메뉴 건너뛰기




Volumn 8, Issue 1, 2014, Pages 27-

An Insight into the Transcriptome of the Digestive Tract of the Bloodsucking Bug, Rhodnius prolixus

(46)  Ribeiro, José M C a   Genta, Fernando A b,c   Sorgine, Marcos H F b   Logullo, Raquel b   Mesquita, Rafael D b   Paiva Silva, Gabriela O b   Majerowicz, David b   Medeiros, Marcelo d   Koerich, Leonardo b   Terra, Walter R b,e   Ferreira, Clélia b,e   Pimentel, André C e   Bisch, Paulo M b   Leite, Daniel C b   Diniz, Michelle M P b   da Junior, João Lídio S G V b,f   Da Silva, Manuela L b,d   Araujo, Ricardo N b,g   Gandara, Ana Caroline P b   Brosson, Sébastien h   more..


Author keywords

[No Author keywords available]

Indexed keywords

TRANSCRIPTOME; INSECT PROTEIN;

EID: 84893795577     PISSN: 19352727     EISSN: 19352735     Source Type: Journal    
DOI: 10.1371/journal.pntd.0002594     Document Type: Article
Times cited : (168)

References (235)
  • 2
    • 84857141774 scopus 로고    scopus 로고
    • Intestinal aspartate proteases TiCatD and TiCatD2 of the haematophagous bug Triatoma infestans (Reduviidae): sequence characterisation, expression pattern and characterisation of proteolytic activity
    • Balczun C, Siemanowski J, Pausch JK, Helling S, Marcus K, et al. (2012) Intestinal aspartate proteases TiCatD and TiCatD2 of the haematophagous bug Triatoma infestans (Reduviidae): sequence characterisation, expression pattern and characterisation of proteolytic activity. Insect Biochem Mol Biol 42: 240-250.
    • (2012) Insect Biochem Mol Biol , vol.42 , pp. 240-250
    • Balczun, C.1    Siemanowski, J.2    Pausch, J.K.3    Helling, S.4    Marcus, K.5
  • 3
    • 0346971251 scopus 로고    scopus 로고
    • WHO, (American trypanosomiasis) Fact sheet N°340
    • WHO (2013) Chagas disease (American trypanosomiasis) Fact sheet N°340.
    • (2013) Chagas disease
  • 4
    • 64449087641 scopus 로고    scopus 로고
    • Classification, evolution, and species groups within the Triatominae
    • Schofield CJ, Galvao C, (2009) Classification, evolution, and species groups within the Triatominae. Acta Trop 110: 88-100.
    • (2009) Acta Trop , vol.110 , pp. 88-100
    • Schofield, C.J.1    Galvao, C.2
  • 6
    • 0036127870 scopus 로고    scopus 로고
    • The biological activity of diuretic factors in Rhodnius prolixus
    • Te Brugge VA, Schooley DA, Orchard I, (2002) The biological activity of diuretic factors in Rhodnius prolixus. Peptides 23: 671-681.
    • (2002) Peptides , vol.23 , pp. 671-681
    • Te Brugge, V.A.1    Schooley, D.A.2    Orchard, I.3
  • 7
    • 0035378362 scopus 로고    scopus 로고
    • The origin and functions of the insect peritrophic membrane and peritrophic gel
    • Terra WR, (2001) The origin and functions of the insect peritrophic membrane and peritrophic gel. Arch Biochem Biophys 47: 47-61.
    • (2001) Arch Biochem Biophys , vol.47 , pp. 47-61
    • Terra, W.R.1
  • 8
    • 52149121136 scopus 로고    scopus 로고
    • Peritrophic membrane role in enhancing digestive efficiency. Theoretical and experimental models
    • Bolognesi R, Terra WR, Ferreira C, (2008) Peritrophic membrane role in enhancing digestive efficiency. Theoretical and experimental models. J Insect Physiol 54: 1413-1422.
    • (2008) J Insect Physiol , vol.54 , pp. 1413-1422
    • Bolognesi, R.1    Terra, W.R.2    Ferreira, C.3
  • 9
    • 0024199846 scopus 로고
    • Physiology and biochemistry of insect digestion: an evolutionary perspective
    • Terra WR, (1988) Physiology and biochemistry of insect digestion: an evolutionary perspective. Braz J Med Biol Res 21: 675-734.
    • (1988) Braz J Med Biol Res , vol.21 , pp. 675-734
    • Terra, W.R.1
  • 10
    • 0018651724 scopus 로고
    • An unusual cell-surface modification - Double plasma-membrane
    • Lane NJ, Harrison JB, (1979) An unusual cell-surface modification- Double plasma-membrane. J Cell Sci 39: 355-372.
    • (1979) J Cell Sci , vol.39 , pp. 355-372
    • Lane, N.J.1    Harrison, J.B.2
  • 11
    • 0022692097 scopus 로고
    • The surface extracellular coat of the midgut in Triatoma infestans. I. Mechanism of development
    • Gutierrez LS, Burgos MH, (1986) The surface extracellular coat of the midgut in Triatoma infestans. I. Mechanism of development. J Ultrastruct Mol Struct Res 95: 75-83.
    • (1986) J Ultrastruct Mol Struct Res , vol.95 , pp. 75-83
    • Gutierrez, L.S.1    Burgos, M.H.2
  • 12
    • 0001444148 scopus 로고
    • Digestive enzymes trapped between and associated with the double plasma-membranes of Rhodnius prolixus posterior midgut cells
    • Ferreira C, Ribeiro AF, Garcia ES, Terra WR, (1988) Digestive enzymes trapped between and associated with the double plasma-membranes of Rhodnius prolixus posterior midgut cells. Insect Biochem 18: 521-530.
    • (1988) Insect Biochem , vol.18 , pp. 521-530
    • Ferreira, C.1    Ribeiro, A.F.2    Garcia, E.S.3    Terra, W.R.4
  • 13
    • 0030267141 scopus 로고    scopus 로고
    • Enzyme markers and isolation of the microvillar and perimicrovillar membranes of Dysdercus peruvianus (Hemiptera: Pyrrhocoridae) midgut cells
    • Silva CP, Ribeiro AF, Terra WR, (1996) Enzyme markers and isolation of the microvillar and perimicrovillar membranes of Dysdercus peruvianus (Hemiptera: Pyrrhocoridae) midgut cells. Insect Biochem Mol Biol 26: 1011-1018.
    • (1996) Insect Biochem Mol Biol , vol.26 , pp. 1011-1018
    • Silva, C.P.1    Ribeiro, A.F.2    Terra, W.R.3
  • 14
    • 0013458966 scopus 로고
    • Symbiotic bacteria in a blood sucking insect, Rhodnius prolixus Stal
    • Wigglesworth VB, (1936) Symbiotic bacteria in a blood sucking insect, Rhodnius prolixus Stal. Parasitology 28: 284-289.
    • (1936) Parasitology , vol.28 , pp. 284-289
    • Wigglesworth, V.B.1
  • 15
    • 0014277651 scopus 로고
    • The use of artificial diets to determine some of the effects of Nocardia rhodnii on the development of Rhodnius prolixus
    • Lake P, Friend WG, (1968) The use of artificial diets to determine some of the effects of Nocardia rhodnii on the development of Rhodnius prolixus. J Insect Physiol 14: 543-562.
    • (1968) J Insect Physiol , vol.14 , pp. 543-562
    • Lake, P.1    Friend, W.G.2
  • 16
    • 0017305415 scopus 로고
    • Rhodnius prolixus and its symbiotic actinomycete: a microbiological, physiological and behavioral study
    • Hill P, Campbell JA, Petrie IA, (1976) Rhodnius prolixus and its symbiotic actinomycete: a microbiological, physiological and behavioral study. Proc R Soc London B 194: 501-525.
    • (1976) Proc R Soc London B , vol.194 , pp. 501-525
    • Hill, P.1    Campbell, J.A.2    Petrie, I.A.3
  • 17
    • 0001601577 scopus 로고
    • The role of the symbiotic bacteria in the nutrition of Rhodnius prolixus
    • Baines S, (1956) The role of the symbiotic bacteria in the nutrition of Rhodnius prolixus. J Exp Biol 33: 533-541.
    • (1956) J Exp Biol , vol.33 , pp. 533-541
    • Baines, S.1
  • 18
    • 0036462171 scopus 로고    scopus 로고
    • Development of symbionts in triatomine bugs and the effects of infections with trypanosomatids
    • Eichler S, Schaub GA, (2002) Development of symbionts in triatomine bugs and the effects of infections with trypanosomatids. Exp Parasitol 100: 17-27.
    • (2002) Exp Parasitol , vol.100 , pp. 17-27
    • Eichler, S.1    Schaub, G.A.2
  • 19
    • 77956883339 scopus 로고    scopus 로고
    • Interactions between intestinal compounds of triatomines and Trypanosoma cruzi
    • Garcia ES, Genta FA, de Azambuja P, Schaub GA, (2010) Interactions between intestinal compounds of triatomines and Trypanosoma cruzi. Trends Parasitol 26: 499-505.
    • (2010) Trends Parasitol , vol.26 , pp. 499-505
    • Garcia, E.S.1    Genta, F.A.2    de Azambuja, P.3    Schaub, G.A.4
  • 20
    • 0000971561 scopus 로고
    • Midgut glycosidases of Rhodnius prolixus
    • Ribeiro JMC, Pereira MEA, (1984) Midgut glycosidases of Rhodnius prolixus. Insect Biochem 14: 103-108.
    • (1984) Insect Biochem , vol.14 , pp. 103-108
    • Ribeiro, J.M.C.1    Pereira, M.E.A.2
  • 21
    • 34248587892 scopus 로고    scopus 로고
    • Lipid metabolism in Rhodnius prolixus (Hemiptera: Reduviidae): Role of a midgut triacylglycerol-lipase
    • Grillo LA, Majerowicz D, Gondim KC, (2007) Lipid metabolism in Rhodnius prolixus (Hemiptera: Reduviidae): Role of a midgut triacylglycerol-lipase. Insect Biochem Mol Biol 37: 579-588.
    • (2007) Insect Biochem Mol Biol , vol.37 , pp. 579-588
    • Grillo, L.A.1    Majerowicz, D.2    Gondim, K.C.3
  • 22
    • 0017427889 scopus 로고
    • Control of protease secretion in the intestine of fifth instar larvae of Rhodnius prolixus
    • Garcia ED, Garcia ML, (1977) Control of protease secretion in the intestine of fifth instar larvae of Rhodnius prolixus. J Insect Physiol 23: 247-251.
    • (1977) J Insect Physiol , vol.23 , pp. 247-251
    • Garcia, E.D.1    Garcia, M.L.2
  • 23
    • 0017820669 scopus 로고
    • Purification and characterization of a sulfhydryl-dependent protease from Rhodnius prolixus midgut
    • Garcia ES, Guimaraes JA, Prado JL, (1978) Purification and characterization of a sulfhydryl-dependent protease from Rhodnius prolixus midgut. Arch Biochem Biophys 188: 315-322.
    • (1978) Arch Biochem Biophys , vol.188 , pp. 315-322
    • Garcia, E.S.1    Guimaraes, J.A.2    Prado, J.L.3
  • 24
    • 0001624454 scopus 로고
    • Origin, distribution, properties and functions of the major Rhodnius prolixus midgut hydrolases
    • Terra WR, Ferreira C, Garcia ES, (1988) Origin, distribution, properties and functions of the major Rhodnius prolixus midgut hydrolases. Insect Biochemistry 18: 423-434.
    • (1988) Insect Biochemistry , vol.18 , pp. 423-434
    • Terra, W.R.1    Ferreira, C.2    Garcia, E.S.3
  • 25
    • 11044235318 scopus 로고    scopus 로고
    • Activity and sequence characterization of two cysteine proteases in the digestive tract of the reduviid bug Triatoma infestans
    • Kollien AH, Waniek PJ, Nisbet AJ, Billingsley PF, Schaub GA, (2004) Activity and sequence characterization of two cysteine proteases in the digestive tract of the reduviid bug Triatoma infestans. Insect Mol Biol 13: 569-579.
    • (2004) Insect Mol Biol , vol.13 , pp. 569-579
    • Kollien, A.H.1    Waniek, P.J.2    Nisbet, A.J.3    Billingsley, P.F.4    Schaub, G.A.5
  • 26
    • 0018791132 scopus 로고
    • Proteolytic enzymes in the Rhodnius prolixus midgut
    • Garcia ES, Guimaraes JA, (1979) Proteolytic enzymes in the Rhodnius prolixus midgut. Experientia 35: 305-306.
    • (1979) Experientia , vol.35 , pp. 305-306
    • Garcia, E.S.1    Guimaraes, J.A.2
  • 29
    • 0021136195 scopus 로고
    • Scanning electron microscopic studies of Trypanosoma cruzi in the rectum of its vector Triatoma infestans
    • Böker CA, Schaub GA, (1984) Scanning electron microscopic studies of Trypanosoma cruzi in the rectum of its vector Triatoma infestans. Z Parasitenkd 70: 459-469.
    • (1984) Z Parasitenkd , vol.70 , pp. 459-469
    • Böker, C.A.1    Schaub, G.A.2
  • 30
    • 83755185910 scopus 로고    scopus 로고
    • A deep insight into the sialotranscriptome of the Gulf Coast tick, Amblyomma maculatum
    • Karim S, Singh P, Ribeiro JM, (2011) A deep insight into the sialotranscriptome of the Gulf Coast tick, Amblyomma maculatum. PLoS ONE 6: e28525.
    • (2011) PLoS ONE , vol.6
    • Karim, S.1    Singh, P.2    Ribeiro, J.M.3
  • 32
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, et al. (2011) MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 28: 2731-2739.
    • (2011) Mol Biol Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5
  • 33
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M, (1996) Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem 68: 850-858.
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 35
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25: 3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5
  • 37
    • 0345552048 scopus 로고    scopus 로고
    • A peritrophin-like protein expressed in the embryonic tracheae of Drosophila melanogaster
    • Barry MK, Triplett AA, Christensen AC, (1999) A peritrophin-like protein expressed in the embryonic tracheae of Drosophila melanogaster. Insect Biochem Mol Biol 29: 319-327.
    • (1999) Insect Biochem Mol Biol , vol.29 , pp. 319-327
    • Barry, M.K.1    Triplett, A.A.2    Christensen, A.C.3
  • 38
    • 0242370068 scopus 로고    scopus 로고
    • Cloning and characterization of five cDNAs encoding peritrophin-A domains from the cat flea, Ctenocephalides felis
    • Gaines PJ, Walmsley SJ, Wisnewski N, (2003) Cloning and characterization of five cDNAs encoding peritrophin-A domains from the cat flea, Ctenocephalides felis. Insect Biochem Mol Biol 33: 1061-1073.
    • (2003) Insect Biochem Mol Biol , vol.33 , pp. 1061-1073
    • Gaines, P.J.1    Walmsley, S.J.2    Wisnewski, N.3
  • 39
    • 77950516324 scopus 로고    scopus 로고
    • Genes encoding proteins with peritrophin A-type chitin-binding domains in Tribolium castaneum are grouped into three distinct families based on phylogeny, expression and function
    • Jasrapuria S, Arakane Y, Osman G, Kramer KJ, Beeman RW, et al. (2010) Genes encoding proteins with peritrophin A-type chitin-binding domains in Tribolium castaneum are grouped into three distinct families based on phylogeny, expression and function. Insect Biochem Mol Biol 40: 214-227.
    • (2010) Insect Biochem Mol Biol , vol.40 , pp. 214-227
    • Jasrapuria, S.1    Arakane, Y.2    Osman, G.3    Kramer, K.J.4    Beeman, R.W.5
  • 40
    • 58549085625 scopus 로고    scopus 로고
    • The Aedes aegypti larval transcriptome: a comparative perspective with emphasis on trypsins and the domain structure of peritrophins
    • Venancio TM, Cristofoletti PT, Ferreira C, Verjovski-Almeida S, Terra WR, (2009) The Aedes aegypti larval transcriptome: a comparative perspective with emphasis on trypsins and the domain structure of peritrophins. Insect Mol Biol 18: 33-44.
    • (2009) Insect Mol Biol , vol.18 , pp. 33-44
    • Venancio, T.M.1    Cristofoletti, P.T.2    Ferreira, C.3    Verjovski-Almeida, S.4    Terra, W.R.5
  • 41
    • 33747090621 scopus 로고    scopus 로고
    • Identification of the Aedes aegypti peritrophic matrix protein AeIMUCI as a heme-binding protein
    • Devenport M, Alvarenga PH, Shao L, Fujioka H, Bianconi ML, et al. (2006) Identification of the Aedes aegypti peritrophic matrix protein AeIMUCI as a heme-binding protein. Biochemistry 45: 9540-9549.
    • (2006) Biochemistry , vol.45 , pp. 9540-9549
    • Devenport, M.1    Alvarenga, P.H.2    Shao, L.3    Fujioka, H.4    Bianconi, M.L.5
  • 42
    • 36048942112 scopus 로고    scopus 로고
    • Gel-forming mucins appeared early in metazoan evolution
    • Lang T, Hansson GC, Samuelsson T, (2007) Gel-forming mucins appeared early in metazoan evolution. Proc Natl Acad Sci U S A 104: 16209-16214.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 16209-16214
    • Lang, T.1    Hansson, G.C.2    Samuelsson, T.3
  • 43
    • 60549096559 scopus 로고    scopus 로고
    • New insights into peritrophic matrix synthesis, architecture, and function
    • Hegedus D, Erlandson M, Gillott C, Toprak U, (2009) New insights into peritrophic matrix synthesis, architecture, and function. Annu Rev Entomol 54: 285-302.
    • (2009) Annu Rev Entomol , vol.54 , pp. 285-302
    • Hegedus, D.1    Erlandson, M.2    Gillott, C.3    Toprak, U.4
  • 45
    • 33745865149 scopus 로고    scopus 로고
    • Purification, characterization, and cloning of a Spodoptera frugiperda Sf9 beta-N-acetylhexosaminidase that hydrolyzes terminal N-acetylglucosamine on the N-glycan core
    • Tomiya N, Narang S, Park J, Abdul-Rahman B, Choi O, et al. (2006) Purification, characterization, and cloning of a Spodoptera frugiperda Sf9 beta-N-acetylhexosaminidase that hydrolyzes terminal N-acetylglucosamine on the N-glycan core. J Biol Chem 281: 19545-19560.
    • (2006) J Biol Chem , vol.281 , pp. 19545-19560
    • Tomiya, N.1    Narang, S.2    Park, J.3    Abdul-Rahman, B.4    Choi, O.5
  • 46
    • 44349193870 scopus 로고    scopus 로고
    • Functional specialization among insect chitinase family genes revealed by RNA interference
    • Zhu Q, Arakane Y, Beeman RW, Kramer KJ, Muthukrishnan S, (2008) Functional specialization among insect chitinase family genes revealed by RNA interference. Proc Natl Acad Sci U S A 105: 6650-6655.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 6650-6655
    • Zhu, Q.1    Arakane, Y.2    Beeman, R.W.3    Kramer, K.J.4    Muthukrishnan, S.5
  • 47
    • 0017801227 scopus 로고
    • The action of lysozyme on partially deacetylated chitin
    • Amano K, Ito E, (1978) The action of lysozyme on partially deacetylated chitin. Eur J Biochem 85: 97-104.
    • (1978) Eur J Biochem , vol.85 , pp. 97-104
    • Amano, K.1    Ito, E.2
  • 48
    • 59849111960 scopus 로고    scopus 로고
    • Cloning, purification and comparative characterization of two digestive lysozymes from Musca domestica larvae
    • Cancado FC, Chimoy Effio P, Terra WR, Marana SR, (2008) Cloning, purification and comparative characterization of two digestive lysozymes from Musca domestica larvae. Braz J Med Biol Res 41: 969-977.
    • (2008) Braz J Med Biol Res , vol.41 , pp. 969-977
    • Cancado, F.C.1    Chimoy Effio, P.2    Terra, W.R.3    Marana, S.R.4
  • 49
    • 0032078495 scopus 로고    scopus 로고
    • Molecular adaptation of Drosophila melanogaster lysozymes to a digestive function
    • Regel R, Matioli SR, Terra WR, (1998) Molecular adaptation of Drosophila melanogaster lysozymes to a digestive function. Insect Biochem Mol Biol 28: 309-319.
    • (1998) Insect Biochem Mol Biol , vol.28 , pp. 309-319
    • Regel, R.1    Matioli, S.R.2    Terra, W.R.3
  • 50
    • 77449097393 scopus 로고    scopus 로고
    • Cellulolytic systems in insects
    • Watanabe H, Tokuda G, (2010) Cellulolytic systems in insects. Annu Rev Entomol 55: 609-632.
    • (2010) Annu Rev Entomol , vol.55 , pp. 609-632
    • Watanabe, H.1    Tokuda, G.2
  • 51
    • 1842637589 scopus 로고    scopus 로고
    • Occurrence of midgut perimicrovillar membranes in paraneopteran insect orders with comments on their function and evolutionary significance
    • Silva CP, Silva JR, Vasconcelos FF, Petretski MD, Damatta RA, et al. (2004) Occurrence of midgut perimicrovillar membranes in paraneopteran insect orders with comments on their function and evolutionary significance. Arthropod Struct Dev 33: 139-148.
    • (2004) Arthropod Struct Dev , vol.33 , pp. 139-148
    • Silva, C.P.1    Silva, J.R.2    Vasconcelos, F.F.3    Petretski, M.D.4    Damatta, R.A.5
  • 53
    • 85069944088 scopus 로고    scopus 로고
    • Biochemistry of digestion
    • In: Gilbert LI, Iatrou K, Gill SS, editors, Oxford: Elsevier
    • Terra WR, Ferreira C (2005) Biochemistry of digestion. In: Gilbert LI, Iatrou K, Gill SS, editors. Comprehensive Insect Molecular Science. Oxford: Elsevier. pp. 171-224.
    • (2005) Comprehensive Insect Molecular Science , pp. 171-224
    • Terra, W.R.1    Ferreira, C.2
  • 54
    • 0023726861 scopus 로고
    • Morphometric analysis of Rhodnius prolixus Stal (Hemiptera:Reduviidae) midgut cells during blood digestion
    • Billingsley PF, (1988) Morphometric analysis of Rhodnius prolixus Stal (Hemiptera:Reduviidae) midgut cells during blood digestion. Tissue Cell 20: 291-301.
    • (1988) Tissue Cell , vol.20 , pp. 291-301
    • Billingsley, P.F.1
  • 55
    • 70449642350 scopus 로고    scopus 로고
    • Sequence and function of lysosomal and digestive cathepsin D-like proteinases of Musca domestica midgut
    • Padilha MH, Pimentel AC, Ribeiro AF, Terra WR, (2009) Sequence and function of lysosomal and digestive cathepsin D-like proteinases of Musca domestica midgut. Insect Biochem Mol Biol 39: 782-791.
    • (2009) Insect Biochem Mol Biol , vol.39 , pp. 782-791
    • Padilha, M.H.1    Pimentel, A.C.2    Ribeiro, A.F.3    Terra, W.R.4
  • 56
    • 0034782251 scopus 로고    scopus 로고
    • Characterization of a cDNA encoding a cathepsin L-like protein of Rhodnius prolixus
    • Lopez-Ordonez T, Rodriguez MH, Hernandez-Hernandez FD, (2001) Characterization of a cDNA encoding a cathepsin L-like protein of Rhodnius prolixus. Insect Mol Biol 10: 505-511.
    • (2001) Insect Mol Biol , vol.10 , pp. 505-511
    • Lopez-Ordonez, T.1    Rodriguez, M.H.2    Hernandez-Hernandez, F.D.3
  • 57
    • 12044253640 scopus 로고
    • The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity
    • Musil D, Zucic D, Turk D, Engh RA, Mayr I, et al. (1991) The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity. Embo J 10: 2321-2330.
    • (1991) Embo J , vol.10 , pp. 2321-2330
    • Musil, D.1    Zucic, D.2    Turk, D.3    Engh, R.A.4    Mayr, I.5
  • 58
    • 0033384702 scopus 로고    scopus 로고
    • The human cathepsin F gene-a fusion product between an ancestral cathepsin and cystatin gene
    • Wex T, Wex H, Bromme D, (1999) The human cathepsin F gene-a fusion product between an ancestral cathepsin and cystatin gene. Biol Chem 380: 1439-1442.
    • (1999) Biol Chem , vol.380 , pp. 1439-1442
    • Wex, T.1    Wex, H.2    Bromme, D.3
  • 59
    • 0039642231 scopus 로고    scopus 로고
    • Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen
    • Nagler DK, Sulea T, Menard R, (1999) Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen. Biochem Biophys Res Commun 257: 313-318.
    • (1999) Biochem Biophys Res Commun , vol.257 , pp. 313-318
    • Nagler, D.K.1    Sulea, T.2    Menard, R.3
  • 60
    • 77951951376 scopus 로고    scopus 로고
    • A salivary serine protease of the haematophagous reduviid Panstrongylus megistus: sequence characterization, expression pattern and characterization of proteolytic activity
    • Meiser CK, Piechura H, Meyer HE, Warscheid B, Schaub GA, et al. (2010) A salivary serine protease of the haematophagous reduviid Panstrongylus megistus: sequence characterization, expression pattern and characterization of proteolytic activity. Insect Mol Biol 19: 409-421.
    • (2010) Insect Mol Biol , vol.19 , pp. 409-421
    • Meiser, C.K.1    Piechura, H.2    Meyer, H.E.3    Warscheid, B.4    Schaub, G.A.5
  • 61
    • 0035104602 scopus 로고    scopus 로고
    • Triapsin, an unusual activatable serine protease from the saliva of the hematophagous vector of Chagas' disease Triatoma infestans (Hemiptera: Reduviidae)
    • Amino R, Tanaka AS, Schenkman S, (2001) Triapsin, an unusual activatable serine protease from the saliva of the hematophagous vector of Chagas' disease Triatoma infestans (Hemiptera: Reduviidae). Insect Biochem Mol Biol 31: 465-472.
    • (2001) Insect Biochem Mol Biol , vol.31 , pp. 465-472
    • Amino, R.1    Tanaka, A.S.2    Schenkman, S.3
  • 62
    • 77954142550 scopus 로고    scopus 로고
    • Transporters involved in glucose and water absorption in the Dysdercus peruvianus (Hemiptera: Pyrrhocoridae) anterior midgut
    • Bifano TD, Alegria TG, Terra WR, (2010) Transporters involved in glucose and water absorption in the Dysdercus peruvianus (Hemiptera: Pyrrhocoridae) anterior midgut. Comp Biochem Physiol B Biochem Mol Biol 157: 1-9.
    • (2010) Comp Biochem Physiol B Biochem Mol Biol , vol.157 , pp. 1-9
    • Bifano, T.D.1    Alegria, T.G.2    Terra, W.R.3
  • 63
    • 0032946360 scopus 로고    scopus 로고
    • Vacuolar and plasma membrane proton-adenosinetriphosphatases
    • Nelson N, Harvey WR, (1999) Vacuolar and plasma membrane proton-adenosinetriphosphatases. Physiol Rev 79: 361-385.
    • (1999) Physiol Rev , vol.79 , pp. 361-385
    • Nelson, N.1    Harvey, W.R.2
  • 64
    • 0038474360 scopus 로고    scopus 로고
    • Dipetalogastin, a potent thrombin inhibitor from the blood-sucking insect. Dipetalogaster maximus cDNA cloning, expression and characterization
    • Mende K, Petoukhova O, Koulitchkova V, Schaub GA, Lange U, et al. (1999) Dipetalogastin, a potent thrombin inhibitor from the blood-sucking insect. Dipetalogaster maximus cDNA cloning, expression and characterization. Eur J Biochem 266: 583-590.
    • (1999) Eur J Biochem , vol.266 , pp. 583-590
    • Mende, K.1    Petoukhova, O.2    Koulitchkova, V.3    Schaub, G.A.4    Lange, U.5
  • 65
    • 0027172205 scopus 로고
    • A Kazal-type inhibitor with thrombin specificity from Rhodnius prolixus
    • Friedrich T, Kroger B, Bialojan S, Lemaire HG, Hoffken HW, et al. (1993) A Kazal-type inhibitor with thrombin specificity from Rhodnius prolixus. J Biol Chem 268: 16216-16222.
    • (1993) J Biol Chem , vol.268 , pp. 16216-16222
    • Friedrich, T.1    Kroger, B.2    Bialojan, S.3    Lemaire, H.G.4    Hoffken, H.W.5
  • 67
    • 33745949100 scopus 로고    scopus 로고
    • The full-length cDNA of anticoagulant protein infestin revealed a novel releasable Kazal domain, a neutrophil elastase inhibitor lacking anticoagulant activity
    • Lovato DV, Nicolau de Campos IT, Amino R, Tanaka AS, (2006) The full-length cDNA of anticoagulant protein infestin revealed a novel releasable Kazal domain, a neutrophil elastase inhibitor lacking anticoagulant activity. Biochimie 88: 673-681.
    • (2006) Biochimie , vol.88 , pp. 673-681
    • Lovato, D.V.1    Nicolau de Campos, I.T.2    Amino, R.3    Tanaka, A.S.4
  • 68
    • 8844236924 scopus 로고    scopus 로고
    • Identification and characterization of a novel factor XIIa inhibitor in the hematophagous insect, Triatoma infestans (Hemiptera: Reduviidae)
    • Campos IT, Tanaka-Azevedo AM, Tanaka AS, (2004) Identification and characterization of a novel factor XIIa inhibitor in the hematophagous insect, Triatoma infestans (Hemiptera: Reduviidae). FEBS Lett 577: 512-516.
    • (2004) FEBS Lett , vol.577 , pp. 512-516
    • Campos, I.T.1    Tanaka-Azevedo, A.M.2    Tanaka, A.S.3
  • 69
    • 0036712320 scopus 로고    scopus 로고
    • Infestin, a thrombin inhibitor presents in Triatoma infestans midgut, a Chagas' disease vector: Gene cloning, expression and characterization of the inhibitor
    • Campos IT, Amino R, Sampaio CA, Auerswald EA, Friedrich T, et al. (2002) Infestin, a thrombin inhibitor presents in Triatoma infestans midgut, a Chagas' disease vector: Gene cloning, expression and characterization of the inhibitor. Insect Biochem Mol Biol 32: 991-997.
    • (2002) Insect Biochem Mol Biol , vol.32 , pp. 991-997
    • Campos, I.T.1    Amino, R.2    Sampaio, C.A.3    Auerswald, E.A.4    Friedrich, T.5
  • 70
    • 0028784163 scopus 로고
    • Two heads are better than one: crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin
    • van de Locht ALD, Bauer MHR, Friedrich TKB, Hoffken W, Bode W, (1995) Two heads are better than one: crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin. EMBO J 14: 5149-5157.
    • (1995) EMBO J , vol.14 , pp. 5149-5157
    • van de Locht, A.L.D.1    Bauer, M.H.R.2    Friedrich, T.K.B.3    Hoffken, W.4    Bode, W.5
  • 71
    • 34548092050 scopus 로고    scopus 로고
    • Brasiliensin: A novel intestinal thrombin inhibitor from Triatoma brasiliensis (Hemiptera: Reduviidae) with an important role in blood intake
    • Araujo RN, Campos IT, Tanaka AS, Santos A, Gontijo NF, et al. (2007) Brasiliensin: A novel intestinal thrombin inhibitor from Triatoma brasiliensis (Hemiptera: Reduviidae) with an important role in blood intake. Int J Parasitol 37: 1351-1358.
    • (2007) Int J Parasitol , vol.37 , pp. 1351-1358
    • Araujo, R.N.1    Campos, I.T.2    Tanaka, A.S.3    Santos, A.4    Gontijo, N.F.5
  • 72
    • 32444450253 scopus 로고    scopus 로고
    • Vasotab, a vasoactive peptide from horse fly Hybomitra bimaculata (Diptera, Tabanidae) salivary glands
    • Takac P, Nunn MA, Meszaros J, Pechanova O, Vrbjar N, et al. (2006) Vasotab, a vasoactive peptide from horse fly Hybomitra bimaculata (Diptera, Tabanidae) salivary glands. J Exp Biol 209: 343-352.
    • (2006) J Exp Biol , vol.209 , pp. 343-352
    • Takac, P.1    Nunn, M.A.2    Meszaros, J.3    Pechanova, O.4    Vrbjar, N.5
  • 73
    • 21444452401 scopus 로고    scopus 로고
    • Structure-activity relationship within the serine protease inhibitors of the pacifastin family
    • Kellenberger C, Roussel A, (2005) Structure-activity relationship within the serine protease inhibitors of the pacifastin family. Protein Pept Lett 12: 409-414.
    • (2005) Protein Pept Lett , vol.12 , pp. 409-414
    • Kellenberger, C.1    Roussel, A.2
  • 74
    • 0346729741 scopus 로고    scopus 로고
    • Genomics, evolution and biological functions of the pacifastin peptide family: a conserved serine protease inhibitor family in arthropods
    • Simonet G, Claeys I, Franssens V, De Loof A, Broeck JV, (2003) Genomics, evolution and biological functions of the pacifastin peptide family: a conserved serine protease inhibitor family in arthropods. Peptides 24: 1633-1644.
    • (2003) Peptides , vol.24 , pp. 1633-1644
    • Simonet, G.1    Claeys, I.2    Franssens, V.3    De Loof, A.4    Broeck, J.V.5
  • 75
    • 77952544534 scopus 로고    scopus 로고
    • The first pacifastin elastase inhibitor characterized from a blood sucking animal
    • de Marco R, Lovato DV, Torquato RJ, Clara RO, Buarque DS, et al. (2010) The first pacifastin elastase inhibitor characterized from a blood sucking animal. Peptides 31: 1280-1286.
    • (2010) Peptides , vol.31 , pp. 1280-1286
    • de Marco, R.1    Lovato, D.V.2    Torquato, R.J.3    Clara, R.O.4    Buarque, D.S.5
  • 76
    • 0034684168 scopus 로고    scopus 로고
    • The lipocalin protein family: structural and sequence overview
    • Flower DR, North AC, Sansom CE, (2000) The lipocalin protein family: structural and sequence overview. Biochim Biophys Acta 1482: 9-24.
    • (2000) Biochim Biophys Acta , vol.1482 , pp. 9-24
    • Flower, D.R.1    North, A.C.2    Sansom, C.E.3
  • 79
    • 0030837756 scopus 로고    scopus 로고
    • Inhibition of thrombin-mediated cellular effects by triabin, a highly potent anion-binding exosite thrombin inhibitor
    • Glusa E, Bretschneider E, Daum J, Noeske-Jungblut C, (1997) Inhibition of thrombin-mediated cellular effects by triabin, a highly potent anion-binding exosite thrombin inhibitor. Thromb Haemost 77: 1196-1200.
    • (1997) Thromb Haemost , vol.77 , pp. 1196-1200
    • Glusa, E.1    Bretschneider, E.2    Daum, J.3    Noeske-Jungblut, C.4
  • 80
    • 0030666566 scopus 로고    scopus 로고
    • Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug
    • Fuentes-Prior P, Noeske-Jungblut C, Donner P, Schleuning WD, Huber R, et al. (1997) Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug. Proc Natl Acad Sci U S A 94: 11845-11850.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 11845-11850
    • Fuentes-Prior, P.1    Noeske-Jungblut, C.2    Donner, P.3    Schleuning, W.D.4    Huber, R.5
  • 81
    • 0028149038 scopus 로고
    • Structural analysis and classification of lipocalins and related proteins using a profile-search method
    • Sansom CE, North ACT, Sawyer L, (1994) Structural analysis and classification of lipocalins and related proteins using a profile-search method. Biochim Biophys Acta 1208: 247-255.
    • (1994) Biochim Biophys Acta , vol.1208 , pp. 247-255
    • Sansom, C.E.1    North, A.C.T.2    Sawyer, L.3
  • 82
    • 0028147872 scopus 로고
    • An inhibitor of collagen-induced platelet aggregation from the saliva of Triatoma pallidipennis
    • Noeske-Jungblut C, Krätzschmar J, Haendler B, Alagon A, Possani L, et al. (1994) An inhibitor of collagen-induced platelet aggregation from the saliva of Triatoma pallidipennis. J Biol Chem 269: 5050-5053.
    • (1994) J Biol Chem , vol.269 , pp. 5050-5053
    • Noeske-Jungblut, C.1    Krätzschmar, J.2    Haendler, B.3    Alagon, A.4    Possani, L.5
  • 83
    • 0028905848 scopus 로고
    • Expression of active recombinant pallidipin, a novel platelet aggregation inhibitor, in the periplasm of Escherichia coli
    • Haendler B, Becker A, C N-J, Krätzschmar J, Donner P, et al. (1995) Expression of active recombinant pallidipin, a novel platelet aggregation inhibitor, in the periplasm of Escherichia coli. Biochem J 307: 465-470.
    • (1995) Biochem J , vol.307 , pp. 465-470
    • Haendler, B.1    Becker, A.C.N.-J.2    Krätzschmar, J.3    Donner, P.4
  • 84
    • 0033815980 scopus 로고    scopus 로고
    • takeout, a novel Drosophila gene under circadian clock transcriptional regulation
    • So WV, Sarov-Blat L, Kotarski CK, McDonald MJ, Allada R, et al. (2000) takeout, a novel Drosophila gene under circadian clock transcriptional regulation. Mol Cell Biol 20: 6935-6944.
    • (2000) Mol Cell Biol , vol.20 , pp. 6935-6944
    • So, W.V.1    Sarov-Blat, L.2    Kotarski, C.K.3    McDonald, M.J.4    Allada, R.5
  • 85
    • 0031081053 scopus 로고    scopus 로고
    • Juvenile hormone controls early trypsin gene transcription in the midgut of Aedes aegypti
    • Noriega FG, Shah DK, Wells MA, (1997) Juvenile hormone controls early trypsin gene transcription in the midgut of Aedes aegypti. Insect Mol Biol 6: 63-66.
    • (1997) Insect Mol Biol , vol.6 , pp. 63-66
    • Noriega, F.G.1    Shah, D.K.2    Wells, M.A.3
  • 86
    • 38349035845 scopus 로고    scopus 로고
    • Characterization of a juvenile hormone-regulated chymotrypsin-like serine protease gene in Aedes aegypti mosquito
    • Bian G, Raikhel AS, Zhu J, (2008) Characterization of a juvenile hormone-regulated chymotrypsin-like serine protease gene in Aedes aegypti mosquito. Insect Biochem Mol Biol 38: 190-200.
    • (2008) Insect Biochem Mol Biol , vol.38 , pp. 190-200
    • Bian, G.1    Raikhel, A.S.2    Zhu, J.3
  • 87
    • 0026485561 scopus 로고
    • Purification and localization of p10, a novel protein that increases in nymphal regenerating legs of Periplaneta americana (American cockroach)
    • Nomura A, Kawasaki K, Kubo T, Natori S, (1992) Purification and localization of p10, a novel protein that increases in nymphal regenerating legs of Periplaneta americana (American cockroach). Int J Dev Biol 36: 391-398.
    • (1992) Int J Dev Biol , vol.36 , pp. 391-398
    • Nomura, A.1    Kawasaki, K.2    Kubo, T.3    Natori, S.4
  • 88
    • 34047268684 scopus 로고    scopus 로고
    • The host defense of Drosophila melanogaster
    • Lemaitre B, Hoffmann J, (2007) The host defense of Drosophila melanogaster. Annu Rev Immunol 25: 697-743.
    • (2007) Annu Rev Immunol , vol.25 , pp. 697-743
    • Lemaitre, B.1    Hoffmann, J.2
  • 89
    • 70349617469 scopus 로고    scopus 로고
    • Invasive and indigenous microbiota impact intestinal stem cell activity through multiple pathways in Drosophila
    • Buchon N, Broderick NA, Chakrabarti S, Lemaitre B, (2009) Invasive and indigenous microbiota impact intestinal stem cell activity through multiple pathways in Drosophila. Genes Dev 23: 2333-2344.
    • (2009) Genes Dev , vol.23 , pp. 2333-2344
    • Buchon, N.1    Broderick, N.A.2    Chakrabarti, S.3    Lemaitre, B.4
  • 90
    • 70049114176 scopus 로고    scopus 로고
    • Anopheles gambiae PGRPLC-mediated defense against bacteria modulates infections with malaria parasites
    • Meister S, Agianian B, Turlure F, Relogio A, Morlais I, et al. (2009) Anopheles gambiae PGRPLC-mediated defense against bacteria modulates infections with malaria parasites. Plos Pathogens 5: e1000542.
    • (2009) Plos Pathogens , vol.5
    • Meister, S.1    Agianian, B.2    Turlure, F.3    Relogio, A.4    Morlais, I.5
  • 91
    • 67249119415 scopus 로고    scopus 로고
    • Implication of the mosquito midgut microbiota in the defense against malaria parasites
    • Dong Y, Manfredini F, Dimopoulos G, (2009) Implication of the mosquito midgut microbiota in the defense against malaria parasites. PLoS Pathog 5: e1000423.
    • (2009) PLoS Pathog , vol.5
    • Dong, Y.1    Manfredini, F.2    Dimopoulos, G.3
  • 92
  • 93
    • 1642504737 scopus 로고    scopus 로고
    • Innate immune responses of a lepidopteran insect, Manduca sexta
    • Kanost MR, Jiang H, Yu XQ, (2004) Innate immune responses of a lepidopteran insect, Manduca sexta. Immunol Rev 198: 97-105.
    • (2004) Immunol Rev , vol.198 , pp. 97-105
    • Kanost, M.R.1    Jiang, H.2    Yu, X.Q.3
  • 94
    • 67650473295 scopus 로고    scopus 로고
    • Effect of intestinal erythrocyte agglutination on the feeding performance of Triatoma brasiliensis (Hemiptera: Reduviidae)
    • Araujo RN, Pereira MH, Soares AC, Pereira ID, Diotaiuti L, et al. (2009) Effect of intestinal erythrocyte agglutination on the feeding performance of Triatoma brasiliensis (Hemiptera: Reduviidae). J Insect Physiol 55: 862-868.
    • (2009) J Insect Physiol , vol.55 , pp. 862-868
    • Araujo, R.N.1    Pereira, M.H.2    Soares, A.C.3    Pereira, I.D.4    Diotaiuti, L.5
  • 95
    • 77149137065 scopus 로고    scopus 로고
    • A repertoire of the dominant transcripts from the salivary glands of the blood-sucking bug, Triatoma dimidiata, a vector of Chagas disease
    • Kato H, Jochim RC, Gomez EA, Sakoda R, Iwata H, et al. (2010) A repertoire of the dominant transcripts from the salivary glands of the blood-sucking bug, Triatoma dimidiata, a vector of Chagas disease. Infect Genet Evol 10: 184-191.
    • (2010) Infect Genet Evol , vol.10 , pp. 184-191
    • Kato, H.1    Jochim, R.C.2    Gomez, E.A.3    Sakoda, R.4    Iwata, H.5
  • 96
    • 0019363489 scopus 로고
    • Lectins of distinct specificity in Rhodnius prolixus interact selectively with Trypanosoma cruzi
    • Pereira ME, Andrade AF, Ribeiro JM, (1981) Lectins of distinct specificity in Rhodnius prolixus interact selectively with Trypanosoma cruzi. Science 211: 597-600.
    • (1981) Science , vol.211 , pp. 597-600
    • Pereira, M.E.1    Andrade, A.F.2    Ribeiro, J.M.3
  • 97
    • 0030176297 scopus 로고    scopus 로고
    • Trypanosoma cruzi and erythrocyte agglutinins: a comparative study of occurrence and properties in the gut and hemolymph of Rhodnius prolixus
    • Ratcliffe NA, Nigam Y, Mello CB, Garcia ES, Azambuja P, (1996) Trypanosoma cruzi and erythrocyte agglutinins: a comparative study of occurrence and properties in the gut and hemolymph of Rhodnius prolixus. Exp Parasitol 83: 83-93.
    • (1996) Exp Parasitol , vol.83 , pp. 83-93
    • Ratcliffe, N.A.1    Nigam, Y.2    Mello, C.B.3    Garcia, E.S.4    Azambuja, P.5
  • 98
    • 0029803741 scopus 로고    scopus 로고
    • Identification and characterization of differentially expressed cDNAs of the vector mosquito, Anopheles gambiae
    • Dimopoulos G, Richman A, dellaTorre A, Kafatos FC, Louis C, (1996) Identification and characterization of differentially expressed cDNAs of the vector mosquito, Anopheles gambiae. Proc Natl Acad Sci USA 93: 13066-13071.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13066-13071
    • Dimopoulos, G.1    Richman, A.2    dellaTorre, A.3    Kafatos, F.C.4    Louis, C.5
  • 99
    • 0032476592 scopus 로고    scopus 로고
    • Malaria infection of the mosquito Anopheles gambiae activates immune-responsive genes during critical transition stages of the parasite life cycle
    • Dimopoulos G, Seeley D, Wolf A, Kafatos FC, (1998) Malaria infection of the mosquito Anopheles gambiae activates immune-responsive genes during critical transition stages of the parasite life cycle. EMBO J 17: 6115-6123.
    • (1998) EMBO J , vol.17 , pp. 6115-6123
    • Dimopoulos, G.1    Seeley, D.2    Wolf, A.3    Kafatos, F.C.4
  • 102
    • 0035477868 scopus 로고    scopus 로고
    • A Drosophila haemocyte-specific protein, hemolectin, similar to human von Willebrand factor
    • Goto A, Kumagai T, Kumagai C, Hirose J, Narita H, et al. (2001) A Drosophila haemocyte-specific protein, hemolectin, similar to human von Willebrand factor. Biochem J 359: 99-108.
    • (2001) Biochem J , vol.359 , pp. 99-108
    • Goto, A.1    Kumagai, T.2    Kumagai, C.3    Hirose, J.4    Narita, H.5
  • 103
    • 0344925804 scopus 로고    scopus 로고
    • Drosophila hemolectin gene is expressed in embryonic and larval hemocytes and its knock down causes bleeding defects
    • Goto A, Kadowaki T, Kitagawa Y, (2003) Drosophila hemolectin gene is expressed in embryonic and larval hemocytes and its knock down causes bleeding defects. Dev Biol 264: 582-591.
    • (2003) Dev Biol , vol.264 , pp. 582-591
    • Goto, A.1    Kadowaki, T.2    Kitagawa, Y.3
  • 104
    • 35748967867 scopus 로고    scopus 로고
    • A role for Hemolectin in coagulation and immunity in Drosophila melanogaster
    • Lesch C, Goto A, Lindgren M, Bidla G, Dushay MS, et al. (2007) A role for Hemolectin in coagulation and immunity in Drosophila melanogaster. Dev Comp Immunol 31: 1255-1263.
    • (2007) Dev Comp Immunol , vol.31 , pp. 1255-1263
    • Lesch, C.1    Goto, A.2    Lindgren, M.3    Bidla, G.4    Dushay, M.S.5
  • 105
    • 74849098506 scopus 로고    scopus 로고
    • Innate immunity and gut-microbe mutualism in Drosophila
    • Ryu JH, Ha EM, Lee WJ, (2010) Innate immunity and gut-microbe mutualism in Drosophila. Dev Comp Immunol 34: 369-376.
    • (2010) Dev Comp Immunol , vol.34 , pp. 369-376
    • Ryu, J.H.1    Ha, E.M.2    Lee, W.J.3
  • 106
    • 0032934595 scopus 로고    scopus 로고
    • Oligomerisation of Tube and Pelle leads to nuclear localisation of dorsal
    • Grosshans J, Schnorrer F, Nusslein-Volhard C, (1999) Oligomerisation of Tube and Pelle leads to nuclear localisation of dorsal. Mech Dev 81: 127-138.
    • (1999) Mech Dev , vol.81 , pp. 127-138
    • Grosshans, J.1    Schnorrer, F.2    Nusslein-Volhard, C.3
  • 107
    • 0033567388 scopus 로고    scopus 로고
    • ECSIT is an evolutionarily conserved intermediate in the Toll/IL-1 signal transduction pathway
    • Kopp E, Medzhitov R, Carothers J, Xiao C, Douglas I, et al. (1999) ECSIT is an evolutionarily conserved intermediate in the Toll/IL-1 signal transduction pathway. Genes Dev 13: 2059-2071.
    • (1999) Genes Dev , vol.13 , pp. 2059-2071
    • Kopp, E.1    Medzhitov, R.2    Carothers, J.3    Xiao, C.4    Douglas, I.5
  • 108
    • 33750842525 scopus 로고    scopus 로고
    • Caspar, a suppressor of antibacterial immunity in Drosophila
    • Kim M, Lee JH, Lee SY, Kim E, Chung J, (2006) Caspar, a suppressor of antibacterial immunity in Drosophila. Proc Natl Acad Sci U S A 103: 16358-16363.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 16358-16363
    • Kim, M.1    Lee, J.H.2    Lee, S.Y.3    Kim, E.4    Chung, J.5
  • 110
    • 59849086113 scopus 로고    scopus 로고
    • Genetic analysis of Drosophila melanogaster susceptibility to intestinal Vibrio cholerae infection
    • Berkey CD, Blow N, Watnick PI, (2009) Genetic analysis of Drosophila melanogaster susceptibility to intestinal Vibrio cholerae infection. Cell Microbiol 11: 461-474.
    • (2009) Cell Microbiol , vol.11 , pp. 461-474
    • Berkey, C.D.1    Blow, N.2    Watnick, P.I.3
  • 111
    • 77958509512 scopus 로고    scopus 로고
    • The dark side of fly TNF: an ancient developmental proof reading mechanism turned into tumor promoter
    • Vidal M, (2010) The dark side of fly TNF: an ancient developmental proof reading mechanism turned into tumor promoter. Cell Cycle 9: 3851-3856.
    • (2010) Cell Cycle , vol.9 , pp. 3851-3856
    • Vidal, M.1
  • 112
    • 0141868916 scopus 로고    scopus 로고
    • R2D2, a bridge between the initiation and effector steps of the Drosophila RNAi pathway
    • Liu Q, Rand TA, Kalidas S, Du F, Kim HE, et al. (2003) R2D2, a bridge between the initiation and effector steps of the Drosophila RNAi pathway. Science 301: 1921-1925.
    • (2003) Science , vol.301 , pp. 1921-1925
    • Liu, Q.1    Rand, T.A.2    Kalidas, S.3    Du, F.4    Kim, H.E.5
  • 113
    • 27744537851 scopus 로고    scopus 로고
    • Human RISC couples microRNA biogenesis and posttranscriptional gene silencing
    • Gregory RI, Chendrimada TP, Cooch N, Shiekhattar R, (2005) Human RISC couples microRNA biogenesis and posttranscriptional gene silencing. Cell 123: 631-640.
    • (2005) Cell , vol.123 , pp. 631-640
    • Gregory, R.I.1    Chendrimada, T.P.2    Cooch, N.3    Shiekhattar, R.4
  • 114
    • 22744454230 scopus 로고    scopus 로고
    • Processing of pre-microRNAs by the Dicer-1-Loquacious complex in Drosophila cells
    • Saito K, Ishizuka A, Siomi H, Siomi MC, (2005) Processing of pre-microRNAs by the Dicer-1-Loquacious complex in Drosophila cells. PLoS Biol 3: e235.
    • (2005) PLoS Biol , vol.3
    • Saito, K.1    Ishizuka, A.2    Siomi, H.3    Siomi, M.C.4
  • 115
    • 40849086137 scopus 로고    scopus 로고
    • Identification and characterization of two novel lysozymes from Rhodnius prolixus, a vector of Chagas disease
    • Ursic-Bedoya RJ, Nazzari H, Cooper D, Triana O, Wolff M, et al. (2008) Identification and characterization of two novel lysozymes from Rhodnius prolixus, a vector of Chagas disease. J Insect Physiol 54: 593-603.
    • (2008) J Insect Physiol , vol.54 , pp. 593-603
    • Ursic-Bedoya, R.J.1    Nazzari, H.2    Cooper, D.3    Triana, O.4    Wolff, M.5
  • 116
    • 36749050987 scopus 로고    scopus 로고
    • Sequence characterization of an unusual lysozyme gene expressed in the intestinal tract of the reduviid bug Triatoma infestans (Insecta)
    • Balczun C, Knorr E, Topal H, Meiser CK, Kollien AH, et al. (2008) Sequence characterization of an unusual lysozyme gene expressed in the intestinal tract of the reduviid bug Triatoma infestans (Insecta). Parasitol Res 102: 229-232.
    • (2008) Parasitol Res , vol.102 , pp. 229-232
    • Balczun, C.1    Knorr, E.2    Topal, H.3    Meiser, C.K.4    Kollien, A.H.5
  • 117
    • 33745753244 scopus 로고    scopus 로고
    • Sequence characterization and expression patterns of defensin and lysozyme encoding genes from the gut of the reduviid bug Triatoma brasiliensis
    • Araujo CA, Waniek PJ, Stock P, Mayer C, Jansen AM, et al. (2006) Sequence characterization and expression patterns of defensin and lysozyme encoding genes from the gut of the reduviid bug Triatoma brasiliensis. Insect Biochem Mol Biol 36: 547-560.
    • (2006) Insect Biochem Mol Biol , vol.36 , pp. 547-560
    • Araujo, C.A.1    Waniek, P.J.2    Stock, P.3    Mayer, C.4    Jansen, A.M.5
  • 118
    • 0042469442 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA encoding for a lysozyme from the gut of the reduviid bug Triatoma infestans
    • Kollien AH, Fechner S, Waniek PJ, Schaub GA, (2003) Isolation and characterization of a cDNA encoding for a lysozyme from the gut of the reduviid bug Triatoma infestans. Arch Insect Biochem Physiol 53: 134-145.
    • (2003) Arch Insect Biochem Physiol , vol.53 , pp. 134-145
    • Kollien, A.H.1    Fechner, S.2    Waniek, P.J.3    Schaub, G.A.4
  • 119
    • 1642545489 scopus 로고    scopus 로고
    • Anti-microbial peptides: from invertebrates to vertebrates
    • Bulet P, Stocklin R, Menin L, (2004) Anti-microbial peptides: from invertebrates to vertebrates. Immunol Rev 198: 169-184.
    • (2004) Immunol Rev , vol.198 , pp. 169-184
    • Bulet, P.1    Stocklin, R.2    Menin, L.3
  • 120
    • 0026863621 scopus 로고
    • Two-dimensional 1H NMR study of recombinant insect defensin A in water: Resonance assignments, secondary structure and global folding
    • Bonmatin JM, Bonnat JL, Gallet X, Vovelle F, Ptak M, et al. (1992) Two-dimensional 1H NMR study of recombinant insect defensin A in water: Resonance assignments, secondary structure and global folding. J Biomol NMR 2: 235-256.
    • (1992) J Biomol NMR , vol.2 , pp. 235-256
    • Bonmatin, J.M.1    Bonnat, J.L.2    Gallet, X.3    Vovelle, F.4    Ptak, M.5
  • 121
    • 0033022730 scopus 로고    scopus 로고
    • Antimicrobial peptides in insects; structure and function
    • Bulet P, Hetru C, Dimarcq JL, Hoffmann D, (1999) Antimicrobial peptides in insects; structure and function. Dev Comp Immunol 23: 329-344.
    • (1999) Dev Comp Immunol , vol.23 , pp. 329-344
    • Bulet, P.1    Hetru, C.2    Dimarcq, J.L.3    Hoffmann, D.4
  • 122
    • 0037384739 scopus 로고    scopus 로고
    • Isolation and characterization of a novel insect defensin from Rhodnius prolixus, a vector of Chagas disease
    • Lopez L, Morales G, Ursic R, Wolff M, Lowenberger C, (2003) Isolation and characterization of a novel insect defensin from Rhodnius prolixus, a vector of Chagas disease. Insect Biochem Mol Biol 33: 439-447.
    • (2003) Insect Biochem Mol Biol , vol.33 , pp. 439-447
    • Lopez, L.1    Morales, G.2    Ursic, R.3    Wolff, M.4    Lowenberger, C.5
  • 123
    • 0030198769 scopus 로고    scopus 로고
    • Aedes aegypti: induced antibacterial proteins reduce the establishment and development of Brugia malayi
    • Lowenberger CA, Ferdig MT, Bulet P, Khalili S, Hoffmann JA, et al. (1996) Aedes aegypti: induced antibacterial proteins reduce the establishment and development of Brugia malayi. Exp Parasitol 83: 191-201.
    • (1996) Exp Parasitol , vol.83 , pp. 191-201
    • Lowenberger, C.A.1    Ferdig, M.T.2    Bulet, P.3    Khalili, S.4    Hoffmann, J.A.5
  • 124
    • 0032790518 scopus 로고    scopus 로고
    • Mosquito-Plasmodium interactions in response to immune activation of the vector
    • Lowenberger CA, Kamal S, Chiles J, Paskewitz S, Bulet P, et al. (1999) Mosquito-Plasmodium interactions in response to immune activation of the vector. Exp Parasitol 91: 59-69.
    • (1999) Exp Parasitol , vol.91 , pp. 59-69
    • Lowenberger, C.A.1    Kamal, S.2    Chiles, J.3    Paskewitz, S.4    Bulet, P.5
  • 125
    • 57349149450 scopus 로고    scopus 로고
    • The CAP superfamily: cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins-roles in reproduction, cancer, and immune defense
    • Gibbs GM, Roelants K, O'Bryan MK, (2008) The CAP superfamily: cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins-roles in reproduction, cancer, and immune defense. Endocr Rev 29: 865-897.
    • (2008) Endocr Rev , vol.29 , pp. 865-897
    • Gibbs, G.M.1    Roelants, K.2    O'Bryan, M.K.3
  • 126
    • 33846694747 scopus 로고    scopus 로고
    • Intestinal morphogenesis
    • Rubin DC, (2007) Intestinal morphogenesis. Curr Opin Gastroenterol 23: 111-114.
    • (2007) Curr Opin Gastroenterol , vol.23 , pp. 111-114
    • Rubin, D.C.1
  • 127
    • 51349115110 scopus 로고    scopus 로고
    • Phosphatases of regenerating liver: a novel target in human solid tumors
    • Zhao WB, Wang X, (2008) Phosphatases of regenerating liver: a novel target in human solid tumors. Chin Med J (Engl) 121: 1469-1474.
    • (2008) Chin Med J (Engl) , vol.121 , pp. 1469-1474
    • Zhao, W.B.1    Wang, X.2
  • 128
    • 63449110425 scopus 로고    scopus 로고
    • Ste20-related proline/alanine-rich kinase: a novel regulator of intestinal inflammation
    • Yan Y, Merlin D, (2008) Ste20-related proline/alanine-rich kinase: a novel regulator of intestinal inflammation. World J Gastroenterol 14: 6115-6121.
    • (2008) World J Gastroenterol , vol.14 , pp. 6115-6121
    • Yan, Y.1    Merlin, D.2
  • 131
    • 2542506202 scopus 로고    scopus 로고
    • Protein kinase C (PKC) betaII induces cell invasion through a Ras/Mek-, PKC iota/Rac 1-dependent signaling pathway
    • Zhang J, Anastasiadis PZ, Liu Y, Thompson EA, Fields AP, (2004) Protein kinase C (PKC) betaII induces cell invasion through a Ras/Mek-, PKC iota/Rac 1-dependent signaling pathway. J Biol Chem 279: 22118-22123.
    • (2004) J Biol Chem , vol.279 , pp. 22118-22123
    • Zhang, J.1    Anastasiadis, P.Z.2    Liu, Y.3    Thompson, E.A.4    Fields, A.P.5
  • 132
    • 74649083141 scopus 로고    scopus 로고
    • High expression of atypical protein kinase C lambda/iota in gastric cancer as a prognostic factor for recurrence
    • Takagawa R, Akimoto K, Ichikawa Y, Akiyama H, Kojima Y, et al. (2010) High expression of atypical protein kinase C lambda/iota in gastric cancer as a prognostic factor for recurrence. Ann Surg Oncol 17: 81-88.
    • (2010) Ann Surg Oncol , vol.17 , pp. 81-88
    • Takagawa, R.1    Akimoto, K.2    Ichikawa, Y.3    Akiyama, H.4    Kojima, Y.5
  • 133
    • 33645746316 scopus 로고    scopus 로고
    • The PAR-aPKC system: lessons in polarity
    • Suzuki A, Ohno S, (2006) The PAR-aPKC system: lessons in polarity. J Cell Sci 119: 979-987.
    • (2006) J Cell Sci , vol.119 , pp. 979-987
    • Suzuki, A.1    Ohno, S.2
  • 134
    • 77955501804 scopus 로고    scopus 로고
    • Widely conserved signaling pathways in the establishment of cell polarity
    • McCaffrey LM, Macara IG, (2009) Widely conserved signaling pathways in the establishment of cell polarity. Cold Spring Harb Perspect Biol 1: a001370.
    • (2009) Cold Spring Harb Perspect Biol , vol.1
    • McCaffrey, L.M.1    Macara, I.G.2
  • 135
    • 67650898228 scopus 로고    scopus 로고
    • LKB1 and AMPK family signaling: the intimate link between cell polarity and energy metabolism
    • Jansen M, Ten Klooster JP, Offerhaus GJ, Clevers H, (2009) LKB1 and AMPK family signaling: the intimate link between cell polarity and energy metabolism. Physiol Rev 89: 777-798.
    • (2009) Physiol Rev , vol.89 , pp. 777-798
    • Jansen, M.1    Ten Klooster, J.P.2    Offerhaus, G.J.3    Clevers, H.4
  • 136
    • 0036864358 scopus 로고    scopus 로고
    • Regulation of fatty acid synthesis and oxidation by the AMP-activated protein kinase
    • Hardie DG, Pan DA, (2002) Regulation of fatty acid synthesis and oxidation by the AMP-activated protein kinase. Biochem Soc Trans 30: 1064-1070.
    • (2002) Biochem Soc Trans , vol.30 , pp. 1064-1070
    • Hardie, D.G.1    Pan, D.A.2
  • 137
    • 35748943872 scopus 로고    scopus 로고
    • Dialogue between LKB1 and AMPK: a hot topic at the cellular pole
    • Forcet C, Billaud M, (2007) Dialogue between LKB1 and AMPK: a hot topic at the cellular pole. Sci STKE 2007: pe51.
    • (2007) Sci STKE , vol.2007
    • Forcet, C.1    Billaud, M.2
  • 138
    • 34250827107 scopus 로고    scopus 로고
    • Energy-dependent regulation of cell structure by AMP-activated protein kinase
    • Lee JH, Koh H, Kim M, Kim Y, Lee SY, et al. (2007) Energy-dependent regulation of cell structure by AMP-activated protein kinase. Nature 447: 1017-1020.
    • (2007) Nature , vol.447 , pp. 1017-1020
    • Lee, J.H.1    Koh, H.2    Kim, M.3    Kim, Y.4    Lee, S.Y.5
  • 139
    • 23144467910 scopus 로고    scopus 로고
    • An expanding role for mTOR in cancer
    • Guertin DA, Sabatini DM, (2005) An expanding role for mTOR in cancer. Trends Mol Med 11: 353-361.
    • (2005) Trends Mol Med , vol.11 , pp. 353-361
    • Guertin, D.A.1    Sabatini, D.M.2
  • 140
    • 50849126062 scopus 로고    scopus 로고
    • TOR signaling is required for amino acid stimulation of early trypsin protein synthesis in the midgut of Aedes aegypti mosquitoes
    • Brandon MC, Pennington JE, Isoe J, Zamora J, Schillinger AS, et al. (2008) TOR signaling is required for amino acid stimulation of early trypsin protein synthesis in the midgut of Aedes aegypti mosquitoes. Insect Biochem Mol Biol 38: 916-922.
    • (2008) Insect Biochem Mol Biol , vol.38 , pp. 916-922
    • Brandon, M.C.1    Pennington, J.E.2    Isoe, J.3    Zamora, J.4    Schillinger, A.S.5
  • 141
    • 35448941973 scopus 로고    scopus 로고
    • Effect of insulin and 20-hydroxyecdysone in the fat body of the yellow fever mosquito, Aedes aegypti
    • Roy SG, Hansen IA, Raikhel AS, (2007) Effect of insulin and 20-hydroxyecdysone in the fat body of the yellow fever mosquito, Aedes aegypti. Insect Biochem Mol Biol 37: 1317-1326.
    • (2007) Insect Biochem Mol Biol , vol.37 , pp. 1317-1326
    • Roy, S.G.1    Hansen, I.A.2    Raikhel, A.S.3
  • 142
    • 67549133157 scopus 로고    scopus 로고
    • Cytokine/Jak/Stat signaling mediates regeneration and homeostasis in the Drosophila midgut
    • Jiang H, Patel PH, Kohlmaier A, Grenley MO, McEwen DG, et al. (2009) Cytokine/Jak/Stat signaling mediates regeneration and homeostasis in the Drosophila midgut. Cell 137: 1343-1355.
    • (2009) Cell , vol.137 , pp. 1343-1355
    • Jiang, H.1    Patel, P.H.2    Kohlmaier, A.3    Grenley, M.O.4    McEwen, D.G.5
  • 143
    • 54549104587 scopus 로고    scopus 로고
    • Paracrine Wingless signalling controls self-renewal of Drosophila intestinal stem cells
    • Lin G, Xu N, Xi R, (2008) Paracrine Wingless signalling controls self-renewal of Drosophila intestinal stem cells. Nature 455: 1119-1123.
    • (2008) Nature , vol.455 , pp. 1119-1123
    • Lin, G.1    Xu, N.2    Xi, R.3
  • 144
    • 0032416837 scopus 로고    scopus 로고
    • Drosophila endoderm development requires a novel homeobox gene which is a target of Wingless and Dpp signalling
    • Fuss B, Hoch M, (1998) Drosophila endoderm development requires a novel homeobox gene which is a target of Wingless and Dpp signalling. Mech Dev 79: 83-97.
    • (1998) Mech Dev , vol.79 , pp. 83-97
    • Fuss, B.1    Hoch, M.2
  • 145
    • 0032167471 scopus 로고    scopus 로고
    • A novel homeobox gene mediates the Dpp signal to establish functional specificity within target cells
    • Nakagoshi H, Hoshi M, Nabeshima Y, Matsuzaki F, (1998) A novel homeobox gene mediates the Dpp signal to establish functional specificity within target cells. Genes Dev 12: 2724-2734.
    • (1998) Genes Dev , vol.12 , pp. 2724-2734
    • Nakagoshi, H.1    Hoshi, M.2    Nabeshima, Y.3    Matsuzaki, F.4
  • 146
    • 0036382972 scopus 로고    scopus 로고
    • Refinement of wingless expression by a wingless- and notch-responsive homeodomain protein, defective proventriculus
    • Nakagoshi H, Shirai T, Nabeshima Y, Matsuzaki F, (2002) Refinement of wingless expression by a wingless- and notch-responsive homeodomain protein, defective proventriculus. Dev Biol 249: 44-56.
    • (2002) Dev Biol , vol.249 , pp. 44-56
    • Nakagoshi, H.1    Shirai, T.2    Nabeshima, Y.3    Matsuzaki, F.4
  • 147
    • 0242268101 scopus 로고    scopus 로고
    • Differential requirement of EGFR signaling for the expression of defective proventriculus gene in the Drosophila endoderm and ectoderm
    • Shirai T, Maehara A, Kiritooshi N, Matsuzaki F, Handa H, et al. (2003) Differential requirement of EGFR signaling for the expression of defective proventriculus gene in the Drosophila endoderm and ectoderm. Biochem Biophys Res Commun 311: 473-477.
    • (2003) Biochem Biophys Res Commun , vol.311 , pp. 473-477
    • Shirai, T.1    Maehara, A.2    Kiritooshi, N.3    Matsuzaki, F.4    Handa, H.5
  • 148
    • 79959694148 scopus 로고    scopus 로고
    • Spatial and temporal requirement of defective proventriculus activity during Drosophila midgut development
    • Nakagawa Y, Fujiwara-Fukuta S, Yorimitsu T, Tanaka S, Minami R, et al. (2011) Spatial and temporal requirement of defective proventriculus activity during Drosophila midgut development. Mech Dev 128: 258-267.
    • (2011) Mech Dev , vol.128 , pp. 258-267
    • Nakagawa, Y.1    Fujiwara-Fukuta, S.2    Yorimitsu, T.3    Tanaka, S.4    Minami, R.5
  • 150
    • 21644464069 scopus 로고    scopus 로고
    • Notch signaling functions as a binary switch for the determination of glandular and luminal fates of endodermal epithelium during chicken stomach development
    • Matsuda Y, Wakamatsu Y, Kohyama J, Okano H, Fukuda K, et al. (2005) Notch signaling functions as a binary switch for the determination of glandular and luminal fates of endodermal epithelium during chicken stomach development. Development 132: 2783-2793.
    • (2005) Development , vol.132 , pp. 2783-2793
    • Matsuda, Y.1    Wakamatsu, Y.2    Kohyama, J.3    Okano, H.4    Fukuda, K.5
  • 151
    • 34547180739 scopus 로고    scopus 로고
    • The gastrointestinal tract stem cell niche
    • Yen TH, Wright NA, (2006) The gastrointestinal tract stem cell niche. Stem Cell Rev 2: 203-212.
    • (2006) Stem Cell Rev , vol.2 , pp. 203-212
    • Yen, T.H.1    Wright, N.A.2
  • 152
    • 0035001937 scopus 로고    scopus 로고
    • The basic helix-loop-helix protein family: comparative genomics and phylogenetic analysis
    • Ledent V, Vervoort M, (2001) The basic helix-loop-helix protein family: comparative genomics and phylogenetic analysis. Genome Res 11: 754-770.
    • (2001) Genome Res , vol.11 , pp. 754-770
    • Ledent, V.1    Vervoort, M.2
  • 153
    • 26444536535 scopus 로고    scopus 로고
    • Regulating the dynamics of EGF receptor signaling in space and time
    • Shilo BZ, (2005) Regulating the dynamics of EGF receptor signaling in space and time. Development 132: 4017-4027.
    • (2005) Development , vol.132 , pp. 4017-4027
    • Shilo, B.Z.1
  • 154
    • 0034708076 scopus 로고    scopus 로고
    • A neurofibromatosis-1-regulated pathway is required for learning in Drosophila
    • Guo HF, Tong J, Hannan F, Luo L, Zhong Y, (2000) A neurofibromatosis-1-regulated pathway is required for learning in Drosophila. Nature 403: 895-898.
    • (2000) Nature , vol.403 , pp. 895-898
    • Guo, H.F.1    Tong, J.2    Hannan, F.3    Luo, L.4    Zhong, Y.5
  • 156
    • 34047151226 scopus 로고    scopus 로고
    • Life extension through neurofibromin mitochondrial regulation and antioxidant therapy for neurofibromatosis-1 in Drosophila melanogaster
    • Tong JJ, Schriner SE, McCleary D, Day BJ, Wallace DC, (2007) Life extension through neurofibromin mitochondrial regulation and antioxidant therapy for neurofibromatosis-1 in Drosophila melanogaster. Nat Genet 39: 476-485.
    • (2007) Nat Genet , vol.39 , pp. 476-485
    • Tong, J.J.1    Schriner, S.E.2    McCleary, D.3    Day, B.J.4    Wallace, D.C.5
  • 157
    • 0030005957 scopus 로고    scopus 로고
    • Molecular sequencing and modeling of Neobellieria bullata trypsin. Evidence for translational control by Neobellieria trypsin-modulating oostatic factor
    • Borovsky D, Janssen I, Vanden Broeck J, Huybrechts R, Verhaert P, et al. (1996) Molecular sequencing and modeling of Neobellieria bullata trypsin. Evidence for translational control by Neobellieria trypsin-modulating oostatic factor. Eur J Biochem 237: 279-287.
    • (1996) Eur J Biochem , vol.237 , pp. 279-287
    • Borovsky, D.1    Janssen, I.2    Vanden Broeck, J.3    Huybrechts, R.4    Verhaert, P.5
  • 158
    • 0033103371 scopus 로고    scopus 로고
    • Increase in the size of the amino acid pool is sufficient to activate translation of early trypsin mRNA in Aedes aegypti midgut
    • Noriega FG, Colonna AE, Wells MA, (1999) Increase in the size of the amino acid pool is sufficient to activate translation of early trypsin mRNA in Aedes aegypti midgut. Insect Biochem Mol Biol 29: 243-247.
    • (1999) Insect Biochem Mol Biol , vol.29 , pp. 243-247
    • Noriega, F.G.1    Colonna, A.E.2    Wells, M.A.3
  • 159
    • 0033015768 scopus 로고    scopus 로고
    • A molecular view of trypsin synthesis in the midgut of Aedes aegypti
    • Noriega FG, Wells MA, (1999) A molecular view of trypsin synthesis in the midgut of Aedes aegypti. J Insect Physiol 45: 613-620.
    • (1999) J Insect Physiol , vol.45 , pp. 613-620
    • Noriega, F.G.1    Wells, M.A.2
  • 160
    • 0036009755 scopus 로고    scopus 로고
    • Cloning and molecular characterization of two mosquito iron regulatory proteins
    • Zhang D, Dimopoulos G, Wolf A, Minana B, Kafatos FC, et al. (2002) Cloning and molecular characterization of two mosquito iron regulatory proteins. Insect Biochem Mol Biol 32: 579-589.
    • (2002) Insect Biochem Mol Biol , vol.32 , pp. 579-589
    • Zhang, D.1    Dimopoulos, G.2    Wolf, A.3    Minana, B.4    Kafatos, F.C.5
  • 161
    • 59049100529 scopus 로고    scopus 로고
    • Knockdown of proteins involved in iron metabolism limits tick reproduction and development
    • Hajdusek O, Sojka D, Kopacek P, Buresova V, Franta Z, et al. (2009) Knockdown of proteins involved in iron metabolism limits tick reproduction and development. Proc Natl Acad Sci U S A 106: 1033-1038.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 1033-1038
    • Hajdusek, O.1    Sojka, D.2    Kopacek, P.3    Buresova, V.4    Franta, Z.5
  • 162
    • 0034517679 scopus 로고    scopus 로고
    • Differential regulation of ribosomal protein gene expression in Aedes aegypti mosquitoes before and after the blood meal
    • Niu LL, Fallon AM, (2000) Differential regulation of ribosomal protein gene expression in Aedes aegypti mosquitoes before and after the blood meal. Insect Mol Biol 9: 613-623.
    • (2000) Insect Mol Biol , vol.9 , pp. 613-623
    • Niu, L.L.1    Fallon, A.M.2
  • 163
    • 77953656943 scopus 로고    scopus 로고
    • tRNA stabilization by modified nucleotides
    • Motorin Y, Helm M, (2010) tRNA stabilization by modified nucleotides. Biochemistry 49: 4934-4944.
    • (2010) Biochemistry , vol.49 , pp. 4934-4944
    • Motorin, Y.1    Helm, M.2
  • 164
    • 29544450711 scopus 로고    scopus 로고
    • Rapid tRNA decay can result from lack of nonessential modifications
    • Alexandrov A, Chernyakov I, Gu W, Hiley SL, Hughes TR, et al. (2006) Rapid tRNA decay can result from lack of nonessential modifications. Mol Cell 21: 87-96.
    • (2006) Mol Cell , vol.21 , pp. 87-96
    • Alexandrov, A.1    Chernyakov, I.2    Gu, W.3    Hiley, S.L.4    Hughes, T.R.5
  • 165
    • 84866074106 scopus 로고    scopus 로고
    • RNA cytosine methylation by Dnmt2 and NSun2 promotes tRNA stability and protein synthesis
    • Tuorto F, Liebers R, Musch T, Schaefer M, Hofmann S, et al. (2012) RNA cytosine methylation by Dnmt2 and NSun2 promotes tRNA stability and protein synthesis. Nat Struct Mol Biol 19: 900-905.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 900-905
    • Tuorto, F.1    Liebers, R.2    Musch, T.3    Schaefer, M.4    Hofmann, S.5
  • 166
    • 0037053384 scopus 로고    scopus 로고
    • Accurate translation of the genetic code depends on tRNA modified nucleosides
    • Yarian C, Townsend H, Czestkowski W, Sochacka E, Malkiewicz AJ, et al. (2002) Accurate translation of the genetic code depends on tRNA modified nucleosides. J Biol Chem 277: 16391-16395.
    • (2002) J Biol Chem , vol.277 , pp. 16391-16395
    • Yarian, C.1    Townsend, H.2    Czestkowski, W.3    Sochacka, E.4    Malkiewicz, A.J.5
  • 167
    • 0035801515 scopus 로고    scopus 로고
    • Improvement of reading frame maintenance is a common function for several tRNA modifications
    • Urbonavicius J, Qian Q, Durand JM, Hagervall TG, Bjork GR, (2001) Improvement of reading frame maintenance is a common function for several tRNA modifications. EMBO J 20: 4863-4873.
    • (2001) EMBO J , vol.20 , pp. 4863-4873
    • Urbonavicius, J.1    Qian, Q.2    Durand, J.M.3    Hagervall, T.G.4    Bjork, G.R.5
  • 168
    • 0344223281 scopus 로고    scopus 로고
    • Transfer RNA modification: influence on translational frameshifting and metabolism
    • Bjork GR, Durand JM, Hagervall TG, Leipuviene R, Lundgren HK, et al. (1999) Transfer RNA modification: influence on translational frameshifting and metabolism. FEBS Lett 452: 47-51.
    • (1999) FEBS Lett , vol.452 , pp. 47-51
    • Bjork, G.R.1    Durand, J.M.2    Hagervall, T.G.3    Leipuviene, R.4    Lundgren, H.K.5
  • 169
    • 67650604265 scopus 로고    scopus 로고
    • Stressing out over tRNA cleavage
    • Thompson DM, Parker R, (2009) Stressing out over tRNA cleavage. Cell 138: 215-219.
    • (2009) Cell , vol.138 , pp. 215-219
    • Thompson, D.M.1    Parker, R.2
  • 170
    • 77955884641 scopus 로고    scopus 로고
    • RNA methylation by Dnmt2 protects transfer RNAs against stress-induced cleavage
    • Schaefer M, Pollex T, Hanna K, Tuorto F, Meusburger M, et al. (2010) RNA methylation by Dnmt2 protects transfer RNAs against stress-induced cleavage. Genes Devel 24: 1590-1595.
    • (2010) Genes Devel , vol.24 , pp. 1590-1595
    • Schaefer, M.1    Pollex, T.2    Hanna, K.3    Tuorto, F.4    Meusburger, M.5
  • 171
    • 0026727639 scopus 로고
    • Thiolation of transfer RNA in Escherichia coli varies with growth rate
    • Emilsson V, Naslund AK, Kurland CG, (1992) Thiolation of transfer RNA in Escherichia coli varies with growth rate. Nucleic Acids Res 20: 4499-4505.
    • (1992) Nucleic Acids Res , vol.20 , pp. 4499-4505
    • Emilsson, V.1    Naslund, A.K.2    Kurland, C.G.3
  • 172
    • 84864828979 scopus 로고    scopus 로고
    • Reprogramming of tRNA modifications controls the oxidative stress response by codon-biased translation of proteins
    • Chan CT, Pang YL, Deng W, Babu IR, Dyavaiah M, et al. (2012) Reprogramming of tRNA modifications controls the oxidative stress response by codon-biased translation of proteins. Nat Commun 3: 937.
    • (2012) Nat Commun , vol.3 , pp. 937
    • Chan, C.T.1    Pang, Y.L.2    Deng, W.3    Babu, I.R.4    Dyavaiah, M.5
  • 174
    • 15944389880 scopus 로고    scopus 로고
    • Functional analysis of seven genes encoding eight translation initiation factor 4E (eIF4E) isoforms in Drosophila
    • Hernandez G, Altmann M, Sierra JM, Urlaub H, del Corral RD, et al. (2005) Functional analysis of seven genes encoding eight translation initiation factor 4E (eIF4E) isoforms in Drosophila. Mech Dev 122: 529-543.
    • (2005) Mech Dev , vol.122 , pp. 529-543
    • Hernandez, G.1    Altmann, M.2    Sierra, J.M.3    Urlaub, H.4    del Corral, R.D.5
  • 175
    • 21844442364 scopus 로고    scopus 로고
    • Functional diversity of the eukaryotic translation initiation factors belonging to eIF4 families
    • Hernandez G, Vazquez-Pianzola P, (2005) Functional diversity of the eukaryotic translation initiation factors belonging to eIF4 families. Mech Dev 122: 865-876.
    • (2005) Mech Dev , vol.122 , pp. 865-876
    • Hernandez, G.1    Vazquez-Pianzola, P.2
  • 176
    • 18844397041 scopus 로고    scopus 로고
    • A new paradigm for translational control: Inhibition via 5′-3′ mRNA tethering by Bicoid and the eIF4E cognate 4EHP
    • Cho PF, Poulin F, Cho-Park YA, Cho-Park IB, Chicoine JD, et al. (2005) A new paradigm for translational control: Inhibition via 5′-3′ mRNA tethering by Bicoid and the eIF4E cognate 4EHP. Cell 121: 411-423.
    • (2005) Cell , vol.121 , pp. 411-423
    • Cho, P.F.1    Poulin, F.2    Cho-Park, Y.A.3    Cho-Park, I.B.4    Chicoine, J.D.5
  • 177
    • 67949106616 scopus 로고    scopus 로고
    • The exocyst complex in polarized exocytosis
    • He B, Guo W, (2009) The exocyst complex in polarized exocytosis. Curr Opin Cell Biol 21: 537-542.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 537-542
    • He, B.1    Guo, W.2
  • 178
    • 0028964475 scopus 로고
    • The absence of Emp24p, a component of ER-derived COPPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi
    • Schimmoller F, Singerkruger B, Schroder S, Kruger U, Barlowe C, et al. (1995) The absence of Emp24p, a component of ER-derived COPPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi. Embo J 14: 1329-1339.
    • (1995) Embo J , vol.14 , pp. 1329-1339
    • Schimmoller, F.1    Singerkruger, B.2    Schroder, S.3    Kruger, U.4    Barlowe, C.5
  • 179
    • 3042734383 scopus 로고    scopus 로고
    • The Drosophila ARF6-GEF schizo controls commissure formation by regulating slit
    • Onel S, Bolke L, Klambt C, (2004) The Drosophila ARF6-GEF schizo controls commissure formation by regulating slit. Development 131: 2587-2594.
    • (2004) Development , vol.131 , pp. 2587-2594
    • Onel, S.1    Bolke, L.2    Klambt, C.3
  • 180
    • 38149035199 scopus 로고    scopus 로고
    • Haemozoin formation
    • Egan TJ, (2008) Haemozoin formation. Mol Biochem Parasitol 157: 127-136.
    • (2008) Mol Biochem Parasitol , vol.157 , pp. 127-136
    • Egan, T.J.1
  • 181
    • 13544269468 scopus 로고    scopus 로고
    • Insect glutathione transferases and insecticide resistance
    • Enayati AA, Ranson H, Hemingway J, (2005) Insect glutathione transferases and insecticide resistance. Insect Mol Biol 14: 3-8.
    • (2005) Insect Mol Biol , vol.14 , pp. 3-8
    • Enayati, A.A.1    Ranson, H.2    Hemingway, J.3
  • 182
    • 0030448635 scopus 로고    scopus 로고
    • Insecticide resistance genes in mosquitoes: their mutations, migration, and selection in field populations
    • Pasteur N, Raymond M, (1996) Insecticide resistance genes in mosquitoes: their mutations, migration, and selection in field populations. J Hered 87: 444-449.
    • (1996) J Hered , vol.87 , pp. 444-449
    • Pasteur, N.1    Raymond, M.2
  • 184
    • 77952641390 scopus 로고    scopus 로고
    • Transcription profiling of eleven cytochrome P450s potentially involved in xenobiotic metabolism in the mosquito Aedes aegypti
    • Poupardin R, Riaz MA, Vontas J, David JP, Reynaud S, (2010) Transcription profiling of eleven cytochrome P450s potentially involved in xenobiotic metabolism in the mosquito Aedes aegypti. Insect Mol Biol 19: 185-193.
    • (2010) Insect Mol Biol , vol.19 , pp. 185-193
    • Poupardin, R.1    Riaz, M.A.2    Vontas, J.3    David, J.P.4    Reynaud, S.5
  • 185
    • 34248657991 scopus 로고    scopus 로고
    • Evolution of insect P450
    • Feyereisen R, (2006) Evolution of insect P450. Biochem Soc Trans 34: 1252-1255.
    • (2006) Biochem Soc Trans , vol.34 , pp. 1252-1255
    • Feyereisen, R.1
  • 187
    • 55749090372 scopus 로고    scopus 로고
    • P450 reductase and cytochrome b5 interactions with cytochrome P450: effects on house fly CYP6A1 catalysis
    • Murataliev MB, Guzov VM, Walker FA, Feyereisen R, (2008) P450 reductase and cytochrome b5 interactions with cytochrome P450: effects on house fly CYP6A1 catalysis. Insect Biochem Mol Biol 38: 1008-1015.
    • (2008) Insect Biochem Mol Biol , vol.38 , pp. 1008-1015
    • Murataliev, M.B.1    Guzov, V.M.2    Walker, F.A.3    Feyereisen, R.4
  • 188
    • 0033013763 scopus 로고    scopus 로고
    • Insect P450 enzymes
    • Feyereisen R, (1999) Insect P450 enzymes. Annu Rev Entomol 44: 507-533.
    • (1999) Annu Rev Entomol , vol.44 , pp. 507-533
    • Feyereisen, R.1
  • 189
    • 34248634319 scopus 로고    scopus 로고
    • The Halloween genes code for cytochrome P450 enzymes mediating synthesis of the insect moulting hormone
    • Rewitz KF, Rybczynski R, Warren JT, Gilbert LI, (2006) The Halloween genes code for cytochrome P450 enzymes mediating synthesis of the insect moulting hormone. Biochem Soc Trans 34: 1256-1260.
    • (2006) Biochem Soc Trans , vol.34 , pp. 1256-1260
    • Rewitz, K.F.1    Rybczynski, R.2    Warren, J.T.3    Gilbert, L.I.4
  • 190
    • 0035490861 scopus 로고    scopus 로고
    • Hydrogen peroxide detoxification in the midgut of the blood-sucking insect, Rhodnius prolixus
    • Paes MC, Oliveira MB, Oliveira PL, (2001) Hydrogen peroxide detoxification in the midgut of the blood-sucking insect, Rhodnius prolixus. Arch Insect Biochem Physiol 48: 63-71.
    • (2001) Arch Insect Biochem Physiol , vol.48 , pp. 63-71
    • Paes, M.C.1    Oliveira, M.B.2    Oliveira, P.L.3
  • 191
    • 0000276976 scopus 로고    scopus 로고
    • Extracellular glutathione peroxidase from the blood-sucking bug, Rhodnius prolixus
    • Paes MC, Oliveira PL, (1999) Extracellular glutathione peroxidase from the blood-sucking bug, Rhodnius prolixus. Arch Insect Biochem Physiol 41: 171-177.
    • (1999) Arch Insect Biochem Physiol , vol.41 , pp. 171-177
    • Paes, M.C.1    Oliveira, P.L.2
  • 192
    • 34648829796 scopus 로고    scopus 로고
    • Sulfation of nitrotyrosine: biochemistry and functional implications
    • Liu MC, Yasuda S, Idell S, (2007) Sulfation of nitrotyrosine: biochemistry and functional implications. IUBMB Life 59: 622-627.
    • (2007) IUBMB Life , vol.59 , pp. 622-627
    • Liu, M.C.1    Yasuda, S.2    Idell, S.3
  • 193
    • 79851511094 scopus 로고    scopus 로고
    • Sulfation of chlorotyrosine and nitrotyrosine by human lung endothelial and epithelial cells: Role of the human SULT1A3
    • Yasuda S, Yasuda T, Liu MY, Shetty S, Idell S, et al. (2011) Sulfation of chlorotyrosine and nitrotyrosine by human lung endothelial and epithelial cells: Role of the human SULT1A3. Toxicol Appl Pharmacol 251: 104-109.
    • (2011) Toxicol Appl Pharmacol , vol.251 , pp. 104-109
    • Yasuda, S.1    Yasuda, T.2    Liu, M.Y.3    Shetty, S.4    Idell, S.5
  • 194
    • 33744960001 scopus 로고    scopus 로고
    • The dehydrogenase-mediated recycling of NADPH is a key antioxidant system against salt-induced oxidative stress in olive plants
    • Valderrama R, Corpas FJ, Carreras A, Gomez-Rodriguez MV, Chaki M, et al. (2006) The dehydrogenase-mediated recycling of NADPH is a key antioxidant system against salt-induced oxidative stress in olive plants. Plant Cell Environment 29: 1449-1459.
    • (2006) Plant Cell Environment , vol.29 , pp. 1449-1459
    • Valderrama, R.1    Corpas, F.J.2    Carreras, A.3    Gomez-Rodriguez, M.V.4    Chaki, M.5
  • 195
    • 77953690176 scopus 로고    scopus 로고
    • A mammalian siderophore synthesized by an enzyme with a bacterial homolog involved in enterobactin production
    • Devireddy LR, Hart DO, Goetz DH, Green MR, (2010) A mammalian siderophore synthesized by an enzyme with a bacterial homolog involved in enterobactin production. Cell 141: 1006-1017.
    • (2010) Cell , vol.141 , pp. 1006-1017
    • Devireddy, L.R.1    Hart, D.O.2    Goetz, D.H.3    Green, M.R.4
  • 196
    • 0033511832 scopus 로고    scopus 로고
    • Cell biology of heme
    • Ponka P, (1999) Cell biology of heme. Am J Med Sci 318: 241-256.
    • (1999) Am J Med Sci , vol.318 , pp. 241-256
    • Ponka, P.1
  • 197
    • 0035106507 scopus 로고    scopus 로고
    • Heme biosynthesis and oogenesis in the blood-sucking bug, Rhodnius prolixus
    • Braz GR, Abreu L, Masuda H, Oliveira PL, (2001) Heme biosynthesis and oogenesis in the blood-sucking bug, Rhodnius prolixus. Insect Biochem Mol Biol 31: 359-364.
    • (2001) Insect Biochem Mol Biol , vol.31 , pp. 359-364
    • Braz, G.R.1    Abreu, L.2    Masuda, H.3    Oliveira, P.L.4
  • 198
    • 0028938344 scopus 로고
    • Antioxidant role of Rhodnius prolixus heme-binding protein. Protection against heme-induced lipid peroxidation
    • Dansa-Petretski M, Ribeiro JM, Atella GC, Masuda H, Oliveira PL, (1995) Antioxidant role of Rhodnius prolixus heme-binding protein. Protection against heme-induced lipid peroxidation. J Biol Chem 270: 10893-10896.
    • (1995) J Biol Chem , vol.270 , pp. 10893-10896
    • Dansa-Petretski, M.1    Ribeiro, J.M.2    Atella, G.C.3    Masuda, H.4    Oliveira, P.L.5
  • 199
    • 4544264523 scopus 로고    scopus 로고
    • Identification of a human heme exporter that is essential for erythropoiesis
    • Quigley JG, Yang Z, Worthington MT, Phillips JD, Sabo KM, et al. (2004) Identification of a human heme exporter that is essential for erythropoiesis. Cell 118: 757-766.
    • (2004) Cell , vol.118 , pp. 757-766
    • Quigley, J.G.1    Yang, Z.2    Worthington, M.T.3    Phillips, J.D.4    Sabo, K.M.5
  • 201
    • 78649630468 scopus 로고    scopus 로고
    • Sn-protoporphyrin inhibits both heme degradation and hemozoin formation in Rhodnius prolixus midgut
    • Caiaffa CD, Stiebler R, Oliveira MF, Lara FA, Paiva-Silva GO, et al. (2010) Sn-protoporphyrin inhibits both heme degradation and hemozoin formation in Rhodnius prolixus midgut. Insect Biochem Mol Biol 40: 855-860.
    • (2010) Insect Biochem Mol Biol , vol.40 , pp. 855-860
    • Caiaffa, C.D.1    Stiebler, R.2    Oliveira, M.F.3    Lara, F.A.4    Paiva-Silva, G.O.5
  • 203
    • 33645091619 scopus 로고    scopus 로고
    • Insect iron binding proteins: insights from the genomes
    • Dunkov B, Georgieva T, (2006) Insect iron binding proteins: insights from the genomes. Insect Biochem Mol Biol 36: 300-309.
    • (2006) Insect Biochem Mol Biol , vol.36 , pp. 300-309
    • Dunkov, B.1    Georgieva, T.2
  • 204
    • 0000003821 scopus 로고
    • The midgut ultrastructure of hematophagous insects
    • Billingsley PF, (1990) The midgut ultrastructure of hematophagous insects. Ann Rev Entomol 35: 219-248.
    • (1990) Ann Rev Entomol , vol.35 , pp. 219-248
    • Billingsley, P.F.1
  • 205
    • 0029417470 scopus 로고
    • Loading of lipophorin particles with phospholipids at the midgut of Rhodnius prolixus
    • Atella GC, Gondim C, Masuda H, (1995) Loading of lipophorin particles with phospholipids at the midgut of Rhodnius prolixus. Arch Insect Biochem Physiol 30: 337-350.
    • (1995) Arch Insect Biochem Physiol , vol.30 , pp. 337-350
    • Atella, G.C.1    Gondim, C.2    Masuda, H.3
  • 207
    • 0031926312 scopus 로고    scopus 로고
    • Hydrophobic attachment of Trypanosoma cruzi to a superficial layer of the rectal cuticle in the bug Triatoma infestans
    • Schmidt J, Kleffmann T, Schaub GA, (1998) Hydrophobic attachment of Trypanosoma cruzi to a superficial layer of the rectal cuticle in the bug Triatoma infestans. Parasitol Res 84: 527-536.
    • (1998) Parasitol Res , vol.84 , pp. 527-536
    • Schmidt, J.1    Kleffmann, T.2    Schaub, G.A.3
  • 208
    • 0043172415 scopus 로고    scopus 로고
    • The SREBP pathway-insights from Insigs and insects
    • Rawson RB, (2003) The SREBP pathway-insights from Insigs and insects. Nat Rev Mol Cell Biol 4: 631-640.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 631-640
    • Rawson, R.B.1
  • 209
    • 33847264996 scopus 로고    scopus 로고
    • Drosophila NPC1b promotes an early step in sterol absorption from the midgut epithelium
    • Voght SP, Fluegel ML, Andrews LA, Pallanck LJ, (2007) Drosophila NPC1b promotes an early step in sterol absorption from the midgut epithelium. Cell Metab 5: 195-205.
    • (2007) Cell Metab , vol.5 , pp. 195-205
    • Voght, S.P.1    Fluegel, M.L.2    Andrews, L.A.3    Pallanck, L.J.4
  • 210
    • 0034086945 scopus 로고    scopus 로고
    • Phosphatidylcholine metabolism in human endothelial cells: modulation by phosphocholine
    • Wong JT, Chan M, Lee D, Jiang JY, Skrzypczak M, et al. (2000) Phosphatidylcholine metabolism in human endothelial cells: modulation by phosphocholine. Mol Cell Biochem 207: 95-100.
    • (2000) Mol Cell Biochem , vol.207 , pp. 95-100
    • Wong, J.T.1    Chan, M.2    Lee, D.3    Jiang, J.Y.4    Skrzypczak, M.5
  • 212
    • 0016302040 scopus 로고
    • Phospholipid exchange between membranes. Purification of bovine brain proteins that preferentially catalyze the transfer of phosphatidylinositol
    • Helmkamp GM Jr, Harvey MS, Wirtz KW, Van Deenen LL, (1974) Phospholipid exchange between membranes. Purification of bovine brain proteins that preferentially catalyze the transfer of phosphatidylinositol. J Biol Chem 249: 6382-6389.
    • (1974) J Biol Chem , vol.249 , pp. 6382-6389
    • Helmkamp Jr., G.M.1    Harvey, M.S.2    Wirtz, K.W.3    Van Deenen, L.L.4
  • 213
    • 0032077354 scopus 로고    scopus 로고
    • Phosphatidylinositol transfer proteins: a requirement in signal transduction and vesicle traffic
    • Cockcroft S, (1998) Phosphatidylinositol transfer proteins: a requirement in signal transduction and vesicle traffic. Bioessays 20: 423-432.
    • (1998) Bioessays , vol.20 , pp. 423-432
    • Cockcroft, S.1
  • 215
    • 58249144741 scopus 로고    scopus 로고
    • Lysophosphatidic acid signaling in airway epithelium: Role in airway inflammation and remodeling
    • Zhao Y, Natarajan V, (2009) Lysophosphatidic acid signaling in airway epithelium: Role in airway inflammation and remodeling. Cell Signal 21: 367-377.
    • (2009) Cell Signal , vol.21 , pp. 367-377
    • Zhao, Y.1    Natarajan, V.2
  • 216
    • 0041845324 scopus 로고    scopus 로고
    • Lysophosphatidylcholine acts as an anti-hemostatic molecule in the saliva of the blood-sucking bug Rhodnius prolixus
    • Golodne DM, Monteiro RQ, Graca-Souza AV, Silva-Neto MA, Atella GC, (2003) Lysophosphatidylcholine acts as an anti-hemostatic molecule in the saliva of the blood-sucking bug Rhodnius prolixus. J Biol Chem 278: 27766-27771.
    • (2003) J Biol Chem , vol.278 , pp. 27766-27771
    • Golodne, D.M.1    Monteiro, R.Q.2    Graca-Souza, A.V.3    Silva-Neto, M.A.4    Atella, G.C.5
  • 217
    • 33746781022 scopus 로고    scopus 로고
    • Identification and characterization of a lysophosphatidylcholine acyltransferase in alveolar type II cells
    • Chen X, Hyatt BA, Mucenski ML, Mason RJ, Shannon JM, (2006) Identification and characterization of a lysophosphatidylcholine acyltransferase in alveolar type II cells. Proc Natl Acad Sci U S A 103: 11724-11729.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 11724-11729
    • Chen, X.1    Hyatt, B.A.2    Mucenski, M.L.3    Mason, R.J.4    Shannon, J.M.5
  • 218
    • 0028903101 scopus 로고
    • Lysophosphatidic acid signalling
    • Moolenaar WH, (1995) Lysophosphatidic acid signalling. Curr Opin Cell Biol 7: 203-210.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 203-210
    • Moolenaar, W.H.1
  • 220
    • 0030581304 scopus 로고    scopus 로고
    • Phosphatidylcholine transfer protein from bovine liver contains highly unsaturated phosphatidylcholine species
    • Geijtenbeek TB, Westerman J, Heerma W, Wirtz KW, (1996) Phosphatidylcholine transfer protein from bovine liver contains highly unsaturated phosphatidylcholine species. FEBS Lett 391: 333-335.
    • (1996) FEBS Lett , vol.391 , pp. 333-335
    • Geijtenbeek, T.B.1    Westerman, J.2    Heerma, W.3    Wirtz, K.W.4
  • 221
    • 34249813409 scopus 로고    scopus 로고
    • Structure and function of phosphatidylcholine transfer protein (PC-TP)/StarD2
    • Kanno K, Wu MK, Scapa EF, Roderick SL, Cohen DE, (2007) Structure and function of phosphatidylcholine transfer protein (PC-TP)/StarD2. Biochim Biophys Acta 1771: 654-662.
    • (2007) Biochim Biophys Acta , vol.1771 , pp. 654-662
    • Kanno, K.1    Wu, M.K.2    Scapa, E.F.3    Roderick, S.L.4    Cohen, D.E.5
  • 222
    • 40849145708 scopus 로고    scopus 로고
    • Lipid droplets in lipogenesis and lipolysis
    • Ducharme NA, Bickel PE, (2008) Lipid droplets in lipogenesis and lipolysis. Endocrinology 149: 942-949.
    • (2008) Endocrinology , vol.149 , pp. 942-949
    • Ducharme, N.A.1    Bickel, P.E.2
  • 223
    • 77950607704 scopus 로고    scopus 로고
    • Adoption of PERILIPIN as a unifying nomenclature for the mammalian PAT-family of intracellular lipid storage droplet proteins
    • Kimmel AR, Brasaemle DL, McAndrews-Hill M, Sztalryd C, Londos C, (2010) Adoption of PERILIPIN as a unifying nomenclature for the mammalian PAT-family of intracellular lipid storage droplet proteins. J Lipid Res 51: 468-471.
    • (2010) J Lipid Res , vol.51 , pp. 468-471
    • Kimmel, A.R.1    Brasaemle, D.L.2    McAndrews-Hill, M.3    Sztalryd, C.4    Londos, C.5
  • 224
    • 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 JW, Brzostowski J, Parisi MJ, Schultz CJ, et al. (2002) Functional conservation for lipid storage droplet association among perilipin, ADRP, and TIP47 (PAT)-related proteins in mammals, Drosophila, and Dictyostelium. J Biol Chem 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
  • 225
    • 20744447492 scopus 로고    scopus 로고
    • Activation of the lipid droplet controls the rate of lipolysis of triglycerides in the insect fat body
    • Patel RT, Soulages JL, Hariharasundaram B, Arrese EL, (2005) Activation of the lipid droplet controls the rate of lipolysis of triglycerides in the insect fat body. J Biol Chem 280: 22624-22631.
    • (2005) J Biol Chem , vol.280 , pp. 22624-22631
    • Patel, R.T.1    Soulages, J.L.2    Hariharasundaram, B.3    Arrese, E.L.4
  • 227
    • 0037090313 scopus 로고    scopus 로고
    • Cells expressing indoleamine 2,3-dioxygenase inhibit T cell responses
    • Mellor AL, Keskin DB, Johnson T, Chandler P, Munn DH, (2002) Cells expressing indoleamine 2,3-dioxygenase inhibit T cell responses. J Immunol 168: 3771-3776.
    • (2002) J Immunol , vol.168 , pp. 3771-3776
    • Mellor, A.L.1    Keskin, D.B.2    Johnson, T.3    Chandler, P.4    Munn, D.H.5
  • 228
    • 0032546376 scopus 로고    scopus 로고
    • Identification of xanthurenic acid as the putative inducer of malaria development in the mosquito
    • Billker O, Lindo V, Panico M, Etienne AE, Paxton T, et al. (1998) Identification of xanthurenic acid as the putative inducer of malaria development in the mosquito. Nature 392: 289-292.
    • (1998) Nature , vol.392 , pp. 289-292
    • Billker, O.1    Lindo, V.2    Panico, M.3    Etienne, A.E.4    Paxton, T.5
  • 229
    • 84862173717 scopus 로고    scopus 로고
    • The antioxidant role of xanthurenic acid in the Aedes aegypti midgut during digestion of a blood meal
    • Lima VL, Dias F, Nunes RD, Pereira LO, Santos TS, et al. (2012) The antioxidant role of xanthurenic acid in the Aedes aegypti midgut during digestion of a blood meal. PLoS One 7: e38349.
    • (2012) PLoS One , vol.7
    • Lima, V.L.1    Dias, F.2    Nunes, R.D.3    Pereira, L.O.4    Santos, T.S.5
  • 230
    • 77955828068 scopus 로고    scopus 로고
    • Indoleamine 2,3-dioxigenase (IDO) is critical for host resistance against Trypanosoma cruzi
    • Knubel CP, Martinez FF, Fretes RE, Diaz Lujan C, Theumer MG, et al. (2010) Indoleamine 2,3-dioxigenase (IDO) is critical for host resistance against Trypanosoma cruzi. FASEB J 24: 2689-2701.
    • (2010) FASEB J , vol.24 , pp. 2689-2701
    • Knubel, C.P.1    Martinez, F.F.2    Fretes, R.E.3    Diaz Lujan, C.4    Theumer, M.G.5
  • 231
    • 77954053306 scopus 로고    scopus 로고
    • A new method for accurately measuring Delta(1)-pyrroline-5-carboxylate synthetase activity
    • Parre E, de Virville J, Cochet F, Leprince AS, Richard L, et al. (2010) A new method for accurately measuring Delta(1)-pyrroline-5-carboxylate synthetase activity. Methods Mol Biol 639: 333-340.
    • (2010) Methods Mol Biol , vol.639 , pp. 333-340
    • Parre, E.1    de Virville, J.2    Cochet, F.3    Leprince, A.S.4    Richard, L.5
  • 232
    • 0038687028 scopus 로고    scopus 로고
    • Proline can be utilized as an energy substrate during flight of Aedes aegypti females
    • Scaraffia PY, Wells MA, (2003) Proline can be utilized as an energy substrate during flight of Aedes aegypti females. J Insect Physiol 49: 591-601.
    • (2003) J Insect Physiol , vol.49 , pp. 591-601
    • Scaraffia, P.Y.1    Wells, M.A.2
  • 233
    • 0032530665 scopus 로고    scopus 로고
    • Selective histamine uptake rescues photo- and mechanoreceptor function of histidine decarboxylase-deficient Drosophila mutant
    • Melzig J, Burg M, Gruhn M, Pak WL, Buchner E, (1998) Selective histamine uptake rescues photo- and mechanoreceptor function of histidine decarboxylase-deficient Drosophila mutant. J Neurosci 18: 7160-7166.
    • (1998) J Neurosci , vol.18 , pp. 7160-7166
    • Melzig, J.1    Burg, M.2    Gruhn, M.3    Pak, W.L.4    Buchner, E.5
  • 234
    • 34548768028 scopus 로고    scopus 로고
    • Widespread lateral gene transfer from intracellular bacteria to multicellular eukaryotes
    • Dunning Hotopp JC, Clark ME, Oliveira DC, Foster JM, Fischer P, et al. (2007) Widespread lateral gene transfer from intracellular bacteria to multicellular eukaryotes. Science 317: 1753-1756.
    • (2007) Science , vol.317 , pp. 1753-1756
    • Dunning Hotopp, J.C.1    Clark, M.E.2    Oliveira, D.C.3    Foster, J.M.4    Fischer, P.5
  • 235
    • 0036533525 scopus 로고    scopus 로고
    • bc10: A novel human bladder cancer-associated protein with a conserved genomic structure downregulated in invasive cancer
    • Gromova I, Gromov P, Celis JE, (2002) bc10: A novel human bladder cancer-associated protein with a conserved genomic structure downregulated in invasive cancer. Int J Cancer 98: 539-546.
    • (2002) Int J Cancer , vol.98 , pp. 539-546
    • Gromova, I.1    Gromov, P.2    Celis, J.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.