메뉴 건너뛰기




Volumn 138, Issue 2, 2004, Pages 229-239

Differential gene expression during wing morph differentiation of the ectoparasitoid Melittobia digitata (Hym., Eulophidae)

Author keywords

Gene expression; long wing morph; LWM; Metabolism; Nutrition; Polyphenism; short wing morph; SSH; suppression subtractive hybridization; SWM; Trade off; Wing differentiation

Indexed keywords

COMPLEMENTARY DNA; MESSENGER RNA;

EID: 3242678153     PISSN: 10956433     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2004.04.002     Document Type: Article
Times cited : (13)

References (51)
  • 1
    • 0033385940 scopus 로고    scopus 로고
    • The Drosophila JNK pathway controls the morphogenesis of imaginal discs during metamorphosis
    • Agnès F., Suzanne M., Noselli S. The Drosophila JNK pathway controls the morphogenesis of imaginal discs during metamorphosis. Development. 126:1999;5453-5462
    • (1999) Development , vol.126 , pp. 5453-5462
    • Agnès, F.1    Suzanne, M.2    Noselli, S.3
  • 3
    • 0027312491 scopus 로고
    • The Drosophila stubble-stubbloid gene encodes an apparent transmembrane serine protease required for epithelial morphogenesis
    • Appel L.F., Prout M., Abu-Shumays R., Hammonds A., Garbe J.C., Fristom D. The Drosophila stubble-stubbloid gene encodes an apparent transmembrane serine protease required for epithelial morphogenesis. Proc. Natl. Acad. Sci. U. S. A. 90:1993;4937-4941
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 4937-4941
    • Appel, L.F.1    Prout, M.2    Abu-Shumays, R.3    Hammonds, A.4    Garbe, J.C.5    Fristom, D.6
  • 4
    • 0034646417 scopus 로고    scopus 로고
    • Notch signaling directly controls cell proliferation in the Drosophila wing disc
    • Baonza A., Garcia-Bellido A. Notch signaling directly controls cell proliferation in the Drosophila wing disc. Proc. Natl. Acad. Sci. U. S. A. 97:2000;2609-2614
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 2609-2614
    • Baonza, A.1    Garcia-Bellido, A.2
  • 5
    • 0029036451 scopus 로고
    • Evolutionary families of metallopeptidases
    • Barrett A.J., Rawlings N.D. Evolutionary families of metallopeptidases. Methods Enzymol. 248:1995;183-228
    • (1995) Methods Enzymol. , vol.248 , pp. 183-228
    • Barrett, A.J.1    Rawlings, N.D.2
  • 8
    • 0032713635 scopus 로고    scopus 로고
    • The gon-1 gene is required for gonodal morphogenesis in Caenorhabditis elegans
    • Blelloch R., Anna-Arriola S.S., Gao D., Li Y., Hodgkin J., Kimble J. The gon-1 gene is required for gonodal morphogenesis in Caenorhabditis elegans. Dev. Biol. 216:1999;382-393
    • (1999) Dev. Biol. , vol.216 , pp. 382-393
    • Blelloch, R.1    Anna-Arriola, S.S.2    Gao, D.3    Li, Y.4    Hodgkin, J.5    Kimble, J.6
  • 9
    • 0027453804 scopus 로고
    • Axis specification in the developing Drosophila appendage, the role of wingless, decapentaplegic, and the homeobox gene aristaless
    • Campbell G., Weaver T., Tomlinson A. Axis specification in the developing Drosophila appendage, the role of wingless, decapentaplegic, and the homeobox gene aristaless. Cell. 74:1993;1113-1123
    • (1993) Cell , vol.74 , pp. 1113-1123
    • Campbell, G.1    Weaver, T.2    Tomlinson, A.3
  • 10
    • 0036308582 scopus 로고    scopus 로고
    • Clutch size, development and wing morph differentiation of Melittobia digitata
    • Cônsoli F.L., Vinson S.B. Clutch size, development and wing morph differentiation of Melittobia digitata. Entomol. Exp. Appl. 102:2002;135-143
    • (2002) Entomol. Exp. Appl. , vol.102 , pp. 135-143
    • Cônsoli, F.L.1    Vinson, S.B.2
  • 11
    • 0041820728 scopus 로고    scopus 로고
    • Larval development and feeding behavior of the wing morphs of Melittobia digitata Dahms (Hymenoptera: Eulophidae)
    • Cônsoli F.L., Vinson S.B. Larval development and feeding behavior of the wing morphs of Melittobia digitata Dahms (Hymenoptera: Eulophidae). J. Hymenopt. Res. 11:2002;188-196
    • (2002) J. Hymenopt. Res. , vol.11 , pp. 188-196
    • Cônsoli, F.L.1    Vinson, S.B.2
  • 12
    • 0000506184 scopus 로고
    • A review of the biology of species in the genus Melittobia (Hymenoptera: Eulophidae) with interpretations and additions using observations on Melittobia australica
    • Dahms E.C. A review of the biology of species in the genus Melittobia (Hymenoptera: Eulophidae) with interpretations and additions using observations on Melittobia australica. Mem. Queensl. Mus. 21:1984;337-360
    • (1984) Mem. Queensl. Mus. , vol.21 , pp. 337-360
    • Dahms, E.C.1
  • 14
    • 0030867913 scopus 로고    scopus 로고
    • Molecular immune responses of the mosquito Anopheles gambiae to bacteria and malaria parasites
    • Dimopoulos G., Richaman A., Muller H.M., Kafatos F.C. Molecular immune responses of the mosquito Anopheles gambiae to bacteria and malaria parasites. Proc. Natl. Acad. Sci. U. S. A. 94:1997;11508-11513
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 11508-11513
    • Dimopoulos, G.1    Richaman, A.2    Muller, H.M.3    Kafatos, F.C.4
  • 15
    • 51249170661 scopus 로고
    • Wing dimorphism and the migratory syndrome: Correlated traits for migratory tendency in wing dimorphic insects
    • Fairbain D.J. Wing dimorphism and the migratory syndrome: correlated traits for migratory tendency in wing dimorphic insects. Res. Popul. Ecol. 36:1994;157-163
    • (1994) Res. Popul. Ecol. , vol.36 , pp. 157-163
    • Fairbain, D.J.1
  • 17
    • 0035999904 scopus 로고    scopus 로고
    • Association of midgut defensin with a novel serine protease in the blood-sucking fly Stomoxys calcitrans
    • Hamilton J.V., Munks R.J.L., Lehane S.M., Lehane M.J. Association of midgut defensin with a novel serine protease in the blood-sucking fly Stomoxys calcitrans. Insect Mol. Biol. 11:2002;197-205
    • (2002) Insect Mol. Biol. , vol.11 , pp. 197-205
    • Hamilton, J.V.1    Munks, R.J.L.2    Lehane, S.M.3    Lehane, M.J.4
  • 18
    • 0021215865 scopus 로고
    • Isolation of cDNA clones encoding T cell-specific membrane-associated proteins
    • Hedrick S.M., Cohen D.I., Neilson E.A., Davis M.M. Isolation of cDNA clones encoding T cell-specific membrane-associated proteins. Nature. 308:1984;149-153
    • (1984) Nature , vol.308 , pp. 149-153
    • Hedrick, S.M.1    Cohen, D.I.2    Neilson, E.A.3    Davis, M.M.4
  • 19
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Higgins D., Thompson J., Gibson T., Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Higgins, D.1    Thompson, J.2    Gibson, T.3    Thompson, J.D.4    Higgins, D.G.5    Gibson, T.J.6
  • 20
    • 0034616025 scopus 로고    scopus 로고
    • A cell adhesion protein from the crayfish Pacifastacus leniusculus, a serine proteinase homologue similar to Drosophila masquerade
    • Huang T., Wang H., Lee S.Y., Johansson M.W., Söderhall K., Cerenius L. A cell adhesion protein from the crayfish Pacifastacus leniusculus, a serine proteinase homologue similar to Drosophila masquerade. J. Biol. Chem. 275:2000;9996-10001
    • (2000) J. Biol. Chem. , vol.275 , pp. 9996-10001
    • Huang, T.1    Wang, H.2    Lee, S.Y.3    Johansson, M.W.4    Söderhall, K.5    Cerenius, L.6
  • 21
    • 0037312507 scopus 로고    scopus 로고
    • TOR signalling in bugs, brain and brawn
    • Jacinto E., Hall M.N. TOR signalling in bugs, brain and brawn. Mol. Cell. Biol. 4:2003;117-126
    • (2003) Mol. Cell. Biol. , vol.4 , pp. 117-126
    • Jacinto, E.1    Hall, M.N.2
  • 22
    • 0030566866 scopus 로고    scopus 로고
    • Limulus factor D, a 43 kDa protein isolated from horseshoe crab hemocytes, is a serine proteinase homologue with antimicrobial activity
    • Kawabata S., Tokunaga F., Kugi Y., Motoyama S., Miura Y., Hirata M., Iwanaga S. Limulus factor D, a 43 kDa protein isolated from horseshoe crab hemocytes, is a serine proteinase homologue with antimicrobial activity. FEBS Lett. 398:1996;146-150
    • (1996) FEBS Lett. , vol.398 , pp. 146-150
    • Kawabata, S.1    Tokunaga, F.2    Kugi, Y.3    Motoyama, S.4    Miura, Y.5    Hirata, M.6    Iwanaga, S.7
  • 23
    • 0030671306 scopus 로고    scopus 로고
    • Production of a DPP activity gradient in the early Drosophila embryo through the opposing actions of the SOG and TLD proteins
    • Marques G., Musacchio M., Shimell M.J., Wunnenberg S.K., Cho K.W., O'Connor M.B. Production of a DPP activity gradient in the early Drosophila embryo through the opposing actions of the SOG and TLD proteins. Cell. 91:1997;417-426
    • (1997) Cell , vol.91 , pp. 417-426
    • Marques, G.1    Musacchio, M.2    Shimell, M.J.3    Wunnenberg, S.K.4    Cho, K.W.5    O'Connor, M.B.6
  • 24
    • 0034671686 scopus 로고    scopus 로고
    • Notch signaling: From the outside in
    • Mumm J.S., Kopan R. Notch signaling: from the outside in. Dev. Biol. 228:2000;151-168
    • (2000) Dev. Biol. , vol.228 , pp. 151-168
    • Mumm, J.S.1    Kopan, R.2
  • 25
    • 0035543638 scopus 로고    scopus 로고
    • Regulation of midgut defensin production in the blood-sucking insect Stomoxys calcitrans
    • Munks R.J.L., Hamilton J.V., Lehane S.M., Lehane M.J. Regulation of midgut defensin production in the blood-sucking insect Stomoxys calcitrans. Insect Mol. Biol. 10:2001;561-571
    • (2001) Insect Mol. Biol. , vol.10 , pp. 561-571
    • Munks, R.J.L.1    Hamilton, J.V.2    Lehane, S.M.3    Lehane, M.J.4
  • 26
    • 0029167738 scopus 로고
    • Masquerade, a novel secreted serine proteinase-like molecule is required for somatic muscle attachment in Drosophila embryo
    • Murugasu-Oei B., Rodrigues V., Yang X., Chia W. Masquerade, a novel secreted serine proteinase-like molecule is required for somatic muscle attachment in Drosophila embryo. Gene Dev. 9:1995;139-154
    • (1995) Gene Dev. , vol.9 , pp. 139-154
    • Murugasu-Oei, B.1    Rodrigues, V.2    Yang, X.3    Chia, W.4
  • 27
    • 0035933371 scopus 로고    scopus 로고
    • Two isoforms of a member of the arthropod defensin from the soft tick, Ornithodoros moubata (Acari: Argasidae)
    • Nakajima Y., van Naters-Yasui A.V., Taylor D., Yamakawa M. Two isoforms of a member of the arthropod defensin from the soft tick, Ornithodoros moubata (Acari: Argasidae). Insect Biochem. Mol. Biol. 31:2001;747-751
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 747-751
    • Nakajima, Y.1    Van Naters-Yasui, A.V.2    Taylor, D.3    Yamakawa, M.4
  • 28
    • 0002785632 scopus 로고
    • Adaptive plasticity in amphibian metamorphosis
    • Newman R.A. Adaptive plasticity in amphibian metamorphosis. Bioscience. 42:1992;671-678
    • (1992) Bioscience , vol.42 , pp. 671-678
    • Newman, R.A.1
  • 29
    • 0033044637 scopus 로고    scopus 로고
    • Machine learning approaches to the prediction of signal peptides and other protein sorting signals
    • Nielsen H., Brunak S., von Heijne G. Machine learning approaches to the prediction of signal peptides and other protein sorting signals. Protein Eng. 12:1999;3-9
    • (1999) Protein Eng. , vol.12 , pp. 3-9
    • Nielsen, H.1    Brunak, S.2    Von Heijne, G.3
  • 30
    • 0033071821 scopus 로고    scopus 로고
    • Thrombin and trypsin receptors: The same mechanism of signalling on cellular surfaces
    • Olejar T., Nouza K. Thrombin and trypsin receptors: the same mechanism of signalling on cellular surfaces. Bratisl. Lek. L. 100:1999;75-79
    • (1999) Bratisl. Lek. L. , vol.100 , pp. 75-79
    • Olejar, T.1    Nouza, K.2
  • 31
    • 0032935811 scopus 로고    scopus 로고
    • Immunocompetence: A neglected life history trait or conspicuous red herring?
    • Owens I.P.F., Wilson K. Immunocompetence: a neglected life history trait or conspicuous red herring? TREE. 14:1999;170-172
    • (1999) TREE , vol.14 , pp. 170-172
    • Owens, I.P.F.1    Wilson, K.2
  • 32
    • 0029853148 scopus 로고    scopus 로고
    • WWW-query: An on-line retrieval system for biological sequence banks
    • Perrière G., Gouy M. WWW-query: an on-line retrieval system for biological sequence banks. Biochimie. 78:1996;364-369
    • (1996) Biochimie , vol.78 , pp. 364-369
    • Perrière, G.1    Gouy, M.2
  • 33
    • 0034141195 scopus 로고    scopus 로고
    • The ADAM gene family: Surface proteins with adhesion and protease activity
    • Primakoff P., Miles D.G. The ADAM gene family: surface proteins with adhesion and protease activity. Trends Genet. 16:2000;83-87
    • (2000) Trends Genet. , vol.16 , pp. 83-87
    • Primakoff, P.1    Miles, D.G.2
  • 34
    • 0031149265 scopus 로고    scopus 로고
    • Novel antibacterial peptides isolated from a European bumblebee, Bombus pascuorum (Hymenoptera, Apoidea)
    • Rees J.A., Moniatte M., Bulet P. Novel antibacterial peptides isolated from a European bumblebee, Bombus pascuorum (Hymenoptera, Apoidea). Insect Biochem. Mol. Biol. 27:1997;413-422
    • (1997) Insect Biochem. Mol. Biol. , vol.27 , pp. 413-422
    • Rees, J.A.1    Moniatte, M.2    Bulet, P.3
  • 35
    • 0001148480 scopus 로고
    • The evolution of wing dimorphism in insects
    • Roff D.A. The evolution of wing dimorphism in insects. Evolution. 40:1986;1009-1020
    • (1986) Evolution , vol.40 , pp. 1009-1020
    • Roff, D.A.1
  • 36
    • 0028163948 scopus 로고
    • Habitat persistence and the evolution of wing dimorphism in insects
    • Roff D.A. Habitat persistence and the evolution of wing dimorphism in insects. Am. Nat. 144:1994;772-798
    • (1994) Am. Nat. , vol.144 , pp. 772-798
    • Roff, D.A.1
  • 37
    • 0037472685 scopus 로고    scopus 로고
    • Serine proteases and their homologs in the Drosophila melanogaster genome: An initial analysis of sequence conservation and phylogenetic relationships
    • Ross J., Jiang H., Kanost M.R., Wang Y. Serine proteases and their homologs in the Drosophila melanogaster genome: an initial analysis of sequence conservation and phylogenetic relationships. Gene. 304:2003;117-131
    • (2003) Gene , vol.304 , pp. 117-131
    • Ross, J.1    Jiang, H.2    Kanost, M.R.3    Wang, Y.4
  • 39
    • 0009733197 scopus 로고
    • The polymorphic forms of Melittobia chalybii Ashmead and the determining factors involved in their production (Hymenoptera: Chalcidoidea, Eulophidae)
    • Schmieder R.G. The polymorphic forms of Melittobia chalybii Ashmead and the determining factors involved in their production (Hymenoptera: Chalcidoidea, Eulophidae). Biol. Bull. 65:1933;338-354
    • (1933) Biol. Bull. , vol.65 , pp. 338-354
    • Schmieder, R.G.1
  • 40
    • 0037224740 scopus 로고    scopus 로고
    • The ADAMs family of metalloproteases: Multidomain proteins with multiple functions
    • Seals D.F., Courtneidge S.A. The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev. 17:2003;7-30
    • (2003) Genes Dev. , vol.17 , pp. 7-30
    • Seals, D.F.1    Courtneidge, S.A.2
  • 41
    • 0031457037 scopus 로고    scopus 로고
    • The metalloprotease-disintegrin Kuzbanian participates in Notch activation during growth and patterning of Drosophila imaginal discs
    • Sotillos S., Roch F., Campuzano S. The metalloprotease-disintegrin Kuzbanian participates in Notch activation during growth and patterning of Drosophila imaginal discs. Development. 124:1997;4769-4779
    • (1997) Development , vol.124 , pp. 4769-4779
    • Sotillos, S.1    Roch, F.2    Campuzano, S.3
  • 42
    • 0028969678 scopus 로고
    • The metzincins-topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases
    • Stocker W., Grams F., Baumann U., Reinemer P., Gomis-Ruth F.X., McKay D.B., Bode W. The metzincins-topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. Protein Sci. 4:1995;823-840
    • (1995) Protein Sci. , vol.4 , pp. 823-840
    • Stocker, W.1    Grams, F.2    Baumann, U.3    Reinemer, P.4    Gomis-Ruth, F.X.5    McKay, D.B.6    Bode, W.7
  • 43
    • 0032964297 scopus 로고    scopus 로고
    • Blast 2 sequences - A new tool for comparing protein and nucleotide sequences
    • Tatusova T.A., Madden T.L. Blast 2 sequences - a new tool for comparing protein and nucleotide sequences. FEMS Microbiol. Lett. 174:1999;247-250
    • (1999) FEMS Microbiol. Lett. , vol.174 , pp. 247-250
    • Tatusova, T.A.1    Madden, T.L.2
  • 46
    • 0036849322 scopus 로고    scopus 로고
    • Extracellular peptidases of imaginal discs of Drosophila melanogaster
    • Wilson C.L., Shirras A.D., Isaac R.E. Extracellular peptidases of imaginal discs of Drosophila melanogaster. Peptides. 23:2002;2007-2014
    • (2002) Peptides , vol.23 , pp. 2007-2014
    • Wilson, C.L.1    Shirras, A.D.2    Isaac, R.E.3
  • 47
    • 0035188597 scopus 로고    scopus 로고
    • Two novel insect defensins from larvae of the cupreous chafer, Anomala cuprea: Purification, amino acid sequences and bacterial activity
    • Yamauchi H. Two novel insect defensins from larvae of the cupreous chafer, Anomala cuprea: purification, amino acid sequences and bacterial activity. Insect Biochem. Mol. Biol. 32:2001;75-84
    • (2001) Insect Biochem. Mol. Biol. , vol.32 , pp. 75-84
    • Yamauchi, H.1
  • 48
    • 0030464160 scopus 로고    scopus 로고
    • The Drosophila decapentaplegic and short gastrulation genes function antagonistically during adult wing vein development
    • Yu K., Sturtevant M.A., Biehs B., François V., Padgett R.W., Blackman R.K., Bier E. The Drosophila decapentaplegic and short gastrulation genes function antagonistically during adult wing vein development. Development. 122:1996;4033-4044
    • (1996) Development , vol.122 , pp. 4033-4044
    • Yu, K.1    Sturtevant, M.A.2    Biehs, B.3    François, V.4    Padgett, R.W.5    Blackman, R.K.6    Bier, E.7
  • 50
    • 0030887652 scopus 로고    scopus 로고
    • Physiology and ecology of dispersal polymorphism in insects
    • Zera A.J., Denno R.F. Physiology and ecology of dispersal polymorphism in insects. Annu. Rev. Entomol. 42:1997;207-231
    • (1997) Annu. Rev. Entomol. , vol.42 , pp. 207-231
    • Zera, A.J.1    Denno, R.F.2
  • 51
    • 0035677998 scopus 로고    scopus 로고
    • The physiology of life history trade-offs in animals
    • Zera A.J., Harshman L.G. The physiology of life history trade-offs in animals. Ann. Rev. Ecolog. Syst. 32:2001;95-126
    • (2001) Ann. Rev. Ecolog. Syst. , vol.32 , pp. 95-126
    • Zera, A.J.1    Harshman, L.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.