메뉴 건너뛰기




Volumn 262, Issue 3, 1999, Pages 627-636

Sequencing and characterization of the citrus weevil, Diaprepes abbreviatus, trypsin cDNA. Effect of Aedes trypsin modulating oostatic factor on trypsin biosynthesis

Author keywords

cDNA sequence; Peptide hormone; Trypsin gene; Trypsin modulating oostatic factor; Weevil

Indexed keywords

COMPLEMENTARY DNA; OOSTATIC FACTOR; PEPTIDE HORMONE; SOYBEAN TRYPSIN INHIBITOR; TRYPSIN; UNCLASSIFIED DRUG;

EID: 0033563998     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00411.x     Document Type: Article
Times cited : (27)

References (62)
  • 1
    • 0029108932 scopus 로고
    • Gypsy moth midgut proteinases: Purification and characterization of luminal trypsin, elastase and the brush border membrane leucine aminopeptidase
    • 1. Valaitis, A.P. (1995) Gypsy moth midgut proteinases: purification and characterization of luminal trypsin, elastase and the brush border membrane leucine aminopeptidase. Insect Biochem. Molec. Biol. 25, 139-149.
    • (1995) Insect Biochem. Molec. Biol. , vol.25 , pp. 139-149
    • Valaitis, A.P.1
  • 2
    • 0027833635 scopus 로고
    • Effect of soybean protease inhibitors on the growth and development of larval Helicoverpa armigera
    • 2. Johnston, K.A., Gatehouse, J.A. & Anstee, J.H. (1993) Effect of soybean protease inhibitors on the growth and development of larval Helicoverpa armigera. J. Insect Physiol. 39, 657-664.
    • (1993) J. Insect Physiol. , vol.39 , pp. 657-664
    • Johnston, K.A.1    Gatehouse, J.A.2    Anstee, J.H.3
  • 3
    • 84990406880 scopus 로고
    • Isolation and characterization of highly purified mosquito oostatic hormone
    • 3. Borovsky, D. (1985) Isolation and characterization of highly purified mosquito oostatic hormone. Arch. Insect Biochem. Physiol. 2, 333-349.
    • (1985) Arch. Insect Biochem. Physiol. , vol.2 , pp. 333-349
    • Borovsky, D.1
  • 4
    • 0025242490 scopus 로고
    • Mosquito oostatic factor: A novel decapeptide modulating trypsin-like enzyme biosynthesis in the midgut
    • 4. Borovsky, D., Carlson, D.A., Griffin, P.R., Shabanowitz, J. & Hunt, D.F. (1990) Mosquito oostatic factor: a novel decapeptide modulating trypsin-like enzyme biosynthesis in the midgut. FASEB J. 4, 3015-3020.
    • (1990) FASEB J. , vol.4 , pp. 3015-3020
    • Borovsky, D.1    Carlson, D.A.2    Griffin, P.R.3    Shabanowitz, J.4    Hunt, D.F.5
  • 5
    • 0027661492 scopus 로고
    • Mass spectrometry and characterization of Aedes aegypti trypsin modulating oostatic factor (TMOF) and its analogs
    • 5. Borovsky, D., Carlson, D.A., Griffin, P.R., Shabanowitz, J. & Hunt, D.F. (1993) Mass spectrometry and characterization of Aedes aegypti trypsin modulating oostatic factor (TMOF) and its analogs. Insect Biochem. Mol. Biol. 23, 703-712.
    • (1993) Insect Biochem. Mol. Biol. , vol.23 , pp. 703-712
    • Borovsky, D.1    Carlson, D.A.2    Griffin, P.R.3    Shabanowitz, J.4    Hunt, D.F.5
  • 6
    • 84990468035 scopus 로고
    • Biosynthesis, secretion and cytoimmunochemistry of trypsin modulating oostatic factor of Aedes aegypti
    • 6. Borovsky, D., Song, Q., Ma, M. & Carlson, D.A. (1994) Biosynthesis, secretion and cytoimmunochemistry of trypsin modulating oostatic factor of Aedes aegypti. Arch. Insect Biochem. Physiol. 27, 27-38.
    • (1994) Arch. Insect Biochem. Physiol. , vol.27 , pp. 27-38
    • Borovsky, D.1    Song, Q.2    Ma, M.3    Carlson, D.A.4
  • 8
    • 0001862682 scopus 로고
    • Digestion
    • (Rockstein, M., ed.) Academic Press, New York
    • 8. House, H.L. (1974) Digestion. In The Physiology of Insecta (Rockstein, M., ed.) Vol. 5, pp. 63-117. Academic Press, New York.
    • (1974) The Physiology of Insecta , vol.5 , pp. 63-117
    • House, H.L.1
  • 9
    • 0001794182 scopus 로고
    • Nutrition and digestive organs
    • (Blum, M.S., ed.), Wiley, New York
    • 9. McFarlane, J.E. (1985) Nutrition and digestive organs. In Fundamentals of Insect Physiology (Blum, M.S., ed.), pp. 59-89. Wiley, New York.
    • (1985) Fundamentals of Insect Physiology , pp. 59-89
    • McFarlane, J.E.1
  • 10
    • 0001024899 scopus 로고
    • Biochemistry of digestion
    • (Kurkut, G.A. & Gilbert, L.I., eds) Pergamon Press, London
    • 10. Applebaum, S.W. (1985) Biochemistry of digestion. In Comparative Physiology, Biochemistry and Pharmacology of Insects (Kurkut, G.A. & Gilbert, L.I., eds) Vol. 4, pp. 279-311. Pergamon Press, London.
    • (1985) Comparative Physiology, Biochemistry and Pharmacology of Insects , vol.4 , pp. 279-311
    • Applebaum, S.W.1
  • 12
    • 0029977174 scopus 로고    scopus 로고
    • Midgut proteinases in three divergent species of Coleoptera
    • 12. Terra, W.R. & Cristofoletti, P.T. (1996) Midgut proteinases in three divergent species of Coleoptera. Comp. Biochem. Physiol. 113B, 725-730.
    • (1996) Comp. Biochem. Physiol. , vol.113 B , pp. 725-730
    • Terra, W.R.1    Cristofoletti, P.T.2
  • 13
    • 0000786243 scopus 로고
    • Digestive proteinases of Sitophilus weevils (Coleoptera: Curculionidae) and their response to inhibitors from wheat and corn flour
    • 13. Baker, J.E. (1982) Digestive proteinases of Sitophilus weevils (Coleoptera: Curculionidae) and their response to inhibitors from wheat and corn flour. Can. J. Zool. 60, 3206-3214.
    • (1982) Can. J. Zool. , vol.60 , pp. 3206-3214
    • Baker, J.E.1
  • 14
    • 0001940620 scopus 로고
    • Examination of midgut luminal proteinase activity in six economically important insects
    • 14. Purcell, J.P., Greenplate, J.T. & Sammons, R.D. (1992) Examination of midgut luminal proteinase activity in six economically important insects. Insect Biochem. Molec. Biol. 22, 41-47.
    • (1992) Insect Biochem. Molec. Biol. , vol.22 , pp. 41-47
    • Purcell, J.P.1    Greenplate, J.T.2    Sammons, R.D.3
  • 15
    • 0028427875 scopus 로고
    • Sequence of three cDNAs encoding an alkaline midgut trypsin from. Manduca sexta
    • 15. Peterson, A.M., Barillas-Mury, C.V. & Wells, M.A. (1994) Sequence of three cDNAs encoding an alkaline midgut trypsin from. Manduca sexta. Insect Biochem. Mol. Biol. 24, 463-471.
    • (1994) Insect Biochem. Mol. Biol. , vol.24 , pp. 463-471
    • Peterson, A.M.1    Barillas-Mury, C.V.2    Wells, M.A.3
  • 16
    • 0029360599 scopus 로고
    • Genomic organization and expression of a trypsin gene from the spruce budworm, Choristoneura fumiferana
    • 16. Wang, S., Young, F. & Hicky, D.A. (1995) Genomic organization and expression of a trypsin gene from the spruce budworm, Choristoneura fumiferana. Insect Biochem. Molec. Biol. 25, 899-908.
    • (1995) Insect Biochem. Molec. Biol. , vol.25 , pp. 899-908
    • Wang, S.1    Young, F.2    Hicky, D.A.3
  • 17
    • 0000830174 scopus 로고
    • cDNA and deduced amino acid sequence of a blood meal-induced trypsin from the mosquito, Aedes aegypti
    • 17. Barillas-Mury, C., Graf, R., Hagedorn, H.H. & Wells, M.A. (1991) cDNA and deduced amino acid sequence of a blood meal-induced trypsin from the mosquito, Aedes aegypti. Insect Biochem. 21, 825-831.
    • (1991) Insect Biochem. , vol.21 , pp. 825-831
    • Barillas-Mury, C.1    Graf, R.2    Hagedorn, H.H.3    Wells, M.A.4
  • 18
    • 0027898483 scopus 로고
    • Isolation, sequencing and characterization of two cDNA clones coding for trypsin-like enzymes from the midgut of Aedes aegypti
    • 18. Kalhok, S.E., Tabak, L.M., Prosser, D.E., Brook, W., Downe, A.E.R. & White, B.N. (1993) Isolation, sequencing and characterization of two cDNA clones coding for trypsin-like enzymes from the midgut of Aedes aegypti. Insect Mol. Biol. 2, 71-79.
    • (1993) Insect Mol. Biol. , vol.2 , pp. 71-79
    • Kalhok, S.E.1    Tabak, L.M.2    Prosser, D.E.3    Brook, W.4    Downe, A.E.R.5    White, B.N.6
  • 19
    • 0027296176 scopus 로고
    • Members of a trypsin gene family in Anopheles gambiae are induced in the gut by the blood meal
    • 19. Muller, H.M., Crampton, J.M., del la Torre, A., Sinden, R. & Crisanti, A. (1993) Members of a trypsin gene family in Anopheles gambiae are induced in the gut by the blood meal. EMBO J. 12, 2891-2900.
    • (1993) EMBO J. , vol.12 , pp. 2891-2900
    • Muller, H.M.1    Crampton, J.M.2    Del La Torre, A.3    Sinden, R.4    Crisanti, A.5
  • 20
    • 0030005957 scopus 로고    scopus 로고
    • Molecular sequencing and modeling of Neobellieria bullata trypsin; evidence for translational control by Neobellieria trypsin-modulating oostatic factor
    • 20. Borovsky, D., Janssen, I., Vanden Broeck, J., Huybrechts, R., Verhaert, P., De Bondt, H.L., Bylemans, D. & De Loof, A. (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    De Bondt, H.L.6    Bylemans, D.7    De Loof, A.8
  • 21
  • 22
    • 0031081053 scopus 로고    scopus 로고
    • Juvenile hormone controls early trypsin gene transcription in the midgut of Aedes Aegypti
    • 22. Noriega, F.G., Shah, D.K. & Wells, M.A. (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
  • 23
    • 0028815857 scopus 로고
    • Studies on the synthesis and secretion of trypsin in the midgut of Stomoxys calcitrans
    • 23. Moffatt, M., Blakemore, D. & Lehane, M.J. (1995) Studies on the synthesis and secretion of trypsin in the midgut of Stomoxys calcitrans. Comp. Biochem. Physiol. 110B, 291-300.
    • (1995) Comp. Biochem. Physiol. , vol.110 B , pp. 291-300
    • Moffatt, M.1    Blakemore, D.2    Lehane, M.J.3
  • 24
    • 0029240554 scopus 로고
    • Early trypsin activity is part of the signal transduction system that activates transcription of the late trypsin gene in the midgut of the mosquito, Aedes aegypti
    • 24. Barillas-Mury, C., Noriega, F.G. & Wells, M.A. (1995) Early trypsin activity is part of the signal transduction system that activates transcription of the late trypsin gene in the midgut of the mosquito, Aedes aegypti. Insect Biochem. Molec. Biol. 25, 241-246.
    • (1995) Insect Biochem. Molec. Biol. , vol.25 , pp. 241-246
    • Barillas-Mury, C.1    Noriega, F.G.2    Wells, M.A.3
  • 26
    • 84990474934 scopus 로고
    • Gut chitin synthase and sterols from larvae of Diaprepes abbreviatus (Coleoptera: Curculionidae)
    • 26. Ward, G.B., Mayer, R.T., Feldlaufer, M.F. & Svoboda, J. (1991) Gut chitin synthase and sterols from larvae of Diaprepes abbreviatus (Coleoptera: Curculionidae). Arch. Insect Biochem. Physiol. 18, 105-117.
    • (1991) Arch. Insect Biochem. Physiol. , vol.18 , pp. 105-117
    • Ward, G.B.1    Mayer, R.T.2    Feldlaufer, M.F.3    Svoboda, J.4
  • 27
    • 0013494063 scopus 로고
    • Biology of Diaprepes abbreviatus (Coleoptera: Curculionidae) reared on an artificial diet
    • 27. Beavers, J.B. (1982) Biology of Diaprepes abbreviatus (Coleoptera: Curculionidae) reared on an artificial diet. Fla. Entomol. 65, 263-269.
    • (1982) Fla. Entomol. , vol.65 , pp. 263-269
    • Beavers, J.B.1
  • 28
    • 84990454581 scopus 로고
    • Quantitative determination of trypsin like and chymotrypsin like enzymes in insects
    • 28. Borovsky, D. & Schlein, Y. (1988) Quantitative determination of trypsin like and chymotrypsin like enzymes in insects. Arch. Insect Biochem. Physiol. 8, 249-260.
    • (1988) Arch. Insect Biochem. Physiol. , vol.8 , pp. 249-260
    • Borovsky, D.1    Schlein, Y.2
  • 29
    • 0000749791 scopus 로고
    • Effects of the soybean (Kunitz) trypsin inhibitor on growth and digestive proteases of larvae of Spodoptera litura
    • 29. McManus, M.T. & Burgess, E.P.J. (1995) Effects of the soybean (Kunitz) trypsin inhibitor on growth and digestive proteases of larvae of Spodoptera litura. J. Insect Physiol. 41, 731-738.
    • (1995) J. Insect Physiol. , vol.41 , pp. 731-738
    • McManus, M.T.1    Burgess, E.P.J.2
  • 30
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • 30. Chomczynski, P. & Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 32
    • 0027248268 scopus 로고
    • Rapid amplification of complementary DNA ends for generation of full-length complementary DNAs: Thermal RACE
    • 32. Frohman, M.A. (1993) Rapid amplification of complementary DNA ends for generation of full-length complementary DNAs: thermal RACE. Methods Enzymol. 8, 340-356.
    • (1993) Methods Enzymol. , vol.8 , pp. 340-356
    • Frohman, M.A.1
  • 33
  • 34
    • 0023371227 scopus 로고
    • DNA sequence analysis with a modified bacteriophage T7 DNA polymerase
    • 34. Tabor, S. & Richardson, C.C. (1987) DNA sequence analysis with a modified bacteriophage T7 DNA polymerase. Proc. Natl Acad. Sci. USA 84, 4767-4771.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 4767-4771
    • Tabor, S.1    Richardson, C.C.2
  • 35
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • 35. Kraulis, P. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 36
    • 0001669768 scopus 로고
    • The partial purification and characterization of serine protease activity in midgut of larval Helicoverpa armigera
    • 36. Johnston, K.A., Lee, M.J., Gatehouse, J.A. & Anstee, J.H. (1991) The partial purification and characterization of serine protease activity in midgut of larval Helicoverpa armigera. Insect Biochem. 21, 389-397.
    • (1991) Insect Biochem. , vol.21 , pp. 389-397
    • Johnston, K.A.1    Lee, M.J.2    Gatehouse, J.A.3    Anstee, J.H.4
  • 37
    • 0029152568 scopus 로고
    • Endoproteases from the midgut of larval Spodoptera litoralis, include a chymotrypsin-Iike enzyme with an extended binding site
    • 37. Lee, M.J. & Anstee, J.H. (1995) Endoproteases from the midgut of larval Spodoptera litoralis, include a chymotrypsin-Iike enzyme with an extended binding site. Insect Biochem. Molec. Biol. 25, 49-61.
    • (1995) Insect Biochem. Molec. Biol. , vol.25 , pp. 49-61
    • Lee, M.J.1    Anstee, J.H.2
  • 39
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • 39. von Heijne, G. (1986) A new method for predicting signal sequence cleavage sites. Nucl. Acids Res. 14, 4683-4690.
    • (1986) Nucl. Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 40
    • 33847799412 scopus 로고
    • Structure and mechanism of chymotrypsin
    • 40. Blow, D.M. (1976) Structure and mechanism of chymotrypsin. Acc. Chem. Res. 9, 145-152.
    • (1976) Acc. Chem. Res. , vol.9 , pp. 145-152
    • Blow, D.M.1
  • 42
    • 0013553966 scopus 로고
    • Distribution of proteinases and carbohydrases in the midgut of larvae of the sweetpotato weevil Cylas formicarius elegantulus and response of proteinases to inhibitors from sweet potato
    • 42. Baker, J.E., Woo, S.M. & Mullen, M.A. (1984) Distribution of proteinases and carbohydrases in the midgut of larvae of the sweetpotato weevil Cylas formicarius elegantulus and response of proteinases to inhibitors from sweet potato. Entomol. Exp. Appl. 36, 97-105.
    • (1984) Entomol. Exp. Appl. , vol.36 , pp. 97-105
    • Baker, J.E.1    Woo, S.M.2    Mullen, M.A.3
  • 43
    • 84990467774 scopus 로고
    • Characterization of midgut proteinase activities of white grubs: Lepidiota noxia, Lepidiota negatoria, and Antitrogus consanguineus (Scarabaeidae, Melolonthin)
    • 43. McGhie, T.K., Christeller, J.T., Ford, R. & Allsopp, P.G. (1995) Characterization of midgut proteinase activities of white grubs: Lepidiota noxia, Lepidiota negatoria, and Antitrogus consanguineus (Scarabaeidae, Melolonthin). Arch. Insect Biochem. Physiol. 28, 351-363.
    • (1995) Arch. Insect Biochem. Physiol. , vol.28 , pp. 351-363
    • McGhie, T.K.1    Christeller, J.T.2    Ford, R.3    Allsopp, P.G.4
  • 44
    • 0001260374 scopus 로고
    • The effect of dietary protein on the growth and digestive physiology of larval Heliothis zea and Spodoptera exigua
    • 44. Broadway, R.M. & Duffy, S.A. (1986) The effect of dietary protein on the growth and digestive physiology of larval Heliothis zea and Spodoptera exigua. J. Insect Physiol. 32, 678-680.
    • (1986) J. Insect Physiol. , vol.32 , pp. 678-680
    • Broadway, R.M.1    Duffy, S.A.2
  • 45
    • 0026861559 scopus 로고
    • Biosynthesis of trypsinlike and chymotrypsinlike enzyme in immature Lutzomyia anthophora (Diptera: Psychodidae)
    • 45. Mahmood, F. & Borovsky, D. (1992) Biosynthesis of trypsinlike and chymotrypsinlike enzyme in immature Lutzomyia anthophora (Diptera: Psychodidae). J. Med. Entomol. 29, 489-495.
    • (1992) J. Med. Entomol. , vol.29 , pp. 489-495
    • Mahmood, F.1    Borovsky, D.2
  • 46
    • 0016241602 scopus 로고
    • Untersuchungen uber die proteasen bei Culex pipiens
    • 46. Spiro-Kern, A. (1974) Untersuchungen uber die proteasen bei Culex pipiens. J. Comp. Physiol. 90, 53-70.
    • (1974) J. Comp. Physiol. , vol.90 , pp. 53-70
    • Spiro-Kern, A.1
  • 47
    • 0011090895 scopus 로고
    • Effect of ingested soybean, ovomucoid and corn protease inhibitors on digestive processes of the European corn borer, Ostrinia nubilalis (Lepidoptera: Pyralidae)
    • 47. Larocque, A.M. & Houseman, J.G. (1990) Effect of ingested soybean, ovomucoid and corn protease inhibitors on digestive processes of the European corn borer, Ostrinia nubilalis (Lepidoptera: Pyralidae). J. Insect Physiol. 36, 691-697.
    • (1990) J. Insect Physiol. , vol.36 , pp. 691-697
    • Larocque, A.M.1    Houseman, J.G.2
  • 48
    • 0001260377 scopus 로고
    • Plant proteinase inhibitors: Mechanism of action and effect on the growth and digestive physiology of larval Heliothis zea and Spodoptera exigua
    • 48. Broadway, R.M. & Duffy, S.A. (1986) Plant proteinase inhibitors: mechanism of action and effect on the growth and digestive physiology of larval Heliothis zea and Spodoptera exigua. J. Insect Physiol. 32, 827-833.
    • (1986) J. Insect Physiol. , vol.32 , pp. 827-833
    • Broadway, R.M.1    Duffy, S.A.2
  • 49
    • 0001285211 scopus 로고    scopus 로고
    • Adaptation of Helicoverpa armigera (Lepidoptera: Noctuidae) to a proteinase inhibitor expressed in transgenic tobacco
    • 49. Wu, Y., Lewellyn, D.L., Mathews, A. & Elizabeth, S.D. (1997) Adaptation of Helicoverpa armigera (Lepidoptera: Noctuidae) to a proteinase inhibitor expressed in transgenic tobacco. Mol Breed 3, 371-380.
    • (1997) Mol Breed , vol.3 , pp. 371-380
    • Wu, Y.1    Lewellyn, D.L.2    Mathews, A.3    Elizabeth, S.D.4
  • 50
    • 84990424341 scopus 로고
    • Oostatic hormone inhibits biosynthesis of midgut proteolytic enzymes and egg development in mosquitoes
    • 50. Borovsky, D. (1988) Oostatic hormone inhibits biosynthesis of midgut proteolytic enzymes and egg development in mosquitoes. Arch. Insect Biochem. Physiol. 7, 187-210.
    • (1988) Arch. Insect Biochem. Physiol. , vol.7 , pp. 187-210
    • Borovsky, D.1
  • 51
    • 0031238904 scopus 로고    scopus 로고
    • Dietary regulation of serine proteinases that are resistant to serine proteinase inhibitors
    • 51. Broadway, R.M. (1997) Dietary regulation of serine proteinases that are resistant to serine proteinase inhibitors. J. Insect Physiol. 43, 855-874.
    • (1997) J. Insect Physiol. , vol.43 , pp. 855-874
    • Broadway, R.M.1
  • 52
    • 0026520387 scopus 로고
    • Converting trypsin to chymotrypsin: The role of the surface loops
    • 52. Hedstorm, L., Szilagyi, L. & Rutter, W.J. (1992) Converting trypsin to chymotrypsin: the role of the surface loops. Science 255, 1249-1253.
    • (1992) Science , vol.255 , pp. 1249-1253
    • Hedstorm, L.1    Szilagyi, L.2    Rutter, W.J.3
  • 53
    • 0024963567 scopus 로고
    • Signal sequences
    • 53. Gierasch, L.M. (1989) Signal sequences. Biochemistry 28, 923-930.
    • (1989) Biochemistry , vol.28 , pp. 923-930
    • Gierasch, L.M.1
  • 54
    • 0027401647 scopus 로고
    • Amino acid sequence of alkaliphilic serine protease from silkworm, Bombyx mori, larval digestion juice
    • 54. Sasaki, T., Hishida, T., Ichikawa, K. & Asari, S. (1993) Amino acid sequence of alkaliphilic serine protease from silkworm, Bombyx mori, larval digestion juice. FEBS Lett. 320, 35-37.
    • (1993) FEBS Lett. , vol.320 , pp. 35-37
    • Sasaki, T.1    Hishida, T.2    Ichikawa, K.3    Asari, S.4
  • 55
    • 0002584426 scopus 로고
    • Post feeding induction of trypsin in the midgut of Aedes aegypti L. (Diptera: Culicidae) is separable into two cellular phases
    • 55. Felix, C.R., Betschart, B., Billingsley, P.E. & Freyvogel, T.A. (1991) Post feeding induction of trypsin in the midgut of Aedes aegypti L. (Diptera: Culicidae) is separable into two cellular phases. Insect Biochem. 21, 197-203.
    • (1991) Insect Biochem. , vol.21 , pp. 197-203
    • Felix, C.R.1    Betschart, B.2    Billingsley, P.E.3    Freyvogel, T.A.4
  • 56
    • 0025248551 scopus 로고
    • Regulation of ferritin and transferrin receptor mRNAs
    • 56. Theil, E.C. (1990) Regulation of ferritin and transferrin receptor mRNAs. J. Biol. Chem. 265, 4771-4774.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4771-4774
    • Theil, E.C.1
  • 57
    • 0001563411 scopus 로고
    • mRNAs encoding ribulose-1,5-bisphosphate carboxylase remain bound to polysomes but are not translated in amaranth seedlings transferred to darkness
    • 57. Berry, J.O., Carr, J.P. & Klessig, D.F. (1988) mRNAs encoding ribulose-1,5-bisphosphate carboxylase remain bound to polysomes but are not translated in amaranth seedlings transferred to darkness. Proc. Natl Acad. Sci. USA 85, 4190-4194.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 4190-4194
    • Berry, J.O.1    Carr, J.P.2    Klessig, D.F.3
  • 58
    • 0022555843 scopus 로고
    • The heat shock response
    • 58. Lindquist, S. (1986) The heat shock response. Annu. Rev. Biochem. 55, 1151-1191.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 1151-1191
    • Lindquist, S.1
  • 59
    • 0024291284 scopus 로고
    • Autoregulated instability of β-tubulin mRNAs by recognition of the nascent amino terminus of β-tubulin
    • 59. Yen, T.J., Machlin, P.S. & Cleveland, D.W. (1988) Autoregulated instability of β-tubulin mRNAs by recognition of the nascent amino terminus of β-tubulin. Nature 334, 580-585.
    • (1988) Nature , vol.334 , pp. 580-585
    • Yen, T.J.1    Machlin, P.S.2    Cleveland, D.W.3
  • 60
    • 0027433035 scopus 로고
    • Poly (A) tail metabolism and function in eucaryotes
    • 60. Sachs, A. & Wahle, E. (1993) Poly (A) tail metabolism and function in eucaryotes. J. Biol. Chem. 268, 22955-22958.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22955-22958
    • Sachs, A.1    Wahle, E.2
  • 61
    • 0030087932 scopus 로고    scopus 로고
    • Early trypsin, a female-specific midgut protease in Aedes aegypti: Isolation, amino-terminal sequence determination, and cloning and sequencing of the gene
    • 61. Noriega, F.G., Wang, X.Y., Pennington, J.E., Barillas-Mury, C.V. & Wells, M. A. (1996) Early trypsin, a female-specific midgut protease in Aedes aegypti: isolation, amino-terminal sequence determination, and cloning and sequencing of the gene. Insect Biochem. Molec. Biol. 26, 119-126.
    • (1996) Insect Biochem. Molec. Biol. , vol.26 , pp. 119-126
    • Noriega, F.G.1    Wang, X.Y.2    Pennington, J.E.3    Barillas-Mury, C.V.4    Wells, M.A.5
  • 62
    • 0031970810 scopus 로고    scopus 로고
    • Pitfalls of processed pseudogenes in RT-PCR
    • 62. Mutimer, H., Deacon, N., Crowe, S. & Sonza, S. (1998) Pitfalls of processed pseudogenes in RT-PCR. Biotechniques 24, 585-588.
    • (1998) Biotechniques , vol.24 , pp. 585-588
    • Mutimer, H.1    Deacon, N.2    Crowe, S.3    Sonza, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.