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Volumn 16, Issue 9, 2000, Pages 373-380

The nematode polyprotein allergens/antigens

Author keywords

[No Author keywords available]

Indexed keywords

ALLERGEN; ANTIGEN; PROTEIN;

EID: 0034284857     PISSN: 01694758     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-4758(00)01743-9     Document Type: Conference Paper
Times cited : (46)

References (58)
  • 1
    • 0032509302 scopus 로고    scopus 로고
    • Genome sequence of Caenorhabditis elegans: A platform for investigating biology
    • Genome sequence of Caenorhabditis elegans: a platform for investigating biology. Science. 282:1998;2012-2018.
    • (1998) Science , vol.282 , pp. 2012-2018
  • 2
    • 0028925560 scopus 로고
    • Characterisation of an immunodominant glycoprotein antigen of Onchocerca volvulus with homologues in other filarial nematodes and Caenorhabditis elegans
    • Tree T.I.M.et al. Characterisation of an immunodominant glycoprotein antigen of Onchocerca volvulus with homologues in other filarial nematodes and Caenorhabditis elegans. Mol. Biochem. Parasitol. 69:1995;185-195.
    • (1995) Mol. Biochem. Parasitol. , vol.69 , pp. 185-195
    • Tree, T.I.M.1
  • 3
    • 0030682113 scopus 로고    scopus 로고
    • The Ov20 protein of the parasitic nematode Onchocerca volvulus. A structurally novel class of small helix-rich retinol-binding proteins
    • Kennedy M.W.et al. The Ov20 protein of the parasitic nematode Onchocerca volvulus. A structurally novel class of small helix-rich retinol-binding proteins. J. Biol. Chem. 272:1997;29442-29448.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29442-29448
    • Kennedy, M.W.1
  • 4
    • 0025058793 scopus 로고
    • Identification of the major Ascaris allergen and its purification to homogeneity by high performance liquid chromatography
    • McGibbon A.M.et al. Identification of the major Ascaris allergen and its purification to homogeneity by high performance liquid chromatography. Mol. Biochem. Parasitol. 39:1990;163-172.
    • (1990) Mol. Biochem. Parasitol. , vol.39 , pp. 163-172
    • McGibbon, A.M.1
  • 5
    • 0022749115 scopus 로고
    • Stage-specific secreted antigens of the parasitic larval stages of the nematode Ascaris
    • Kennedy M.W., Qureshi F. Stage-specific secreted antigens of the parasitic larval stages of the nematode Ascaris. Immunology. 58:1986;515-522.
    • (1986) Immunology , vol.58 , pp. 515-522
    • Kennedy, M.W.1    Qureshi, F.2
  • 6
    • 0024343861 scopus 로고
    • MHC restriction of the antibody repertoire to secretory antigens, and a major allergen, of the nematode parasite Ascaris
    • Tomlinson L.A.et al. MHC restriction of the antibody repertoire to secretory antigens, and a major allergen, of the nematode parasite Ascaris. J. Immunol. 143:1989;2349-2356.
    • (1989) J. Immunol. , vol.143 , pp. 2349-2356
    • Tomlinson, L.A.1
  • 7
    • 0025220659 scopus 로고
    • The specificity of the antibody response to internal antigens of Ascaris: Heterogeneity in infected humans, and MHC (H-2) control of the repertoire in mice
    • Kennedy M.W.et al. The specificity of the antibody response to internal antigens of Ascaris: heterogeneity in infected humans, and MHC (H-2) control of the repertoire in mice. Clin. Exp. Immunol. 80:1990;219-224.
    • (1990) Clin. Exp. Immunol. , vol.80 , pp. 219-224
    • Kennedy, M.W.1
  • 8
    • 0025762721 scopus 로고
    • MHC class II (I-A) region control of the IgE antibody repertoire to the ABA-1 allergen of the nematode Ascaris
    • Kennedy M.W.et al. MHC class II (I-A) region control of the IgE antibody repertoire to the ABA-1 allergen of the nematode Ascaris. Immunology. 72:1991;577-579.
    • (1991) Immunology , vol.72 , pp. 577-579
    • Kennedy, M.W.1
  • 9
    • 0025276434 scopus 로고
    • N-terminal amino acid sequence identity between a major allergen of Ascaris lumbricoides and Ascaris suum, and MHC-restricted IgE responses to it
    • Christie J.F.et al. N-terminal amino acid sequence identity between a major allergen of Ascaris lumbricoides and Ascaris suum, and MHC-restricted IgE responses to it. Immunology. 69:1990;596-602.
    • (1990) Immunology , vol.69 , pp. 596-602
    • Christie, J.F.1
  • 10
    • 0015721297 scopus 로고
    • Characterisation of an allergen extracted from Ascaris suum. Determination of the molecular weight, isoelectric point, amino acid and carbohydrate content of the native allergen
    • Ambler J.et al. Characterisation of an allergen extracted from Ascaris suum. Determination of the molecular weight, isoelectric point, amino acid and carbohydrate content of the native allergen. Immunochemistry. 10:1973;815-820.
    • (1973) Immunochemistry , vol.10 , pp. 815-820
    • Ambler, J.1
  • 11
    • 0015608532 scopus 로고
    • Biological techniques for studying the allergenic components of nematodes. II. The characterisation of the allergen released by Ascaris suum maintained in saline
    • Ambler J.et al. Biological techniques for studying the allergenic components of nematodes. II. The characterisation of the allergen released by Ascaris suum maintained in saline. J. Immunol. Methods. 2:1973;315-323.
    • (1973) J. Immunol. Methods , vol.2 , pp. 315-323
    • Ambler, J.1
  • 12
    • 0027400734 scopus 로고
    • Heterogeneity amongst infected children in IgE antibody repertoire to the antigens of the parasitic nematode Ascaris
    • Fraser E.M.et al. Heterogeneity amongst infected children in IgE antibody repertoire to the antigens of the parasitic nematode Ascaris. Int. Arch. Allergy Immunol. 100:1993;283-286.
    • (1993) Int. Arch. Allergy Immunol. , vol.100 , pp. 283-286
    • Fraser, E.M.1
  • 13
    • 0032913166 scopus 로고    scopus 로고
    • Natural immunity to Ascaris lumbricoides associated with immunoglobulin E antibody to ABA-1 allergen and inflammation indicators in children
    • McSharry C.et al. Natural immunity to Ascaris lumbricoides associated with immunoglobulin E antibody to ABA-1 allergen and inflammation indicators in children. Infect. Immun. 67:1999;484-489.
    • (1999) Infect. Immun. , vol.67 , pp. 484-489
    • McSharry, C.1
  • 14
    • 0029097270 scopus 로고
    • Fine specificity of the genetically controlled immune-response to native and recombinant gp15/400 (polyprotein allergen) of Brugia malayi
    • Allen J.E.et al. Fine specificity of the genetically controlled immune-response to native and recombinant gp15/400 (polyprotein allergen) of Brugia malayi. Infect. Immun. 63:1995;2892-2898.
    • (1995) Infect. Immun. , vol.63 , pp. 2892-2898
    • Allen, J.E.1
  • 15
    • 0027311256 scopus 로고
    • Primary structure and IgE response to the repeat subunit of gp15/400 from human lymphatic filarial parasites
    • Paxton W.A.et al. Primary structure and IgE response to the repeat subunit of gp15/400 from human lymphatic filarial parasites. Infect. Immun. 61:1993;2827-2833.
    • (1993) Infect. Immun. , vol.61 , pp. 2827-2833
    • Paxton, W.A.1
  • 16
    • 0026542420 scopus 로고
    • Comparison between the MHC-restricted antibody repertoires to Ascaris antigens elicited by adjuvant-assisted immunisation or infection
    • Christie J.F.et al. Comparison between the MHC-restricted antibody repertoires to Ascaris antigens elicited by adjuvant-assisted immunisation or infection. Parasite Immunol. 14:1992;59-73.
    • (1992) Parasite Immunol. , vol.14 , pp. 59-73
    • Christie, J.F.1
  • 17
    • 0032699916 scopus 로고    scopus 로고
    • Comparative analysis of glycosylated and non-glycosylated filarial homologues of the 20-kilodalton retinol binding protein from Onchocerca volvulus (Ov20)
    • Nirmalan N.et al. Comparative analysis of glycosylated and non-glycosylated filarial homologues of the 20-kilodalton retinol binding protein from Onchocerca volvulus (Ov20). Infect. Immun. 67:1999;6239-6334.
    • (1999) Infect. Immun. , vol.67 , pp. 6239-6334
    • Nirmalan, N.1
  • 18
    • 0033388991 scopus 로고    scopus 로고
    • The cysteine protease activity of the major dust mite allergen Der p 1 selectively enhances the immunoglobulin E antibody response
    • Gough L.et al. The cysteine protease activity of the major dust mite allergen Der p 1 selectively enhances the immunoglobulin E antibody response. J. Exp. Med. 190:1999;1897-1901.
    • (1999) J. Exp. Med. , vol.190 , pp. 1897-1901
    • Gough, L.1
  • 19
    • 0030715264 scopus 로고    scopus 로고
    • Production of IgE antibodies against the 22 kDa tegumental membrane-associated antigen of schistosomes is directed by the antigen itself
    • Waine G.J.et al. Production of IgE antibodies against the 22 kDa tegumental membrane-associated antigen of schistosomes is directed by the antigen itself. Parasite Immunol. 19:1997;531-533.
    • (1997) Parasite Immunol. , vol.19 , pp. 531-533
    • Waine, G.J.1
  • 20
    • 0032784624 scopus 로고    scopus 로고
    • Structural and ligand binding analysis of recombinant Blo t 13 allergen from Blomia tropicalis mites, a fatty acid binding protein
    • Puerta L.et al. Structural and ligand binding analysis of recombinant Blo t 13 allergen from Blomia tropicalis mites, a fatty acid binding protein. Int. Arch. Allergy Immunol. 119:1999;181-184.
    • (1999) Int. Arch. Allergy Immunol. , vol.119 , pp. 181-184
    • Puerta, L.1
  • 21
    • 0027526384 scopus 로고
    • The ABA-1 allergen of the nematode Ascaris suum: Epitope stability, mass spectrometry, and N-terminal sequence comparison with its homologue in Toxocara canis
    • Christie J.F.et al. The ABA-1 allergen of the nematode Ascaris suum: epitope stability, mass spectrometry, and N-terminal sequence comparison with its homologue in Toxocara canis. Clin. Exp. Immunol. 92:1993;125-132.
    • (1993) Clin. Exp. Immunol. , vol.92 , pp. 125-132
    • Christie, J.F.1
  • 22
    • 0023684643 scopus 로고
    • The secreted and somatic antigens of the third stage larva of Anisakis simplex, and antigenic relationship with Ascaris suum, Ascaris lumbricoides, and Toxocara canis
    • Kennedy M.W.et al. The secreted and somatic antigens of the third stage larva of Anisakis simplex, and antigenic relationship with Ascaris suum, Ascaris lumbricoides, and Toxocara canis. Mol. Biochem. Parasitol. 31:1988;35-46.
    • (1988) Mol. Biochem. Parasitol. , vol.31 , pp. 35-46
    • Kennedy, M.W.1
  • 23
    • 0021363438 scopus 로고
    • Characterization of surface and excretory-secretory antigens of Toxocara canis infective larvae
    • Maizels R.M.et al. Characterization of surface and excretory-secretory antigens of Toxocara canis infective larvae. Parasite Immunol. 6:1984;23-37.
    • (1984) Parasite Immunol. , vol.6 , pp. 23-37
    • Maizels, R.M.1
  • 24
    • 0023187641 scopus 로고
    • Shared carbohydrate epitopes on distinct surface and secreted epitopes of the parasitic nematode Toxocara canis
    • Maizels R.M.et al. Shared carbohydrate epitopes on distinct surface and secreted epitopes of the parasitic nematode Toxocara canis. J. Immunol. 139:1984;207-214.
    • (1984) J. Immunol. , vol.139 , pp. 207-214
    • Maizels, R.M.1
  • 25
    • 0026661418 scopus 로고
    • Cloning of a cuticular antigen that contains multiple tandem repeats from the filarial parasite Dirofilaria immitis
    • Poole C.B.et al. Cloning of a cuticular antigen that contains multiple tandem repeats from the filarial parasite Dirofilaria immitis. Proc. Natl. Acad. Sci. U. S. A. 89:1992;5986-5990.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 5986-5990
    • Poole, C.B.1
  • 26
    • 0026642645 scopus 로고
    • Molecular characterization of a Dirofilaria immitis cDNA encoding a highly immunoreactive antigen
    • Culpepper J.et al. Molecular characterization of a Dirofilaria immitis cDNA encoding a highly immunoreactive antigen. Mol. Biochem. Parasitol. 54:1992;51-62.
    • (1992) Mol. Biochem. Parasitol. , vol.54 , pp. 51-62
    • Culpepper, J.1
  • 27
    • 0027173710 scopus 로고
    • Brugia pahangi: A surface-associated glycoprotein (gp15/400) is composed of multiple tandemly repeated units and processed from a 400-kDa precursor
    • Tweedie S.et al. Brugia pahangi: a surface-associated glycoprotein (gp15/400) is composed of multiple tandemly repeated units and processed from a 400-kDa precursor. Exp. Parasitol. 76:1993;156-164.
    • (1993) Exp. Parasitol. , vol.76 , pp. 156-164
    • Tweedie, S.1
  • 28
    • 0027489402 scopus 로고
    • Localization, turnover and conservation of gp15/400 in different stages of Brugia malayi
    • Selkirk M.E.et al. Localization, turnover and conservation of gp15/400 in different stages of Brugia malayi. Parasitology. 107:1993;449-457.
    • (1993) Parasitology , vol.107 , pp. 449-457
    • Selkirk, M.E.1
  • 29
    • 0024211135 scopus 로고
    • Filarial surface antigens: The major 29 kilodalton glycoprotein and a novel 17-200 kilodalton complex from adult Brugia malayi parasites
    • Maizels R.M.et al. Filarial surface antigens: the major 29 kilodalton glycoprotein and a novel 17-200 kilodalton complex from adult Brugia malayi parasites. Mol. Biochem. Parasitol. 32:1989;213-228.
    • (1989) Mol. Biochem. Parasitol. , vol.32 , pp. 213-228
    • Maizels, R.M.1
  • 30
    • 0025733702 scopus 로고
    • Mammalian subtilisins: The long-sought dibasic processing endoproteases
    • Barr P.J. Mammalian subtilisins: the long-sought dibasic processing endoproteases. Cell. 66:1991;1-3.
    • (1991) Cell , vol.66 , pp. 1-3
    • Barr, P.J.1
  • 31
    • 0029088836 scopus 로고
    • Extensive diversity in repeat unit sequences of the cDNA encoding the polyprotein antigen/allergen from the bovine lungworm Dictyocaulus viviparus
    • Britton C.et al. Extensive diversity in repeat unit sequences of the cDNA encoding the polyprotein antigen/allergen from the bovine lungworm Dictyocaulus viviparus. Mol. Biochem. Parasitol. 72:1995;77-88.
    • (1995) Mol. Biochem. Parasitol. , vol.72 , pp. 77-88
    • Britton, C.1
  • 32
    • 0033955614 scopus 로고    scopus 로고
    • The ABA-1 allergen of Ascaris lumbricoides: Sequence polymorphism, stage and tissue-specific expression, lipid binding function, and protein biophysical properties
    • Xia Y.et al. The ABA-1 allergen of Ascaris lumbricoides: sequence polymorphism, stage and tissue-specific expression, lipid binding function, and protein biophysical properties. Parasitology. 120:1999;211-224.
    • (1999) Parasitology , vol.120 , pp. 211-224
    • Xia, Y.1
  • 33
    • 0029024884 scopus 로고
    • The ABA-1 allergen of the parasitic nematode Ascaris suum: Fatty acid and retinoid binding function and structural characterization
    • Kennedy M.W.et al. The ABA-1 allergen of the parasitic nematode Ascaris suum: fatty acid and retinoid binding function and structural characterization. Biochemistry. 34:1995;6700-6710.
    • (1995) Biochemistry , vol.34 , pp. 6700-6710
    • Kennedy, M.W.1
  • 34
    • 0029163048 scopus 로고
    • The DvA-1 polyprotein of the parasitic nematode Dictyocaulus viviparus: A small helix-rich lipid-binding protein
    • Kennedy M.W.et al. The DvA-1 polyprotein of the parasitic nematode Dictyocaulus viviparus: a small helix-rich lipid-binding protein. J. Biol. Chem. 270:1995;19277-19281.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19277-19281
    • Kennedy, M.W.1
  • 35
    • 0029052370 scopus 로고
    • The gp15/400 polyprotein antigen of Brugia malayi binds fatty acid and retinoids
    • Kennedy M.W.et al. The gp15/400 polyprotein antigen of Brugia malayi binds fatty acid and retinoids. Mol. Biochem. Parasitol. 71:1995;41-50.
    • (1995) Mol. Biochem. Parasitol. , vol.71 , pp. 41-50
    • Kennedy, M.W.1
  • 36
    • 0033560970 scopus 로고    scopus 로고
    • Ascaridia galli fatty acid-binding protein, a member of the nematode polyprotein allergens family
    • Timanova A.et al. Ascaridia galli fatty acid-binding protein, a member of the nematode polyprotein allergens family. Eur. J. Biochem. 261:1999;569-576.
    • (1999) Eur. J. Biochem. , vol.261 , pp. 569-576
    • Timanova, A.1
  • 37
    • 0033526977 scopus 로고    scopus 로고
    • Haem detoxification by an insect
    • Oliveira M.F.et al. Haem detoxification by an insect. Nature. 400:1999;517-518.
    • (1999) Nature , vol.400 , pp. 517-518
    • Oliveira, M.F.1
  • 38
    • 0032557156 scopus 로고    scopus 로고
    • Physiological properties and functions of intracellular fatty-acid binding proteins
    • Coe N.R., Bernlohr D.A. Physiological properties and functions of intracellular fatty-acid binding proteins. Biochim. Biophys. Acta. 1391:1998;287-306.
    • (1998) Biochim. Biophys. Acta , vol.1391 , pp. 287-306
    • Coe, N.R.1    Bernlohr, D.A.2
  • 39
    • 0027289149 scopus 로고
    • Three-dimensional structure of the complex between acyl-coenzyme A binding protein and palmitoyl-coenzyme A
    • Kragelund B.B.et al. Three-dimensional structure of the complex between acyl-coenzyme A binding protein and palmitoyl-coenzyme A. J. Mol. Biol. 230:1993;1260-1277.
    • (1993) J. Mol. Biol. , vol.230 , pp. 1260-1277
    • Kragelund, B.B.1
  • 40
    • 1542396885 scopus 로고    scopus 로고
    • Cooking and freezing may not protect against allergenic reactions to ingested Anisakis simplex antigens in humans
    • Audicana L.et al. Cooking and freezing may not protect against allergenic reactions to ingested Anisakis simplex antigens in humans. Vet. Rec. 140:1997;235.
    • (1997) Vet. Rec. , vol.140 , pp. 235
    • Audicana, L.1
  • 41
    • 0025078367 scopus 로고
    • The repeating structure of the units for mouse filaggrin and a comparison of the repeating units
    • Rothnagel J.A., Steinert P.M. The repeating structure of the units for mouse filaggrin and a comparison of the repeating units. J. Biol. Chem. 265:1990;1862-1865.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1862-1865
    • Rothnagel, J.A.1    Steinert, P.M.2
  • 42
    • 0031700043 scopus 로고    scopus 로고
    • Solution structure of barley lipid transfer protein complexed with palmitate. Two different binding modes of palmitate in the homologous maize and barley nonspecific lipid transfer proteins
    • Lerche M.H., Poulsen F.M. Solution structure of barley lipid transfer protein complexed with palmitate. Two different binding modes of palmitate in the homologous maize and barley nonspecific lipid transfer proteins. Protein Sci. 7:1998;2490-2498.
    • (1998) Protein Sci. , vol.7 , pp. 2490-2498
    • Lerche, M.H.1    Poulsen, F.M.2
  • 43
    • 0031454259 scopus 로고    scopus 로고
    • Characterisation and properties of an intracellular lipid-binding protein from the tapeworm Moniezia expansa
    • Barrett J.et al. Characterisation and properties of an intracellular lipid-binding protein from the tapeworm Moniezia expansa. Eur. J. Biochem. 250:1997;269-275.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 269-275
    • Barrett, J.1
  • 44
    • 0024544415 scopus 로고
    • Antigenic relationships between the surface-exposed, secreted and somatic materials of the nematode parasites Ascaris lumbricoides, Ascaris suum, and Toxocara canis
    • Kennedy M.W.et al. Antigenic relationships between the surface-exposed, secreted and somatic materials of the nematode parasites Ascaris lumbricoides, Ascaris suum, and Toxocara canis. Clin. Exp. Immunol. 75:1989;493-500.
    • (1989) Clin. Exp. Immunol. , vol.75 , pp. 493-500
    • Kennedy, M.W.1
  • 45
    • 0025032696 scopus 로고
    • Arachidonate-related lipid mediators
    • Academic Press
    • Murphy R.C., Fitzpatrick F.A. Arachidonate-related lipid mediators. Methods Enzymol. 187:1990;Academic Press.
    • (1990) Methods Enzymol. , vol.187
    • Murphy, R.C.1    Fitzpatrick, F.A.2
  • 46
    • 0034677595 scopus 로고    scopus 로고
    • Prostaglandin D2 as a mediator of allergic asthma
    • Matsuoka T.et al. Prostaglandin D2 as a mediator of allergic asthma. Science. 287:2000;2013-2017.
    • (2000) Science , vol.287 , pp. 2013-2017
    • Matsuoka, T.1
  • 47
    • 0029794132 scopus 로고    scopus 로고
    • A decade of molecular biology of retinoic acid receptors
    • Chambon C. A decade of molecular biology of retinoic acid receptors. FASEB J. 10:1996;940-954.
    • (1996) FASEB J. , vol.10 , pp. 940-954
    • Chambon, C.1
  • 48
    • 0026613039 scopus 로고
    • Release of prostaglandin-E2 by microfilariae of Wuchereria bancrofti and Brugia malayi
    • Liu L.X.et al. Release of prostaglandin-E2 by microfilariae of Wuchereria bancrofti and Brugia malayi. Am. J. Trop. Med. Hyg. 46:1992;520-523.
    • (1992) Am. J. Trop. Med. Hyg. , vol.46 , pp. 520-523
    • Liu, L.X.1
  • 49
    • 0030271356 scopus 로고    scopus 로고
    • Tick salivary prostaglandins: Presence, origin and significance
    • Bowman A.S.et al. Tick salivary prostaglandins: presence, origin and significance. Parasitol. Today. 12:1996;388-396.
    • (1996) Parasitol. Today , vol.12 , pp. 388-396
    • Bowman, A.S.1
  • 50
    • 0030970049 scopus 로고    scopus 로고
    • Secretion of a novel, developmentally regulated fatty acid binding protein into the perivitelline fluid of the parasitic nematode, Ascaris suum
    • Mei B.et al. Secretion of a novel, developmentally regulated fatty acid binding protein into the perivitelline fluid of the parasitic nematode, Ascaris suum. J. Biol. Chem. 272:1997;9933-9941.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9933-9941
    • Mei, B.1
  • 51
    • 0033972648 scopus 로고    scopus 로고
    • Secretion of a novel class of iFABPs in nematodes: Coordinate use of the Ascaris/Caenorhabditis model systems
    • Plenefisch J.et al. Secretion of a novel class of iFABPs in nematodes: coordinate use of the Ascaris/Caenorhabditis model systems. Mol. Biochem. Parasitol. 105:2000;223-236.
    • (2000) Mol. Biochem. Parasitol. , vol.105 , pp. 223-236
    • Plenefisch, J.1
  • 52
    • 0032509180 scopus 로고    scopus 로고
    • Caenorhabditis elegans is a nematode
    • Blaxter M. Caenorhabditis elegans is a nematode. Science. 282:1998;2041-2046.
    • (1998) Science , vol.282 , pp. 2041-2046
    • Blaxter, M.1
  • 53
    • 0029150195 scopus 로고
    • An abundant, trans-spliced mRNA from Toxocara canis infective larvae encodes a 26-kDa protein with homology to phosphatidylethanolamine-binding proteins
    • Gems D.et al. An abundant, trans-spliced mRNA from Toxocara canis infective larvae encodes a 26-kDa protein with homology to phosphatidylethanolamine-binding proteins. J. Biol. Chem. 270:1995;18157-18522.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18157-18522
    • Gems, D.1
  • 54
    • 0025159452 scopus 로고
    • Identification of an Onchocerca volvulus cDNA encoding a low molecular weight antigen uniquely recognized by onchocerciasis infection sera
    • Lobos E.et al. Identification of an Onchocerca volvulus cDNA encoding a low molecular weight antigen uniquely recognized by onchocerciasis infection sera. Mol. Biochem. Parasitol. 39:1990;135-146.
    • (1990) Mol. Biochem. Parasitol. , vol.39 , pp. 135-146
    • Lobos, E.1
  • 55
    • 0030581658 scopus 로고    scopus 로고
    • Carboxy-terminal sequence divergence and processing of the polyprotein antigen from Dirofilaria immitis
    • Poole C.B.et al. Carboxy-terminal sequence divergence and processing of the polyprotein antigen from Dirofilaria immitis. Mol. Biochem. Parasitol. 82:1996;51-65.
    • (1996) Mol. Biochem. Parasitol. , vol.82 , pp. 51-65
    • Poole, C.B.1
  • 56
    • 0033563080 scopus 로고    scopus 로고
    • Sequence-divergent units of the ABA-1 polyprotein array of the nematode Ascaris have similar fatty acid and retinol binding properties but different binding site environments
    • Moore J.et al. Sequence-divergent units of the ABA-1 polyprotein array of the nematode Ascaris have similar fatty acid and retinol binding properties but different binding site environments. Biochem. J. 340:1999;337-343.
    • (1999) Biochem. J. , vol.340 , pp. 337-343
    • Moore, J.1
  • 57
    • 0031875941 scopus 로고    scopus 로고
    • Identification, characterization and expression of Toxocara canis nematode polyprotein allergen TBA-1
    • Yahiro S.et al. Identification, characterization and expression of Toxocara canis nematode polyprotein allergen TBA-1. Parasite Immunol. 20:1998;351-357.
    • (1998) Parasite Immunol. , vol.20 , pp. 351-357
    • Yahiro, S.1
  • 58
    • 0033981221 scopus 로고    scopus 로고
    • The polyprotein lipid binding proteins of nematodes
    • Kennedy M.W. The polyprotein lipid binding proteins of nematodes. Biochim. Biophys. Acta. 1472:2000;149-164.
    • (2000) Biochim. Biophys. Acta , vol.1472 , pp. 149-164
    • Kennedy, M.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.