메뉴 건너뛰기




Volumn 10, Issue 10, 2010, Pages 1906-1916

Blood-feeding and immunogenic Aedes aegypti saliva proteins

Author keywords

Aedes; Animal proteomics; Blood meal; Dengue; Midgut; Salivary glands

Indexed keywords

ACTIN; SALIVA PROTEIN;

EID: 77952375771     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200900626     Document Type: Article
Times cited : (58)

References (58)
  • 1
    • 33845737412 scopus 로고    scopus 로고
    • Double infection of heteroserotypes of dengue viruses in field populations of Aedes aegypti and Aedes albopictus (Diptera: Culicidae) and serological features of dengue viruses found in patients in southern Thailand
    • Thavara, U., Siriyasatien, P., Tawatsin, A., Asavadachanukorn, P. et al., Double infection of heteroserotypes of dengue viruses in field populations of Aedes aegypti and Aedes albopictus (Diptera: Culicidae) and serological features of dengue viruses found in patients in southern Thailand. Southeast Asian J. Trop. Med. Public Health 2006, 37, 468-476.
    • (2006) Southeast Asian J. Trop. Med. Public Health , vol.37 , pp. 468-476
    • Thavara, U.1    Siriyasatien, P.2    Tawatsin, A.3    Asavadachanukorn, P.4
  • 2
    • 0026449642 scopus 로고
    • Accumulation of yolk proteins in insect oocytes
    • Raikhel, A. S., Dhadialla, T. S., Accumulation of yolk proteins in insect oocytes. Annu. Rev. Entomol. 1992, 37, 217-251.
    • (1992) Annu. Rev. Entomol. , vol.37 , pp. 217-251
    • Raikhel, A.S.1    Dhadialla, T.S.2
  • 3
    • 61449132473 scopus 로고    scopus 로고
    • Dengue virus type 2 infections of Aedes aegypti are modulated by the mosquito's RNA interference pathway
    • Sánchez-Vargas, I., Scott, J. C., Poole-Smith, B. K., Franz, A. W. et al., Dengue virus type 2 infections of Aedes aegypti are modulated by the mosquito's RNA interference pathway. PLoS Pathog. 2009, 5, e1000299.
    • (2009) PLoS Pathog. , vol.5
    • Sánchez-Vargas, I.1    Scott, J.C.2    Poole-Smith, B.K.3    Franz, A.W.4
  • 5
    • 62349138444 scopus 로고    scopus 로고
    • Proteomic identification of Bacillus thuringiensis subsp. israelensis toxin Cry4Ba binding proteins in midgut membranes from Aedes (Stegomyia) aegypti Linnaeus (Diptera, Culicidae) larvae
    • Bayyareddy, K., Andacht, T. M., Abdullah, M. A., Adang, M. J., Proteomic identification of Bacillus thuringiensis subsp. israelensis toxin Cry4Ba binding proteins in midgut membranes from Aedes (Stegomyia) aegypti Linnaeus (Diptera, Culicidae) larvae. Insect Biochem Mol. Biol. 2009, 39, 279-286.
    • (2009) Insect Biochem Mol. Biol. , vol.39 , pp. 279-286
    • Bayyareddy, K.1    Andacht, T.M.2    Abdullah, M.A.3    Adang, M.J.4
  • 6
    • 59649089740 scopus 로고    scopus 로고
    • Proteomic analysis of the mosquito Aedes aegypti midgut brush border membrane vesicles
    • Popova-Butler, A., Dean, D. H., Proteomic analysis of the mosquito Aedes aegypti midgut brush border membrane vesicles. J. Insect Physiol. 2009, 55, 264-272.
    • (2009) J. Insect Physiol. , vol.55 , pp. 264-272
    • Popova-Butler, A.1    Dean, D.H.2
  • 7
    • 0037208861 scopus 로고    scopus 로고
    • Role of arthropod saliva in blood feeding: Sialome and post-sialome perspectives
    • Ribeiro, J. M., Francischetti, I. M., Role of arthropod saliva in blood feeding: Sialome and post-sialome perspectives. Annu. Rev. Entomol. 2003, 48, 73-88.
    • (2003) Annu. Rev. Entomol. , vol.48 , pp. 73-88
    • Ribeiro, J.M.1    Francischetti, I.M.2
  • 8
    • 0029090233 scopus 로고
    • Blood-feeding arthropods: Live syringes or invertebrate pharmacologists?
    • Ribeiro, J. M., Blood-feeding arthropods: Live syringes or invertebrate pharmacologists? Infect. Agents Dis. 1995, 4, 143-152.
    • (1995) Infect. Agents Dis. , vol.4 , pp. 143-152
    • Ribeiro, J.M.1
  • 9
    • 34948814739 scopus 로고    scopus 로고
    • The salivary glands and saliva of Anopheles gambiae as an essential step in the Plasmodium life cycle: A global proteomic study
    • DOI 10.1002/pmic.200700334
    • Choumet, V., Carmi-Leroy, A., Laurent, C., Lenormand, P. et al., The salivary glands and saliva of Anopheles gambiae as an essential step in the Plasmodium life cycle: a global proteomic study. Proteomics 2007, 7, 3384-3394. (Pubitemid 47517953)
    • (2007) Proteomics , vol.7 , Issue.18 , pp. 3384-3394
    • Choumet, V.1    Carmi-Leroy, A.2    Laurent, C.3    Lenormand, P.4    Rousselle, J.-C.5    Namane, A.6    Roth, C.7    Brey, P.T.8
  • 11
    • 29944443580 scopus 로고    scopus 로고
    • Blood-feeding arthropod salivary glands and saliva
    • Marquardt, W. C., Kondratieff, B. C., Black, W. C, IV., Moore, C. G., et al. (Eds.), Elsevier Academic Press, Amsterdam
    • Valenzuela, J. G., Blood-feeding arthropod salivary glands and saliva, in: Marquardt, W. C., Kondratieff, B. C., Black, W. C, IV., Moore, C. G., et al. (Eds.), Biology of Diseases Vectors, Elsevier Academic Press, Amsterdam 2005, pp. 377-385.
    • (2005) Biology of Diseases Vectors , pp. 377-385
    • Valenzuela, J.G.1
  • 12
  • 13
    • 34250375290 scopus 로고    scopus 로고
    • Malaria Plasmodium agent induces alteration in the head proteome of their Anopheles mosquito host
    • Lefevre, T., Thomas, F., Schwartz, A., Levashina, E. et al., Malaria Plasmodium agent induces alteration in the head proteome of their Anopheles mosquito host. Proteomics 2007, 7, 1908-1915.
    • (2007) Proteomics , vol.7 , pp. 1908-1915
    • Lefevre, T.1    Thomas, F.2    Schwartz, A.3    Levashina, E.4
  • 14
    • 0031557882 scopus 로고    scopus 로고
    • Cross-species protein identification using amino acid composition, peptide mass fingerprinting, isoelectric point and molecular mass: A theoretical evaluation
    • Wilkins, M. R., Williams, K. L., Cross-species protein identification using amino acid composition, peptide mass fingerprinting, isoelectric point and molecular mass: a theoretical evaluation. J. Theor. Biol. 1997, 186, 7-15.
    • (1997) J. Theor. Biol. , vol.186 , pp. 7-15
    • Wilkins, M.R.1    Williams, K.L.2
  • 15
    • 0033561091 scopus 로고    scopus 로고
    • A CD4-independent interaction of human immunodeficiency virus-1 gp120 with CXCR4 induces their cointernalization, cell signaling, and T-cell chemotaxis
    • Missé, D., Cerutti, M., Noraz, N., Jourdan, P. et al., A CD4-independent interaction of human immunodeficiency virus-1 gp120 with CXCR4 induces their cointernalization, cell signaling, and T-cell chemotaxis. Blood 1999, 93, 2454-2462.
    • (1999) Blood , vol.93 , pp. 2454-2462
    • Missé, D.1    Cerutti, M.2    Noraz, N.3    Jourdan, P.4
  • 17
    • 33846957116 scopus 로고    scopus 로고
    • An annotated catalogue of salivary gland transcripts in the adult female mosquito, des gypti
    • DOI 10.1186/1471-2164-8-6
    • Ribeiro, J. M., Arcá, B., Lombardo, F., Calvo, E. et al., An annotated catalogue of salivary gland transcripts in the adult female mosquito, Aedes aegypti. BMC Genomics 2007, 8, 6. (Pubitemid 46242720)
    • (2007) BMC Genomics , vol.8 , pp. 6
    • Ribeiro, J.M.C.1    Arca, B.2    Lombardo, F.3    Calvo, E.4    Phan, V.M.5    Chandra, P.K.6    Wikel, S.K.7
  • 18
    • 0028859094 scopus 로고
    • The salivary gland-specific apyrase of the mosquito Aedes aegypti is a member of the 5′-nucleotidase family
    • Champagne, D. E., Smartt, C. T., Ribeiro, J. M., James, A. A., The salivary gland-specific apyrase of the mosquito Aedes aegypti is a member of the 5′-nucleotidase family. Proc. Natl. Acad. Sci. USA 1995, 92, 694-698.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 694-698
    • Champagne, D.E.1    Smartt, C.T.2    Ribeiro, J.M.3    James, A.A.4
  • 19
    • 0035999904 scopus 로고    scopus 로고
    • Association of midgut defensin with a novel serine protease in the blood-sucking fly Stomoxys calcitrans
    • Hamilton, J. V., Munks, R. J., Lehane, S. M., Lehane, M. J., Association of midgut defensin with a novel serine protease in the blood-sucking fly Stomoxys calcitrans. Insect Mol. Biol. 2002, 11, 197-205.
    • (2002) Insect Mol. Biol. , vol.11 , pp. 197-205
    • Hamilton, J.V.1    Munks, R.J.2    Lehane, S.M.3    Lehane, M.J.4
  • 20
    • 33644872473 scopus 로고    scopus 로고
    • Function and evolution of a mosquito salivary protein family
    • DOI 10.1074/jbc.M510359200
    • Calvo, E., Mans, B. J., Andersen, J. F., Ribeiro, J. M., Function and evolution of a mosquito salivary protein family. J. Biol. Chem. 2006, 281, 1935-1942. (Pubitemid 43845779)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.4 , pp. 1935-1942
    • Calvo, E.1    Mans, B.J.2    Andersen, J.F.3    Ribeiro, J.M.C.4
  • 21
    • 10944245809 scopus 로고    scopus 로고
    • Profiling the proteome complement of the secretion from hypopharyngeal gland of Africanized nursehoneybees (Apis mellifera L.)
    • Santos, K. S., dos Santos, L. D., Mendes, M. A., de Souza, B. M. et al., Profiling the proteome complement of the secretion from hypopharyngeal gland of Africanized nursehoneybees (Apis mellifera L.). Insect Biochem. Mol. Biol. 2005, 35, 85-91.
    • (2005) Insect Biochem. Mol. Biol. , vol.35 , pp. 85-91
    • Santos, K.S.1    Dos Santos, L.D.2    Mendes, M.A.3    De Souza, B.M.4
  • 22
    • 37749035133 scopus 로고    scopus 로고
    • A worldwide polymorphism in aldehyde dehydrogenase in Drosophila melanogaster: Evidence for selection mediated by dietary ethanol
    • Fry, J. D., Donlon, K., Saweikis, M., A worldwide polymorphism in aldehyde dehydrogenase in Drosophila melanogaster: evidence for selection mediated by dietary ethanol. Evolution 2008, 62, 66-75.
    • (2008) Evolution , vol.62 , pp. 66-75
    • Fry, J.D.1    Donlon, K.2    Saweikis, M.3
  • 24
    • 0035746062 scopus 로고    scopus 로고
    • The salivary adenosine deaminase activity of the mosquitoes Culex quinquefasciatus and Aedes Aegypti
    • Ribeiro, J. M., Charlab, R., Valenzuela, J. G., The salivary adenosine deaminase activity of the mosquitoes Culex quinquefasciatus and Aedes aegypti. J. Exp. Biol. 2001, 204, 2001-2010. (Pubitemid 34869517)
    • (2001) Journal of Experimental Biology , vol.204 , Issue.11 , pp. 2001-2010
    • Ribeiro, J.M.C.1    Charlab, R.2    Valenzuela, J.G.3
  • 25
    • 0034650334 scopus 로고    scopus 로고
    • Inosine inhibits inflammatory cytokine production by a posttranscriptional mechanism and protects against endotoxin-induced shock
    • Haskó, G., Kuhel, D. G., Németh, Z. H., Mabley, J. G. et al., Inosine inhibits inflammatory cytokine production by a posttranscriptional mechanism and protects against endotoxin-induced shock. J. Immunol. 2000, 164, 1013-1019.
    • (2000) J. Immunol. , vol.164 , pp. 1013-1019
    • Haskó, G.1    Kuhel, D.G.2    Németh, Z.H.3    Mabley, J.G.4
  • 26
    • 26244432935 scopus 로고    scopus 로고
    • Control of the coagulation system by serpins. Getting by with a little help from glycosaminoglycans
    • Pike, R. N., Buckle, A. M., le Bonniec, B. F., Church, F. C., Control of the coagulation system by serpins. Getting by with a little help from glycosaminoglycans. FEBS J. 2005, 272, 4842-4851.
    • (2005) FEBS J. , vol.272 , pp. 4842-4851
    • Pike, R.N.1    Buckle, A.M.2    Le Bonniec, B.F.3    Church, F.C.4
  • 27
    • 17644379634 scopus 로고    scopus 로고
    • Identification of plasma proteases inhibited by Manduca sexta serpin-4 and serpin-5 and their association with components of the prophenol oxidase activation pathway
    • DOI 10.1074/jbc.M500532200
    • Tong, Y., Jiang, H., Kanost, M. R., Identification of plasma proteases inhibited by Manduca sexta serpin-4 and serpin-5 and their association with components of the prophenol oxidase activation pathway. J. Biol. Chem. 2005, 280, 14932-14942. (Pubitemid 40562844)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 14932-14942
    • Tong, Y.1    Jiang, H.2    Kanost, M.R.3
  • 28
    • 67349105011 scopus 로고    scopus 로고
    • The serpin gene family in Anopheles gambiae
    • Suwanchaichinda, C., Kanost, M. R., The serpin gene family in Anopheles gambiae. Gene 2009, 442, 47-54.
    • (2009) Gene , vol.442 , pp. 47-54
    • Suwanchaichinda, C.1    Kanost, M.R.2
  • 29
    • 33646950787 scopus 로고    scopus 로고
    • Expression of functional recombinant mosquito salivary apyrase: A potential therapeutic platelet aggregation inhibitor
    • DOI 10.1080/09537100500460234, PII J2940107728351
    • Sun, D., McNicol, A., James, A. A., Peng, Z., Expression of functional recombinant mosquito salivary apyrase: a potential therapeutic platelet aggregation inhibitor. Platelets 2006, 17, 178-184. (Pubitemid 43791630)
    • (2006) Platelets , vol.17 , Issue.3 , pp. 178-184
    • Sun, D.1    Mcnicol, A.2    James, A.A.3    Peng, Z.4
  • 30
    • 0029934620 scopus 로고    scopus 로고
    • Apyrase and alpha-glucosidase in the salivary glands of Aedes albopictus
    • Marinotti, O., de Brito, M., Moreira, C. K., Apyrase and alpha-glucosidase in the salivary glands of Aedes albopictus. Comp. Biochem. Physiol. B. 1996, 113, 675-679.
    • (1996) Comp. Biochem. Physiol. B. , vol.113 , pp. 675-679
    • Marinotti, O.1    De Brito, M.2    Moreira, C.K.3
  • 31
    • 0029559632 scopus 로고
    • The apyrase gene of the vector mosquito, Aedes aegypti, is expressed specifically in the adult female salivary glands
    • Smartt, C. T., Kim, A. P., Grossman, G. L., James, A. A., The apyrase gene of the vector mosquito, Aedes aegypti, is expressed specifically in the adult female salivary glands. Exp. Parasitol. 1995, 81, 239-248.
    • (1995) Exp. Parasitol. , vol.81 , pp. 239-248
    • Smartt, C.T.1    Kim, A.P.2    Grossman, G.L.3    James, A.A.4
  • 32
    • 0036671719 scopus 로고    scopus 로고
    • Toward a catalog for the transcripts and proteins (sialome) from the salivary gland of the malaria vector Anopheles gambiae
    • Francischetti, I. M., Valenzuela, J. G., Pham, V. M., Garfield, M. K., Ribeiro, J. M., Toward a catalog for the transcripts and proteins (sialome) from the salivary gland of the malaria vector Anopheles gambiae. J. Exp. Biol. 2002, 205, 2429-2451.
    • (2002) J. Exp. Biol. , vol.205 , pp. 2429-2451
    • Francischetti, I.M.1    Valenzuela, J.G.2    Pham, V.M.3    Garfield, M.K.4    Ribeiro, J.M.5
  • 34
    • 1542376710 scopus 로고    scopus 로고
    • Mosquito Allergy: Immune Mechanisms and Recombinant Salivary Allergens
    • DOI 10.1159/000076787
    • Peng, Z., Simons, F. E., Mosquito allergy: immune mechanisms and recombinant salivary allergens. Int. Arch. Allergy Immunol. 2004, 133, 198-209. (Pubitemid 38314652)
    • (2004) International Archives of Allergy and Immunology , vol.133 , Issue.2 , pp. 198-209
    • Peng, Z.1    Simons, F.E.R.2
  • 35
    • 0028933699 scopus 로고
    • Analysis of the paramyosin/miniparamyosin gene. Miniparamyosin is an independently transcribed, distinct paramyosin isoform, widely distributed in invertebrates
    • Maroto, M., Arredondo, J. J., San Román, M., Marco, R., Cervera, M., Analysis of the paramyosin/miniparamyosin gene. Miniparamyosin is an independently transcribed, distinct paramyosin isoform, widely distributed in invertebrates. J. Biol. Chem. 1995, 270, 4375-4382.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4375-4382
    • Maroto, M.1    Arredondo, J.J.2    San Román, M.3    Marco, R.4    Cervera, M.5
  • 36
    • 0035071665 scopus 로고    scopus 로고
    • Functional specificity of actin isoforms
    • Khaitlina, S. Y., Functional specificity of actin isoforms. Int. Rev. Cytol. 2001, 202, 35-98.
    • (2001) Int. Rev. Cytol. , vol.202 , pp. 35-98
    • Khaitlina, S.Y.1
  • 37
    • 2942532202 scopus 로고    scopus 로고
    • Functional characterization of a second porin isoform in Drosophila melanogaster: DmPorin2 forms voltage-independent cation-selective pores
    • DOI 10.1074/jbc.M310572200
    • Aiello, R., Messina, A., Schiffler, B., Benz, R. et al., Functional characterization of a second porin isoform in Drosophila melanogaster. DmPorin2 forms voltage-independent cation-selective pores. J. Biol. Chem. 2004, 279, 25364-25373. (Pubitemid 38756793)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.24 , pp. 25364-25373
    • Aiello, R.1    Messina, A.2    Schiffler, B.3    Benz, R.4    Tasco, G.5    Casadio, R.6    De Pinto, V.7
  • 39
    • 0034637123 scopus 로고    scopus 로고
    • Pyruvate cycling and implications for regulation of gluconeogenesis in the insect, Manduca sexta L
    • Thompson, S. N., Pyruvate cycling and implications for regulation of gluconeogenesis in the insect, Manduca sexta L. Biochem. Biophys. Res. Commun. 2000, 274, 787-793.
    • (2000) Biochem. Biophys. Res. Commun. , vol.274 , pp. 787-793
    • Thompson, S.N.1
  • 40
    • 67749094901 scopus 로고    scopus 로고
    • Identification and characterization of the mitochondrial targeting sequence and mechanism in human citrate synthase
    • Cheng, T. L., Liao, C. C., Tsai, W. H., Lin, C. C. et al., Identification and characterization of the mitochondrial targeting sequence and mechanism in human citrate synthase. J. Cell. Biochem. 2009, 107, 1002-1015.
    • (2009) J. Cell. Biochem. , vol.107 , pp. 1002-1015
    • Cheng, T.L.1    Liao, C.C.2    Tsai, W.H.3    Lin, C.C.4
  • 41
    • 34249824285 scopus 로고    scopus 로고
    • Unique aspects of lysine nutrition and metabolism
    • Benevenga, N. J., Blemings, K. P., Unique aspects of lysine nutrition and metabolism. J. Nutr. 2007, 137, 1610S-1615S.
    • (2007) J. Nutr. , vol.137
    • Benevenga, N.J.1    Blemings, K.P.2
  • 42
    • 33645236495 scopus 로고    scopus 로고
    • Lysine catabolism, an effective versatile regulator of lysine level in plants
    • Stepansky, A., Less, H., Angelovici, R., Aharon, R. et al., Lysine catabolism, an effective versatile regulator of lysine level in plants. Amino Acid 2006, 30, 121-125.
    • (2006) Amino Acid , vol.30 , pp. 121-125
    • Stepansky, A.1    Less, H.2    Angelovici, R.3    Aharon, R.4
  • 43
    • 0029040665 scopus 로고
    • Structure and mechanism of action of the acyl-CoA dehydrogenases
    • Thorpe, C., Kim, J. J., Structure and mechanism of action of the acyl-CoA dehydrogenases. FASEB J. 1995, 9, 718-725.
    • (1995) FASEB J. , vol.9 , pp. 718-725
    • Thorpe, C.1    Kim, J.J.2
  • 44
    • 57049106773 scopus 로고    scopus 로고
    • Supercomplex organization of the oxidative phosphorylation enzymes in yeast mitochondria
    • Stuart, R. A., Supercomplex organization of the oxidative phosphorylation enzymes in yeast mitochondria. J. Bioenerg. Biomembr. 2008, 40, 411-417.
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 411-417
    • Stuart, R.A.1
  • 45
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., Engelbrecht, J., Brunak, S., von Heijne, G., Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 1997, 10, 1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 46
    • 77952332322 scopus 로고    scopus 로고
    • Salivary gland protein repertoire from Aedes aegypti mosquitoes
    • online ahead of print
    • Almeras, L., Fontaine, A., Belghazi, M., Bourdon, S. et al., Salivary gland protein repertoire from Aedes aegypti mosquitoes. Vector Borne Zoonotic Dis. 2009, online ahead of print.
    • (2009) Vector Borne Zoonotic Dis.
    • Almeras, L.1    Fontaine, A.2    Belghazi, M.3    Bourdon, S.4
  • 47
    • 0030991367 scopus 로고    scopus 로고
    • Localization of proteins to the apico-lateral junctions of Drosophila epithelia
    • Woods, D. F., Wu, J. W., Bryant, P. J., Localization of proteins to the apico-lateral junctions of Drosophila epithelia. Dev. Genet. 1997, 20, 111-118.
    • (1997) Dev. Genet. , vol.20 , pp. 111-118
    • Woods, D.F.1    Wu, J.W.2    Bryant, P.J.3
  • 48
    • 0023818748 scopus 로고
    • Pathogenesis of dengue: Challenges to molecular biology
    • Halstead, S. B., Pathogenesis of dengue: challenges to molecular biology. Science 1988, 239, 476-481.
    • (1988) Science , vol.239 , pp. 476-481
    • Halstead, S.B.1
  • 49
    • 34248140776 scopus 로고    scopus 로고
    • HLA-A, -B, -C, and -DRB1 allele frequencies in Cuban individuals with antecedents of dengue 2 disease: Advantages of the Cuban population for HLA studies of dengue virus infection
    • Sierra, B., Alegre, R., Pérez, A. B., García, G. et al., HLA-A, -B, -C, and -DRB1 allele frequencies in Cuban individuals with antecedents of dengue 2 disease: advantages of the Cuban population for HLA studies of dengue virus infection. Hum. Immunol. 2007, 68, 531-540.
    • (2007) Hum. Immunol. , vol.68 , pp. 531-540
    • Sierra, B.1    Alegre, R.2    Pérez, A.B.3    García, G.4
  • 50
    • 0034101043 scopus 로고    scopus 로고
    • Modulation of dengue virus infection in human cells by alpha, beta, and gamma interferons
    • Diamond, M. S., Roberts, T. G., Edgil, D., Lu, B. et al., Modulation of dengue virus infection in human cells by alpha, beta, and gamma interferons. J. Virol. 2000, 74, 4957-4966.
    • (2000) J. Virol. , vol.74 , pp. 4957-4966
    • Diamond, M.S.1    Roberts, T.G.2    Edgil, D.3    Lu, B.4
  • 51
    • 0033970916 scopus 로고    scopus 로고
    • Dengue viremia titer, antibody response pattern, and virus serotype correlate with disease severity
    • Vaughn, D. W., Green, S., Kalayanarooj, S., Innis, B. L. et al., Dengue viremia titer, antibody response pattern, and virus serotype correlate with disease severity. J. Infect. Dis. 2000, 181, 2-9.
    • (2000) J. Infect. Dis. , vol.181 , pp. 2-9
    • Vaughn, D.W.1    Green, S.2    Kalayanarooj, S.3    Innis, B.L.4
  • 52
    • 0027405289 scopus 로고
    • Nutritional status of children with dengue hemorrhagic fever
    • Thisyakorn, U., Nimmannitya, S., Nutritional status of children with dengue hemorrhagic fever. Clin. Infect. Dis. 1993, 16, 295-297.
    • (1993) Clin. Infect. Dis. , vol.16 , pp. 295-297
    • Thisyakorn, U.1    Nimmannitya, S.2
  • 53
    • 31744436449 scopus 로고    scopus 로고
    • Evaluation of the antibody response to Anopheles salivary antigens as a potential marker of risk of malaria
    • Remoue, F., Cisse, B., Ba, F., Sokhna, C. et al., Evaluation of the antibody response to Anopheles salivary antigens as a potential marker of risk of malaria. Trans. R. Soc. Trop. Med. Hyg. 2006, 100, 363-370.
    • (2006) Trans. R. Soc. Trop. Med. Hyg. , vol.100 , pp. 363-370
    • Remoue, F.1    Cisse, B.2    Ba, F.3    Sokhna, C.4
  • 54
    • 49649127149 scopus 로고    scopus 로고
    • Novel peptide marker corresponding to salivary protein gSG6 potentially identifies exposure to Anopheles bites
    • Poinsignon, A., Cornelie, S., Mestres-Simon, M., Lanfrancotti, A., Novel peptide marker corresponding to salivary protein gSG6 potentially identifies exposure to Anopheles bites. PLoS One 2008, 3, e2472.
    • (2008) PLoS One , vol.3
    • Poinsignon, A.1    Cornelie, S.2    Mestres-Simon, M.3    Lanfrancotti, A.4
  • 55
    • 34047175959 scopus 로고    scopus 로고
    • Human/vector relationships during human African trypanosomiasis: Initial screening of immunogenic salivary proteins of Glossina species
    • Poinsignon, A., Cornelie, S., Remoue, F., Grébaut, P. et al., Human/vector relationships during human African trypanosomiasis: Initial screening of immunogenic salivary proteins of Glossina species. Am. J. Trop. Med. Hyg. 2007, 76, 327-333.
    • (2007) Am. J. Trop. Med. Hyg. , vol.76 , pp. 327-333
    • Poinsignon, A.1    Cornelie, S.2    Remoue, F.3    Grébaut, P.4
  • 56
    • 0035500911 scopus 로고    scopus 로고
    • Sandfly maxadilan exacerbates infection with Leishmania major and vaccinating against it protects against L. major infection
    • Morris, R. V., Shoemaker, C. B., David, J. R., Lanzaro, G. C., Titus, R. G., Sandfly maxadilan exacerbates infection with Leishmania major and vaccinating against it protects against L. major infection. Insect Biochem. Mol. Biol. 2001, 167, 5226-5230.
    • (2001) Insect Biochem. Mol. Biol. , vol.167 , pp. 5226-5230
    • Morris, R.V.1    Shoemaker, C.B.2    David, J.R.3    Lanzaro, G.C.4    Titus, R.G.5
  • 57
    • 0035817332 scopus 로고    scopus 로고
    • Toward a defined anti-Leishmania vaccine targeting vector antigens. Characterization of a protective salivary protein
    • Valenzuela, J. G., Belkaid, Y., Garfield, M. K., Mendez, S. et al., Toward a defined anti-Leishmania vaccine targeting vector antigens. Characterization of a protective salivary protein. J. Exp. Med. 2001, 194, 331-342.
    • (2001) J. Exp. Med. , vol.194 , pp. 331-342
    • Valenzuela, J.G.1    Belkaid, Y.2    Garfield, M.K.3    Mendez, S.4
  • 58
    • 0036208433 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis in proteomics: Old, old fashioned, but it still climbs up the mountains
    • DOI 10.1002/1615-9861(200201)2:1<3::AID-PROT3>3.0.CO;2-R
    • Rabilloud, T., Two-dimensional gel electrophoresis in proteomics: old, old fashioned, but it still climbs up the mountains. Proteomics 2002, 2, 3-10. (Pubitemid 34273093)
    • (2002) Proteomics , vol.2 , Issue.1 , pp. 3-10
    • Rabilloud, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.