
    • Lipopolysaccharide binding of an exchangeable apolipoprotein, apolipophorin III, from Galleria mellonella
    • Pratt CC, Weers PMM. Lipopolysaccharide binding of an exchangeable apolipoprotein, apolipophorin III, from Galleria mellonella. Biol. Chem. 385: 1113-1119, 2004.
    • (2004) Biol. Chem. , vol.385 , pp. 1113-1119
    • Pratt, C.C.1    Weers, P.M.M.2
  • 55
    • 0028977999 scopus 로고
    • Alignment of the apolipophorin-III α-helices in complex with dimyristoylphosphatidylcholine
    • Raussens V, Narayanaswami V, Goormaghtigh E, Ryan RO, Ruysschaert J. Alignment of the apolipophorin-III α-helices in complex with dimyristoylphosphatidylcholine. J. Biol. Chem. 270: 12542-12547, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12542-12547
    • Raussens, V.1    Narayanaswami, V.2    Goormaghtigh, E.3    Ryan, R.O.4    Ruysschaert, J.5
  • 56
    • 80455173990 scopus 로고    scopus 로고
    • Apolipophorin III and transmission electron microscopy as toxicity indicators for harmaline and tea saponin in Spodoptera exigua (Noctuidae: Lepidoptera)
    • Rizwan-Ul-Haq M, Gong L, Hu M, Luo J. Apolipophorin III and transmission electron microscopy as toxicity indicators for harmaline and tea saponin in Spodoptera exigua (Noctuidae: Lepidoptera). Chemosphere 85: 995-1001, 2011.
    • (2011) Chemosphere , vol.85 , pp. 995-1001
    • Rizwan-Ul-Haq, M.1    Gong, L.2    Hu, M.3    Luo, J.4
  • 57
    • 0031687891 scopus 로고    scopus 로고
    • Apolipoprotein E-deficient mice have impaired innate immune responses to Listeria monocytogenes in vivo
    • Roselaar SE, Daugherty A. Apolipoprotein E-deficient mice have impaired innate immune responses to Listeria monocytogenes in vivo. J. Lipid Res. 39: 1740-1743, 1998.
    • (1998) J. Lipid Res. , vol.39 , pp. 1740-1743
    • Roselaar, S.E.1    Daugherty, A.2
  • 58
    • 84990431596 scopus 로고
    • Chemical and immunological properties of lipophorins from seven insect orders
    • Ryan RO, Schmidt J O, Law JH. Chemical and immunological properties of lipophorins from seven insect orders. Arch. Insect Biochem. Physiol. 1: 375-384, 1984.
    • (1984) Arch. Insect Biochem. Physiol. , vol.1 , pp. 375-384
    • Ryan, R.O.1    Schmidt, J.O.2    Law, J.H.3
  • 59
    • 0034107475 scopus 로고    scopus 로고
    • Lipid Transport biochemistry and its role in energy production
    • Ryan RO, Van der Horst DJ. Lipid Transport biochemistry and its role in energy production. Annu. Rev. Entomol. 45:233-260, 2000.
    • (2000) Annu. Rev. Entomol. , vol.45 , pp. 233-260
    • Ryan, R.O.1    Van der Horst, D.J.2
  • 60
    • 0031914422 scopus 로고    scopus 로고
    • Fluorescence studies of exchangeable apolipoprotein-lipid interactions. Superficial association of apolipophorin III with lipoprotein surfaces
    • Sahoo D, Narayanaswami V. Kay CM, Ryan RO. Fluorescence studies of exchangeable apolipoprotein-lipid interactions. Superficial association of apolipophorin III with lipoprotein surfaces. J. Biol. Chem. 273: 1403-1408, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1403-1408
    • Sahoo, D.1    Narayanaswami, V.2    Kay, C.M.3    Ryan, R.O.4
  • 61
    • 0036384368 scopus 로고    scopus 로고
    • Lipid triggered molecular switch of apoLp-III helix bundle to en extended helix conformation
    • Sahoo D, Weers PMM, Ryan RO, Narayanaswami V. Lipid triggered molecular switch of apoLp-III helix bundle to en extended helix conformation. J. Mol. Biol. 321: 201-214, 2002.
    • (2002) J. Mol. Biol. , vol.321 , pp. 201-214
    • Sahoo, D.1    Weers, P.M.M.2    Ryan, R.O.3    Narayanaswami, V.4
  • 62
    • 3242656580 scopus 로고    scopus 로고
    • Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins
    • Saito H, Lund-Katz S, Phillips MC. Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins. Prog. Lipid Res. 43: 350-380, 2004.
    • (2004) Prog. Lipid Res. , vol.43 , pp. 350-380
    • Saito, H.1    Lund-Katz, S.2    Phillips, M.C.3
  • 63
    • 1842665810 scopus 로고    scopus 로고
    • Isolation and characterization of hemolymph clotting factors in Drosophila melanogaster by a pullout method
    • Scherfer C, Karlsson C, Loseva O, Bidla G, Goto A, Havemann J, et al. Isolation and characterization of hemolymph clotting factors in Drosophila melanogaster by a pullout method. Curr. Biol. 14: 625-629, 2004.
    • (2004) Curr. Biol. , vol.14 , pp. 625-629
    • Scherfer, C.1    Karlsson, C.2    Loseva, O.3    Bidla, G.4    Goto, A.5    Havemann, J.6
  • 65
    • 78751575329 scopus 로고    scopus 로고
    • Immunosuppression induced by entomopathogens is rescued by addition of apolipophorin III in the diamondback moth, Plutella xylostella
    • Son Y, Kim Y. Immunosuppression induced by entomopathogens is rescued by addition of apolipophorin III in the diamondback moth, Plutella xylostella. J. Invertebr. Pathol. 106: 217-222, 2011.
    • (2011) J. Invertebr. Pathol. , vol.106 , pp. 217-222
    • Son, Y.1    Kim, Y.2
  • 66
    • 77950296913 scopus 로고    scopus 로고
    • Proteomic analysis of parasitized Plutella xylostella larvae plasma
    • Song KH, Jung MK, Eum JH, Hwang IC, Han SS. Proteomic analysis of parasitized Plutella xylostella larvae plasma. J. Insect Physiol. 54: 1270-1280, 2008.
    • (2008) J. Insect Physiol. , vol.54 , pp. 1270-1280
    • Song, K.H.1    Jung, M.K.2    Eum, J.H.3    Hwang, I.C.4    Han, S.S.5
  • 67
    • 0029048818 scopus 로고
    • Low concentrations of diacylglycerol promote the binding of apolipophorin III to a phospholipid bilayer: A surface plasmon resonance spectroscopy study
    • Soulages JL, Salamon Z, Wells MA, Tollin G. Low concentrations of diacylglycerol promote the binding of apolipophorin III to a phospholipid bilayer: A surface plasmon resonance spectroscopy study. Proc. Natl. Acad. Sci. USA 92: 5650-5654, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5650-5654
    • Soulages, J.L.1    Salamon, Z.2    Wells, M.A.3    Tollin, G.4
  • 68
    • 0001481326 scopus 로고
    • Adipokinetic hormone causes formation of low density lipophorin in the house cricket, Acheta domesticus
    • Strobel LM, Kanost MR, Ziegler R, Wells MA. Adipokinetic hormone causes formation of low density lipophorin in the house cricket, Acheta domesticus. Insect Biochem. 20: 859-863, 1990.
    • (1990) Insect Biochem. , vol.20 , pp. 859-863
    • Strobel, L.M.1    Kanost, M.R.2    Ziegler, R.3    Wells, M.A.4
  • 69
    • 0028900812 scopus 로고
    • Apolipophorin III is dramatically up-regulated during the programmed death of insect skeletal muscle and neurons
    • Sun D, Ziegler R, Milligan CE, Fahrbach S, Schwartz LM. Apolipophorin III is dramatically up-regulated during the programmed death of insect skeletal muscle and neurons. J. Neurobiol. 26: 119-129, 1995.
    • (1995) J. Neurobiol. , vol.26 , pp. 119-129
    • Sun, D.1    Ziegler, R.2    Milligan, C.E.3    Fahrbach, S.4    Schwartz, L.M.5
  • 70
    • 84860838940 scopus 로고    scopus 로고
    • Molecular characterization and gene expression of apolipophorin III from the ghost moth, Thitarodes pui (Lepidoptera, Hepialidae)
    • Sun Z, Yu J, Wu W, Zhang G. Molecular characterization and gene expression of apolipophorin III from the ghost moth, Thitarodes pui (Lepidoptera, Hepialidae). Arch. Insect Biochem. Physiol. 80: 1-14, 2012.
    • (2012) Arch. Insect Biochem. Physiol. , vol.80 , pp. 1-14
    • Sun, Z.1    Yu, J.2    Wu, W.3    Zhang, G.4
  • 72
    • 0000037418 scopus 로고
    • Lipophorin in developing adults of Hyalophora cecropia: Support of yolk formation and preparation for flight
    • Telfer W, Pan M-L, Law JH. Lipophorin in developing adults of Hyalophora cecropia: support of yolk formation and preparation for flight. Insect Biochem. 21: 653-663, 1991.
    • (1991) Insect Biochem. , vol.21 , pp. 653-663
    • Telfer, W.1    Pan, M.-L.2    Law, J.H.3
  • 77
    • 1542398216 scopus 로고    scopus 로고
    • Insect adipokinetic hormones: Release and integration of flight energy metabolism
    • Van der Horst DJ. Insect adipokinetic hormones: release and integration of flight energy metabolism. Comp. Biochem. Physiol. 136B: 217-226, 2003.
    • (2003) Comp. Biochem. Physiol. , vol.136 B , pp. 217-226
    • Van der Horst, D.J.1
  • 78
    • 0032192211 scopus 로고    scopus 로고
    • Biosynthesis of Aedes aegypti lipophorin and gene expression of its apolipoproteins
    • Van Heusden MC, Thompson F, Dennis J. Biosynthesis of Aedes aegypti lipophorin and gene expression of its apolipoproteins. Insect Biochem. Mol. Biol. 28: 733-738, 1998.
    • (1998) Insect Biochem. Mol. Biol. , vol.28 , pp. 733-738
    • Van Heusden, M.C.1    Thompson, F.2    Dennis, J.3
  • 80
    • 38249038017 scopus 로고
    • Synthesis and release of lipophorin in larvae of the southwestern corn borer, Diatraea grandiosella: An in vitro study
    • Venkatesh K, Lenz CJ, Bergman DK, Chippendale GM. Synthesis and release of lipophorin in larvae of the southwestern corn borer, Diatraea grandiosella: an in vitro study. Insect Biochem. 17: 1173-1180, 1987.
    • (1987) Insect Biochem. , vol.17 , pp. 1173-1180
    • Venkatesh, K.1    Lenz, C.J.2    Bergman, D.K.3    Chippendale, G.M.4
  • 81
    • 78650610654 scopus 로고    scopus 로고
    • Apolipoprotein-induced conversion of phosphatidylcholine bilayer vesicles into nanodisks
    • Wan Ch-PL, Chiu MH, Wu X, Lee SK. Apolipoprotein-induced conversion of phosphatidylcholine bilayer vesicles into nanodisks. Biochim. Biophys. Acta 1808: 606-613, 2011.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 606-613
    • Wan, C.-P.L.1    Chiu, M.H.2    Wu, X.3    Lee, S.K.4
  • 82
    • 0030875963 scopus 로고    scopus 로고
    • Insight into lipid surface recognition and reversible conformational adaptations of an exchangeable apolipoprotein by multidimensional heteronuclear NMR techniques
    • Wang J, Gagne S, Sykes BD, Ryan RO. Insight into lipid surface recognition and reversible conformational adaptations of an exchangeable apolipoprotein by multidimensional heteronuclear NMR techniques. J. Biol. Chem. 272: 17912-17920, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17912-17920
    • Wang, J.1    Gagne, S.2    Sykes, B.D.3    Ryan, R.O.4
  • 83
    • 0033618275 scopus 로고    scopus 로고
    • Interaction of an exchangeable apolipoprotein with phospholipid vesicles and lipoprotein particles
    • Weers PMM, Narayanaswami V, Kay CM, Ryan RO. Interaction of an exchangeable apolipoprotein with phospholipid vesicles and lipoprotein particles. J. Biol. Chem. 274: 21804-21810, 1999.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21804-21810
    • Weers, P.M.M.1    Narayanaswami, V.2    Kay, C.M.3    Ryan, R.O.4
  • 84
    • 0345447061 scopus 로고    scopus 로고
    • Apolipophorin III: A lipid-triggered molecular switch
    • Weers PMM, Ryan RO. Apolipophorin III: a lipid-triggered molecular switch. Insect Biochem. Mol. Biol. 33: 1249-1260, 2003.
    • (2003) Insect Biochem. Mol. Biol. , vol.33 , pp. 1249-1260
    • Weers, P.M.M.1    Ryan, R.O.2
  • 85
    • 0034111173 scopus 로고    scopus 로고
    • Interaction of locust apolipophorin III with lipoproteins and phospholipid vesicles: Effect of glycosylation
    • Weers PMM, Van der Horst DJ, Ryan RO. Interaction of locust apolipophorin III with lipoproteins and phospholipid vesicles: effect of glycosylation. J. Lipid Res. 41: 416-423, 2000.
    • (2000) J. Lipid Res. , vol.41 , pp. 416-423
    • Weers, P.M.M.1    Van der Horst, D.J.2    Ryan, R.O.3
  • 87
    • 0027506080 scopus 로고
    • Biosynthesis of locust lipophorin: Apolipophorin I and apolipophorin II originate from a common precursor
    • Weers PMM, Van Marrewijk WJA, Beenakkers AMT, Van der Horst DJ. Biosynthesis of locust lipophorin: apolipophorin I and apolipophorin II originate from a common precursor. J. Biol. Chem. 268: 4300-4303, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4300-4303
    • Weers, P.M.M.1    Van Marrewijk, W.J.A.2    Beenakkers, A.M.T.3    Van der Horst, D.J.4
  • 88
    • 0031761879 scopus 로고    scopus 로고
    • Primary structure of apolipophorin-III from the greater wax moth, Galleria mellonella
    • Weise Ch, Franke P, Kopáček P, Wiesner A. Primary structure of apolipophorin-III from the greater wax moth, Galleria mellonella. J. Protein Chem. 17: 633-641, 1998.
    • (1998) J. Protein Chem. , vol.17 , pp. 633-641
    • Weise, C.1    Franke, P.2    Kopáček, P.3    Wiesner, A.4
  • 89
    • 0023664091 scopus 로고
    • The role of apolipophorin III in in vivo lipoprotein interconversion in adult Manduca sexta
    • Wells MA, Ryan RO, Kawooya JK, Law JH. The role of apolipophorin III in in vivo lipoprotein interconversion in adult Manduca sexta. J. Biol. Chem. 262: 4172-4176, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4172-4176
    • Wells, M.A.1    Ryan, R.O.2    Kawooya, J.K.3    Law, J.H.4
  • 90
    • 0023900109 scopus 로고
    • Human apolipoprotein E3 in aqueous solution I. Evidence for two structural domains
    • Wetterau JR, Aggerbeck LP, Rall SC, Weisgraber KH. Human apolipoprotein E3 in aqueous solution I. Evidence for two structural domains. J. Biol. Chem. 263:6240-6248, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6240-6248
    • Wetterau, J.R.1    Aggerbeck, L.P.2    Rall, S.C.3    Weisgraber, K.H.4
  • 91
    • 0842300362 scopus 로고    scopus 로고
    • A novel role for an insect apolipoprotein (apolipophorin III) in β-1, 3-glucan pattern recognition and cellular encapsulation reactions
    • Whitten MMA, Tew IF, Lee BL, Ratcliffe NA. A novel role for an insect apolipoprotein (apolipophorin III) in β-1, 3-glucan pattern recognition and cellular encapsulation reactions. J. Immunol. 172: 2177-2185, 2004.
    • (2004) J. Immunol. , vol.172 , pp. 2177-2185
    • Whitten, M.M.A.1    Tew, I.F.2    Lee, B.L.3    Ratcliffe, N.A.4
  • 92
    • 0028108646 scopus 로고
    • Binding of insect apolipophorin III to dimyristoylphosphatidylcholine vesicles. Evidence for a conformational change
    • Wientzek M, Kay CM, Oikawa K, Ryan RO. Binding of insect apolipophorin III to dimyristoylphosphatidylcholine vesicles. Evidence for a conformational change. J. Biol. Chem. 269: 4605-4612, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4605-4612
    • Wientzek, M.1    Kay, C.M.2    Oikawa, K.3    Ryan, R.O.4
  • 93
    • 0030786580 scopus 로고    scopus 로고
    • Isolated apolipophorin III from Galleria mellonella stimulates the immune reactions of the insect
    • Wiesner A, Losen S, Kopacek P, Weise C, Götz P. Isolated apolipophorin III from Galleria mellonella stimulates the immune reactions of the insect. J. Insect Physiol. 43: 383-391, 1997.
    • (1997) J. Insect Physiol. , vol.43 , pp. 383-391
    • Wiesner, A.1    Losen, S.2    Kopacek, P.3    Weise, C.4    Götz, P.5
  • 94
    • 0025860481 scopus 로고
    • Three dimensional structure of the LDL receptor-binding domain of human apolipoprotein E
    • Wilson C, Wardell MR, Weisgraber KH, Mahley RW, Agard DA. Three dimensional structure of the LDL receptor-binding domain of human apolipoprotein E. Science 252: 1817-1822, 1991.
    • (1991) Science , vol.252 , pp. 1817-1822
    • Wilson, C.1    Wardell, M.R.2    Weisgraber, K.H.3    Mahley, R.W.4    Agard, D.A.5
  • 96
    • 0036648993 scopus 로고    scopus 로고
    • Apolipophorin-III affects the activity of the haemocytes of Galleria mellonella larvae
    • Zakarian RJ, Dunphy GB, Albert PJ, Rau ME. Apolipophorin-III affects the activity of the haemocytes of Galleria mellonella larvae. J. Insect Physiol. 48: 715-723, 2002.
    • (2002) J. Insect Physiol. , vol.48 , pp. 715-723
    • Zakarian, R.J.1    Dunphy, G.B.2    Albert, P.J.3    Rau, M.E.4
  • 97
    • 78649630851 scopus 로고    scopus 로고
    • Involvement of apolipophorin III in antibacterial defense of Galleria mellonella larvae
    • Zdybicka-Barabas A, Cytryńska M. Involvement of apolipophorin III in antibacterial defense of Galleria mellonella larvae. Comp. Biochem. Physiol. 158B: 90-98, 2011.
    • (2011) Comp. Biochem. Physiol. , vol.158 B , pp. 90-98
    • Zdybicka-Barabas, A.1    Cytryńska, M.2
  • 99
    • 79955810376 scopus 로고    scopus 로고
    • An atomic force microscopy study of Galleria mellonella apolipophorin III effect on bacteria
    • Zdybicka-Barabas A, Januszanis B, Mak P, Cytryńska M. An atomic force microscopy study of Galleria mellonella apolipophorin III effect on bacteria. Biochim. Biophys. Acta 1808: 1896-1906, 2011.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 1896-1906
    • Zdybicka-Barabas, A.1    Januszanis, B.2    Mak, P.3    Cytryńska, M.4
  • 100
    • 84864027740 scopus 로고    scopus 로고
    • Synergistic action of Galleria mellonella anionic peptide 2 and lysozyme against Gram-negative bacteria
    • Zdybicka-Barabas A, Mak P, Klys A, Skrzypiec K, Mendyk E, Fiołka M, et al. Synergistic action of Galleria mellonella anionic peptide 2 and lysozyme against Gram-negative bacteria. Biochim. Biophys. Acta 1818: 2623-2635, 2012.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 2623-2635
    • Zdybicka-Barabas, A.1    Mak, P.2    Klys, A.3    Skrzypiec, K.4    Mendyk, E.5    Fiołka, M.6
  • 102
    • 0027286472 scopus 로고
    • Calorimetric and spectroscopic studies of the interaction of Manduca sexta apolipophorin III with zwitterionic, anionic and nonionic lipids
    • Zhang Y, Lewis R, McElhaney R, Ryan RO. Calorimetric and spectroscopic studies of the interaction of Manduca sexta apolipophorin III with zwitterionic, anionic and nonionic lipids. Biochemistry 32: 3942-395, 1993.
    • (1993) Biochemistry , vol.32
    • Zhang, Y.1    Lewis, R.2    McElhaney, R.3    Ryan, R.O.4


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