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Volumn , Issue , 2012, Pages 317-345

Lipid Transport

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EID: 84882502434     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-384747-8.10009-1     Document Type: Chapter
Times cited : (13)

References (267)
  • 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 S.A., Roberts J.L., Easy R.H., Ross N.W. Competition between immune function and lipid transport for the protein apolipophorin III leads to stress-induced immunosuppression in crickets. J. Exp. Biol. 2008, 211:531-538.
    • (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
    • 76849098343 scopus 로고    scopus 로고
    • Insect fat body: Energy, metabolism, and regulation
    • Arrese E.L., Soulages J.L. Insect fat body: Energy, metabolism, and regulation. Annu. Rev. Entomol. 2010, 55:207-225.
    • (2010) Annu. Rev. Entomol. , vol.55 , pp. 207-225
    • Arrese, E.L.1    Soulages, J.L.2
  • 3
    • 0028021203 scopus 로고
    • Purification and properties of a phosphorylatable triacylglycerol lipase from the fat body of an insect
    • Arrese E.L., Wells M.A. Purification and properties of a phosphorylatable triacylglycerol lipase from the fat body of an insect. Manduca sexta. J. Lipid Res. 1994, 35:1652-1660.
    • (1994) Manduca sexta. J. Lipid Res. , vol.35 , pp. 1652-1660
    • Arrese, E.L.1    Wells, M.A.2
  • 4
    • 0031025274 scopus 로고    scopus 로고
    • Adipokinetic hormone-induced lipolysis in the fat body of an insect, Manduca sexta: Synthesis of sn-1,2-diacylglycerols
    • Arrese E.L., Wells M.A. Adipokinetic hormone-induced lipolysis in the fat body of an insect, Manduca sexta: Synthesis of sn-1,2-diacylglycerols. J. Lipid Res. 1997, 38:68-76.
    • (1997) J. Lipid Res. , vol.38 , pp. 68-76
    • Arrese, E.L.1    Wells, M.A.2
  • 6
    • 33845584694 scopus 로고    scopus 로고
    • The main triglyceride-lipase from the insect fat body is an active phospholipase A(1): Identification and characterization
    • Arrese E.L., Patel R.T., Soulages J.L. The main triglyceride-lipase from the insect fat body is an active phospholipase A(1): Identification and characterization. J. Lipid Res. 2006, 47:2656-2667.
    • (2006) J. Lipid Res. , vol.47 , pp. 2656-2667
    • Arrese, E.L.1    Patel, R.T.2    Soulages, J.L.3
  • 7
    • 52749090184 scopus 로고    scopus 로고
    • Purification and characterization of recombinant lipid storage protein-2 from Drosophila melanogaster
    • Arrese E.L., Rivera L., Hamada M., Soulages J.L. Purification and characterization of recombinant lipid storage protein-2 from Drosophila melanogaster. Protein Pept. Lett. 2008, 15:1027-1032.
    • (2008) Protein Pept. Lett. , vol.15 , pp. 1027-1032
    • Arrese, E.L.1    Rivera, L.2    Hamada, M.3    Soulages, J.L.4
  • 8
    • 41849111245 scopus 로고    scopus 로고
    • Function and structure of lipid storage droplet protein 1 studied in lipoprotein complexes
    • Arrese E.L., Rivera L., Hamada M., Mirza S., Hartson S.D., et al. Function and structure of lipid storage droplet protein 1 studied in lipoprotein complexes. Arch. Biochem. Biophys. 2008, 473:42-47.
    • (2008) Arch. Biochem. Biophys. , vol.473 , pp. 42-47
    • Arrese, E.L.1    Rivera, L.2    Hamada, M.3    Mirza, S.4    Hartson, S.D.5
  • 9
    • 55749099804 scopus 로고    scopus 로고
    • Expression of lipid storage droplet protein-1 may define the role of AKH as a lipid mobilizing hormone in Manduca sexta
    • Arrese E.L., Mirza S., Rivera L., Howard A.D., Chetty P.S., et al. Expression of lipid storage droplet protein-1 may define the role of AKH as a lipid mobilizing hormone in Manduca sexta. Insect Biochem. Mol. Biol. 2008, 38:993-1000.
    • (2008) Insect Biochem. Mol. Biol. , vol.38 , pp. 993-1000
    • Arrese, E.L.1    Mirza, S.2    Rivera, L.3    Howard, A.D.4    Chetty, P.S.5
  • 10
    • 0033050294 scopus 로고    scopus 로고
    • Apolipophorin II/I, apolipoprotein B, vitellogenin, and microsomal triglyceride transfer protein genes are derived from a common ancestor
    • Babin P.J., Bogerd J., Kooiman F.P., Van Marrewijk W.J.A., Van der Horst D.J. Apolipophorin II/I, apolipoprotein B, vitellogenin, and microsomal triglyceride transfer protein genes are derived from a common ancestor. J. Mol. Evol. 1999, 49:150-160.
    • (1999) J. Mol. Evol. , vol.49 , pp. 150-160
    • Babin, P.J.1    Bogerd, J.2    Kooiman, F.P.3    Van Marrewijk, W.J.A.4    Van der Horst, D.J.5
  • 11
    • 0036126460 scopus 로고    scopus 로고
    • New insights in adipokinetic hormone (AKH) precursor processing in Locusta migratoria obtained by capillary liquid chromatography-tandem mass spectrometry
    • Baggerman G., Huybrechts J., Clynen E., Hens K., Harthoorn L., et al. New insights in adipokinetic hormone (AKH) precursor processing in Locusta migratoria obtained by capillary liquid chromatography-tandem mass spectrometry. Peptides 2002, 23:635-644.
    • (2002) Peptides , vol.23 , pp. 635-644
    • Baggerman, G.1    Huybrechts, J.2    Clynen, E.3    Hens, K.4    Harthoorn, L.5
  • 12
    • 0001206743 scopus 로고
    • Immunocytochemical localization of lipophorin in the fat body of dragonfly larvae (Aeshna cyanea)
    • Bauerfeind R., Komnick H. Immunocytochemical localization of lipophorin in the fat body of dragonfly larvae (Aeshna cyanea). J. Insect Physiol. 1992, 38:185-198.
    • (1992) J. Insect Physiol. , vol.38 , pp. 185-198
    • Bauerfeind, R.1    Komnick, H.2
  • 13
    • 77951903021 scopus 로고    scopus 로고
    • Membrane protein assembly into Nanodiscs
    • Bayburt T.H., Sligar S.G. Membrane protein assembly into Nanodiscs. FEBS Lett. 2010, 584:1721-1727.
    • (2010) FEBS Lett. , vol.584 , pp. 1721-1727
    • Bayburt, T.H.1    Sligar, S.G.2
  • 15
    • 20444383144 scopus 로고    scopus 로고
    • The LDL receptor: How acid pulls the trigger
    • Beglova N., Blacklow S.C. The LDL receptor: How acid pulls the trigger. Trends Biochem. Sci. 2005, 30:309-317.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 309-317
    • Beglova, N.1    Blacklow, S.C.2
  • 16
    • 6344253104 scopus 로고    scopus 로고
    • Cooperation between fixed and low pH-inducible interfaces controls lipoprotein release by the LDL receptor
    • Beglova N., Jeon H., Fisher C., Blacklow S.C. Cooperation between fixed and low pH-inducible interfaces controls lipoprotein release by the LDL receptor. Mol. Cell 2004, 16:281-292.
    • (2004) Mol. Cell , vol.16 , pp. 281-292
    • Beglova, N.1    Jeon, H.2    Fisher, C.3    Blacklow, S.C.4
  • 17
    • 8744235290 scopus 로고    scopus 로고
    • Structural features of the low-density lipoprotein receptor facilitating ligand binding and release
    • Beglova N., Jeon H., Fisher C., Blacklow S.C. Structural features of the low-density lipoprotein receptor facilitating ligand binding and release. Biochem. Soc. Trans. 2004, 32:721-723.
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 721-723
    • Beglova, N.1    Jeon, H.2    Fisher, C.3    Blacklow, S.C.4
  • 18
    • 56849110119 scopus 로고    scopus 로고
    • COPI complex is a regulator of lipid homeostasis
    • doi:10.1371/journal.pbio.0060292
    • Beller M., Sztalryd C., Southall N., Bell M., Jäckle H., et al. COPI complex is a regulator of lipid homeostasis. PLoS Biol 2008, 6:e292. doi:10.1371/journal.pbio.0060292.
    • (2008) PLoS Biol , vol.6
    • Beller, M.1    Sztalryd, C.2    Southall, N.3    Bell, M.4    Jäckle, H.5
  • 19
    • 33646069647 scopus 로고    scopus 로고
    • Identification of four evolutionarily related G protein-coupled receptors from the malaria mosquito Anopheles gambiae
    • Belmont M., Cazzamali G., Williamson M., Hauser F., Grimmelikhuijzen C.J. Identification of four evolutionarily related G protein-coupled receptors from the malaria mosquito Anopheles gambiae. Biochem. Biophys. Res. Commun. 2006, 344:160-165.
    • (2006) Biochem. Biophys. Res. Commun. , vol.344 , pp. 160-165
    • Belmont, M.1    Cazzamali, G.2    Williamson, M.3    Hauser, F.4    Grimmelikhuijzen, C.J.5
  • 20
    • 55549143025 scopus 로고    scopus 로고
    • A glucagon-like endocrine pathway in Drosophila modulates both lipid and carbohydrate homeostasis
    • Bharucha K.N., Tarr P., Zipursky S.L. A glucagon-like endocrine pathway in Drosophila modulates both lipid and carbohydrate homeostasis. J. Exp. Biol. 2008, 211:3103-3110.
    • (2008) J. Exp. Biol. , vol.211 , pp. 3103-3110
    • Bharucha, K.N.1    Tarr, P.2    Zipursky, S.L.3
  • 21
    • 66349128492 scopus 로고    scopus 로고
    • PAT proteins, an ancient family of lipid droplet proteins that regulate cellular lipid stores
    • Bickel P.E., Tansey J.T., Welte M.A. PAT proteins, an ancient family of lipid droplet proteins that regulate cellular lipid stores. Biochim. Biophys. Acta 2009, 1791:419-440.
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 419-440
    • Bickel, P.E.1    Tansey, J.T.2    Welte, M.A.3
  • 23
    • 0028894767 scopus 로고
    • Structural studies of Manduca sexta lipid transfer particle with apolipoprotein-specific antibodies
    • Blacklock B.J., Ryan R.O. Structural studies of Manduca sexta lipid transfer particle with apolipoprotein-specific antibodies. J. Lipid. Res 1995, 35:108-116.
    • (1995) J. Lipid. Res , vol.35 , pp. 108-116
    • Blacklock, B.J.1    Ryan, R.O.2
  • 24
    • 0026740804 scopus 로고
    • Manduca sexta lipid transfer particle can facilitate lipid transfer via a carrier-mediated mechanism
    • Blacklock B.J., Smillie M., Ryan R.O. Manduca sexta lipid transfer particle can facilitate lipid transfer via a carrier-mediated mechanism. J. Biol. Chem. 1992, 267:14033-14037.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14033-14037
    • Blacklock, B.J.1    Smillie, M.2    Ryan, R.O.3
  • 25
    • 0029162740 scopus 로고
    • Molecular cloning of three distinct cDNAs, each encoding a different adipokinetic hormone precursor, of the migratory locust, Locusta migratoria: Differential expression of the distinct adipokinetic hormone precursor genes during flight activity
    • Bogerd J., Kooiman F.P., Pijnenburg M.A.P., Hekking L.H.P., Oudejans R.C.H.M., et al. Molecular cloning of three distinct cDNAs, each encoding a different adipokinetic hormone precursor, of the migratory locust, Locusta migratoria: Differential expression of the distinct adipokinetic hormone precursor genes during flight activity. J. Biol. Chem. 1995, 270:23038-23043.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23038-23043
    • Bogerd, J.1    Kooiman, F.P.2    Pijnenburg, M.A.P.3    Hekking, L.H.P.4    Oudejans, R.C.H.M.5
  • 26
    • 0034722866 scopus 로고    scopus 로고
    • Molecular characterization and gene expression in the eye of the apolipophorin II/I precursor from Locusta migratoria
    • Bogerd J., Babin P.J., Kooiman F.P., André M., Ballagny C., et al. Molecular characterization and gene expression in the eye of the apolipophorin II/I precursor from Locusta migratoria. J. Comp. Neurol. 2000, 427:546-558.
    • (2000) J. Comp. Neurol. , vol.427 , pp. 546-558
    • Bogerd, J.1    Babin, P.J.2    Kooiman, F.P.3    André, M.4    Ballagny, C.5
  • 27
    • 34447533581 scopus 로고    scopus 로고
    • Is membrane transport of FFA mediated by lipid, protein, or both? Mechanisms and regulation of protein-mediated cellular fatty acid uptake: Molecular, biochemical, and physiological evidence
    • Bonen A., Chabowski A., Luiken J.J.F.P., Glatz J.F.C. Is membrane transport of FFA mediated by lipid, protein, or both? Mechanisms and regulation of protein-mediated cellular fatty acid uptake: Molecular, biochemical, and physiological evidence. Physiol. (Bethesda) 2007, 22:15-29.
    • (2007) Physiol. (Bethesda) , vol.22 , pp. 15-29
    • Bonen, A.1    Chabowski, A.2    Luiken, J.J.F.P.3    Glatz, J.F.C.4
  • 28
    • 0036212621 scopus 로고    scopus 로고
    • Cytoplasmic fatty acid-binding proteins: Emerging roles in metabolism and atherosclerosis
    • Boord J.B., Fazio S., Linton M.F. Cytoplasmic fatty acid-binding proteins: Emerging roles in metabolism and atherosclerosis. Curr. Opin. Lipidol. 2002, 13:141-147.
    • (2002) Curr. Opin. Lipidol. , vol.13 , pp. 141-147
    • Boord, J.B.1    Fazio, S.2    Linton, M.F.3
  • 29
    • 0032030919 scopus 로고    scopus 로고
    • Identification of the low density lipoprotein receptor-binding site in apolipoprotein B100 and the modulation of its binding activity by the carboxyl terminus in familial defective apo-B100
    • Borén J., Lee I., Zhu W., Arnold K., Taylor S., et al. Identification of the low density lipoprotein receptor-binding site in apolipoprotein B100 and the modulation of its binding activity by the carboxyl terminus in familial defective apo-B100. J. Clin. Invest. 1998, 101:1084-1093.
    • (1998) J. Clin. Invest. , vol.101 , pp. 1084-1093
    • Borén, J.1    Lee, I.2    Zhu, W.3    Arnold, K.4    Taylor, S.5
  • 30
    • 3142724817 scopus 로고    scopus 로고
    • Global defects in the expression and function of the low density lipoprotein receptor (LDLR) associated with two familial hypercholesterolemia mutations resulting in misfolding of the LDLR epidermal growth factor-AB pair
    • Boswell E.J., Jeon H., Blacklow S.C., Downing A.K. Global defects in the expression and function of the low density lipoprotein receptor (LDLR) associated with two familial hypercholesterolemia mutations resulting in misfolding of the LDLR epidermal growth factor-AB pair. J. Biol. Chem. 2004, 279:30611-30621.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30611-30621
    • Boswell, E.J.1    Jeon, H.2    Blacklow, S.C.3    Downing, A.K.4
  • 31
    • 36649015243 scopus 로고    scopus 로고
    • The perilipin family of structural lipid droplet proteins: Stabilization of lipid droplets and control of lipolysis
    • Brasaemle D.L. The perilipin family of structural lipid droplet proteins: Stabilization of lipid droplets and control of lipolysis. J. Lipid Res. 2007, 48:2547-2559.
    • (2007) J. Lipid Res. , vol.48 , pp. 2547-2559
    • Brasaemle, D.L.1
  • 32
    • 0026101543 scopus 로고
    • Molecular structure of an apolipoprotein determined at 2.5-Å resolution
    • Breiter D.R., Kanost M.R., Benning M.M., Wesenberg G., Law J.H., et al. Molecular structure of an apolipoprotein determined at 2.5-Å resolution. Biochemistry 1991, 30:603-608.
    • (1991) Biochemistry , vol.30 , pp. 603-608
    • Breiter, D.R.1    Kanost, M.R.2    Benning, M.M.3    Wesenberg, G.4    Law, J.H.5
  • 33
    • 0022549920 scopus 로고
    • A receptor-mediated pathway for cholesterol homeostasis
    • Brown M.S., Goldstein J.L. A receptor-mediated pathway for cholesterol homeostasis. Science 1986, 232:34-47.
    • (1986) Science , vol.232 , pp. 34-47
    • Brown, M.S.1    Goldstein, J.L.2
  • 34
    • 0035933365 scopus 로고    scopus 로고
    • Role of lipid transfer particle in delivery of diacylglycerol from midgut to lipophorin in larval Manduca sexta
    • Canavoso L.E., Wells M.A. Role of lipid transfer particle in delivery of diacylglycerol from midgut to lipophorin in larval Manduca sexta. Insect Biochem. Mol. Biol. 2001, 31:783-790.
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 783-790
    • Canavoso, L.E.1    Wells, M.A.2
  • 36
    • 0036837496 scopus 로고    scopus 로고
    • Adipokinetic hormone concentrations in the haemolymph of Schistocerca gregaria, measured by radioimmunoassay
    • Candy D.J. Adipokinetic hormone concentrations in the haemolymph of Schistocerca gregaria, measured by radioimmunoassay. Insect Biochem. Mol. Biol. 2002, 32:1361-1367.
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , pp. 1361-1367
    • Candy, D.J.1
  • 37
    • 1942440368 scopus 로고    scopus 로고
    • CDNA cloning and transcriptional regulation of the vitellogenin receptor from the fire ant, Solenopsis invicta Buren (Hymenoptera: Formicidae)
    • Chen M.-E., Lewis D.K., Keeley L.L., Pietrantonio P.V. cDNA cloning and transcriptional regulation of the vitellogenin receptor from the fire ant, Solenopsis invicta Buren (Hymenoptera: Formicidae). Insect Molecular Biology 2004, 13:195-204.
    • (2004) Insect Molecular Biology , vol.13 , pp. 195-204
    • Chen, M.-E.1    Lewis, D.K.2    Keeley, L.L.3    Pietrantonio, P.V.4
  • 38
    • 0035933472 scopus 로고    scopus 로고
    • Molecular characterization of the VLDL receptor homolog mediating uptake of lipophorin in oocytes of the mosquito Aedes aegypti
    • Cheon H.-M., Seo S.-J., Sun J., Sappington T.W., Raikhel A.S. Molecular characterization of the VLDL receptor homolog mediating uptake of lipophorin in oocytes of the mosquito Aedes aegypti. Insect Biochem. Mol. Biol. 2001, 31:753-760.
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 753-760
    • Cheon, H.-M.1    Seo, S.-J.2    Sun, J.3    Sappington, T.W.4    Raikhel, A.S.5
  • 39
    • 0348224056 scopus 로고    scopus 로고
    • Role of helices and loops in the ability of apolipophorin-III to interact with native lipoproteins and form discoidal lipoprotein complexes
    • Chetty P.S., Arrese E.L., Rodriguez V., Soulages J.L. Role of helices and loops in the ability of apolipophorin-III to interact with native lipoproteins and form discoidal lipoprotein complexes. Biochemistry 2003, 42:15061-15067.
    • (2003) Biochemistry , vol.42 , pp. 15061-15067
    • Chetty, P.S.1    Arrese, E.L.2    Rodriguez, V.3    Soulages, J.L.4
  • 40
    • 0001390691 scopus 로고
    • Lipid transport: Biochemistry of hemolymph lipophorin
    • Pergamon Press, Oxford, UK, G.A. Kerkut, L.I. Gilbert (Eds.)
    • Chino H. Lipid transport: Biochemistry of hemolymph lipophorin. Comprehensive Insect Physiology, Biochemistry, and Pharmacology 1985, Vol. 10:115-134. Pergamon Press, Oxford, UK. G.A. Kerkut, L.I. Gilbert (Eds.).
    • (1985) Comprehensive Insect Physiology, Biochemistry, and Pharmacology , vol.10 , pp. 115-134
    • Chino, H.1
  • 41
    • 70349501783 scopus 로고    scopus 로고
    • Apolipophorin III interaction with model membranes composed of phosphatidylcholine and sphingomyelin using differential scanning calorimetry
    • Chiu M.H., Wan C.P., Weers P.M.M., Prenner E.J. Apolipophorin III interaction with model membranes composed of phosphatidylcholine and sphingomyelin using differential scanning calorimetry. Biochim. Biophys. Acta 2009, 1788:2160-2168.
    • (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
  • 42
    • 36448937124 scopus 로고    scopus 로고
    • Different apolipoproteins impact nanolipoprotein particle formation
    • Chromy B.A., Arroyo E., Blanchette C.D., Bench G., Benner H., et al. Different apolipoproteins impact nanolipoprotein particle formation. J. Am. Chem. Soc. 2007, 129:14348-14354.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 14348-14354
    • Chromy, B.A.1    Arroyo, E.2    Blanchette, C.D.3    Bench, G.4    Benner, H.5
  • 43
    • 34547667022 scopus 로고    scopus 로고
    • Structural and RNAi characterization of the German cockroach lipophorin receptor, and the evolutionary relationships of lipoprotein receptors
    • Ciudad L., Bellés X., Piulachs M.-D. Structural and RNAi characterization of the German cockroach lipophorin receptor, and the evolutionary relationships of lipoprotein receptors. BMC Mol. Biol. 2007, 8:53.
    • (2007) BMC Mol. Biol. , vol.8 , pp. 53
    • Ciudad, L.1    Bellés, X.2    Piulachs, M.-D.3
  • 44
    • 67650586984 scopus 로고    scopus 로고
    • Peptidomic survey of the locust neuroendocrine system
    • Clynen E., Schoofs L. Peptidomic survey of the locust neuroendocrine system. Insect Biochem. Mol. Biol. 2009, 39:491-507.
    • (2009) Insect Biochem. Mol. Biol. , vol.39 , pp. 491-507
    • Clynen, E.1    Schoofs, L.2
  • 45
    • 0023664932 scopus 로고
    • Primary structure and comparative sequence analysis of an insect apolipoprotein: Apolipophorin III from Manduca sexta
    • Cole K.D., Fernando-Warnakulasuriya G.J.P., Boguski M.S., Freeman M., Gordon J.I., et al. Primary structure and comparative sequence analysis of an insect apolipoprotein: Apolipophorin III from Manduca sexta. J. Biol. Chem. 1987, 262:11794-11800.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11794-11800
    • Cole, K.D.1    Fernando-Warnakulasuriya, G.J.P.2    Boguski, M.S.3    Freeman, M.4    Gordon, J.I.5
  • 47
    • 0030889032 scopus 로고    scopus 로고
    • Developmental down-regulation of receptor-mediated endocytosis of an insect lipoprotein
    • Dantuma N.P., Pijnenburg M.A.P., Diederen J.H.B., Van der Horst D.J. Developmental down-regulation of receptor-mediated endocytosis of an insect lipoprotein. J. Lipid. Res. 1997, 38:254-265.
    • (1997) J. Lipid. Res. , vol.38 , pp. 254-265
    • Dantuma, N.P.1    Pijnenburg, M.A.P.2    Diederen, J.H.B.3    Van der Horst, D.J.4
  • 48
    • 0032923363 scopus 로고    scopus 로고
    • An insect homolog of the vertebrate very low density lipoprotein receptor mediates endocytosis of lipophorins
    • Dantuma N.P., Potters M., De Winther M.P.J., Tensen C.P., Kooiman F.P., et al. An insect homolog of the vertebrate very low density lipoprotein receptor mediates endocytosis of lipophorins. J. Lipid. Res. 1999, 40:973-978.
    • (1999) J. Lipid. Res. , vol.40 , pp. 973-978
    • Dantuma, N.P.1    Potters, M.2    De Winther, M.P.J.3    Tensen, C.P.4    Kooiman, F.P.5
  • 49
    • 65449187579 scopus 로고    scopus 로고
    • APRP, the second peptide encoded by the adipokinetic hormone gene(s), is highly conserved in evolution: A role in control of ecdysteroidogenesis?
    • De Loof A., Vandersmissen T., Huybrechts J., Landuyt B., Baggerman G., et al. APRP, the second peptide encoded by the adipokinetic hormone gene(s), is highly conserved in evolution: A role in control of ecdysteroidogenesis?. Ann. NY Acad. Sci. 2009, 1163:376-378.
    • (2009) Ann. NY Acad. Sci. , vol.1163 , pp. 376-378
    • De Loof, A.1    Vandersmissen, T.2    Huybrechts, J.3    Landuyt, B.4    Baggerman, G.5
  • 50
    • 0035852986 scopus 로고    scopus 로고
    • An N-terminal three-helix fragment of an exchangeable insect apolipoprotein, apolipophorin III, conserves the lipid binding properties of the full length protein
    • Dettloff M., Weers P.M.M., Niere M., Kay C.M., Ryan R.O., et al. An N-terminal three-helix fragment of an exchangeable insect apolipoprotein, apolipophorin III, conserves the lipid binding properties of the full length protein. Biochemistry 2001, 40:3150-3157.
    • (2001) Biochemistry , vol.40 , pp. 3150-3157
    • Dettloff, M.1    Weers, P.M.M.2    Niere, M.3    Kay, C.M.4    Ryan, R.O.5
  • 51
    • 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. 2001, 47:789-797.
    • (2001) J. Insect Physiol. , vol.47 , pp. 789-797
    • Dettloff, M.1    Kaiser, B.2    Wiesner, A.3
  • 52
    • 0035213499 scopus 로고    scopus 로고
    • Lipophorin of a lower density is formed during immune responses in the lepidopteran insect
    • 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. 2001, 306:449-458.
    • (2001) Galleria mellonella. Cell Tissue Res. , vol.306 , pp. 449-458
    • Dettloff, M.1    Wittwer, D.2    Weise, C.3    Wiesner, A.4
  • 53
    • 0037199431 scopus 로고    scopus 로고
    • Differential lipid binding of truncation mutants of Galleria mellonella apolipophorin III
    • Dettloff M., Niere M., Ryan R.O., Kay C.M., Wiesner A., et al. Differential lipid binding of truncation mutants of Galleria mellonella apolipophorin III. Biochemistry 2002, 41:9688-9695.
    • (2002) Biochemistry , vol.41 , pp. 9688-9695
    • Dettloff, M.1    Niere, M.2    Ryan, R.O.3    Kay, C.M.4    Wiesner, A.5
  • 54
    • 0036467983 scopus 로고    scopus 로고
    • Cell biology of the adipokinetic hormone-producing neurosecretory cells in the locust corpus cardiacum
    • Diederen J.H.B., Oudejans R.C.H.M., Harthoorn L.F., Van der Horst D.J. Cell biology of the adipokinetic hormone-producing neurosecretory cells in the locust corpus cardiacum. Microsc. Res. Tech. 2002, 56:227-236.
    • (2002) Microsc. Res. Tech. , vol.56 , pp. 227-236
    • Diederen, J.H.B.1    Oudejans, R.C.H.M.2    Harthoorn, L.F.3    Van der Horst, D.J.4
  • 55
    • 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. 1997, 43:1023-1029.
    • (1997) J. Insect Physiol. , vol.43 , pp. 1023-1029
    • Dunphy, G.1    Halwani, A.2
  • 56
    • 0034746299 scopus 로고    scopus 로고
    • 13C assignments of an exchangeable apolipoprotein, Locusta migratoria apolipophorin III
    • 13C assignments of an exchangeable apolipoprotein, Locusta migratoria apolipophorin III. J. Biomol. NMR 2001, 19:83-84.
    • (2001) J. Biomol. NMR , vol.19 , pp. 83-84
    • Fan, D.1    Reese, L.2    Ren, X.3    Weers, P.M.M.4    Ryan, R.O.5
  • 57
    • 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. 2003, 278:21210-21220.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21210-21220
    • Fan, D.1    Zheng, Y.2    Yang, D.3    Wang, J.4
  • 58
    • 39049143349 scopus 로고    scopus 로고
    • Immune system responses and fitness costs associated with consumption of bacteria in larvae of Trichoplusia ni
    • Freitak D., Wheat C.W., Heckel D.G., Vogel H. Immune system responses and fitness costs associated with consumption of bacteria in larvae of Trichoplusia ni. BMC Biol. 2007, 5:56.
    • (2007) BMC Biol. , vol.5 , pp. 56
    • Freitak, D.1    Wheat, C.W.2    Heckel, D.G.3    Vogel, H.4
  • 59
    • 0030239126 scopus 로고    scopus 로고
    • The revolution in insect neuropeptides illustrated by the adipokinetic hormone/red pigment-concentrating hormone family of peptides
    • Gäde G. The revolution in insect neuropeptides illustrated by the adipokinetic hormone/red pigment-concentrating hormone family of peptides. Z. Naturforsch 1996, 51C:607-617.
    • (1996) Z. Naturforsch , vol.51 C , pp. 607-617
    • Gäde, G.1
  • 60
    • 0030628549 scopus 로고    scopus 로고
    • The explosion of structural information on insect neuropeptides
    • Gäde G. The explosion of structural information on insect neuropeptides. Prog. Chem. Organ. Nat. Prod 1997, 71:1-128.
    • (1997) Prog. Chem. Organ. Nat. Prod , vol.71 , pp. 1-128
    • Gäde, G.1
  • 61
    • 65449140599 scopus 로고    scopus 로고
    • Peptides of the adipokinetic hormone/red pigment-concentrating hormone family: A new take on biodiversity
    • Gäde G. Peptides of the adipokinetic hormone/red pigment-concentrating hormone family: A new take on biodiversity. Ann. NY Acad. Sci. 2009, 1163:125-136.
    • (2009) Ann. NY Acad. Sci. , vol.1163 , pp. 125-136
    • Gäde, G.1
  • 62
    • 0038522675 scopus 로고    scopus 로고
    • Mode of action of neuropeptides from the adipokinetic hormone family
    • Gäde G., Auerswald L. Mode of action of neuropeptides from the adipokinetic hormone family. Gen. Comp. Endocrinol. 2003, 132:10-20.
    • (2003) Gen. Comp. Endocrinol. , vol.132 , pp. 10-20
    • Gäde, G.1    Auerswald, L.2
  • 63
    • 0030727771 scopus 로고    scopus 로고
    • Hormonal regulation in insects: Facts, gaps and future directions
    • Gäde G., Hoffmann K.H., Spring J.H. Hormonal regulation in insects: Facts, gaps and future directions. Physiol. Rev. 1997, 77:963-1032.
    • (1997) Physiol. Rev. , vol.77 , pp. 963-1032
    • Gäde, G.1    Hoffmann, K.H.2    Spring, J.H.3
  • 64
    • 0037482458 scopus 로고    scopus 로고
    • Structure of apolipophorin III in discoidal lipoproteins: Inter-helical distances in the lipid-bound state and conformational change upon binding to lipid
    • Garda H.A., Arrese E.L., Soulages J.L. Structure of apolipophorin III in discoidal lipoproteins: Inter-helical distances in the lipid-bound state and conformational change upon binding to lipid. J. Biol. Chem. 2002, 262:11794-11800.
    • (2002) J. Biol. Chem. , vol.262 , pp. 11794-11800
    • Garda, H.A.1    Arrese, E.L.2    Soulages, J.L.3
  • 65
    • 0032481105 scopus 로고    scopus 로고
    • Calcium uptake via endocytosis with rapid release from acidifying endosomes
    • Gerasimenko J.V., Tepikin A.V., Petersen O.H., Gerasimenko O.V. Calcium uptake via endocytosis with rapid release from acidifying endosomes. Curr. Biol. 1998, 8:1335-1338.
    • (1998) Curr. Biol. , vol.8 , pp. 1335-1338
    • Gerasimenko, J.V.1    Tepikin, A.V.2    Petersen, O.H.3    Gerasimenko, O.V.4
  • 66
    • 0028085865 scopus 로고
    • Quantification of low density lipoprotein and transferrin endocytic sorting HEp2 cells using confocal microscopy
    • Ghosh R.N., Gelman D.L., Maxfield F.R. Quantification of low density lipoprotein and transferrin endocytic sorting HEp2 cells using confocal microscopy. J. Cell Sci. 1994, 107:2177-2189.
    • (1994) J. Cell Sci. , vol.107 , pp. 2177-2189
    • Ghosh, R.N.1    Gelman, D.L.2    Maxfield, F.R.3
  • 67
    • 39649120566 scopus 로고    scopus 로고
    • Surface antigens of Xenorhabdus nematophila (F. Enterobacteriaceae) and Bacillus subtilis (F. Bacillaceae) react with antibacterial factors of Malacosoma disstria (C. Insecta: O. Lepidoptera) hemolymph
    • Giannoulis P., Brooks C.L., Dunphy G.B., Niven D.F., Mandato C.A. Surface antigens of Xenorhabdus nematophila (F. Enterobacteriaceae) and Bacillus subtilis (F. Bacillaceae) react with antibacterial factors of Malacosoma disstria (C. Insecta: O. Lepidoptera) hemolymph. J. Invertebr. Pathol 2008, 97:211-222.
    • (2008) J. Invertebr. Pathol , vol.97 , pp. 211-222
    • Giannoulis, P.1    Brooks, C.L.2    Dunphy, G.B.3    Niven, D.F.4    Mandato, C.A.5
  • 69
    • 0032918750 scopus 로고    scopus 로고
    • Identification and distribution of dietary precursors of the Drosophila visual pigment chromophore: Analysis of carotenoids in wild type and ninaD mutants by HPLC
    • Giovannucci D.R., Stephenson R.S. Identification and distribution of dietary precursors of the Drosophila visual pigment chromophore: Analysis of carotenoids in wild type and ninaD mutants by HPLC. Vision Res. 1999, 39:219-229.
    • (1999) Vision Res. , vol.39 , pp. 219-229
    • Giovannucci, D.R.1    Stephenson, R.S.2
  • 70
    • 74949084316 scopus 로고    scopus 로고
    • Membrane fatty acid transporters as regulators of lipid metabolism: Implications for metabolic disease
    • Glatz J.F.C., Luiken J.J.F.P., Bonen A. Membrane fatty acid transporters as regulators of lipid metabolism: Implications for metabolic disease. Physiol. Rev. 2010, 90:367-417.
    • (2010) Physiol. Rev. , vol.90 , pp. 367-417
    • Glatz, J.F.C.1    Luiken, J.J.F.P.2    Bonen, A.3
  • 73
    • 0035957739 scopus 로고    scopus 로고
    • Purification and characterization of a lipid transfer particle in Rhodnius prolixus: Phospholipid transfer
    • Golodne D.M., Van Heusden M.C., Gondim K.C., Masuda H., Atella G.C. Purification and characterization of a lipid transfer particle in Rhodnius prolixus: Phospholipid transfer. Insect Biochem. Mol. Biol. 2001, 31:563-571.
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 563-571
    • Golodne, D.M.1    Van Heusden, M.C.2    Gondim, K.C.3    Masuda, H.4    Atella, G.C.5
  • 74
    • 33646791490 scopus 로고    scopus 로고
    • Lipophorin receptor of Bombyx mori: cDNA cloning, genomic structure, alternative splicing, and isolation of a new isoform
    • Gopalapillai R., Kadono-Okuda K., Tsuchida K., Yamamoto K., Nohata J., et al. Lipophorin receptor of Bombyx mori: cDNA cloning, genomic structure, alternative splicing, and isolation of a new isoform. J. Lipid Res. 2006, 47:1005-1013.
    • (2006) J. Lipid Res. , vol.47 , pp. 1005-1013
    • Gopalapillai, R.1    Kadono-Okuda, K.2    Tsuchida, K.3    Yamamoto, K.4    Nohata, J.5
  • 76
    • 26944489689 scopus 로고    scopus 로고
    • Brummer lipase is an evolutionary conserved fat storage regulator in Drosophila
    • Grönke S., Mildner A., Fellert S., Tennagels N., Petry S., et al. Brummer lipase is an evolutionary conserved fat storage regulator in Drosophila. Cell Metabol. 2005, 1:323-330.
    • (2005) Cell Metabol. , vol.1 , pp. 323-330
    • Grönke, S.1    Mildner, A.2    Fellert, S.3    Tennagels, N.4    Petry, S.5
  • 77
    • 34250306022 scopus 로고    scopus 로고
    • Dual lipolytic control of body fat storage and mobilization in Drosophila
    • doi:10.1371/journal.pbio.0050137
    • Grönke S., Müller G., Hirsch J., Fellert S., Andreou A., et al. Dual lipolytic control of body fat storage and mobilization in Drosophila. PLoS Biol 2007, 5:e137. doi:10.1371/journal.pbio.0050137.
    • (2007) PLoS Biol , vol.5
    • Grönke, S.1    Müller, G.2    Hirsch, J.3    Fellert, S.4    Andreou, A.5
  • 78
    • 31444438260 scopus 로고    scopus 로고
    • Dynamics of lipid droplet-associated proteins during hormonally stimulated lipolysis in engineered adipocytes: Stabilization and lipid droplet binding of adipocyte differentiation-related protein/adipophilin
    • Gross D.N., Miyoshi H., Hosaka T., Zhang H.-H., Pino E.C., et al. Dynamics of lipid droplet-associated proteins during hormonally stimulated lipolysis in engineered adipocytes: Stabilization and lipid droplet binding of adipocyte differentiation-related protein/adipophilin. Mol. Endocrinol 2006, 20:459-466.
    • (2006) Mol. Endocrinol , vol.20 , pp. 459-466
    • Gross, D.N.1    Miyoshi, H.2    Hosaka, T.3    Zhang, H.-H.4    Pino, E.C.5
  • 79
    • 0036089558 scopus 로고    scopus 로고
    • Seasonal dynamics of flight muscle fatty acid binding protein and catabolic enzymes in a migratory shorebird
    • Guglielmo C.G., Haunerland N.H., Hochachka P.W., Williams T.D. Seasonal dynamics of flight muscle fatty acid binding protein and catabolic enzymes in a migratory shorebird. Am. J. Physiol. 2002, 282:R1405-R1413.
    • (2002) Am. J. Physiol. , vol.282
    • Guglielmo, C.G.1    Haunerland, N.H.2    Hochachka, P.W.3    Williams, T.D.4
  • 80
    • 48549099661 scopus 로고    scopus 로고
    • Expression analysis of putative vitellogenin and lipophorin receptors in honey bee (Apis mellifera L.) queens and workers
    • Guidugli-Lazzarini K.R., do Nascimento A.M., Tanaka E.D., Piulachs M.-D., Hartfelder K., et al. Expression analysis of putative vitellogenin and lipophorin receptors in honey bee (Apis mellifera L.) queens and workers. J. Insect Physiol. 2008, 54:1138-1147.
    • (2008) J. Insect Physiol. , vol.54 , pp. 1138-1147
    • Guidugli-Lazzarini, K.R.1    do Nascimento, A.M.2    Tanaka, E.D.3    Piulachs, M.-D.4    Hartfelder, K.5
  • 81
    • 44449095056 scopus 로고    scopus 로고
    • Functional genomic screen reveals genes involved in lipid-droplet formation and utilization
    • Guo Y., Walther T.C., Rao M., Stuurman N., Goshima G., et al. Functional genomic screen reveals genes involved in lipid-droplet formation and utilization. Nature 2008, 453:657-661.
    • (2008) Nature , vol.453 , pp. 657-661
    • Guo, Y.1    Walther, T.C.2    Rao, M.3    Stuurman, N.4    Goshima, G.5
  • 82
    • 0034521485 scopus 로고    scopus 로고
    • Apolipophorin-III and the interactions of lipoteichoic acids with the immediate immune responses of Galleria mellonella
    • Halwani A.E., Niven D.F., Dunphy G.B. Apolipophorin-III and the interactions of lipoteichoic acids with the immediate immune responses of Galleria mellonella. J. Invertebr. Pathol. 2000, 76:233-241.
    • (2000) J. Invertebr. Pathol. , vol.76 , pp. 233-241
    • Halwani, A.E.1    Niven, D.F.2    Dunphy, G.B.3
  • 84
    • 0027405920 scopus 로고
    • Structure of the Asn-linked oligosaccharides of apolipophorin III from the insect Locusta migratoria: Carbohydrate-linked 2-amino-ethylphosphonate as a constituent of a glycoprotein
    • Hård K., Van Doorn J.M., Thomas-Oates J.E., Kamerling J.P., Van der Horst D.J. Structure of the Asn-linked oligosaccharides of apolipophorin III from the insect Locusta migratoria: Carbohydrate-linked 2-amino-ethylphosphonate as a constituent of a glycoprotein. Biochemistry 1993, 32:766-775.
    • (1993) Biochemistry , vol.32 , pp. 766-775
    • Hård, K.1    Van Doorn, J.M.2    Thomas-Oates, J.E.3    Kamerling, J.P.4    Van der Horst, D.J.5
  • 85
    • 0032712538 scopus 로고    scopus 로고
    • Differential location of peptide hormones in the secretory pathway of insect adipokinetic cells
    • Harthoorn L.F., Diederen J.H.B., Oudejans R.C.H.M., Van der Horst D.J. Differential location of peptide hormones in the secretory pathway of insect adipokinetic cells. Cell Tissue Res. 1999, 298:361-369.
    • (1999) Cell Tissue Res. , vol.298 , pp. 361-369
    • Harthoorn, L.F.1    Diederen, J.H.B.2    Oudejans, R.C.H.M.3    Van der Horst, D.J.4
  • 88
    • 0033208657 scopus 로고    scopus 로고
    • Tests of potential adipokinetic hormone precursor-related peptide (APRP) functions: Lack of responses
    • Hatle J.D., Spring J.H. Tests of potential adipokinetic hormone precursor-related peptide (APRP) functions: Lack of responses. Arch. Insect Biochem. Physiol. 1999, 42:163-166.
    • (1999) Arch. Insect Biochem. Physiol. , vol.42 , pp. 163-166
    • Hatle, J.D.1    Spring, J.H.2
  • 89
    • 0030798344 scopus 로고    scopus 로고
    • Transport and utilization of lipids in insect flight muscle
    • Haunerland N.H. Transport and utilization of lipids in insect flight muscle. Comp. Biochem. Physiol. B 1997, 117:475-482.
    • (1997) Comp. Biochem. Physiol. B , vol.117 , pp. 475-482
    • Haunerland, N.H.1
  • 90
    • 0027076755 scopus 로고
    • Fatty-acid-binding protein in locust flight muscle. Developmental changes of expression, concentration and intracellular distribution
    • Haunerland N.H., Andolfatto P., Chisholm J.M., Wang Z., Chen X. Fatty-acid-binding protein in locust flight muscle. Developmental changes of expression, concentration and intracellular distribution. Eur. J. Biochem. 1992, 210:1045-1051.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 1045-1051
    • Haunerland, N.H.1    Andolfatto, P.2    Chisholm, J.M.3    Wang, Z.4    Chen, X.5
  • 91
    • 0035004325 scopus 로고    scopus 로고
    • Deconstructing the LDL receptor - a rhapsody in pieces
    • Herz J. Deconstructing the LDL receptor - a rhapsody in pieces. Nat. Struct. Biol. 2002, 8:476-478.
    • (2002) Nat. Struct. Biol. , vol.8 , pp. 476-478
    • Herz, J.1
  • 92
    • 0025306734 scopus 로고
    • Lipid transfer particle in locust hemolymph: Purification and characterization
    • Hirayama Y., Chino H. Lipid transfer particle in locust hemolymph: Purification and characterization. J. Lipid Res. 1990, 31:793-799.
    • (1990) J. Lipid Res. , vol.31 , pp. 793-799
    • Hirayama, Y.1    Chino, H.2
  • 95
    • 0037147180 scopus 로고    scopus 로고
    • Structural biology: LDL receptor's beta-propeller displaces LDL
    • Innerarity T.L. Structural biology: LDL receptor's beta-propeller displaces LDL. Science 2002, 298:2337-2339.
    • (2002) Science , vol.298 , pp. 2337-2339
    • Innerarity, T.L.1
  • 96
    • 0031610767 scopus 로고    scopus 로고
    • Hemagglutinating properties of apolipophorin III from the hemolymph of Galleria mellonella larvae
    • Ishikawa H., Yamamoto K., Sehnal F. Hemagglutinating properties of apolipophorin III from the hemolymph of Galleria mellonella larvae. Arch. Insect Biochem. Physiol. 1998, 38:119-125.
    • (1998) Arch. Insect Biochem. Physiol. , vol.38 , pp. 119-125
    • Ishikawa, H.1    Yamamoto, K.2    Sehnal, F.3
  • 97
    • 22244478077 scopus 로고    scopus 로고
    • Structure and physiologic function of the low-density lipoprotein receptor
    • Jeon H., Blacklow S.C. Structure and physiologic function of the low-density lipoprotein receptor. Annu. Rev. Biochem. 2005, 74:535-562.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 535-562
    • Jeon, H.1    Blacklow, S.C.2
  • 98
    • 0032489436 scopus 로고    scopus 로고
    • Scavenger receptor class B type I as mediator of cellular cholesterol efflux to lipoproteins and phospholipid acceptors
    • Jian B., de la Llera-Moya M., Ji Y., Wang N., Phillips M.C., et al. Scavenger receptor class B type I as mediator of cellular cholesterol efflux to lipoproteins and phospholipid acceptors. J. Biol. Chem. 1998, 273:5599-5606.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5599-5606
    • Jian, B.1    de la Llera-Moya, M.2    Ji, Y.3    Wang, N.4    Phillips, M.C.5
  • 99
    • 0037311544 scopus 로고    scopus 로고
    • Transfer of cholesterol and diacylglycerol from lipophorin to Bombyx mori ovarioles in vitro: Role of lipid transfer particle
    • Jouni Z.E., Takada N., Gazard J., Maekawa H., Wells M.A., et al. Transfer of cholesterol and diacylglycerol from lipophorin to Bombyx mori ovarioles in vitro: Role of lipid transfer particle. Insect Biochem. Mol. Biol. 2003, 33:145-153.
    • (2003) Insect Biochem. Mol. Biol. , vol.33 , pp. 145-153
    • Jouni, Z.E.1    Takada, N.2    Gazard, J.3    Maekawa, H.4    Wells, M.A.5
  • 100
    • 0024278941 scopus 로고
    • Primary structure of apolipophorin-III from the migratory locust, Locusta migratoria
    • Kanost M.R., Boguski M.S., Freeman M., Gordon J.I., Wyatt G.R., et al. Primary structure of apolipophorin-III from the migratory locust, Locusta migratoria. J. Biol. Chem. 1988, 263:10568-10573.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10568-10573
    • Kanost, M.R.1    Boguski, M.S.2    Freeman, M.3    Gordon, J.I.4    Wyatt, G.R.5
  • 101
    • 70449622749 scopus 로고    scopus 로고
    • The adipokinetic hormone system in Culicinae (Diptera: Culicidae): Molecular identification and characterization of two adipokinetic hormone (AKH) precursors from Aedes aegypti and Culex pipiens and two putative AKH receptor variants from Ae. aegypti
    • Kaufmann C., Merzendorfer H., Gäde G. The adipokinetic hormone system in Culicinae (Diptera: Culicidae): Molecular identification and characterization of two adipokinetic hormone (AKH) precursors from Aedes aegypti and Culex pipiens and two putative AKH receptor variants from Ae. aegypti. Insect Biochem. Mol. Biol. 2009, 39:770-781.
    • (2009) Insect Biochem. Mol. Biol. , vol.39 , pp. 770-781
    • Kaufmann, C.1    Merzendorfer, H.2    Gäde, G.3
  • 102
    • 0024296931 scopus 로고
    • Role of lipophorin in lipid transport to the insect egg
    • Kawooya J.K., Law J.H. Role of lipophorin in lipid transport to the insect egg. J. Biol. Chem. 1988, 263:8748-8753.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8748-8753
    • Kawooya, J.K.1    Law, J.H.2
  • 105
    • 0024296905 scopus 로고
    • Uptake of the major lipoprotein and its transformation in the insect egg
    • Kawooya J.K., Osir E.O., Law J.H. Uptake of the major lipoprotein and its transformation in the insect egg. J. Biol. Chem. 1988, 263:8740-8747.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8740-8747
    • Kawooya, J.K.1    Osir, E.O.2    Law, J.H.3
  • 106
    • 0024318973 scopus 로고
    • A strategy for solubilizing delipidated apolipoprotein with lysophosphatidylcholine and reconstitution with phosphatidylcholine
    • Kawooya J.K., Wells M.A., Law J.H. A strategy for solubilizing delipidated apolipoprotein with lysophosphatidylcholine and reconstitution with phosphatidylcholine. Biochemistry 1989, 28:6658-6667.
    • (1989) Biochemistry , vol.28 , pp. 6658-6667
    • Kawooya, J.K.1    Wells, M.A.2    Law, J.H.3
  • 107
    • 0036677393 scopus 로고    scopus 로고
    • A class B scavenger receptor mediates the cullular uptake of carotenoids in Drosophila
    • Kiefer C., Sumser E., Wernet M.F., von Lintig J. A class B scavenger receptor mediates the cullular uptake of carotenoids in Drosophila. Proc. Natl. Acad. Sci. USA 2002, 99:10581-10586.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10581-10586
    • Kiefer, C.1    Sumser, E.2    Wernet, M.F.3    von Lintig, J.4
  • 108
    • 4744367572 scopus 로고    scopus 로고
    • Immune activation of apolipophorin-III and its distribution in hemocytes from Hyphantria cunea
    • Kim H.J., Je H.J., Park S.Y., Lee I.H., Jin B.R., et al. Immune activation of apolipophorin-III and its distribution in hemocytes from Hyphantria cunea. Insect Biochem. Mol. Biol. 2004, 34:1011-1023.
    • (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
  • 109
    • 0036712111 scopus 로고    scopus 로고
    • Comparative models for human apolipoprotein A-I bound to lipid in discoidal high-density lipoprotein particles
    • Klon A.E., Segrest J.P., Harvey S.C. Comparative models for human apolipoprotein A-I bound to lipid in discoidal high-density lipoprotein particles. Biochemistry 2002, 41:10895-10905.
    • (2002) Biochemistry , vol.41 , pp. 10895-10905
    • Klon, A.E.1    Segrest, J.P.2    Harvey, S.C.3
  • 110
    • 0033851170 scopus 로고    scopus 로고
    • Structure elucidation and biological activity of an unusual adipokinetic hormone from corpora cardiaca of the butterfly, Vanessa cardui
    • Köllisch G.V., Lorenz M.W., Kellner R., Verhaert P.D., Hoffman K.H. Structure elucidation and biological activity of an unusual adipokinetic hormone from corpora cardiaca of the butterfly, Vanessa cardui. Eur. J. Biochem. 2000, 267:5502-5508.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5502-5508
    • Köllisch, G.V.1    Lorenz, M.W.2    Kellner, R.3    Verhaert, P.D.4    Hoffman, K.H.5
  • 113
    • 33646825823 scopus 로고    scopus 로고
    • Self-association and lipid binding properties of the lipoprotein initiating domain of apolipoprotein B
    • Ledford A.S., Weinberg R.B., Cook V.R., Hantgan R.R., Shelness G.S. Self-association and lipid binding properties of the lipoprotein initiating domain of apolipoprotein B. J. Biol. Chem. 2006, 281:8871-8876.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8871-8876
    • Ledford, A.S.1    Weinberg, R.B.2    Cook, V.R.3    Hantgan, R.R.4    Shelness, G.S.5
  • 114
    • 0142058215 scopus 로고    scopus 로고
    • Wax moth, Galleria mellonella, fat body receptor for high-density lipophorin (HDLp)
    • Lee C.S., Han J.H., Lee S.M., Hwang J.S., Kang S.W., et al. Wax moth, Galleria mellonella, fat body receptor for high-density lipophorin (HDLp). Arch. Insect Biochem. Physiol. 2003, 54:14-24.
    • (2003) Arch. Insect Biochem. Physiol. , vol.54 , pp. 14-24
    • Lee, C.S.1    Han, J.H.2    Lee, S.M.3    Hwang, J.S.4    Kang, S.W.5
  • 115
    • 0043210481 scopus 로고    scopus 로고
    • Wax moth, Galleria mellonella, high density lipophorin receptor: Alternative splicing, tissue-specific expression, and developmental regulation
    • Lee C.S., Han J.H., Kim B.S., Lee S.M., Hwang J.S., et al. Wax moth, Galleria mellonella, high density lipophorin receptor: Alternative splicing, tissue-specific expression, and developmental regulation. Insect Biochem. Mol. Biol 2003, 33:761-771.
    • (2003) Insect Biochem. Mol. Biol , vol.33 , pp. 761-771
    • Lee, C.S.1    Han, J.H.2    Kim, B.S.3    Lee, S.M.4    Hwang, J.S.5
  • 116
    • 33746309850 scopus 로고    scopus 로고
    • Tyrosine fluorescence analysis of apolipophorin III-lipopolysaccharide interaction
    • Leon L.J., Pratt C.C., Vasquez L.J., Weers P.M.M. Tyrosine fluorescence analysis of apolipophorin III-lipopolysaccharide interaction. Arch. Biochem. Biophys 2006, 452:38-45.
    • (2006) Arch. Biochem. Biophys , vol.452 , pp. 38-45
    • Leon, L.J.1    Pratt, C.C.2    Vasquez, L.J.3    Weers, P.M.M.4
  • 117
  • 118
    • 58549100926 scopus 로고    scopus 로고
    • Adipokinetic hormone signaling through the gonadotropin-releasing hormone receptor modulates egg-laying in Caenorhabditis elegans
    • Lindemans M., Liu F., Janssen T., Husson S.J., Mertens I., et al. Adipokinetic hormone signaling through the gonadotropin-releasing hormone receptor modulates egg-laying in Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA 2009, 106:1642-1647.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 1642-1647
    • Lindemans, M.1    Liu, F.2    Janssen, T.3    Husson, S.J.4    Mertens, I.5
  • 119
    • 0025899612 scopus 로고
    • Role of lipid transfer particle in transformation of lipophorin in insect oocytes
    • Liu H., Ryan R.O. Role of lipid transfer particle in transformation of lipophorin in insect oocytes. Biochim. Biophys. Acta 1991, 1085:112-118.
    • (1991) Biochim. Biophys. Acta , vol.1085 , pp. 112-118
    • Liu, H.1    Ryan, R.O.2
  • 120
    • 0027524130 scopus 로고
    • Prevention of phospholipase-C induced aggregation of low density lipoprotein by amphipathic apolipoproteins
    • Liu H., Scraba D.G., Ryan R.O. Prevention of phospholipase-C induced aggregation of low density lipoprotein by amphipathic apolipoproteins. FEBS Lett. 1993, 316:27-33.
    • (1993) FEBS Lett. , vol.316 , pp. 27-33
    • Liu, H.1    Scraba, D.G.2    Ryan, R.O.3
  • 121
    • 0033071156 scopus 로고    scopus 로고
    • Perilipins, ADRP, and other proteins that associate with intracellular neutral lipid droplets in animal cells
    • Londos C., Brasaemle D.L., Schultz C.J., Segrest J.P., Kimmel A.R. Perilipins, ADRP, and other proteins that associate with intracellular neutral lipid droplets in animal cells. Semin. Cell Dev. Biol. 1999, 10:51-58.
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 51-58
    • Londos, C.1    Brasaemle, D.L.2    Schultz, C.J.3    Segrest, J.P.4    Kimmel, A.R.5
  • 123
    • 33646891301 scopus 로고    scopus 로고
    • Fatty-acid-binding protein from the flight muscle of Locusta migratoria: Evolutionary variations in fatty acid binding
    • Lücke C., Qiao Y., Van Moerkerk H.T., Veerkamp J.H., Hamilton J.A. Fatty-acid-binding protein from the flight muscle of Locusta migratoria: Evolutionary variations in fatty acid binding. Biochemistry 2006, 45:6296-6305.
    • (2006) Biochemistry , vol.45 , pp. 6296-6305
    • Lücke, C.1    Qiao, Y.2    Van Moerkerk, H.T.3    Veerkamp, J.H.4    Hamilton, J.A.5
  • 125
    • 33646168160 scopus 로고    scopus 로고
    • Lipid droplets: A unified view of a dynamic organelle
    • Martin S., Parton R.G. Lipid droplets: A unified view of a dynamic organelle. Nat. Rev. Mol. Cell Biol. 2006, 7:373-378.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 373-378
    • Martin, S.1    Parton, R.G.2
  • 127
    • 0029752791 scopus 로고    scopus 로고
    • Endocytosis and molecular sorting
    • Mellman I. Endocytosis and molecular sorting. Annu. Rev. Cell Devel. Biol. 1996, 12:575-625.
    • (1996) Annu. Rev. Cell Devel. Biol. , vol.12 , pp. 575-625
    • Mellman, I.1
  • 128
    • 0037200026 scopus 로고    scopus 로고
    • Functional conservation for lipid storage droplet association among Perilipin, ADRP, and TIP47 (PAT)-related proteins in mammals, Drosophila, and Dictyostelium
    • Miura S., Gan J.W., Brzostowski J., Parisi M.J., Schultz C.J., et al. Functional conservation for lipid storage droplet association among Perilipin, ADRP, and TIP47 (PAT)-related proteins in mammals, Drosophila, and Dictyostelium. J. Biol. Chem. 2002, 277:32253-32257.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32253-32257
    • Miura, S.1    Gan, J.W.2    Brzostowski, J.3    Parisi, M.J.4    Schultz, C.J.5
  • 130
    • 0037967636 scopus 로고    scopus 로고
    • Changes in lipophorins are related to the activation of phenoloxidase in the haemolymph of Locusta migratoria in response to injection of immunogens
    • Mullen L., Goldsworthy G. Changes in lipophorins are related to the activation of phenoloxidase in the haemolymph of Locusta migratoria in response to injection of immunogens. Insect Biochem. Mol. Biol. 2003, 33:661-670.
    • (2003) Insect Biochem. Mol. Biol. , vol.33 , pp. 661-670
    • Mullen, L.1    Goldsworthy, G.2
  • 131
    • 67349280293 scopus 로고    scopus 로고
    • Lipid droplet-organelle interactions: Sharing the fats
    • Murphy S., Martin S., Parton R.G. Lipid droplet-organelle interactions: Sharing the fats. Biochim. Biophys. Acta 2009, 1791:441-447.
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 441-447
    • Murphy, S.1    Martin, S.2    Parton, R.G.3
  • 132
    • 0038179218 scopus 로고
    • Diglyceride-transporting lipoproteins in Locusta
    • Mwangi R.W., Goldsworthy G.J. Diglyceride-transporting lipoproteins in Locusta. J. Comp. Physiol. 1977, 114:177-190.
    • (1977) J. Comp. Physiol. , vol.114 , pp. 177-190
    • Mwangi, R.W.1    Goldsworthy, G.J.2
  • 133
    • 0343585824 scopus 로고
    • Diacylglycerol-transporting lipoproteins and flight in Locusta
    • Mwangi R.W., Goldsworthy G.J. Diacylglycerol-transporting lipoproteins and flight in Locusta. J. Insect Physiol 1981, 27:47-50.
    • (1981) J. Insect Physiol , vol.27 , pp. 47-50
    • Mwangi, R.W.1    Goldsworthy, G.J.2
  • 134
    • 0033991858 scopus 로고    scopus 로고
    • The molecular basis of exchangeable apolipoprotein function
    • Narayanaswami V., Ryan R.O. The molecular basis of exchangeable apolipoprotein function. Biochim. Biophys. Acta 2000, 1483:15-36.
    • (2000) Biochim. Biophys. Acta , vol.1483 , pp. 15-36
    • Narayanaswami, V.1    Ryan, R.O.2
  • 135
    • 0029967954 scopus 로고    scopus 로고
    • Disulfide bond engineering to monitor conformational opening of apolipophorin III during lipid binding
    • Narayanaswami V., Wang J., Kay C.M., Scraba D.G., Ryan R.O. Disulfide bond engineering to monitor conformational opening of apolipophorin III during lipid binding. J. Biol. Chem. 1996, 271:26855-26862.
    • (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
  • 136
    • 0030270732 scopus 로고    scopus 로고
    • Fluorescence studies of lipid-association induced conformational adaptations of an exchangeable amphipathic apolipoprotein
    • Narayanaswami V., Frolov A., Schroeder F., Oikawa K., Kay C.M., et al. Fluorescence studies of lipid-association induced conformational adaptations of an exchangeable amphipathic apolipoprotein. Arch. Biochem. Biophys. 1996, 334:143-150.
    • (1996) Arch. Biochem. Biophys. , vol.334 , pp. 143-150
    • Narayanaswami, V.1    Frolov, A.2    Schroeder, F.3    Oikawa, K.4    Kay, C.M.5
  • 137
    • 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 C.M., Ryan R.O. A molecular trigger of lipid-binding induced opening of a helix bundle exchangeable apolipoprotein. Proc. Natl. Acad. Sci. USA 1999, 96:4366-4371.
    • (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
  • 138
    • 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 2001, 40:11502-11508.
    • (2001) Biochemistry , vol.40 , pp. 11502-11508
    • Niere, M.1    Dettloff, M.2    Maier, T.3    Ziegler, M.4    Wiesner, A.5
  • 139
    • 0026064174 scopus 로고
    • Isolation and structure elucidation of a novel adipokinetic hormone (Lom-AKH-III) from the glandular lobes of the corpus cardiacum of the migratory locust, Locusta migratoria
    • Oudejans R.C.H.M., Kooiman F.P., Heerma W., Versluis C., Slotboom A.J., et al. Isolation and structure elucidation of a novel adipokinetic hormone (Lom-AKH-III) from the glandular lobes of the corpus cardiacum of the migratory locust, Locusta migratoria. Eur. J. Biochem. 1991, 195:351-359.
    • (1991) Eur. J. Biochem. , vol.195 , pp. 351-359
    • Oudejans, R.C.H.M.1    Kooiman, F.P.2    Heerma, W.3    Versluis, C.4    Slotboom, A.J.5
  • 140
    • 0027376995 scopus 로고
    • Adipokinetic peptide hormone content and biosynthesis during locust development
    • Oudejans R.C.H.M., Mes T.H.M., Kooiman F.P., Van der Horst D.J. Adipokinetic peptide hormone content and biosynthesis during locust development. Peptides 1993, 14:877-881.
    • (1993) Peptides , vol.14 , pp. 877-881
    • Oudejans, R.C.H.M.1    Mes, T.H.M.2    Kooiman, F.P.3    Van der Horst, D.J.4
  • 141
    • 0029738627 scopus 로고    scopus 로고
    • Locust adipokinetic hormones: Carrier-independent transport and differential inactivation at physiological concentrations during rest and flight
    • Oudejans R.C.H.M., Vroemen S.F., Jansen R.F.R., Van der Horst D.J. Locust adipokinetic hormones: Carrier-independent transport and differential inactivation at physiological concentrations during rest and flight. Proc. Natl. Acad. Sci. USA 1996, 93:8654-8659.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8654-8659
    • Oudejans, R.C.H.M.1    Vroemen, S.F.2    Jansen, R.F.R.3    Van der Horst, D.J.4
  • 142
    • 1542530717 scopus 로고    scopus 로고
    • Adipokinetic hormones: Structure and biosynthesis
    • Academic Press, London, H.L. Henry, A.W. Norman (Eds.)
    • Oudejans R.C.H.M., Van der Horst D.J. Adipokinetic hormones: Structure and biosynthesis. Encyclopedia of Hormones 2003, vol. 1:38-42. Academic Press, London. H.L. Henry, A.W. Norman (Eds.).
    • (2003) Encyclopedia of Hormones , vol.1 , pp. 38-42
    • Oudejans, R.C.H.M.1    Van der Horst, D.J.2
  • 143
    • 33750036424 scopus 로고    scopus 로고
    • Adipokinetic hormone-induced mobilization of fat body triglyceride stores in Manduca sexta: Role of TG-lipase and lipid droplets
    • Patel R.T., Soulages J.L., Arrese E.L. Adipokinetic hormone-induced mobilization of fat body triglyceride stores in Manduca sexta: Role of TG-lipase and lipid droplets. Arch. Insect Biochem. Physiol. 2006, 63:73-81.
    • (2006) Arch. Insect Biochem. Physiol. , vol.63 , pp. 73-81
    • Patel, R.T.1    Soulages, J.L.2    Arrese, E.L.3
  • 144
    • 0017854716 scopus 로고
    • Kinetics of lipid-protein interactions: Interaction of apolipoprotein A-I from human plasma high density lipoproteins with phosphatidylcholines
    • Pownall H.J., Massey J.B., Kusserow S.K., Gotto A.M. Kinetics of lipid-protein interactions: Interaction of apolipoprotein A-I from human plasma high density lipoproteins with phosphatidylcholines. Biochemistry 1978, 17:1183-1188.
    • (1978) Biochemistry , vol.17 , pp. 1183-1188
    • Pownall, H.J.1    Massey, J.B.2    Kusserow, S.K.3    Gotto, A.M.4
  • 145
    • 0022591516 scopus 로고
    • Changes in lipoprotein composition during larval-pupal metamorphosis of an insect, Manduca sexta
    • Prasad S.V., Ryan R.O., Wells M.A., Law J.H. Changes in lipoprotein composition during larval-pupal metamorphosis of an insect, Manduca sexta. J. Biol. Chem. 1986, 261:558-562.
    • (1986) J. Biol. Chem. , vol.261 , pp. 558-562
    • Prasad, S.V.1    Ryan, R.O.2    Wells, M.A.3    Law, J.H.4
  • 146
    • 10044286925 scopus 로고    scopus 로고
    • Lipopolysaccharide binding of an exchangeable apolipoprotein, apolipophorin III, from Galleria mellonella
    • Pratt C.C., Weers P.M.M. Lipopolysaccharide binding of an exchangeable apolipoprotein, apolipophorin III, from Galleria mellonella. Biol. Chem. 2004, 385:1113-1119.
    • (2004) Biol. Chem. , vol.385 , pp. 1113-1119
    • Pratt, C.C.1    Weers, P.M.M.2
  • 147
    • 34248682956 scopus 로고    scopus 로고
    • Fatty acid-dependent expression of the muscle FABP gene - comparative analysis of gene control in functionally related, but evolutionary distant animal systems
    • Qu H., Cui L., Rickers-Haunerland J., Haunerland N.H. Fatty acid-dependent expression of the muscle FABP gene - comparative analysis of gene control in functionally related, but evolutionary distant animal systems. Mol. Cell. Biochem. 2007, 299:45-53.
    • (2007) Mol. Cell. Biochem. , vol.299 , pp. 45-53
    • Qu, H.1    Cui, L.2    Rickers-Haunerland, J.3    Haunerland, N.H.4
  • 148
    • 0036784612 scopus 로고    scopus 로고
    • Molecular biology of mosquito vitellogenesis: From basic studies to genetic engineering of antipathogen immunity
    • Raikhel A.S., Kokoza V.A., Zhu J., Martin D., Wang S.F., et al. Molecular biology of mosquito vitellogenesis: From basic studies to genetic engineering of antipathogen immunity. Insect Biochem. Mol. Biol. 2002, 32:1275-1286.
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , pp. 1275-1286
    • Raikhel, A.S.1    Kokoza, V.A.2    Zhu, J.3    Martin, D.4    Wang, S.F.5
  • 149
    • 0028977999 scopus 로고
    • Alignment of apolipophorin III α-helices in complex with dimyristoylphosphatidylcholine: A unique spatial orientation
    • Raussens V., Goormaghtigh E., Narayanaswami V., Ryan R.O., Ruysschaert J.M. Alignment of apolipophorin III α-helices in complex with dimyristoylphosphatidylcholine: A unique spatial orientation. J. Biol. Chem. 1995, 270:12542-12547.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12542-12547
    • Raussens, V.1    Goormaghtigh, E.2    Narayanaswami, V.3    Ryan, R.O.4    Ruysschaert, J.M.5
  • 150
    • 0029813440 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange kinetics of apolipophorin III in lipid free and phospholipid bound states: An analysis by Fourier transform infrared spectroscopy
    • Raussens V., Narayanaswami V., Goormaghtigh E., Ryan R.O., Ruysschaert J.M. Hydrogen/deuterium exchange kinetics of apolipophorin III in lipid free and phospholipid bound states: An analysis by Fourier transform infrared spectroscopy. J. Biol. Chem. 1996, 271:23089-23095.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23089-23095
    • Raussens, V.1    Narayanaswami, V.2    Goormaghtigh, E.3    Ryan, R.O.4    Ruysschaert, J.M.5
  • 151
    • 20544475890 scopus 로고    scopus 로고
    • Assembly of lipoprotein particles containing apolipoprotein-B: Structural model for the native lipoprotein particle
    • Richardson P.E., Manchekar M., Dashti N., Jones M.K., Beigneux A., et al. Assembly of lipoprotein particles containing apolipoprotein-B: Structural model for the native lipoprotein particle. Biophys. J. 2005, 88:2789-2800.
    • (2005) Biophys. J. , vol.88 , pp. 2789-2800
    • Richardson, P.E.1    Manchekar, M.2    Dashti, N.3    Jones, M.K.4    Beigneux, A.5
  • 152
    • 23944448331 scopus 로고    scopus 로고
    • Lipoprotein-mediated lipid transport in insects: Analogy to the mammalian lipid carrier system and novel concepts for the functioning of LDL receptor family members
    • Rodenburg K.W., Van der Horst D.J. Lipoprotein-mediated lipid transport in insects: Analogy to the mammalian lipid carrier system and novel concepts for the functioning of LDL receptor family members. Biochim. Biophys. Acta 2005, 1736:10-29.
    • (2005) Biochim. Biophys. Acta , vol.1736 , pp. 10-29
    • Rodenburg, K.W.1    Van der Horst, D.J.2
  • 153
    • 33645064268 scopus 로고    scopus 로고
    • Sequence analysis of the non-recurring C-terminal domains shows that insect lipoprotein receptors constitute a distinct group of LDL receptor family members
    • Rodenburg K.W., Smolenaars M.M.W., Van Hoof D., Van der Horst D.J. Sequence analysis of the non-recurring C-terminal domains shows that insect lipoprotein receptors constitute a distinct group of LDL receptor family members. Insect Biochem. Mol. Biol. 2006, 36:250-263.
    • (2006) Insect Biochem. Mol. Biol. , vol.36 , pp. 250-263
    • Rodenburg, K.W.1    Smolenaars, M.M.W.2    Van Hoof, D.3    Van der Horst, D.J.4
  • 154
    • 41549099204 scopus 로고    scopus 로고
    • The complex of the insect LDL receptor homologue, LpR, and its lipoprotein ligand does not dissociate at endosomal conditions
    • Roosendaal S.D., Kerver J., Schipper M., Rodenburg K.W., Van der Horst D.J. The complex of the insect LDL receptor homologue, LpR, and its lipoprotein ligand does not dissociate at endosomal conditions. FEBS J. 2008, 275:1751-1766.
    • (2008) FEBS J. , vol.275 , pp. 1751-1766
    • Roosendaal, S.D.1    Kerver, J.2    Schipper, M.3    Rodenburg, K.W.4    Van der Horst, D.J.5
  • 155
    • 60549089812 scopus 로고    scopus 로고
    • Delipidation of insect lipoprotein, lipophorin, affects its binding to the lipophorin receptor, LpR: Implications for the role of LpR-mediated endocytosis
    • Roosendaal S.D., Van Doorn J.M., Valentijn K.M., Van der Horst D.J., Rodenburg K.W. Delipidation of insect lipoprotein, lipophorin, affects its binding to the lipophorin receptor, LpR: Implications for the role of LpR-mediated endocytosis. Insect Biochem. Mol. Biol. 2009, 39:135-144.
    • (2009) Insect Biochem. Mol. Biol. , vol.39 , pp. 135-144
    • Roosendaal, S.D.1    Van Doorn, J.M.2    Valentijn, K.M.3    Van der Horst, D.J.4    Rodenburg, K.W.5
  • 156
    • 0037147281 scopus 로고    scopus 로고
    • Structure of the LDL receptor extracellular domain at endosomal pH
    • Rudenko G., Henry L., Henderson K., Ichtchenko K., Brown M.S., et al. Structure of the LDL receptor extracellular domain at endosomal pH. Science 2002, 298:2353-2358.
    • (2002) Science , vol.298 , pp. 2353-2358
    • Rudenko, G.1    Henry, L.2    Henderson, K.3    Ichtchenko, K.4    Brown, M.S.5
  • 157
    • 0024993524 scopus 로고
    • The dynamics of insect lipophorin metabolism
    • Ryan R.O. The dynamics of insect lipophorin metabolism. J. Lipid Res. 1990, 31:1725-1739.
    • (1990) J. Lipid Res. , vol.31 , pp. 1725-1739
    • Ryan, R.O.1
  • 158
    • 41449092116 scopus 로고    scopus 로고
    • Nanodisks: Hydrophobic drug delivery vehicles
    • Ryan R.O. Nanodisks: Hydrophobic drug delivery vehicles. Expert Opin. Drug Deliv 2008, 3:343-351.
    • (2008) Expert Opin. Drug Deliv , vol.3 , pp. 343-351
    • Ryan, R.O.1
  • 159
    • 0034107475 scopus 로고    scopus 로고
    • Lipid transport biochemistry and its role in energy production
    • Ryan R.O., Van der Horst D.J. Lipid transport biochemistry and its role in energy production. Annu. Rev. Entomol. 2000, 45:233-260.
    • (2000) Annu. Rev. Entomol. , vol.45 , pp. 233-260
    • Ryan, R.O.1    Van der Horst, D.J.2
  • 160
    • 0022600993 scopus 로고
    • Lipoprotein interconversions in an insect, Manduca sexta: Evidence for a lipid transfer factor in the hemolymph
    • Ryan R.O., Prasad S.V., Henriksen E.J., Wells M.A., Law J.H. Lipoprotein interconversions in an insect, Manduca sexta: Evidence for a lipid transfer factor in the hemolymph. J. Biol. Chem. 1986, 261:563-568.
    • (1986) J. Biol. Chem. , vol.261 , pp. 563-568
    • Ryan, R.O.1    Prasad, S.V.2    Henriksen, E.J.3    Wells, M.A.4    Law, J.H.5
  • 162
    • 0024279274 scopus 로고
    • Facilitated diacylglycerol exchange between insect hemolymph lipophorins: Properties of Manduca sexta lipid transfer particle
    • Ryan R.O., Senthilathipan K.R., Wells M.A., Law J.H. Facilitated diacylglycerol exchange between insect hemolymph lipophorins: Properties of Manduca sexta lipid transfer particle. J. Biol. Chem. 1988, 263:14140-14145.
    • (1988) J. Biol. Chem. , vol.263 , pp. 14140-14145
    • Ryan, R.O.1    Senthilathipan, K.R.2    Wells, M.A.3    Law, J.H.4
  • 163
    • 0025327738 scopus 로고
    • Studies of the morphology and structure of the plasma lipid transfer particle from the tobacco hornworm
    • Ryan R.O., Howe A., Scraba D.G. Studies of the morphology and structure of the plasma lipid transfer particle from the tobacco hornworm. Manduca sexta. J. Lipid Res. 1990, 31:871-879.
    • (1990) Manduca sexta. J. Lipid Res. , vol.31 , pp. 871-879
    • Ryan, R.O.1    Howe, A.2    Scraba, D.G.3
  • 164
    • 0025367346 scopus 로고
    • Insect lipid transfer particle catalyzes bidirectional vectorial transfer of diacylglycerol from lipophorin to human low density lipoprotein
    • Ryan R.O., Wessler A.N., Ando S., Price H.M., Yokoyama S. Insect lipid transfer particle catalyzes bidirectional vectorial transfer of diacylglycerol from lipophorin to human low density lipoprotein. J. Biol. Chem. 1990, 265:10551-10555.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10551-10555
    • Ryan, R.O.1    Wessler, A.N.2    Ando, S.3    Price, H.M.4    Yokoyama, S.5
  • 165
    • 0027391142 scopus 로고
    • Conformational, thermodynamic and stability properties of Manduca sexta apolipophorin III
    • Ryan R.O., Oikawa K., Kay C.M. Conformational, thermodynamic and stability properties of Manduca sexta apolipophorin III. J. Biol. Chem. 1993, 268:1525-1530.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1525-1530
    • Ryan, R.O.1    Oikawa, K.2    Kay, C.M.3
  • 166
    • 0029074476 scopus 로고
    • Bacterial expression and site directed mutagenesis of a functional recombinant apolipoprotein
    • Ryan R.O., Schieve D.S., Wientzek M., Narayanaswami V., Oikawa K., et al. Bacterial expression and site directed mutagenesis of a functional recombinant apolipoprotein. J. Lipid Res. 1995, 36:1066-1072.
    • (1995) J. Lipid Res. , vol.36 , pp. 1066-1072
    • Ryan, R.O.1    Schieve, D.S.2    Wientzek, M.3    Narayanaswami, V.4    Oikawa, K.5
  • 167
    • 0034612303 scopus 로고    scopus 로고
    • Pyrene excimer fluorescence: A spatially sensitive probe to monitor lipid induced rearrangement of apolipophorin III
    • Sahoo D., Narayanaswami V., Kay C.M., Ryan R.O. Pyrene excimer fluorescence: A spatially sensitive probe to monitor lipid induced rearrangement of apolipophorin III. Biochemistry 2000, 39:6594-6601.
    • (2000) Biochemistry , vol.39 , pp. 6594-6601
    • Sahoo, D.1    Narayanaswami, V.2    Kay, C.M.3    Ryan, R.O.4
  • 168
    • 0036384368 scopus 로고    scopus 로고
    • Lipid-triggered conformational switch of apolipophorin III helix bundle to an extended helix organization
    • Sahoo D., Weers P.M.M., Ryan R.O., Narayanaswami V. Lipid-triggered conformational switch of apolipophorin III helix bundle to an extended helix organization. J. Mol. Biol. 2002, 321:201-214.
    • (2002) J. Mol. Biol. , vol.321 , pp. 201-214
    • Sahoo, D.1    Weers, P.M.M.2    Ryan, R.O.3    Narayanaswami, V.4
  • 169
    • 25644452640 scopus 로고    scopus 로고
    • BmStart1, a novel carotenoid-binding protein isoform from Bombyx mori, is orthologous to MLN64, a mammalian cholesterol transporter
    • Sakudoh T., Tsuchida K., Kataoka H. BmStart1, a novel carotenoid-binding protein isoform from Bombyx mori, is orthologous to MLN64, a mammalian cholesterol transporter. Biochem. Biophys. Res. Commun 2005, 336:1125-1135.
    • (2005) Biochem. Biophys. Res. Commun , vol.336 , pp. 1125-1135
    • Sakudoh, T.1    Tsuchida, K.2    Kataoka, H.3
  • 170
    • 34547483580 scopus 로고    scopus 로고
    • Carotenoid silk coloration is controlled by a carotenoid-binding protein, a product of the Yellow blood gene
    • Sakudoh T., Sezutsu H., Nakashima T., Kobayashi I., Fujimoto H., et al. Carotenoid silk coloration is controlled by a carotenoid-binding protein, a product of the Yellow blood gene. Proc. Natl. Acad. Sci. USA 2007, 104:8941-8946.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 8941-8946
    • Sakudoh, T.1    Sezutsu, H.2    Nakashima, T.3    Kobayashi, I.4    Fujimoto, H.5
  • 171
    • 77951242221 scopus 로고    scopus 로고
    • A CD36-related transmembrane protein is coordinated with an intracellular lipid-binding protein in selective carotenoid transport for cocoon coloration
    • Sakudoh T., Iizuka T., Narukawa J., Sezutsu H., Kobayashi I., et al. A CD36-related transmembrane protein is coordinated with an intracellular lipid-binding protein in selective carotenoid transport for cocoon coloration. J. Biol. Chem. 2010, 285:7739-7751.
    • (2010) J. Biol. Chem. , vol.285 , pp. 7739-7751
    • Sakudoh, T.1    Iizuka, T.2    Narukawa, J.3    Sezutsu, H.4    Kobayashi, I.5
  • 172
    • 0032078463 scopus 로고    scopus 로고
    • Molecular characteristics of insect vitellogenins and vitellogenin receptors
    • Sappington T.W., Raikhel A.S. Molecular characteristics of insect vitellogenins and vitellogenin receptors. Insect Biochem. Mol. Biol. 1998, 28:277-300.
    • (1998) Insect Biochem. Mol. Biol. , vol.28 , pp. 277-300
    • Sappington, T.W.1    Raikhel, A.S.2
  • 173
    • 0029808992 scopus 로고    scopus 로고
    • Molecular characterization of the mosquito vitellogenin receptor reveals unexpected high homology to the Drosophila yolk protein receptor
    • Sappington T.W., Kokoza V.A., Cho W.L., Raikhel A.S. Molecular characterization of the mosquito vitellogenin receptor reveals unexpected high homology to the Drosophila yolk protein receptor. Proc. Natl. Acad. Sci. USA 1996, 93:8934-8939.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8934-8939
    • Sappington, T.W.1    Kokoza, V.A.2    Cho, W.L.3    Raikhel, A.S.4
  • 175
    • 0028964133 scopus 로고
    • The Drosophila yolkless gene encodes a vitellogenin receptor belonging to the low-density lipoprotein receptor superfamily
    • Schonbaum C.P., Lee S., Mahowald A.P. The Drosophila yolkless gene encodes a vitellogenin receptor belonging to the low-density lipoprotein receptor superfamily. Proc. Natl. Acad. Sci. USA 1995, 92:1485-1489.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1485-1489
    • Schonbaum, C.P.1    Lee, S.2    Mahowald, A.P.3
  • 176
    • 0035655157 scopus 로고    scopus 로고
    • Structure of apolipoprotein B-100 in low density lipoproteins
    • Segrest J.P., Jones M.K., De Loof H., Dashti N. Structure of apolipoprotein B-100 in low density lipoproteins. J. Lipid Res. 2001, 42:1346-1367.
    • (2001) J. Lipid Res. , vol.42 , pp. 1346-1367
    • Segrest, J.P.1    Jones, M.K.2    De Loof, H.3    Dashti, N.4
  • 177
    • 0038143355 scopus 로고    scopus 로고
    • A Drosophila microsomal triglyceride transfer protein homolog promotes the assembly and secretion of human apolipoprotein B: Implications for human and insect lipid transport and metabolism
    • Sellers J.A., Hou L., Athar H., Hussain M.M., Shelness G.S. A Drosophila microsomal triglyceride transfer protein homolog promotes the assembly and secretion of human apolipoprotein B: Implications for human and insect lipid transport and metabolism. J. Biol. Chem. 2003, 278:20367-20373.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20367-20373
    • Sellers, J.A.1    Hou, L.2    Athar, H.3    Hussain, M.M.4    Shelness, G.S.5
  • 178
    • 0142149154 scopus 로고    scopus 로고
    • Tissue- and stage-specific expression of two lipophorin receptor variants with seven and eight ligand-binding repeats in the adult mosquito
    • Seo S.-J., Cheon H.-M., Sun J., Sappington T.W., Raikhel A.S. Tissue- and stage-specific expression of two lipophorin receptor variants with seven and eight ligand-binding repeats in the adult mosquito. J. Biol. Chem. 2003, 278:41954-41962.
    • (2003) J. Biol. Chem. , vol.278 , pp. 41954-41962
    • Seo, S.-J.1    Cheon, H.-M.2    Sun, J.3    Sappington, T.W.4    Raikhel, A.S.5
  • 179
    • 55549145013 scopus 로고    scopus 로고
    • Apolipophorin III from Hyphantria cunea shows different anti-oxidant ability against LDL oxidation in the lipid-free and lipid-bound state
    • Seo S.J., Park K.H., Cho K.H. Apolipophorin III from Hyphantria cunea shows different anti-oxidant ability against LDL oxidation in the lipid-free and lipid-bound state. Comp. Biochem. Physiol. B 2008, 151:433-439.
    • (2008) Comp. Biochem. Physiol. B , vol.151 , pp. 433-439
    • Seo, S.J.1    Park, K.H.2    Cho, K.H.3
  • 180
    • 0035085155 scopus 로고    scopus 로고
    • Very-low-density lipoprotein assembly and secretion
    • Shelness G.S., Sellers J.A. Very-low-density lipoprotein assembly and secretion. Curr. Opin. Lipidol. 2001, 12:151-157.
    • (2001) Curr. Opin. Lipidol. , vol.12 , pp. 151-157
    • Shelness, G.S.1    Sellers, J.A.2
  • 181
    • 0025805452 scopus 로고
    • Lipid transfer particle catalyzed transfer of lipoprotein-associated diacylglycerol and long chain aliphatic hydrocarbons
    • Singh T.K.A., Ryan R.O. Lipid transfer particle catalyzed transfer of lipoprotein-associated diacylglycerol and long chain aliphatic hydrocarbons. Arch. Biochem. Biophys. 1991, 286:376-382.
    • (1991) Arch. Biochem. Biophys. , vol.286 , pp. 376-382
    • Singh, T.K.A.1    Ryan, R.O.2
  • 182
    • 0026803139 scopus 로고
    • Conversion of human low density lipoprotein into a very low density lipoprotein like particle in vitro
    • Singh T.K.A., Scraba D.G., Ryan R.O. Conversion of human low density lipoprotein into a very low density lipoprotein like particle in vitro. J. Biol. Chem. 1992, 267:9275-9280.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9275-9280
    • Singh, T.K.A.1    Scraba, D.G.2    Ryan, R.O.3
  • 183
    • 0028138564 scopus 로고
    • Exchangeable apolipoproteins of insects share a common structural motif
    • Smith A.F., Owen L.M., Strobel L.M., Chen H., Kanost M.R., et al. Exchangeable apolipoproteins of insects share a common structural motif. J. Lipid Res. 1994, 35:1976-1984.
    • (1994) J. Lipid Res. , vol.35 , pp. 1976-1984
    • Smith, A.F.1    Owen, L.M.2    Strobel, L.M.3    Chen, H.4    Kanost, M.R.5
  • 184
    • 17144375387 scopus 로고    scopus 로고
    • Biosynthesis and secretion of insect lipoprotein: Involvement of furin in cleavage of the apoB homolog, apolipophorin-II/I
    • Smolenaars M.M.W., Kasperaitis M.A.M., Richardson P.E., Rodenburg K.W., Van der Horst D.J. Biosynthesis and secretion of insect lipoprotein: Involvement of furin in cleavage of the apoB homolog, apolipophorin-II/I. J. Lipid Res. 2005, 46:412-421.
    • (2005) J. Lipid Res. , vol.46 , pp. 412-421
    • Smolenaars, M.M.W.1    Kasperaitis, M.A.M.2    Richardson, P.E.3    Rodenburg, K.W.4    Van der Horst, D.J.5
  • 185
    • 33947190010 scopus 로고    scopus 로고
    • Molecular diversity and evolution of the large lipid transfer protein superfamily
    • Smolenaars M.M.W., Madsen O., Rodenburg K.W., Van der Horst D.J. Molecular diversity and evolution of the large lipid transfer protein superfamily. J. Lipid Res. 2007, 48:489-502.
    • (2007) J. Lipid Res. , vol.48 , pp. 489-502
    • Smolenaars, M.M.W.1    Madsen, O.2    Rodenburg, K.W.3    Van der Horst, D.J.4
  • 186
    • 34548399017 scopus 로고    scopus 로고
    • Insect lipoprotein biogenesis depends on an amphipathic β cluster in apolipophorin-II/I and is stimulated by microsomal triglyceride transfer protein
    • Smolenaars M.M.W., De Morrée A., Kerver J., Van der Horst D.J., Rodenburg K.W. Insect lipoprotein biogenesis depends on an amphipathic β cluster in apolipophorin-II/I and is stimulated by microsomal triglyceride transfer protein. J. Lipid Res. 2007, 48:1955-1965.
    • (2007) J. Lipid Res. , vol.48 , pp. 1955-1965
    • Smolenaars, M.M.W.1    De Morrée, A.2    Kerver, J.3    Van der Horst, D.J.4    Rodenburg, K.W.5
  • 187
    • 0034625447 scopus 로고    scopus 로고
    • Dynamics and hydration of the α-helices of apolipophorin III
    • Soulages J.L., Arrese E.L. Dynamics and hydration of the α-helices of apolipophorin III. J. Biol. Chem. 2000, 275:17501-17509.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17501-17509
    • Soulages, J.L.1    Arrese, E.L.2
  • 188
    • 0034730078 scopus 로고    scopus 로고
    • Fluorescence spectroscopy of single tryptophan mutants of apolipophorin-III in discoidal lipoproteins of dymyristoylphosphatidylcholine
    • Soulages J.L., Arrese E.L. Fluorescence spectroscopy of single tryptophan mutants of apolipophorin-III in discoidal lipoproteins of dymyristoylphosphatidylcholine. Biochemistry 2000, 39:10574-10580.
    • (2000) Biochemistry , vol.39 , pp. 10574-10580
    • Soulages, J.L.1    Arrese, E.L.2
  • 189
    • 0035960643 scopus 로고    scopus 로고
    • Interaction of the α-helices of apolipophorin III with phospholipid acyl chains in discoidal lipoprotein particle: a fluorescence quenching study
    • Soulages J.L., Arrese E.L. Interaction of the α-helices of apolipophorin III with phospholipid acyl chains in discoidal lipoprotein particle: a fluorescence quenching study. Biochemistry 2001, 40:14279-14290.
    • (2001) Biochemistry , vol.40 , pp. 14279-14290
    • Soulages, J.L.1    Arrese, E.L.2
  • 190
    • 0028216403 scopus 로고
    • Lipophorin: The structure of an insect lipoprotein and its role in lipid transport in insects
    • Soulages J.L., Wells M.A. Lipophorin: The structure of an insect lipoprotein and its role in lipid transport in insects. Adv. Protein Chem. 1994, 45:371-415.
    • (1994) Adv. Protein Chem. , vol.45 , pp. 371-415
    • Soulages, J.L.1    Wells, M.A.2
  • 191
    • 0028279012 scopus 로고
    • Effect of diacylglycerol content on some physicochemical properties of the insect lipoprotein, lipophorin: Correlation with the binding of apolipophorin-III
    • Soulages J.L., Wells M.A. Effect of diacylglycerol content on some physicochemical properties of the insect lipoprotein, lipophorin: Correlation with the binding of apolipophorin-III. Biochemistry 1994, 33:2356-2362.
    • (1994) Biochemistry , vol.33 , pp. 2356-2362
    • Soulages, J.L.1    Wells, M.A.2
  • 192
    • 0029048818 scopus 로고
    • Low concentrations of diacylglycerol promote the binding of apolipophorin III to a phospholipid bilayer: A surface plasmon resonance spectroscopy study
    • Soulages J.L., Salamon Z., Wells M.A., 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 1995, 92:5650-5654.
    • (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
  • 193
    • 0029874763 scopus 로고    scopus 로고
    • Role of diacylglycerol and apolipophorin-III in regulation of physicochemical properties of the lipophorin surface: Metabolic implications
    • Soulages J.L., Van Antwerpen R., Wells M.A. Role of diacylglycerol and apolipophorin-III in regulation of physicochemical properties of the lipophorin surface: Metabolic implications. Biochemistry 1996, 35:5191-5198.
    • (1996) Biochemistry , vol.35 , pp. 5191-5198
    • Soulages, J.L.1    Van Antwerpen, R.2    Wells, M.A.3
  • 194
    • 0032512547 scopus 로고    scopus 로고
    • Role of glycosylation in the lipid-binding activity of the exchangeable apolipoprotein, apolipophorin-III
    • Soulages J.L., Pennington J., Bendavid O., Wells M.A. Role of glycosylation in the lipid-binding activity of the exchangeable apolipoprotein, apolipophorin-III. Biochem. Biophys. Res. Commun 1998, 243:372-376.
    • (1998) Biochem. Biophys. Res. Commun , vol.243 , pp. 372-376
    • Soulages, J.L.1    Pennington, J.2    Bendavid, O.3    Wells, M.A.4
  • 195
    • 0035823624 scopus 로고    scopus 로고
    • Essential role of the conformational flexibility of helices 1 and 5 on the lipid binding activity of apolipophorin III
    • Soulages J.L., Arrese E.L., Chetty P.S., Rodriguez V. Essential role of the conformational flexibility of helices 1 and 5 on the lipid binding activity of apolipophorin III. J. Biol. Chem. 2001, 276:34162-34166.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34162-34166
    • Soulages, J.L.1    Arrese, E.L.2    Chetty, P.S.3    Rodriguez, V.4
  • 197
    • 66349121402 scopus 로고    scopus 로고
    • Structural and functional analysis of fatty acid-binding proteins
    • Storch J., McDermott L. Structural and functional analysis of fatty acid-binding proteins. J. Lipid Res 2009, 50(Suppl.):126-131.
    • (2009) J. Lipid Res , vol.50 , Issue.SUPPL. , pp. 126-131
    • Storch, J.1    McDermott, L.2
  • 198
    • 0028900812 scopus 로고
    • Apolipophorin III is dramatically up-regulated during the programmed cell death of insect skeletal muscle and neurons
    • Sun D., Ziegler R., Milligan C.E., Fahrbach S., Schwartz L.M. Apolipophorin III is dramatically up-regulated during the programmed cell death of insect skeletal muscle and neurons. J. Neurobiol. 1995, 26:119-129.
    • (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
  • 200
    • 0037477829 scopus 로고    scopus 로고
    • Perilipin A is essential for the translocation of hormone-sensitive lipase during lipolytic activation
    • Sztalryd C., Xu G., Dorward H., Tansey J.T., Contreras J.A., et al. Perilipin A is essential for the translocation of hormone-sensitive lipase during lipolytic activation. J. Cell Biol. 2003, 161:1093-1103.
    • (2003) J. Cell Biol. , vol.161 , pp. 1093-1103
    • Sztalryd, C.1    Xu, G.2    Dorward, H.3    Tansey, J.T.4    Contreras, J.A.5
  • 201
    • 0037200007 scopus 로고    scopus 로고
    • Isolation, characterization, and cDNA sequence of a carotenoid binding protein from the silk gland of Bombyx mori larvae
    • Tabunoki H., Sugiyama H., Tanaka Y., Fujii H., Banno Y., et al. Isolation, characterization, and cDNA sequence of a carotenoid binding protein from the silk gland of Bombyx mori larvae. J. Biol. Chem. 2002, 277:32133-32140.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32133-32140
    • Tabunoki, H.1    Sugiyama, H.2    Tanaka, Y.3    Fujii, H.4    Banno, Y.5
  • 202
    • 2942566457 scopus 로고    scopus 로고
    • A carotenoid-binding protein (CBP) plays a crucial role in cocoon pigmentation of silkworm (Bombyx mori) larvae
    • Tabunoki H., Higurashi S., Ninagi O., Fujii H., Banno Y., et al. A carotenoid-binding protein (CBP) plays a crucial role in cocoon pigmentation of silkworm (Bombyx mori) larvae. FEBS Lett. 2004, 567:175-178.
    • (2004) FEBS Lett. , vol.567 , pp. 175-178
    • Tabunoki, H.1    Higurashi, S.2    Ninagi, O.3    Fujii, H.4    Banno, Y.5
  • 203
    • 0027513958 scopus 로고
    • Lipid transfer particle in the hemolymph of the American cockroach: Evidence for its capacity to transfer hydrocarbons between lipophorin particles
    • Takeuchi N., Chino H. Lipid transfer particle in the hemolymph of the American cockroach: Evidence for its capacity to transfer hydrocarbons between lipophorin particles. J. Lipid Res. 1993, 34:543-551.
    • (1993) J. Lipid Res. , vol.34 , pp. 543-551
    • Takeuchi, N.1    Chino, H.2
  • 204
    • 0141672132 scopus 로고    scopus 로고
    • Drosophila Perilipin/ADRP homologue Lsd2 regulates lipid metabolism
    • Teixeira L., Rabouille C., Rorth P., Ephrussi A., Vanzo N.F. Drosophila Perilipin/ADRP homologue Lsd2 regulates lipid metabolism. Mech. Devel. 2003, 120:1071-1081.
    • (2003) Mech. Devel. , vol.120 , pp. 1071-1081
    • Teixeira, L.1    Rabouille, C.2    Rorth, P.3    Ephrussi, A.4    Vanzo, N.F.5
  • 205
    • 0037199420 scopus 로고    scopus 로고
    • Lipid-protein interactions in lipovitellin
    • Thompson J.R., Banaszak L.J. Lipid-protein interactions in lipovitellin. Biochemistry 2002, 41:9398-9409.
    • (2002) Biochemistry , vol.41 , pp. 9398-9409
    • Thompson, J.R.1    Banaszak, L.J.2
  • 206
    • 0031552063 scopus 로고    scopus 로고
    • Purification and properties of a lipid transfer particle from Bombyx mori: Comparison to the lipid transfer particle from Manduca sexta
    • Tsuchida K., Soulages J.L., Moribayashi A., Suzuki K., Maekawa H., et al. Purification and properties of a lipid transfer particle from Bombyx mori: Comparison to the lipid transfer particle from Manduca sexta. Biochim. Biophys. Acta 1997, 1337:57-65.
    • (1997) Biochim. Biophys. Acta , vol.1337 , pp. 57-65
    • Tsuchida, K.1    Soulages, J.L.2    Moribayashi, A.3    Suzuki, K.4    Maekawa, H.5
  • 207
    • 0032421849 scopus 로고    scopus 로고
    • Lipid transfer particle catalyzes transfer of carotenoids between lipophorins of Bombyx mori
    • Tsuchida K., Arai M., Tanaka Y., Ishihara R., Ryan R.O., et al. Lipid transfer particle catalyzes transfer of carotenoids between lipophorins of Bombyx mori. Insect Biochem. Mol. Biol. 1998, 28:927-934.
    • (1998) Insect Biochem. Mol. Biol. , vol.28 , pp. 927-934
    • Tsuchida, K.1    Arai, M.2    Tanaka, Y.3    Ishihara, R.4    Ryan, R.O.5
  • 208
    • 7244259056 scopus 로고    scopus 로고
    • The basis for colorless hemolymph and cocoons in the Y-gene recessive Bombyx mori mutants: A defect in the cellular uptake of carotenoids
    • Tsuchida K., Katagiri C., Tanaka Y., Tabunoki H., Sato R., et al. The basis for colorless hemolymph and cocoons in the Y-gene recessive Bombyx mori mutants: A defect in the cellular uptake of carotenoids. J. Insect Physiol. 2004, 50:975-983.
    • (2004) J. Insect Physiol. , vol.50 , pp. 975-983
    • Tsuchida, K.1    Katagiri, C.2    Tanaka, Y.3    Tabunoki, H.4    Sato, R.5
  • 209
    • 11144356032 scopus 로고    scopus 로고
    • Characterization of the carotenoid-binding protein of the Y-gene dominant mutants of Bombyx mori
    • Tsuchida K., Jouni Z.E., Gardetto J., Kobayashi Y., Tabunoki H., et al. Characterization of the carotenoid-binding protein of the Y-gene dominant mutants of Bombyx mori. J. Insect Physiol 2004, 50:363-372.
    • (2004) J. Insect Physiol , vol.50 , pp. 363-372
    • Tsuchida, K.1    Jouni, Z.E.2    Gardetto, J.3    Kobayashi, Y.4    Tabunoki, H.5
  • 210
    • 55749115780 scopus 로고    scopus 로고
    • Molecular characteristics of insect vitellogenins
    • Tufail M., Takeda M. Molecular characteristics of insect vitellogenins. J. Insect Physiol 2008, 54:1447-1458.
    • (2008) J. Insect Physiol , vol.54 , pp. 1447-1458
    • Tufail, M.1    Takeda, M.2
  • 211
    • 58149510104 scopus 로고    scopus 로고
    • Insect vitellogenin/lipophorin receptors: Molecular structures, role in oogenesis, and regulatory mechanisms
    • Tufail M., Takeda M. Insect vitellogenin/lipophorin receptors: Molecular structures, role in oogenesis, and regulatory mechanisms. J. Insect Physiol. 2009, 55:87-103.
    • (2009) J. Insect Physiol. , vol.55 , pp. 87-103
    • Tufail, M.1    Takeda, M.2
  • 212
    • 67249117244 scopus 로고    scopus 로고
    • Molecular cloning, characterization, expression pattern and cellular distribution of an ovarian lipophorin receptor in the cockroach, Leucophaea maderae
    • Tufail M., Elmogy M., Ali Fouda M.M., Elgendy A.M., Bembenek J., et al. Molecular cloning, characterization, expression pattern and cellular distribution of an ovarian lipophorin receptor in the cockroach, Leucophaea maderae. Insect Mol. Biol. 2009, 18:281-294.
    • (2009) Insect Mol. Biol. , vol.18 , pp. 281-294
    • Tufail, M.1    Elmogy, M.2    Ali Fouda, M.M.3    Elgendy, A.M.4    Bembenek, J.5
  • 214
    • 0035464770 scopus 로고    scopus 로고
    • Insect G protein-coupled receptors and signal transduction
    • Vanden Broeck J. Insect G protein-coupled receptors and signal transduction. Arch. Insect Biochem. Physiol. 2001, 48:1-12.
    • (2001) Arch. Insect Biochem. Physiol. , vol.48 , pp. 1-12
    • Vanden Broeck, J.1
  • 215
    • 0025201274 scopus 로고
    • Lipid transport function of lipoproteins in flying insects
    • Van der Horst D.J. Lipid transport function of lipoproteins in flying insects. Biochim. Biophys. Acta 1990, 1047:195-211.
    • (1990) Biochim. Biophys. Acta , vol.1047 , pp. 195-211
    • Van der Horst, D.J.1
  • 216
    • 1542398216 scopus 로고    scopus 로고
    • Insect adipokinetic hormones: Release and integration of flight energy metabolism
    • Van der Horst D.J. Insect adipokinetic hormones: Release and integration of flight energy metabolism. Comp. Biochem. Physiol. B 2003, 136:217-226.
    • (2003) Comp. Biochem. Physiol. B , vol.136 , pp. 217-226
    • Van der Horst, D.J.1
  • 217
    • 84882524568 scopus 로고    scopus 로고
    • Adipokinetic hormones and lipid mobilization
    • Academic Press, London, UK, H.L. Henry, A.W. Norman (Eds.)
    • Van der Horst D.J., Oudejans R.C.H.M. Adipokinetic hormones and lipid mobilization. Encyclopedia of Hormones 2003, Vol. 1:34-38. Academic Press, London, UK. H.L. Henry, A.W. Norman (Eds.).
    • (2003) Encyclopedia of Hormones , vol.1 , pp. 34-38
    • Van der Horst, D.J.1    Oudejans, R.C.H.M.2
  • 218
    • 80053133520 scopus 로고    scopus 로고
    • Lipoprotein assembly and function in an evolutionary perspective
    • Van der Horst D.J., Rodenburg K.W. Lipoprotein assembly and function in an evolutionary perspective. BioMol. Concepts 2010, 1,:165-183.
    • (2010) BioMol. Concepts , pp. 165-183
    • Van der Horst, D.J.1    Rodenburg, K.W.2
  • 219
    • 77954309787 scopus 로고    scopus 로고
    • Locust flight activity as a model for hormonal regulation of lipid mobilization and transport
    • Van der Horst D.J., Rodenburg K.W. Locust flight activity as a model for hormonal regulation of lipid mobilization and transport. J. Insect Physiol. 2010, 56:844-853.
    • (2010) J. Insect Physiol. , vol.56 , pp. 844-853
    • Van der Horst, D.J.1    Rodenburg, K.W.2
  • 221
    • 85069918436 scopus 로고    scopus 로고
    • Lipid transport
    • Elsevier, Amsterdam, L.I. Gilbert, K. Iatrou, S.S. Gill (Eds.)
    • Van der Horst D.J., Ryan R.O. Lipid transport. Comprehensive Molecular Insect Science 2005, Vol. 4:225-246. Elsevier, Amsterdam. L.I. Gilbert, K. Iatrou, S.S. Gill (Eds.).
    • (2005) Comprehensive Molecular Insect Science , vol.4 , pp. 225-246
    • Van der Horst, D.J.1    Ryan, R.O.2
  • 222
    • 0001471365 scopus 로고
    • Effects of the adipokinetic hormone on the release and turnover of hemolymph diglycerides and on the function of the diglyceride-transporting lipoprotein system during locust flight
    • Van der Horst D.J., Van Doorn J.M., Beenakkers A.M.T. Effects of the adipokinetic hormone on the release and turnover of hemolymph diglycerides and on the function of the diglyceride-transporting lipoprotein system during locust flight. Insect Biochem. 1979, 9:627-635.
    • (1979) Insect Biochem. , vol.9 , pp. 627-635
    • Van der Horst, D.J.1    Van Doorn, J.M.2    Beenakkers, A.M.T.3
  • 223
    • 0000243374 scopus 로고
    • Interconversions of diacylglycerol-transporting lipoproteins in the haemolymph of Locusta migratoria
    • Van der Horst D.J., Van Doorn J.M., De Keijzer A.N., Beenakkers A.M.T. Interconversions of diacylglycerol-transporting lipoproteins in the haemolymph of Locusta migratoria. Insect Biochem. 1981, 11:717-723.
    • (1981) Insect Biochem. , vol.11 , pp. 717-723
    • Van der Horst, D.J.1    Van Doorn, J.M.2    De Keijzer, A.N.3    Beenakkers, A.M.T.4
  • 226
    • 0033427493 scopus 로고    scopus 로고
    • Metabolic neurohormones: Release, signal transduction and physiological responses of adipokinetic hormones in insects
    • Van der Horst D.J., Van Marrewijk W.J.A., Vullings H.G.B., Diederen J.H.B. Metabolic neurohormones: Release, signal transduction and physiological responses of adipokinetic hormones in insects. Eur. J. Entomol. 1999, 96:299-308.
    • (1999) Eur. J. Entomol. , vol.96 , pp. 299-308
    • Van der Horst, D.J.1    Van Marrewijk, W.J.A.2    Vullings, H.G.B.3    Diederen, J.H.B.4
  • 227
    • 0034786469 scopus 로고    scopus 로고
    • Adipokinetic hormones of insect: Release, signal transduction, and responses
    • Van der Horst D.J., Van Marrewijk W.J.A., Diederen J.H.B. Adipokinetic hormones of insect: Release, signal transduction, and responses. Int. Rev. Cytol. 2001, 211:179-240.
    • (2001) Int. Rev. Cytol. , vol.211 , pp. 179-240
    • Van der Horst, D.J.1    Van Marrewijk, W.J.A.2    Diederen, J.H.B.3
  • 229
    • 67349275023 scopus 로고    scopus 로고
    • Circulatory lipid transport: Lipoprotein assembly and function from an evolutionary perspective
    • Van der Horst D.J., Roosendaal S.D., Rodenburg K.W. Circulatory lipid transport: Lipoprotein assembly and function from an evolutionary perspective. Mol. Cell. Biochem. 2009, 326:105-119.
    • (2009) Mol. Cell. Biochem. , vol.326 , pp. 105-119
    • Van der Horst, D.J.1    Roosendaal, S.D.2    Rodenburg, K.W.3
  • 230
    • 0024971523 scopus 로고
    • An insect lipid transfer particle promotes lipid loading from fat body to lipoprotein
    • Van Heusden M.C., Law J.H. An insect lipid transfer particle promotes lipid loading from fat body to lipoprotein. J. Biol. Chem. 1989, 264:17287-17292.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17287-17292
    • Van Heusden, M.C.1    Law, J.H.2
  • 232
    • 0036860547 scopus 로고    scopus 로고
    • Insect lipoprotein follows a transferrin-like recycling route that is mediated by the insect LDL receptor homologue
    • Van Hoof D., Rodenburg K.W., Van der Horst D.J. Insect lipoprotein follows a transferrin-like recycling route that is mediated by the insect LDL receptor homologue. J. Cell Sci. 2002, 115:4001-4012.
    • (2002) J. Cell Sci. , vol.115 , pp. 4001-4012
    • Van Hoof, D.1    Rodenburg, K.W.2    Van der Horst, D.J.3
  • 233
    • 0142042405 scopus 로고    scopus 로고
    • Lipophorin receptor-mediated lipoprotein endocytosis in insect fat body cells
    • Van Hoof D., Rodenburg K.W., Van der Horst D.J. Lipophorin receptor-mediated lipoprotein endocytosis in insect fat body cells. J. Lipid Res. 2003, 44:1431-1440.
    • (2003) J. Lipid Res. , vol.44 , pp. 1431-1440
    • Van Hoof, D.1    Rodenburg, K.W.2    Van der Horst, D.J.3
  • 234
    • 12544256444 scopus 로고    scopus 로고
    • Receptor-mediated endocytosis and intracellular trafficking of lipoproteins and transferrin in insect cells
    • Van Hoof D., Rodenburg K.W., Van der Horst D.J. Receptor-mediated endocytosis and intracellular trafficking of lipoproteins and transferrin in insect cells. Insect Biochem. Mol. Biol. 2005, 35:117-128.
    • (2005) Insect Biochem. Mol. Biol. , vol.35 , pp. 117-128
    • Van Hoof, D.1    Rodenburg, K.W.2    Van der Horst, D.J.3
  • 235
    • 17244383541 scopus 로고    scopus 로고
    • Intracellular fate of LDL receptor family members depends on the cooperation between their ligand-binding and EGF domains
    • Van Hoof D., Rodenburg K.W., Van der Horst D.J. Intracellular fate of LDL receptor family members depends on the cooperation between their ligand-binding and EGF domains. J. Cell Sci 2005, 118:1309-1320.
    • (2005) J. Cell Sci , vol.118 , pp. 1309-1320
    • Van Hoof, D.1    Rodenburg, K.W.2    Van der Horst, D.J.3
  • 236
    • 1542425941 scopus 로고    scopus 로고
    • Adipokinetic hormones and carbohydrate metabolism
    • Academic Press, London, UK, H.L. Henry, A.W. Norman (Eds.)
    • Van Marrewijk W.J.A. Adipokinetic hormones and carbohydrate metabolism. Encyclopedia of Hormones 2003, Vol. 1:29-34. Academic Press, London, UK. H.L. Henry, A.W. Norman (Eds.).
    • (2003) Encyclopedia of Hormones , vol.1 , pp. 29-34
    • Van Marrewijk, W.J.A.1
  • 237
    • 0002893363 scopus 로고    scopus 로고
    • Signal transduction of adipokinetic hormone
    • Cambridge University Press, Cambridge, UK, G.M. Coast, S.G. Webster (Eds.)
    • Van Marrewijk W.J.A., Van der Horst D.J. Signal transduction of adipokinetic hormone. Recent Advances in Arthropod Endocrinology 1998, 172-188. Cambridge University Press, Cambridge, UK. G.M. Coast, S.G. Webster (Eds.).
    • (1998) Recent Advances in Arthropod Endocrinology , pp. 172-188
    • Van Marrewijk, W.J.A.1    Van der Horst, D.J.2
  • 238
    • 68749110897 scopus 로고    scopus 로고
    • Apolipophorin III lysine modification: Effect on structure and lipid binding
    • Vasquez L.J., Abdullahi G.E., Wan C.P., Weers P.M.M. Apolipophorin III lysine modification: Effect on structure and lipid binding. Biochim. Biophys. Acta 2009, 1788:1901-1906.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1901-1906
    • Vasquez, L.J.1    Abdullahi, G.E.2    Wan, C.P.3    Weers, P.M.M.4
  • 242
    • 70450260450 scopus 로고    scopus 로고
    • Activation of hormone-sensitive lipase requires two steps, protein phosphorylation and binding to the PAT-1 domain of lipid droplet coat proteins
    • Wang H., Hu L., Dalen K., Dorward H., Marcinkiewicz A., et al. Activation of hormone-sensitive lipase requires two steps, protein phosphorylation and binding to the PAT-1 domain of lipid droplet coat proteins. J. Biol. Chem. 2009, 284:32116-32125.
    • (2009) J. Biol. Chem. , vol.284 , pp. 32116-32125
    • Wang, H.1    Hu, L.2    Dalen, K.3    Dorward, H.4    Marcinkiewicz, A.5
  • 243
    • 0026611612 scopus 로고
    • P-NMR study of the phospholipid moiety of lipophorin subspecies
    • Wang J., Liu H., Sykes B.D., Ryan R.O. P-NMR study of the phospholipid moiety of lipophorin subspecies. Biochemistry 1992, 31:8706-8712.
    • (1992) Biochemistry , vol.31 , pp. 8706-8712
    • Wang, J.1    Liu, H.2    Sykes, B.D.3    Ryan, R.O.4
  • 244
    • 0029071634 scopus 로고
    • Localization of two distinct microenvironments for the diacylglycerol component of lipophorin particles by 13C NMR
    • Wang J., Liu H., Sykes B.D., Ryan R.O. Localization of two distinct microenvironments for the diacylglycerol component of lipophorin particles by 13C NMR. Biochemistry 1995, 34:6755-6761.
    • (1995) Biochemistry , vol.34 , pp. 6755-6761
    • Wang, J.1    Liu, H.2    Sykes, B.D.3    Ryan, R.O.4
  • 245
    • 0000324098 scopus 로고    scopus 로고
    • Multidimensional NMR studies of an exchangeable apolipoprotein and its interaction with lipids
    • Wang J., Sahoo D., Schieve D., Gagne S., Sykes B.D., et al. Multidimensional NMR studies of an exchangeable apolipoprotein and its interaction with lipids. Tech. Protein Chem. 1997, 8:427-438.
    • (1997) Tech. Protein Chem. , vol.8 , pp. 427-438
    • Wang, J.1    Sahoo, D.2    Schieve, D.3    Gagne, S.4    Sykes, B.D.5
  • 246
    • 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 B.D., Ryan R.O. Insight into lipid surface recognition and reversible conformational adaptations of an exchangeable apolipoprotein by multidimensional heteronuclear NMR techniques. J. Biol. Chem. 1997, 272:17912-17920.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17912-17920
    • Wang, J.1    Gagne, S.2    Sykes, B.D.3    Ryan, R.O.4
  • 247
    • 0037022281 scopus 로고    scopus 로고
    • Structural basis for the conformational adaptability of apolipophorin III, a helix bundle exchangeable apolipoprotein
    • Wang J., Sykes B.D., Ryan R.O. Structural basis for the conformational adaptability of apolipophorin III, a helix bundle exchangeable apolipoprotein. Proc. Natl. Acad. Sci. USA 2002, 99:1188-1193.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1188-1193
    • Wang, J.1    Sykes, B.D.2    Ryan, R.O.3
  • 248
    • 34247530855 scopus 로고    scopus 로고
    • Dissection of the pathway required for generation of vitamin A and for Drosophila phototransduction
    • Wang T., Jiao Y., Montell C. Dissection of the pathway required for generation of vitamin A and for Drosophila phototransduction. J. Cell Biol. 2007, 177:305-316.
    • (2007) J. Cell Biol. , vol.177 , pp. 305-316
    • Wang, T.1    Jiao, Y.2    Montell, C.3
  • 249
    • 52449125276 scopus 로고    scopus 로고
    • Regulation and function of triacylglycerol lipases in cellular metabolism
    • Watt M.J., Steinberg G.R. Regulation and function of triacylglycerol lipases in cellular metabolism. Biochem. J. 2008, 414:313-325.
    • (2008) Biochem. J. , vol.414 , pp. 313-325
    • Watt, M.J.1    Steinberg, G.R.2
  • 250
    • 33645057448 scopus 로고    scopus 로고
    • Apolipophorin III: Role model apolipoprotein
    • Weers P.M.M., Ryan R.O. Apolipophorin III: Role model apolipoprotein. Insect Biochem. Mol. Biol. 2006, 36:231-240.
    • (2006) Insect Biochem. Mol. Biol. , vol.36 , pp. 231-240
    • Weers, P.M.M.1    Ryan, R.O.2
  • 251
    • 0027506080 scopus 로고
    • Biosynthesis of locust lipophorin: Apolipophorins I and II originate from a common precursor
    • Weers P.M.M., Van Marrewijk W.J.A., Beenakkers A.M.T., Van der Horst D.J. Biosynthesis of locust lipophorin: Apolipophorins I and II originate from a common precursor. J. Biol. Chem. 1993, 268:4300-4303.
    • (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
  • 252
    • 0028331057 scopus 로고
    • Factors affecting the stability and conformation of Locusta migratoria apolipophorin III
    • Weers P.M.M., Kay C.M., Oikawa K., Wientzek M., Van der Horst D.J., et al. Factors affecting the stability and conformation of Locusta migratoria apolipophorin III. Biochemistry 1994, 33:3617-3624.
    • (1994) Biochemistry , vol.33 , pp. 3617-3624
    • Weers, P.M.M.1    Kay, C.M.2    Oikawa, K.3    Wientzek, M.4    Van der Horst, D.J.5
  • 254
    • 0033618275 scopus 로고    scopus 로고
    • Interaction of an exchangeable apolipoprotein with phospholipid vesicles and lipoprotein particles: Role of leucines 32, 34, and 95 in Locusta migratoria apolipophorin III
    • Weers P.M.M., Narayanaswami V., Kay C.M., Ryan R.O. Interaction of an exchangeable apolipoprotein with phospholipid vesicles and lipoprotein particles: Role of leucines 32, 34, and 95 in Locusta migratoria apolipophorin III. J. Biol. Chem 1999, 274:21804-21810.
    • (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
  • 255
    • 0034111173 scopus 로고    scopus 로고
    • Interaction of locust apolipophorin III with lipoproteins and phospholipid vesicles: Effect of glycosylation
    • Weers P.M.M., Van der Horst D.J., Ryan R.O. Interaction of locust apolipophorin III with lipoproteins and phospholipid vesicles: Effect of glycosylation. J. Lipid Res. 2000, 41:416-423.
    • (2000) J. Lipid Res. , vol.41 , pp. 416-423
    • Weers, P.M.M.1    Van der Horst, D.J.2    Ryan, R.O.3
  • 256
    • 20544455385 scopus 로고    scopus 로고
    • Role of buried polar residues in helix bundle stability and lipid binding of apolipophorin III: Destabilization by threonine 31
    • Weers P.M.M., Abdullahi W.E., Cabrera J.M., Hsu T.C. Role of buried polar residues in helix bundle stability and lipid binding of apolipophorin III: Destabilization by threonine 31. Biochemistry 2005, 44:8810-8816.
    • (2005) Biochemistry , vol.44 , pp. 8810-8816
    • Weers, P.M.M.1    Abdullahi, W.E.2    Cabrera, J.M.3    Hsu, T.C.4
  • 257
    • 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 M.M.A., Tew I.F., Lee B.L., Ratcliffe N.A. A novel role for an insect apolipoprotein (apolipophorin III) in β-1,3-glucan pattern recognition and cellular encapsulation reactions. J. Immunol. 2004, 172:2177-2185.
    • (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
  • 258
    • 33645111244 scopus 로고    scopus 로고
    • Differential receptor activation by cockroach adipokinetic hormones produces differential effects on ion currents, neuronal activity, and locomotion
    • Wicher D., Agricola H.J., Söhler S., Gundel M., Heinemann S.H., et al. Differential receptor activation by cockroach adipokinetic hormones produces differential effects on ion currents, neuronal activity, and locomotion. J. Neurophysiol. 2006, 95:2314-2325.
    • (2006) J. Neurophysiol. , vol.95 , pp. 2314-2325
    • Wicher, D.1    Agricola, H.J.2    Söhler, S.3    Gundel, M.4    Heinemann, S.H.5
  • 259
    • 0028108646 scopus 로고
    • Binding of insect apolipophorin III to dimyristoylphosphatidylcholine vesicles: Evidence for a conformational change
    • Wientzek M., Kay C.M., Oikawa K., Ryan R.O. Binding of insect apolipophorin III to dimyristoylphosphatidylcholine vesicles: Evidence for a conformational change. J. Biol. Chem. 1994, 269:4605-4612.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4605-4612
    • Wientzek, M.1    Kay, C.M.2    Oikawa, K.3    Ryan, R.O.4
  • 260
    • 0030786580 scopus 로고    scopus 로고
    • Isolated apolipophorin III from Galleria mellonella stimulates the immune reactions of this insect
    • Wiesner A., Losen S., Kopacek P., Weise C., Gotz P. Isolated apolipophorin III from Galleria mellonella stimulates the immune reactions of this insect. J. Insect Physiol. 1997, 43:383-391.
    • (1997) J. Insect Physiol. , vol.43 , pp. 383-391
    • Wiesner, A.1    Losen, S.2    Kopacek, P.3    Weise, C.4    Gotz, P.5
  • 261
    • 0036850956 scopus 로고    scopus 로고
    • Sensitivity of larval and adult crickets (Gryllus bimaculatus) to adipokinetic hormone
    • Woodring J., Lorenz M.W., Hoffmann K.H. Sensitivity of larval and adult crickets (Gryllus bimaculatus) to adipokinetic hormone. Comp. Biochem. Physiol. A 2002, 133:637-644.
    • (2002) Comp. Biochem. Physiol. A , vol.133 , pp. 637-644
    • Woodring, J.1    Lorenz, M.W.2    Hoffmann, K.H.3
  • 262
    • 0034711306 scopus 로고    scopus 로고
    • High density lipoprotein phospholipid composition is a major determinant of the bi-directional flux and net movement of cellular free cholesterol mediated by scavenger receptor BI
    • Yancey P.G., de la Llera-Moya M., Swarnakar S., Monzo P., Klein S.M., et al. High density lipoprotein phospholipid composition is a major determinant of the bi-directional flux and net movement of cellular free cholesterol mediated by scavenger receptor BI. J. Biol. Chem. 2000, 275:36596-36604.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36596-36604
    • Yancey, P.G.1    de la Llera-Moya, M.2    Swarnakar, S.3    Monzo, P.4    Klein, S.M.5
  • 263
    • 0036714824 scopus 로고    scopus 로고
    • Characterization of cholesterol transport from midgut to fat body in Manduca sexta larvae
    • Yun H.K., Jouni Z.E., Wells M.A. Characterization of cholesterol transport from midgut to fat body in Manduca sexta larvae. Insect Biochem. Mol. Biol. 2002, 32:1151-1158.
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , pp. 1151-1158
    • Yun, H.K.1    Jouni, Z.E.2    Wells, M.A.3
  • 265
    • 67349157089 scopus 로고    scopus 로고
    • Molecular and functional characterization of adipokinetic hormone receptor and its peptide ligands in Bombyx mori
    • Zhu C., Huang H., Hua R., Li G., Yang D., et al. Molecular and functional characterization of adipokinetic hormone receptor and its peptide ligands in Bombyx mori. FEBS Lett. 2009, 583:1463-1468.
    • (2009) FEBS Lett. , vol.583 , pp. 1463-1468
    • Zhu, C.1    Huang, H.2    Hua, R.3    Li, G.4    Yang, D.5
  • 267


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