메뉴 건너뛰기




Volumn 31, Issue 3, 2010, Pages 489-497

Effects of Manduca sexta allatostatin and an analog on the pea aphid Acyrthosiphon pisum (Hemiptera: Aphididae) and degradation by enzymes from the aphid gut

Author keywords

Carboxypeptidase like; Cathepsin L cysteine protease; Chymotrypsin like; Myoinhibitory; Neuropeptide; Trypsin like

Indexed keywords

ALLATOSTATIN; CARBOXYPEPTIDASE; CATHEPSIN L; CHYMOTRYPSIN; CYSTEINE PROTEINASE; GLUTAMINE; TRYPSIN;

EID: 77049110092     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2009.06.017     Document Type: Article
Times cited : (22)

References (51)
  • 1
    • 0000722909 scopus 로고
    • A method for computing the effectiveness of an insecticide
    • Abbot W.S. A method for computing the effectiveness of an insecticide. J Econ Entomol 1925, 18:265-267.
    • (1925) J Econ Entomol , vol.18 , pp. 265-267
    • Abbot, W.S.1
  • 2
    • 0034955074 scopus 로고    scopus 로고
    • In vivo effects of Manduca sexta allatostatin and allatotropin on larvae of the tomato moth, Lacanobia oleracea
    • Audsley N., Weaver R.J., Edwards J.P. In vivo effects of Manduca sexta allatostatin and allatotropin on larvae of the tomato moth, Lacanobia oleracea. Physiol Entomol 2001, 26:181-188.
    • (2001) Physiol Entomol , vol.26 , pp. 181-188
    • Audsley, N.1    Weaver, R.J.2    Edwards, J.P.3
  • 3
    • 0036126229 scopus 로고    scopus 로고
    • Metabolism of Manduca sexta allatostatin by haemolymph of larvae of the tomato moth, Lacanobia oleracea
    • Audsley N., Weaver R.J., Edwards J.P. Metabolism of Manduca sexta allatostatin by haemolymph of larvae of the tomato moth, Lacanobia oleracea. Peptides 2002, 23:717-723.
    • (2002) Peptides , vol.23 , pp. 717-723
    • Audsley, N.1    Weaver, R.J.2    Edwards, J.P.3
  • 4
    • 0036848395 scopus 로고    scopus 로고
    • Degradation of Manduca sexta allatostatin and allatotropin by proteases associated with the foregut of Lacanobia oleracea larvae
    • Audsley N., Weaver R.J., Edwards J.P. Degradation of Manduca sexta allatostatin and allatotropin by proteases associated with the foregut of Lacanobia oleracea larvae. Peptides 2002, 23:2015-2023.
    • (2002) Peptides , vol.23 , pp. 2015-2023
    • Audsley, N.1    Weaver, R.J.2    Edwards, J.P.3
  • 5
    • 39149084662 scopus 로고    scopus 로고
    • Transepithelial flux of an allatostatin and analogs across the anterior midgut of Manduca sexta larvae in vitro
    • Audsley N., Matthews J., Nachman R.J., Weaver R.J. Transepithelial flux of an allatostatin and analogs across the anterior midgut of Manduca sexta larvae in vitro. Peptides 2008, 29:286-294.
    • (2008) Peptides , vol.29 , pp. 286-294
    • Audsley, N.1    Matthews, J.2    Nachman, R.J.3    Weaver, R.J.4
  • 6
    • 46549083595 scopus 로고    scopus 로고
    • Allatoregulatory peptides in Lepidoptera, structures, distribution and functions
    • Audsley N., Matthews H.J., Price N.R., Weaver R.J. Allatoregulatory peptides in Lepidoptera, structures, distribution and functions. J Insect Physiol 2008, 54(6):969-980.
    • (2008) J Insect Physiol , vol.54 , Issue.6 , pp. 969-980
    • Audsley, N.1    Matthews, H.J.2    Price, N.R.3    Weaver, R.J.4
  • 7
    • 65049083254 scopus 로고    scopus 로고
    • Neuropeptides associated with the regulation of feeding in insects
    • Audsley N., Weaver R.J. Neuropeptides associated with the regulation of feeding in insects. Gen Comp Endocrin 2009, 162:93-104.
    • (2009) Gen Comp Endocrin , vol.162 , pp. 93-104
    • Audsley, N.1    Weaver, R.J.2
  • 8
    • 0010277167 scopus 로고
    • Intestinal absorption of proctolin in Helicoverpa armigera (Lepidoptera; Noctuidae) larvae
    • Bavoso A., Falabella P., Giacometti R., Halane A.J., Ostuni A., Pennacchio F., et al. Intestinal absorption of proctolin in Helicoverpa armigera (Lepidoptera; Noctuidae) larvae. Redia 1995, 78:173-185.
    • (1995) Redia , vol.78 , pp. 173-185
    • Bavoso, A.1    Falabella, P.2    Giacometti, R.3    Halane, A.J.4    Ostuni, A.5    Pennacchio, F.6
  • 9
    • 0242406849 scopus 로고    scopus 로고
    • Typsin-modulating oostatic factor: a potential new larvicide for mosquito control
    • Borovsky D. Typsin-modulating oostatic factor: a potential new larvicide for mosquito control. J Exp Biol 2003, 206:3869-3875.
    • (2003) J Exp Biol , vol.206 , pp. 3869-3875
    • Borovsky, D.1
  • 10
    • 0029012218 scopus 로고
    • Feeding the mosquito Aedes aegypti with TMOF and its analogues; effect on trypsin biosynthesis and egg development
    • Borovsky D., Mahmood F. Feeding the mosquito Aedes aegypti with TMOF and its analogues; effect on trypsin biosynthesis and egg development. Regul Peptides 1995, 57:273-281.
    • (1995) Regul Peptides , vol.57 , pp. 273-281
    • Borovsky, D.1    Mahmood, F.2
  • 12
    • 49749124236 scopus 로고    scopus 로고
    • Impacts of agricultural change for farmland biodiversity
    • Royal Society of Chemistry Publishing, R. Hester, R.M. Harrison (Eds.) Biodiversity under threat
    • Boatman N.D., Parry H.R., Bishop J.D., Cuthbertson A.G.S. Impacts of agricultural change for farmland biodiversity. Issues in environmental science and technology 2007, vol. 25:1-32. Royal Society of Chemistry Publishing. R. Hester, R.M. Harrison (Eds.).
    • (2007) Issues in environmental science and technology , vol.vol. 25 , pp. 1-32
    • Boatman, N.D.1    Parry, H.R.2    Bishop, J.D.3    Cuthbertson, A.G.S.4
  • 13
    • 0003155058 scopus 로고    scopus 로고
    • Appendix II Commercially available proteases
    • Oxford University Press, Oxford, R.J. Beynon, J.S. Bond (Eds.)
    • Bond J.S. Appendix II Commercially available proteases. Proteolytic enzymes: a practical approach 1996, 232-240. Oxford University Press, Oxford. R.J. Beynon, J.S. Bond (Eds.).
    • (1996) Proteolytic enzymes: a practical approach , pp. 232-240
    • Bond, J.S.1
  • 14
    • 0033921079 scopus 로고    scopus 로고
    • Salivary proteins of aphids, a pilot study on identification, separation and immunolocalisation
    • Cherqui A., Tjallingii W.F. Salivary proteins of aphids, a pilot study on identification, separation and immunolocalisation. J Insect Physiol 2000, 46:1177-1186.
    • (2000) J Insect Physiol , vol.46 , pp. 1177-1186
    • Cherqui, A.1    Tjallingii, W.F.2
  • 15
    • 53149144259 scopus 로고    scopus 로고
    • In silico analyses of peptide paracrines/hormones in Aphidoidea
    • Christie A.E. In silico analyses of peptide paracrines/hormones in Aphidoidea. Gen Comp Endo 2008, 159:67-79.
    • (2008) Gen Comp Endo , vol.159 , pp. 67-79
    • Christie, A.E.1
  • 16
    • 0242684461 scopus 로고    scopus 로고
    • Midgut adaptation and digestive enzyme distribution in a phloem feeding insect, the pea aphid Acyrthosiphon pisum
    • Cristofoletti P.T., Ribeiro A.F., Deraison C., Rahbé Y., Terra W.R. Midgut adaptation and digestive enzyme distribution in a phloem feeding insect, the pea aphid Acyrthosiphon pisum. J Insect Physiol 2003, 49:11-24.
    • (2003) J Insect Physiol , vol.49 , pp. 11-24
    • Cristofoletti, P.T.1    Ribeiro, A.F.2    Deraison, C.3    Rahbé, Y.4    Terra, W.R.5
  • 17
    • 33845507459 scopus 로고    scopus 로고
    • Characterization of a membrane bound aminopeptidase purified from Acyrthosiphon pisum midgut cells
    • Cristofoletti P.T., de Sousa F.A.M., Rahbé Y., Terra W.R. Characterization of a membrane bound aminopeptidase purified from Acyrthosiphon pisum midgut cells. FEBS J 2006, 273(24):5574-5588.
    • (2006) FEBS J , vol.273 , Issue.24 , pp. 5574-5588
    • Cristofoletti, P.T.1    de Sousa, F.A.M.2    Rahbé, Y.3    Terra, W.R.4
  • 21
    • 0030285860 scopus 로고    scopus 로고
    • Snowdrop lectin inhibits development and decreases fecundity of the glasshouse potato aphid (Aulacorthum solani) when administered in vitro and via transgenic plants both in laboratory and glasshouse trials
    • Down R.E., Gatehouse A.M.R., Hamilton W.D.O., Gatehouse J.A. Snowdrop lectin inhibits development and decreases fecundity of the glasshouse potato aphid (Aulacorthum solani) when administered in vitro and via transgenic plants both in laboratory and glasshouse trials. J Insect Physiol 1996, 42:1035-1045.
    • (1996) J Insect Physiol , vol.42 , pp. 1035-1045
    • Down, R.E.1    Gatehouse, A.M.R.2    Hamilton, W.D.O.3    Gatehouse, J.A.4
  • 22
    • 0032800156 scopus 로고    scopus 로고
    • Protease activity in the larval stages of the parasitoid wasp, Eulophus pennicornis (Nees) (Hymenoptera: Eulophidae); effects of protease inhibitors
    • Down R.E., Ford L., Mosson H.J., Fitches E., Gatehouse J.A., Gatehouse A.M.R. Protease activity in the larval stages of the parasitoid wasp, Eulophus pennicornis (Nees) (Hymenoptera: Eulophidae); effects of protease inhibitors. Parasitology 1999, 119:157-166.
    • (1999) Parasitology , vol.119 , pp. 157-166
    • Down, R.E.1    Ford, L.2    Mosson, H.J.3    Fitches, E.4    Gatehouse, J.A.5    Gatehouse, A.M.R.6
  • 23
    • 32044468332 scopus 로고    scopus 로고
    • Insecticidal spider venom toxin fused to snowdrop lectin is toxic to the peach-potato aphid, Myzus persicae (Hemiptera: Aphididae) and the rice brown planthopper, Nilaparvata lugens (Hemiptera: Delphacidae)
    • Down R.E., Fitches E.C., Wiles D.P., Corti P., Bell H.A., Gatehouse J.A., et al. Insecticidal spider venom toxin fused to snowdrop lectin is toxic to the peach-potato aphid, Myzus persicae (Hemiptera: Aphididae) and the rice brown planthopper, Nilaparvata lugens (Hemiptera: Delphacidae). Pest Manag Sci 2006, 62:77-85.
    • (2006) Pest Manag Sci , vol.62 , pp. 77-85
    • Down, R.E.1    Fitches, E.C.2    Wiles, D.P.3    Corti, P.4    Bell, H.A.5    Gatehouse, J.A.6
  • 24
    • 0001196169 scopus 로고
    • Influence of the amino acid balance on the improvement of an artificial diet for a biotype of Acyrthosiphon pisum (Homoptera: Aphididae)
    • Febvay G., Delobel B., Rahbé Y. Influence of the amino acid balance on the improvement of an artificial diet for a biotype of Acyrthosiphon pisum (Homoptera: Aphididae). Can J Zoolog 1988, 66:2449-2453.
    • (1988) Can J Zoolog , vol.66 , pp. 2449-2453
    • Febvay, G.1    Delobel, B.2    Rahbé, Y.3
  • 25
    • 19244383044 scopus 로고    scopus 로고
    • Insect peptide hormones: a selective review of their physiology and potential application for pest control
    • Gäde G., Goldsworthy G.J. Insect peptide hormones: a selective review of their physiology and potential application for pest control. Pest Manag Sci 2003, 59:1063-1075.
    • (2003) Pest Manag Sci , vol.59 , pp. 1063-1075
    • Gäde, G.1    Goldsworthy, G.J.2
  • 26
    • 50649088005 scopus 로고    scopus 로고
    • Identification of Lys-Pro-Gln as a Novel Cleavage Site Specificity of Saliva-associated Proteases
    • Helmerhorst E.J., Xiuli S., Salih E., Oppenheim F.G. Identification of Lys-Pro-Gln as a Novel Cleavage Site Specificity of Saliva-associated Proteases. J Biol Chem 2008, 283(29):19957-19966.
    • (2008) J Biol Chem , vol.283 , Issue.29 , pp. 19957-19966
    • Helmerhorst, E.J.1    Xiuli, S.2    Salih, E.3    Oppenheim, F.G.4
  • 27
    • 33746074833 scopus 로고    scopus 로고
    • Soybean aphid resistance in soybean Jackson is controlled by a single dominant gene
    • Hill C.B., Li Y., Hartman G.L. Soybean aphid resistance in soybean Jackson is controlled by a single dominant gene. Crop Sci 2006, 46:1606-1608.
    • (2006) Crop Sci , vol.46 , pp. 1606-1608
    • Hill, C.B.1    Li, Y.2    Hartman, G.L.3
  • 28
    • 0032445750 scopus 로고    scopus 로고
    • Recent advances in hormones in insect pest control
    • Hoffmann K.H., Lorenz M.W. Recent advances in hormones in insect pest control. Phytoparasitica 1998, 26:323-330.
    • (1998) Phytoparasitica , vol.26 , pp. 323-330
    • Hoffmann, K.H.1    Lorenz, M.W.2
  • 29
    • 38249036101 scopus 로고
    • Speculations on biotechnology applications for insect neuroendocrine research
    • Keeley L.L., Hayes T.K. Speculations on biotechnology applications for insect neuroendocrine research. Insect Biochem 1987, 17:639-651.
    • (1987) Insect Biochem , vol.17 , pp. 639-651
    • Keeley, L.L.1    Hayes, T.K.2
  • 31
    • 34547629936 scopus 로고    scopus 로고
    • Insecticide resistance status of Myzus persicae (Hemiptera: Aphididae) populations from peach and tobacco in mainland Greece
    • Margaritopoulos J.T., Skouras P.J., Nikolaidou P., Manolikaki J., Maritsa K., Tsamandani K., et al. Insecticide resistance status of Myzus persicae (Hemiptera: Aphididae) populations from peach and tobacco in mainland Greece. Pest Manag Sci 2007, 63:821-829.
    • (2007) Pest Manag Sci , vol.63 , pp. 821-829
    • Margaritopoulos, J.T.1    Skouras, P.J.2    Nikolaidou, P.3    Manolikaki, J.4    Maritsa, K.5    Tsamandani, K.6
  • 32
    • 53549110516 scopus 로고    scopus 로고
    • In vitro and in vivo effects of myo-active peptides on larvae of the tomato moth Lacanobia oleracea and the cotton leaf worm Spodoptera littoralis (Lepidoptera; Noctuidae)
    • Matthews H.J., Audsley N., Weaver R.J. In vitro and in vivo effects of myo-active peptides on larvae of the tomato moth Lacanobia oleracea and the cotton leaf worm Spodoptera littoralis (Lepidoptera; Noctuidae). Arch Insect Biochem Physiol 2008, 69:60-69.
    • (2008) Arch Insect Biochem Physiol , vol.69 , pp. 60-69
    • Matthews, H.J.1    Audsley, N.2    Weaver, R.J.3
  • 33
    • 0032960554 scopus 로고    scopus 로고
    • Aphid saliva
    • Miles P.W. Aphid saliva. Biol Rev 1999, 74(1):41-85.
    • (1999) Biol Rev , vol.74 , Issue.1 , pp. 41-85
    • Miles, P.W.1
  • 34
    • 0032954543 scopus 로고    scopus 로고
    • Haemolymph and tissue-bound peptidase-resistant analogues of the insect allatostatins
    • Nachman R.J., Garside C.S., Tobe S.S. Haemolymph and tissue-bound peptidase-resistant analogues of the insect allatostatins. Peptides 1999, 20:23-29.
    • (1999) Peptides , vol.20 , pp. 23-29
    • Nachman, R.J.1    Garside, C.S.2    Tobe, S.S.3
  • 35
    • 0036848483 scopus 로고    scopus 로고
    • Enhanced oral availability/pheromonotropic activity of peptidase-resistant topical amphiphilic analogs of pyrokinin/PBAN insect neuropeptides
    • Nachman R.J., Teal P.E.A., Strey A. Enhanced oral availability/pheromonotropic activity of peptidase-resistant topical amphiphilic analogs of pyrokinin/PBAN insect neuropeptides. Peptides 2002, 23:2035-2043.
    • (2002) Peptides , vol.23 , pp. 2035-2043
    • Nachman, R.J.1    Teal, P.E.A.2    Strey, A.3
  • 36
    • 0036126195 scopus 로고    scopus 로고
    • Enhanced in vivo activity of peptidase-resistant analogs of the insect kinin neuropeptide family
    • Nachman R.J., Strey A., Isaac E., Pryor N., Lopez J.D., Deng J.G., et al. Enhanced in vivo activity of peptidase-resistant analogs of the insect kinin neuropeptide family. Peptides 2002, 23:735-745.
    • (2002) Peptides , vol.23 , pp. 735-745
    • Nachman, R.J.1    Strey, A.2    Isaac, E.3    Pryor, N.4    Lopez, J.D.5    Deng, J.G.6
  • 37
    • 0002793994 scopus 로고
    • Alimentary tract
    • Elsevier Science Publishers B.V., Amsterdam, A.K. Minks, P. Harrewijn (Eds.) World crop pests
    • Ponsen M.B. Alimentary tract. Aphids their biology, natural enemies and control 1987, vol. 2A:79-97. Elsevier Science Publishers B.V., Amsterdam. A.K. Minks, P. Harrewijn (Eds.).
    • (1987) Aphids their biology, natural enemies and control , vol.vol. 2A , pp. 79-97
    • Ponsen, M.B.1
  • 38
    • 0027805377 scopus 로고
    • Antimetabolic effects of plant lectins and fungal enzymes on the nymphal stages of two important rice pests, Nilaparvata lugens and Nephotettix cincticeps
    • Powell K.S., Gatehouse A.M.R., Hilder V.A., Gatehouse J.A. Antimetabolic effects of plant lectins and fungal enzymes on the nymphal stages of two important rice pests, Nilaparvata lugens and Nephotettix cincticeps. Entomol Exp Appl 1993, 66:119-126.
    • (1993) Entomol Exp Appl , vol.66 , pp. 119-126
    • Powell, K.S.1    Gatehouse, A.M.R.2    Hilder, V.A.3    Gatehouse, J.A.4
  • 39
    • 0037373527 scopus 로고    scopus 로고
    • Toxicity to the pea aphid Acyrthosiphon pisum of anti-chymotrypsin isoforms and fragments of Bowman-Birk protease inhibitors from pea seeds
    • Rahbé Y., Ferrasson E., Rabesona H., Quillien L. Toxicity to the pea aphid Acyrthosiphon pisum of anti-chymotrypsin isoforms and fragments of Bowman-Birk protease inhibitors from pea seeds. Insect Biochem Mol 2003, 33:299-306.
    • (2003) Insect Biochem Mol , vol.33 , pp. 299-306
    • Rahbé, Y.1    Ferrasson, E.2    Rabesona, H.3    Quillien, L.4
  • 40
    • 0028814176 scopus 로고
    • Toxicity of lectins and processing of ingested proteins in the pea aphid Acyrthosiphon pisum
    • Rahbé Y., Sauvion N., Febvay G., Peumans W.J., Gatehouse A.M.R. Toxicity of lectins and processing of ingested proteins in the pea aphid Acyrthosiphon pisum. Entomol Exp Appl 1995, 76:143-155.
    • (1995) Entomol Exp Appl , vol.76 , pp. 143-155
    • Rahbé, Y.1    Sauvion, N.2    Febvay, G.3    Peumans, W.J.4    Gatehouse, A.M.R.5
  • 41
    • 0028087210 scopus 로고
    • Pheromonotropic activity of orally administered PBAN and its analogues in Helicoverpa zea
    • Raina A.K., Rafeali A., Kingan T.G. Pheromonotropic activity of orally administered PBAN and its analogues in Helicoverpa zea. J. Insect Physiol 1994, 40:393-397.
    • (1994) J. Insect Physiol , vol.40 , pp. 393-397
    • Raina, A.K.1    Rafeali, A.2    Kingan, T.G.3
  • 42
    • 0037020020 scopus 로고    scopus 로고
    • Neuropeptides and peptide hormones in Anopheles gambiae
    • Riehle M.A., Garczynski S.F., Crim J.W., Hill C.A., Brown M.R. Neuropeptides and peptide hormones in Anopheles gambiae. Science 2002, 298(5591):172-175.
    • (2002) Science , vol.298 , Issue.5591 , pp. 172-175
    • Riehle, M.A.1    Garczynski, S.F.2    Crim, J.W.3    Hill, C.A.4    Brown, M.R.5
  • 43
    • 0005273798 scopus 로고
    • Characteristics and nature of proteases from the alimentary canal of the pea aphid, Acyrthosiphon pisum (Harris) (Homoptera: Aphididae)
    • Srivastava P.N., Auclair J.L. Characteristics and nature of proteases from the alimentary canal of the pea aphid, Acyrthosiphon pisum (Harris) (Homoptera: Aphididae). J Insect Physiol 1963, 9:469-474.
    • (1963) J Insect Physiol , vol.9 , pp. 469-474
    • Srivastava, P.N.1    Auclair, J.L.2
  • 44
    • 0033392275 scopus 로고    scopus 로고
    • Development of amphiphylic mimics of insect neuropeptides for pest control
    • Teal P.E.A., Meredith J.A., Nachman R.J. Development of amphiphylic mimics of insect neuropeptides for pest control. Ann N Y Acad Sci 1999, 897:348-360.
    • (1999) Ann N Y Acad Sci , vol.897 , pp. 348-360
    • Teal, P.E.A.1    Meredith, J.A.2    Nachman, R.J.3
  • 45
    • 0027999854 scopus 로고
    • Insect digestive enzymes: properties, compartmentalization and function
    • Terra W.R., Ferreira C. Insect digestive enzymes: properties, compartmentalization and function. Comp Biochem Physiol 1994, 109B:1-62.
    • (1994) Comp Biochem Physiol , vol.109 B , pp. 1-62
    • Terra, W.R.1    Ferreira, C.2
  • 46
    • 0034008834 scopus 로고    scopus 로고
    • Allatostatin-like and AKH/HrTH-like peptides in the aphid Megoura viciae
    • Tilley S.B., Weaver R.J., Isaac R.E. Allatostatin-like and AKH/HrTH-like peptides in the aphid Megoura viciae. Gen Comp Endocr 2000, 117(3):355-365.
    • (2000) Gen Comp Endocr , vol.117 , Issue.3 , pp. 355-365
    • Tilley, S.B.1    Weaver, R.J.2    Isaac, R.E.3
  • 47
    • 61349152304 scopus 로고    scopus 로고
    • Allatostatin C and its paralog allatostatin double C: the arthropod somatostatins
    • Veenstra J.A. Allatostatin C and its paralog allatostatin double C: the arthropod somatostatins. Ins Biochem Mol Biol 2000, 39:161-170.
    • (2000) Ins Biochem Mol Biol , vol.39 , pp. 161-170
    • Veenstra, J.A.1
  • 49
    • 0034813414 scopus 로고    scopus 로고
    • Molecular cloning, genomic organization, and expression of a C-type (Manduca sexta-type) allatostatin preprohormone from Drosophila melanogaster
    • Williamson M., Lenz C., Winther A.M.E., Nassel D.R., Grimmelikhuijzen C.J.P. Molecular cloning, genomic organization, and expression of a C-type (Manduca sexta-type) allatostatin preprohormone from Drosophila melanogaster. Biochem Biophys Res Commun 2001, 282:124-130.
    • (2001) Biochem Biophys Res Commun , vol.282 , pp. 124-130
    • Williamson, M.1    Lenz, C.2    Winther, A.M.E.3    Nassel, D.R.4    Grimmelikhuijzen, C.J.P.5
  • 50
    • 39149104959 scopus 로고    scopus 로고
    • Neuropeptides of the beetle, Tenebrio molitor identified using MALDI-TOF mass spectrometry and deduced sequences from the Tribolium castaneum genome
    • Weaver R.J., Audsley N. Neuropeptides of the beetle, Tenebrio molitor identified using MALDI-TOF mass spectrometry and deduced sequences from the Tribolium castaneum genome. Peptides 2008, 29:168-178.
    • (2008) Peptides , vol.29 , pp. 168-178
    • Weaver, R.J.1    Audsley, N.2
  • 51
    • 0035186967 scopus 로고    scopus 로고
    • In vitro degradation of the Neb-Trypsin Modulating Oostatic Factor (Neb-TMOF) in gut luminal content and hemolymph of the grey fleshfly, Neobellieria bullata
    • Zhu W., Vandingenen A., Huybrechts R., Baggerman G., De Loof A., Poulos C.P., et al. In vitro degradation of the Neb-Trypsin Modulating Oostatic Factor (Neb-TMOF) in gut luminal content and hemolymph of the grey fleshfly, Neobellieria bullata. Insect Biochem Mol Biol 2001, 31:87-95.
    • (2001) Insect Biochem Mol Biol , vol.31 , pp. 87-95
    • Zhu, W.1    Vandingenen, A.2    Huybrechts, R.3    Baggerman, G.4    De Loof, A.5    Poulos, C.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.