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Volumn 29, Issue 2, 1999, Pages 87-101

Peritrophic matrix proteins

Author keywords

Chitin; Chitinase; Chrysomya bezziana; Cysteine rich; Drosophila melanogaster; Lucilia cuprina; Mucin; Peritrophic matrix; Peritrophic membrane; Peritrophin

Indexed keywords

CELL MEMBRANE PROTEIN; CHITIN; CYSTEINE; INSECT PROTEIN; ISOPROTEIN; MUCIN; PERITROPHIN; PROLINE; PROTEINASE; UNCLASSIFIED DRUG;

EID: 0033082444     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0965-1748(98)00123-4     Document Type: Review
Times cited : (330)

References (80)
  • 1
    • 0031575792 scopus 로고    scopus 로고
    • The sequence of the Orgyia pseudotsugata multinucleocapsid nuclear polyhedrosis virus genome
    • Ahrens C.H., Russell R.L.Q., Funk C.J., Evans J.T., Harwood S.H., Rohrmann G.F. The sequence of the Orgyia pseudotsugata multinucleocapsid nuclear polyhedrosis virus genome. Virology. 229:1997;381-399.
    • (1997) Virology , vol.229 , pp. 381-399
    • Ahrens, C.H.1    Russell, R.L.Q.2    Funk, C.J.3    Evans, J.T.4    Harwood, S.H.5    Rohrmann, G.F.6
  • 2
    • 0028086144 scopus 로고
    • The complete DNA sequence of Autographa californica nuclear polyhedrosis virus
    • Ayres M.D., Howard S.C. Jr., Kuzio J., Lopez-Ferber M., Possee R.D. The complete DNA sequence of Autographa californica nuclear polyhedrosis virus. Virology. 202:1994;586-605.
    • (1994) Virology , vol.202 , pp. 586-605
    • Ayres, M.D.1    Howard S.C., Jr.2    Kuzio, J.3    Lopez-Ferber, M.4    Possee, R.D.5
  • 3
    • 0037619448 scopus 로고
    • Observations on the peritrophic membrane of Locusta migratoria migratoroides (R. and F.) nymphs
    • Baines D.M. Observations on the peritrophic membrane of Locusta migratoria migratoroides (R. and F.) nymphs. Acrida. 7:1978;11-21.
    • (1978) Acrida , vol.7 , pp. 11-21
    • Baines, D.M.1
  • 4
    • 0041913759 scopus 로고
    • Etudes anatomiques et histologiques sur le tube digestif des Crytops
    • Balbiani E.G. Etudes anatomiques et histologiques sur le tube digestif des Crytops. Arch. Zool. Exp. Gen. 8:1890;1-82.
    • (1890) Arch. Zool. Exp. Gen. , vol.8 , pp. 1-82
    • Balbiani, E.G.1
  • 5
    • 0007362167 scopus 로고
    • Determination of the formation rate of peritrophic membranes in some Diptera
    • Becker B. Determination of the formation rate of peritrophic membranes in some Diptera. J. Insect Physiol. 24:1978;529-533.
    • (1978) J. Insect Physiol. , vol.24 , pp. 529-533
    • Becker, B.1
  • 6
    • 0027969049 scopus 로고
    • Structural features of plant chitinases and chitin-binding proteins
    • Beintema J.J. Structural features of plant chitinases and chitin-binding proteins. Febs Lett. 350:1994;159-163.
    • (1994) Febs Lett. , vol.350 , pp. 159-163
    • Beintema, J.J.1
  • 7
    • 0020756652 scopus 로고
    • Peritrophic membranes and protease activity in the midgut of the malaria parasite, Anopheles stephensi (Liston) (Insecta: Diptera) under normal and experimental conditions
    • Berner R., Rudin W., Hecker H. Peritrophic membranes and protease activity in the midgut of the malaria parasite, Anopheles stephensi (Liston) (Insecta: Diptera) under normal and experimental conditions. J. Ultrastructure Res. 83:1983;195-204.
    • (1983) J. Ultrastructure Res. , vol.83 , pp. 195-204
    • Berner, R.1    Rudin, W.2    Hecker, H.3
  • 8
    • 0002485638 scopus 로고    scopus 로고
    • Protein motifs in filarial chitinases
    • Blaxter M. Protein motifs in filarial chitinases. Parasitol. Today. 12:1996;42.
    • (1996) Parasitol. Today , vol.12 , pp. 42
    • Blaxter, M.1
  • 9
    • 0008609132 scopus 로고
    • Presence of peritrophic-like membranes in the intestine of 3 bactereriophagous nematodes (Nematoda Rhabditida)
    • Borgonie G., Claeys M., Vanfleteren J., Dewaele D., Coomans A. Presence of peritrophic-like membranes in the intestine of 3 bactereriophagous nematodes (Nematoda Rhabditida). Fund. Appl. Nematol. 18:1995;227-233.
    • (1995) Fund. Appl. Nematol. , vol.18 , pp. 227-233
    • Borgonie, G.1    Claeys, M.2    Vanfleteren, J.3    Dewaele, D.4    Coomans, A.5
  • 10
    • 0028534766 scopus 로고
    • Excretory/secretory chymotrypsin from Lucilia cuprina: Purification, enzymatic specificity, and amino acid sequence deduced from mRNA
    • Casu R.E., Pearson R.D., Jarmey J.M., Cadogan L.C., Riding G.A., Tellam R.L. Excretory/secretory chymotrypsin from Lucilia cuprina: purification, enzymatic specificity, and amino acid sequence deduced from mRNA. Insect Mol. Biol. 3:1994;201-211.
    • (1994) Insect Mol. Biol. , vol.3 , pp. 201-211
    • Casu, R.E.1    Pearson, R.D.2    Jarmey, J.M.3    Cadogan, L.C.4    Riding, G.A.5    Tellam, R.L.6
  • 12
    • 0031040174 scopus 로고    scopus 로고
    • Isolation and characterization of a genome clone for the gene of an insect molting enzyme, chitinase
    • Choi H.K., Choi K.H., Kramer K.J., Muthurkrishnan S. Isolation and characterization of a genome clone for the gene of an insect molting enzyme, chitinase. Insect Mol. Biol. 27:1997;37-47.
    • (1997) Insect Mol. Biol. , vol.27 , pp. 37-47
    • Choi, H.K.1    Choi, K.H.2    Kramer, K.J.3    Muthurkrishnan, S.4
  • 13
    • 0018231626 scopus 로고
    • Physiological functions of connective tissue polysaccharides
    • Comper W.D., Laurent T.C. Physiological functions of connective tissue polysaccharides. Physiol. Rev. 58:1978;255-315.
    • (1978) Physiol. Rev. , vol.58 , pp. 255-315
    • Comper, W.D.1    Laurent, T.C.2
  • 14
    • 0043129799 scopus 로고
    • Localization of sugar components of glycoproteins in peritrophic membranes of larvae of Diptera (Culicidae Simuliidae)
    • Dorner R., Peters W. Localization of sugar components of glycoproteins in peritrophic membranes of larvae of Diptera (Culicidae Simuliidae). Entomol. Gen. 14:1988;11-24.
    • (1988) Entomol. Gen. , vol.14 , pp. 11-24
    • Dorner, R.1    Peters, W.2
  • 17
    • 0030666313 scopus 로고    scopus 로고
    • Lectin-carbohydrate interactions: Different folds, common recognition principles
    • Elgavish S., Shaanan B. Lectin-carbohydrate interactions: different folds, common recognition principles. Trends Biochem. Sci. 22:1997;462-467.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 462-467
    • Elgavish, S.1    Shaanan, B.2
  • 18
    • 0028427823 scopus 로고
    • An estimate of the number of serine protease genes expressed in sheep blowfly larvae (Lucilia cuprina)
    • Elvin C.M., Vuocolo T., Smith W.J.M., Eisemann C.H., Riddles P.W. An estimate of the number of serine protease genes expressed in sheep blowfly larvae (Lucilia cuprina). Insect Mol. Biol. 3:1994;105-115.
    • (1994) Insect Mol. Biol. , vol.3 , pp. 105-115
    • Elvin, C.M.1    Vuocolo, T.2    Smith, W.J.M.3    Eisemann, C.H.4    Riddles, P.W.5
  • 19
    • 0029945647 scopus 로고    scopus 로고
    • Characterization of a major peritrophic membrane protein, peritrophin-44, from the larvae of Lucilia cuprina: CDNA and deduced amino acid sequences
    • Elvin C., Vuocolo T., Pearson R., East I.J., Riding G., Eisemann C., Tellam R.L. Characterization of a major peritrophic membrane protein, peritrophin-44, from the larvae of Lucilia cuprina: cDNA and deduced amino acid sequences. J. Biol. Chem. 271:1996;8925-8935.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8925-8935
    • Elvin, C.1    Vuocolo, T.2    Pearson, R.3    East, I.J.4    Riding, G.5    Eisemann, C.6    Tellam, R.L.7
  • 20
    • 0028197023 scopus 로고
    • Properties of the digestive enzymes and the permeability of the peritrophic membrane of Spodoptera frugiperda (Lepidoptera) larvae
    • Ferreira C., Capella A.N., Sitnik R., Terra W.R. Properties of the digestive enzymes and the permeability of the peritrophic membrane of Spodoptera frugiperda (Lepidoptera) larvae. Comp. Biochem. Physiol. 107a:1994;631-640.
    • (1994) Comp. Biochem. Physiol. , vol.107 , pp. 631-640
    • Ferreira, C.1    Capella, A.N.2    Sitnik, R.3    Terra, W.R.4
  • 21
  • 23
    • 0026565262 scopus 로고
    • Transmission-blocking antibodies recognize microfilarial chitinase in brugian lymphatic filariasis
    • Fuhrman J.A., Lane W.S., Smith R.F., Piessens W.F., Perler F.B. Transmission-blocking antibodies recognize microfilarial chitinase in brugian lymphatic filariasis. Proc. Natl Acad. Sci. 89:1992;1548-1552.
    • (1992) Proc. Natl Acad. Sci. , vol.89 , pp. 1548-1552
    • Fuhrman, J.A.1    Lane, W.S.2    Smith, R.F.3    Piessens, W.F.4    Perler, F.B.5
  • 25
    • 0026507880 scopus 로고
    • Proteoglycans: Many forms and many functions
    • Hardingham T.E., Fosang A.J. Proteoglycans: many forms and many functions. FASEB J. 6:1992;861-870.
    • (1992) FASEB J. , vol.6 , pp. 861-870
    • Hardingham, T.E.1    Fosang, A.J.2
  • 26
    • 0025857170 scopus 로고
    • Malaria parasite chitinase and penetration of the mosquito peritrophic membrane
    • Huber M., Cabib E., Miller L.H. Malaria parasite chitinase and penetration of the mosquito peritrophic membrane. Proc. Natl Acad. Sci. USA. 88:1991;2807-2810.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 2807-2810
    • Huber, M.1    Cabib, E.2    Miller, L.H.3
  • 27
    • 0027666351 scopus 로고
    • The N-terminal cysteine-rich domain of tobacco class 1 chitinase is essential for chitin binding but not for catalytic or antifungal activity
    • Iseli B., Boller T., Neuhaus J.-M. The N-terminal cysteine-rich domain of tobacco class 1 chitinase is essential for chitin binding but not for catalytic or antifungal activity. Plant Physiol. 103:1993;221-226.
    • (1993) Plant Physiol. , vol.103 , pp. 221-226
    • Iseli, B.1    Boller, T.2    Neuhaus, J.-M.3
  • 29
    • 0343018464 scopus 로고
    • An evaluation of the nitrous acid - 3-methyl-2-benzothiazolinone hydrazone hydrochloride - ferric chloride assay for chitin in rust fungi and rust-infected tissue
    • Kaminskyj S.G.W., Heath M.C. An evaluation of the nitrous acid - 3-methyl-2-benzothiazolinone hydrazone hydrochloride - ferric chloride assay for chitin in rust fungi and rust-infected tissue. Can. J. Bot. 60:1982;2575-2580.
    • (1982) Can. J. Bot. , vol.60 , pp. 2575-2580
    • Kaminskyj, S.G.W.1    Heath, M.C.2
  • 30
    • 0031060905 scopus 로고    scopus 로고
    • Transmission-blocking vaccines: Uses and current status of development
    • Kaslow D.C. Transmission-blocking vaccines: uses and current status of development. Int. J. Parasitol. 27:1997;183-189.
    • (1997) Int. J. Parasitol. , vol.27 , pp. 183-189
    • Kaslow, D.C.1
  • 32
    • 0344110241 scopus 로고    scopus 로고
    • Insect chitinases: Molecular biology and potential use as biopesticides
    • Kramer K.J., Muthukrishnan S. Insect chitinases: molecular biology and potential use as biopesticides. Insect Biochem. Molec. Biol. 27:1997;887-900.
    • (1997) Insect Biochem. Molec. Biol. , vol.27 , pp. 887-900
    • Kramer, K.J.1    Muthukrishnan, S.2
  • 33
    • 0015239903 scopus 로고
    • Enzyme reactions in polymer media
    • Laurent T.C. Enzyme reactions in polymer media. Eur. J. Biochem. 21:1971;498-506.
    • (1971) Eur. J. Biochem. , vol.21 , pp. 498-506
    • Laurent, T.C.1
  • 34
    • 0030891189 scopus 로고    scopus 로고
    • Peritrophic matrix structure and function
    • Lehane M.J. Peritrophic matrix structure and function. Annu. Rev. Entomol. 42:1997;525-550.
    • (1997) Annu. Rev. Entomol. , vol.42 , pp. 525-550
    • Lehane, M.J.1
  • 35
    • 0030032286 scopus 로고    scopus 로고
    • Peritrophic matrix composition of the tsetse fly Glossina morsitans morsitans
    • Lehane M.J., Allingham P.G., Weglicki P. Peritrophic matrix composition of the tsetse fly Glossina morsitans morsitans. Cell Tissue Res. 283:1996;375-384.
    • (1996) Cell Tissue Res. , vol.283 , pp. 375-384
    • Lehane, M.J.1    Allingham, P.G.2    Weglicki, P.3
  • 37
    • 0014120299 scopus 로고
    • Specificity of binding of hexopyranosyl polysaccharides with fluorescent brightener
    • Maeda H., Ishida N. Specificity of binding of hexopyranosyl polysaccharides with fluorescent brightener. J. Biochem. 62:1967;276-277.
    • (1967) J. Biochem. , vol.62 , pp. 276-277
    • Maeda, H.1    Ishida, N.2
  • 38
    • 0030293932 scopus 로고    scopus 로고
    • Peritrophic matrix proteins of Anopheles gambiae and Aedes aegypti
    • Moskalyk L.A., Oo M.M., Jacobs-Lorena M. Peritrophic matrix proteins of Anopheles gambiae and Aedes aegypti. Insect Molec. Biol. 5:1996;261-268.
    • (1996) Insect Molec. Biol. , vol.5 , pp. 261-268
    • Moskalyk, L.A.1    Oo, M.M.2    Jacobs-Lorena, M.3
  • 39
    • 0004174372 scopus 로고
    • Peritrophic Membranes
    • D. Bradshaw, W. Burggren, H.C. Heller, S. Ishii, H. Langer, G. Neuweiler, & D.J. Randall. Berlin: Springer-Verlag
    • Peters W. Peritrophic Membranes. Bradshaw D., Burggren W., Heller H.C., Ishii S., Langer H., Neuweiler G., Randall D.J. Zoophysiology, Vol. 130. 1992;Springer-Verlag, Berlin.
    • (1992) Zoophysiology, Vol. 130
    • Peters, W.1
  • 40
    • 0011326613 scopus 로고
    • Aminopeptidases as immobilized enzymes on the peritrophic membranes of insects
    • Peters W., Kalnins M. Aminopeptidases as immobilized enzymes on the peritrophic membranes of insects. Entomol. Gen. 11:1985;25-32.
    • (1985) Entomol. Gen. , vol.11 , pp. 25-32
    • Peters, W.1    Kalnins, M.2
  • 41
    • 0022641753 scopus 로고
    • Electron microscopic localization of chitin using colloidal gold labelled with wheat germ agglutinin
    • Peters W., Latka I. Electron microscopic localization of chitin using colloidal gold labelled with wheat germ agglutinin. Histochemistry. 84:1986;155-160.
    • (1986) Histochemistry , vol.84 , pp. 155-160
    • Peters, W.1    Latka, I.2
  • 42
    • 0030756551 scopus 로고    scopus 로고
    • A novel role for the peritrophic matrix in protecting Leishmania from the hydrolytic activities of the sand fly midgut
    • Pimenta P.F.P., Modi G.B., Pereira S.T., Shahabuddin M., Sacks D.L. A novel role for the peritrophic matrix in protecting Leishmania from the hydrolytic activities of the sand fly midgut. Parasitology. 115:1997;359-369.
    • (1997) Parasitology , vol.115 , pp. 359-369
    • Pimenta, P.F.P.1    Modi, G.B.2    Pereira, S.T.3    Shahabuddin, M.4    Sacks, D.L.5
  • 43
    • 0028280652 scopus 로고
    • Cloning and characterization of a potentially protective chitinase-like recombinant antigen from Wuchereria bancrofti
    • Raghavan N., Freedman D.O., Fitzgerald P.C., Unnash T.R., Ottesen E.A., Nutman T.B. Cloning and characterization of a potentially protective chitinase-like recombinant antigen from Wuchereria bancrofti. Infect. Immun. 62:1994;1901-1908.
    • (1994) Infect. Immun. , vol.62 , pp. 1901-1908
    • Raghavan, N.1    Freedman, D.O.2    Fitzgerald, P.C.3    Unnash, T.R.4    Ottesen, E.A.5    Nutman, T.B.6
  • 44
    • 0027723841 scopus 로고
    • Gut-specific genes from the black fly Simulium vittatum encoding trypsin-like and carboxy-peptidase-like proteins
    • Ramos A., Mahowald A., Jacobs-Lorena M. Gut-specific genes from the black fly Simulium vittatum encoding trypsin-like and carboxy-peptidase-like proteins. Insect Mol. Biol. 1:1993;149-163.
    • (1993) Insect Mol. Biol. , vol.1 , pp. 149-163
    • Ramos, A.1    Mahowald, A.2    Jacobs-Lorena, M.3
  • 45
    • 0028773123 scopus 로고
    • Peritrophic matrix of the black fly Simulium vittatum: Formation, structure and analysis of its protein components
    • Ramos A., Mahowald A., Jacobs-Lorena M. Peritrophic matrix of the black fly Simulium vittatum: formation, structure and analysis of its protein components. J. Exp. Zool. 268:1994;269-281.
    • (1994) J. Exp. Zool. , vol.268 , pp. 269-281
    • Ramos, A.1    Mahowald, A.2    Jacobs-Lorena, M.3
  • 48
    • 0023404890 scopus 로고
    • The role of topogenic sequences in the movement of proteins through membranes
    • Robinson A., Austen B. The role of topogenic sequences in the movement of proteins through membranes. Biochem. J. 246:1987;249-261.
    • (1987) Biochem. J. , vol.246 , pp. 249-261
    • Robinson, A.1    Austen, B.2
  • 49
    • 0024578811 scopus 로고
    • Lectin-binding sites in the midgut of the mosquitoes Anopheles stephensi (Liston) and Aedes aegypti L. (Diptera: Cullicidae)
    • Rudin W., Hecker H. Lectin-binding sites in the midgut of the mosquitoes Anopheles stephensi (Liston) and Aedes aegypti L. (Diptera: Cullicidae). Parasit. Res. 75:1989;268-279.
    • (1989) Parasit. Res. , vol.75 , pp. 268-279
    • Rudin, W.1    Hecker, H.2
  • 50
    • 0026485122 scopus 로고
    • Peritrophic membrane structure and formationin the larva of a moth Heliothis
    • Ryerse J.S., Purcell J.P., Sammons R.D., Lavrik P.B. Peritrophic membrane structure and formationin the larva of a moth Heliothis. Tissue Cell. 24:1992;751-771.
    • (1992) Tissue Cell , vol.24 , pp. 751-771
    • Ryerse, J.S.1    Purcell, J.P.2    Sammons, R.D.3    Lavrik, P.B.4
  • 51
    • 0025830542 scopus 로고
    • Chitinase secreted by Leishmania functions in the sandfly vector
    • Schlein Y., Jacobson R.L., Schlomai J. Chitinase secreted by Leishmania functions in the sandfly vector. Proc. R. Soc. London. 245:1991;121-126.
    • (1991) Proc. R. Soc. London , vol.245 , pp. 121-126
    • Schlein, Y.1    Jacobson, R.L.2    Schlomai, J.3
  • 52
    • 0032004767 scopus 로고    scopus 로고
    • CDNA and deduced amino acid sequences of a peritrophic membrane glycoprotein, 'peritrophin-48', from the larvae of Lucilia cuprina
    • Schorderet S., Pearson R.D., Vuocolo T., Eisemann C., Riding G.A., Tellam R.L. cDNA and deduced amino acid sequences of a peritrophic membrane glycoprotein, 'peritrophin-48', from the larvae of Lucilia cuprina. Insect Biochem. Molec. Biol. 28:1998;99-111.
    • (1998) Insect Biochem. Molec. Biol. , vol.28 , pp. 99-111
    • Schorderet, S.1    Pearson, R.D.2    Vuocolo, T.3    Eisemann, C.4    Riding, G.A.5    Tellam, R.L.6
  • 53
    • 0343164344 scopus 로고
    • Some systems coupling enzymic reactions and other phenomena: Energy conversions
    • E. Selegny. Dordrecht: Reidel Publ
    • Selegny E. Some systems coupling enzymic reactions and other phenomena: energy conversions. Selegny E. Polyelectrolytes. 1974;533 Reidel Publ, Dordrecht.
    • (1974) Polyelectrolytes , pp. 533
    • Selegny, E.1
  • 54
    • 0027208132 scopus 로고
    • Chitinase: A novel target for blocking parasite transmission?
    • Shahabuddin M., Kaslow D.C. Chitinase: a novel target for blocking parasite transmission? Parasitol. Today. 9:1993;252-255.
    • (1993) Parasitol. Today , vol.9 , pp. 252-255
    • Shahabuddin, M.1    Kaslow, D.C.2
  • 55
    • 0027308860 scopus 로고
    • Transmission-blocking activity of a chitinase inhibitor and activation of malarial parasite chitinase by mosquito protease
    • Shahabuddin M., Toyoshima T., Aikawa M., Kaslow D. Transmission-blocking activity of a chitinase inhibitor and activation of malarial parasite chitinase by mosquito protease. Proc. Natl. Acad. Sci. USA. 90:1993;4266-4270.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4266-4270
    • Shahabuddin, M.1    Toyoshima, T.2    Aikawa, M.3    Kaslow, D.4
  • 56
    • 0030044285 scopus 로고    scopus 로고
    • Antibody-mediated inhibition of Aedes aegypti midgut trypsins blocks sporogonic development of Plasmodium gallinaceum
    • Shahabuddin M., Lemos F.J.A., Kaslow D., Jacobs-Lorena M. Antibody-mediated inhibition of Aedes aegypti midgut trypsins blocks sporogonic development of Plasmodium gallinaceum. Infect. Immun. 64:1996;739-743.
    • (1996) Infect. Immun. , vol.64 , pp. 739-743
    • Shahabuddin, M.1    Lemos, F.J.A.2    Kaslow, D.3    Jacobs-Lorena, M.4
  • 57
    • 0032504233 scopus 로고    scopus 로고
    • A type I peritrophic matrix protein from the malaria vector Anopheles gambiae binds to chitin. Cloning, expression and characterization
    • Shen Z., Jacobs-Lorena H. A type I peritrophic matrix protein from the malaria vector Anopheles gambiae binds to chitin. Cloning, expression and characterization. J. Biol. Chem. 273:1998;17665-17670.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17665-17670
    • Shen, Z.1    Jacobs-Lorena, H.2
  • 58
    • 0025402915 scopus 로고
    • Structure of a tobacco endochitinase gene: Evidence that different chitinase genes can arise by transposition of sequences encoding a cysteine-rich domain
    • Shinshi H., Neuhaus J.-M., Ryals J., Meins F. Structure of a tobacco endochitinase gene: evidence that different chitinase genes can arise by transposition of sequences encoding a cysteine-rich domain. Plant Mol. Biol. 14:1990;357-368.
    • (1990) Plant Mol. Biol. , vol.14 , pp. 357-368
    • Shinshi, H.1    Neuhaus, J.-M.2    Ryals, J.3    Meins, F.4
  • 59
    • 0025074376 scopus 로고
    • Scrutineer: A computer program that flexibly seeks and describes motifs and profiles in protein sequence databases
    • Sibbald P.R., Argos P. Scrutineer: a computer program that flexibly seeks and describes motifs and profiles in protein sequence databases. Comp. Appl. Biosci. 6:1990;279-288.
    • (1990) Comp. Appl. Biosci. , vol.6 , pp. 279-288
    • Sibbald, P.R.1    Argos, P.2
  • 60
    • 0041913442 scopus 로고
    • SDS gel electrophoresis of proteins and glycoproteins from peritrophic membranes of some Diptera
    • Stamm B., D'Haese J., Peters W. SDS gel electrophoresis of proteins and glycoproteins from peritrophic membranes of some Diptera. J. Insect Physiol. 24:1978;1-8.
    • (1978) J. Insect Physiol. , vol.24 , pp. 1-8
    • Stamm, B.1    D'Haese, J.2    Peters, W.3
  • 62
    • 0028244625 scopus 로고
    • Sucrose activity and its kinetic properties in peritrophic membrane, and in membrane-bound and soluble fractions of midgut in the silkworm Bombyx mori
    • Sumida M., Yuan X.L., Matsubara F. Sucrose activity and its kinetic properties in peritrophic membrane, and in membrane-bound and soluble fractions of midgut in the silkworm Bombyx mori. Comp. Biochem. Physiol. 108:1994;255-264.
    • (1994) Comp. Biochem. Physiol. , vol.108 , pp. 255-264
    • Sumida, M.1    Yuan, X.L.2    Matsubara, F.3
  • 63
    • 0002548913 scopus 로고    scopus 로고
    • The peritrophic matrix
    • P.F. Billingsley, & M.J. Lehane. London: Chapman and Hall
    • Tellam R.L. The peritrophic matrix. Billingsley P.F., Lehane M.J. The Biology of the Insect Midgut. 1996;86-114 Chapman and Hall, London.
    • (1996) The Biology of the Insect Midgut , pp. 86-114
    • Tellam, R.L.1
  • 64
    • 0030014332 scopus 로고    scopus 로고
    • Protein motifs in filarial chitinases: An alternative view
    • Tellam R.L. Protein motifs in filarial chitinases: an alternative view. Parasitol. Today. 12:1996;291-292.
    • (1996) Parasitol. Today , vol.12 , pp. 291-292
    • Tellam, R.L.1
  • 65
    • 0041412406 scopus 로고    scopus 로고
    • Evolution and function of insect peritrophic membrane. Ciencia e Cultura L
    • Terra W.R. Evolution and function of insect peritrophic membrane. Ciencia e Cultura L. Braz. Assoc. Advan. Sci. 48:1996;317-324.
    • (1996) Braz. Assoc. Advan. Sci. , vol.48 , pp. 317-324
    • Terra, W.R.1
  • 66
    • 0001077802 scopus 로고
    • Distribution of digestive enzymes among the endo- And ectoperitrophic spaces and midgut cells of Rhynchosciara and its physiological significance
    • Terra W.R., Ferreira C., De Bianchi A.G. Distribution of digestive enzymes among the endo- and ectoperitrophic spaces and midgut cells of Rhynchosciara and its physiological significance. J. Insect Physiol. 25:1979;487-494.
    • (1979) J. Insect Physiol. , vol.25 , pp. 487-494
    • Terra, W.R.1    Ferreira, C.2    De Bianchi, A.G.3
  • 69
    • 0000048726 scopus 로고
    • Nuclear polyhedrosis virus pathogenesis
    • Volkman L.E., Keddie B.A. Nuclear polyhedrosis virus pathogenesis. Sem. Virol. 1:1990;249-256.
    • (1990) Sem. Virol. , vol.1 , pp. 249-256
    • Volkman, L.E.1    Keddie, B.A.2
  • 70
    • 0013605261 scopus 로고
    • Dietary modulation and histochemical localization of leucine aminopeptidase activity in Drosophila melanogaster larvae
    • Walker V.K., Geer B.W., Williamson J.H. Dietary modulation and histochemical localization of leucine aminopeptidase activity in Drosophila melanogaster larvae. Insect Biochem. 10:1980;543-548.
    • (1980) Insect Biochem. , vol.10 , pp. 543-548
    • Walker, V.K.1    Geer, B.W.2    Williamson, J.H.3
  • 71
    • 0027344819 scopus 로고
    • Formation and composition of the peritrophic membrane in the sand fly Phlebotomus perniciosus (Diptera: Psychodidae)
    • Walters L.L., Irons K.P., Guzman H., Tesh R.B. Formation and composition of the peritrophic membrane in the sand fly Phlebotomus perniciosus (Diptera: Psychodidae). J. Med. Entomol. 30:1993;179-198.
    • (1993) J. Med. Entomol. , vol.30 , pp. 179-198
    • Walters, L.L.1    Irons, K.P.2    Guzman, H.3    Tesh, R.B.4
  • 72
    • 0030990106 scopus 로고    scopus 로고
    • An intestinal mucin is the target substrate for a baculovirus enhancin
    • Wang P., Granados R.R. An intestinal mucin is the target substrate for a baculovirus enhancin. Proc. Natl Acad. Sci. 94:1997;6977-6982.
    • (1997) Proc. Natl Acad. Sci. , vol.94 , pp. 6977-6982
    • Wang, P.1    Granados, R.R.2
  • 73
    • 0030985902 scopus 로고    scopus 로고
    • Molecular cloning and sequencing of a novel invertebrate intestinal mucin
    • Wang P., Granados R.R. Molecular cloning and sequencing of a novel invertebrate intestinal mucin. J. Biol. Chem. 272:1997;16663-16669.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16663-16669
    • Wang, P.1    Granados, R.R.2
  • 74
    • 0031080395 scopus 로고    scopus 로고
    • Isolation of a cDNA encoding a chitinase family protein from cuticular tissues of the Kuruma prawn Penaeus japonicus
    • Watanabe T., Kono M. Isolation of a cDNA encoding a chitinase family protein from cuticular tissues of the Kuruma prawn Penaeus japonicus. Zool. Sci. 14:1997;65-68.
    • (1997) Zool. Sci. , vol.14 , pp. 65-68
    • Watanabe, T.1    Kono, M.2
  • 75
    • 0242400258 scopus 로고
    • The rate of production of the peritrophic membrane in some insects
    • Waterhouse D.F. The rate of production of the peritrophic membrane in some insects. Aust. J. Biol. Sci. 7:1954;59-72.
    • (1954) Aust. J. Biol. Sci. , vol.7 , pp. 59-72
    • Waterhouse, D.F.1
  • 76
    • 0002274284 scopus 로고
    • The formation of the peritrophic membrane in insects, with special reference to the larvae of mosquitoes
    • Wigglesworth V.B. The formation of the peritrophic membrane in insects, with special reference to the larvae of mosquitoes. Q. J. Microsc. Sci. 73:1930;593-616.
    • (1930) Q. J. Microsc. Sci. , vol.73 , pp. 593-616
    • Wigglesworth, V.B.1
  • 77
    • 0027479701 scopus 로고
    • 'Concealed' antigens: Expanding the range of immunological targets
    • Willadsen P., Eisemann C.H., Tellam R.L. 'Concealed' antigens: expanding the range of immunological targets. Parasitol. Today. 9:1993;132-135.
    • (1993) Parasitol. Today , vol.9 , pp. 132-135
    • Willadsen, P.1    Eisemann, C.H.2    Tellam, R.L.3
  • 79
    • 0028097921 scopus 로고
    • The structure and function of proline-rich regions in proteins
    • Williamson M.P. The structure and function of proline-rich regions in proteins. Biochem. J. 297:1994;249-260.
    • (1994) Biochem. J. , vol.297 , pp. 249-260
    • Williamson, M.P.1
  • 80
    • 0030200167 scopus 로고    scopus 로고
    • Limited proteolysis and reduction-carboxymethylation of rye seed chitinase-a: Role of the chitin-binding domain in its chitinase action
    • Yamagami T., Funatsu G. Limited proteolysis and reduction-carboxymethylation of rye seed chitinase-a: role of the chitin-binding domain in its chitinase action. Biosci. Biotech. Biochem. 60:1996;1081-1086.
    • (1996) Biosci. Biotech. Biochem. , vol.60 , pp. 1081-1086
    • Yamagami, T.1    Funatsu, G.2


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