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Volumn 35, Issue 14, 2005, Pages 1577-1585

Cloning and characterisation of a Heterodera glycines aminopeptidase cDNA

Author keywords

Aminopeptidase; Expression analysis; Heterodera glycines; Plant parasitic nematode; RNA interference

Indexed keywords

AMINOPEPTIDASE; COMPLEMENTARY DNA; DOUBLE STRANDED RNA; MESSENGER RNA; ZINC;

EID: 28244488162     PISSN: 00207519     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijpara.2005.07.017     Document Type: Article
Times cited : (40)

References (45)
  • 1
    • 0038512548 scopus 로고    scopus 로고
    • Use of RNA interference to investigate gene function in the human filarial nematode parasite Brugia malayi
    • A.A. Aboobaker, and M.L. Blaxter Use of RNA interference to investigate gene function in the human filarial nematode parasite Brugia malayi Mol. Biochem. Parasitol. 129 2003 41 51
    • (2003) Mol. Biochem. Parasitol. , vol.129 , pp. 41-51
    • Aboobaker, A.A.1    Blaxter, M.L.2
  • 2
    • 0029788370 scopus 로고    scopus 로고
    • Image analysis of the growth of Globodera pallida and Meloidogyne incognita on transgenic tomato roots expressing cystatins
    • H.J. Atkinson, P.E. Urwin, M.C. Clarke, and M.J. McPherson Image analysis of the growth of Globodera pallida and Meloidogyne incognita on transgenic tomato roots expressing cystatins J. Nematol. 28 1996 209 215
    • (1996) J. Nematol. , vol.28 , pp. 209-215
    • Atkinson, H.J.1    Urwin, P.E.2    Clarke, M.C.3    McPherson, M.J.4
  • 4
    • 0242290371 scopus 로고    scopus 로고
    • The Caenorhabditis elegans orthologue of mammalian puromycin-sensitive aminopeptidase has roles in embryogenesis and reproduction
    • D.R. Brooks, N.M. Hooper, and R.E. Isaac The Caenorhabditis elegans orthologue of mammalian puromycin-sensitive aminopeptidase has roles in embryogenesis and reproduction J. Biol. Chem. 278 2003 42795 42801
    • (2003) J. Biol. Chem. , vol.278 , pp. 42795-42801
    • Brooks, D.R.1    Hooper, N.M.2    Isaac, R.E.3
  • 5
    • 0032341053 scopus 로고    scopus 로고
    • In-situ hybridization to messenger RNA in Heterodera glycines
    • J.M. De Boer, Y. Yan, G. Smant, E.L. Davis, and T.J. Baum In-situ hybridization to messenger RNA in Heterodera glycines J. Nematol. 30 1998 309 312
    • (1998) J. Nematol. , vol.30 , pp. 309-312
    • De Boer, J.M.1    Yan, Y.2    Smant, G.3    Davis, E.L.4    Baum, T.J.5
  • 6
    • 0032701435 scopus 로고    scopus 로고
    • Ontogeny of puromycin-sensitive and insensitive aminopeptidase activities in several subcellular fractions of the rat brain
    • J.M. De Gandarias, J. Irazusta, J. Gil, D. Fernandez, A. Varona, and L. Casis Ontogeny of puromycin-sensitive and insensitive aminopeptidase activities in several subcellular fractions of the rat brain Brain Res. Bull. 50 1999 283 290
    • (1999) Brain Res. Bull. , vol.50 , pp. 283-290
    • De Gandarias, J.M.1    Irazusta, J.2    Gil, J.3    Fernandez, D.4    Varona, A.5    Casis, L.6
  • 7
    • 0032545933 scopus 로고    scopus 로고
    • Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans
    • A. Fire, S. Xu, M.K. Montgomery, S.A. Kostas, S.E. Driver, and C.C. Mello Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans Nature 391 1998 806 811
    • (1998) Nature , vol.391 , pp. 806-811
    • Fire, A.1    Xu, S.2    Montgomery, M.K.3    Kostas, S.A.4    Driver, S.E.5    Mello, C.C.6
  • 8
    • 0027289146 scopus 로고
    • Brugia pahangi: Identification and characterisation of an aminopeptidase associated with larval moulting
    • X. Hong, J. Bouvier, M.M. Wong, G.Y.L. Yamagat, and J.H. McKerrow Brugia pahangi: identification and characterisation of an aminopeptidase associated with larval moulting Exp. Parasitol. 76 1993 127 133
    • (1993) Exp. Parasitol. , vol.76 , pp. 127-133
    • Hong, X.1    Bouvier, J.2    Wong, M.M.3    Yamagat, G.Y.L.4    McKerrow, J.H.5
  • 9
    • 0036079595 scopus 로고    scopus 로고
    • Suppression of secreted acetylcholinesterase expression in Nippostrongylus brasiliensis by RNA interference
    • A.S. Hussein, K. Kichenin, and M.E. Selkirk Suppression of secreted acetylcholinesterase expression in Nippostrongylus brasiliensis by RNA interference Mol. Biochem. Parasitol. 122 2002 91 94
    • (2002) Mol. Biochem. Parasitol. , vol.122 , pp. 91-94
    • Hussein, A.S.1    Kichenin, K.2    Selkirk, M.E.3
  • 10
    • 0035815332 scopus 로고    scopus 로고
    • Functional analysis of leucine aminopeptidase in Caenorhabditis elegans
    • G.W.P. Joshua Functional analysis of leucine aminopeptidase in Caenorhabditis elegans Mol. Biochem. Parasitol. 113 2001 223 232
    • (2001) Mol. Biochem. Parasitol. , vol.113 , pp. 223-232
    • Joshua, G.W.P.1
  • 12
    • 0036020252 scopus 로고    scopus 로고
    • Localisation of Globodera pallida FMRFamide-related peptide encoding genes using in situ hybridisation
    • M.J. Kimber, C.C. Fleming, A. Prior, J.T. Jones, D.W. Halton, and A.G. Maule Localisation of Globodera pallida FMRFamide-related peptide encoding genes using in situ hybridisation Int. J. Parasitol. 32 2002 1095 1105
    • (2002) Int. J. Parasitol. , vol.32 , pp. 1095-1105
    • Kimber, M.J.1    Fleming, C.C.2    Prior, A.3    Jones, J.T.4    Halton, D.W.5    Maule, A.G.6
  • 13
    • 0034792063 scopus 로고    scopus 로고
    • Functional expression and characterization of the cytoplasmic aminopeptidase P of Caenorhabditis elegans
    • V. Laurent, D.R. Brooks, D. Coates, and R.E. Isaac Functional expression and characterization of the cytoplasmic aminopeptidase P of Caenorhabditis elegans Eur. J. Biochem. 268 2001 5430 5438
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5430-5438
    • Laurent, V.1    Brooks, D.R.2    Coates, D.3    Isaac, R.E.4
  • 14
    • 0035173732 scopus 로고    scopus 로고
    • Mutational analysis of the active site of human insulin-regulated aminopeptidase
    • P.G. Laustsen, S. Vang, and T. Kristensen Mutational analysis of the active site of human insulin-regulated aminopeptidase Eur. J. Biochem. 268 2001 98 104
    • (2001) Eur. J. Biochem. , vol.268 , pp. 98-104
    • Laustsen, P.G.1    Vang, S.2    Kristensen, T.3
  • 16
    • 0032512368 scopus 로고    scopus 로고
    • Characterization of Glu350 as a critical residue involved in the N-terminal amine binding site of aminopeptidase N (EC 3.4.11.2): Insights into its mechanism of action
    • N. Luciani, C. Marie-Claire, E. Ruffet, A. Beaumont, B.P. Roques, and M.C. Fournie-Zaluski Characterization of Glu350 as a critical residue involved in the N-terminal amine binding site of aminopeptidase N (EC 3.4.11.2): insights into its mechanism of action Biochemistry 37 1998 686 692
    • (1998) Biochemistry , vol.37 , pp. 686-692
    • Luciani, N.1    Marie-Claire, C.2    Ruffet, E.3    Beaumont, A.4    Roques, B.P.5    Fournie-Zaluski, M.C.6
  • 17
    • 3843130652 scopus 로고    scopus 로고
    • Comparison of alanine aminopeptidase activities in Heterodera glycines and Caenorhabditis elegans
    • E.P. Masler Comparison of alanine aminopeptidase activities in Heterodera glycines and Caenorhabditis elegans Nematology 6 2004 223 229
    • (2004) Nematology , vol.6 , pp. 223-229
    • Masler, E.P.1
  • 18
    • 0034869601 scopus 로고    scopus 로고
    • Aminopeptidase-like activities in Caenorhabditis elegans and the soybean cyst nematode, Heterodera glycines
    • E.P. Masler, E.S. Kovaleva, and S. Sardanelli Aminopeptidase-like activities in Caenorhabditis elegans and the soybean cyst nematode, Heterodera glycines J. Helminthol. 75 2001 267 272
    • (2001) J. Helminthol. , vol.75 , pp. 267-272
    • Masler, E.P.1    Kovaleva, E.S.2    Sardanelli, S.3
  • 19
    • 0023743331 scopus 로고
    • Studies on the tissue distribution of the puromycin-sensitive enkephalin-degrading aminopeptidases
    • S. McLellan, S.H. Dyer, G. Rodriguez, and L.B. Hersh Studies on the tissue distribution of the puromycin-sensitive enkephalin-degrading aminopeptidases J. Neurochem. 51 1988 1552 1559
    • (1988) J. Neurochem. , vol.51 , pp. 1552-1559
    • McLellan, S.1    Dyer, S.H.2    Rodriguez, G.3    Hersh, L.B.4
  • 20
    • 0037135520 scopus 로고    scopus 로고
    • Cloning and characterization of a leucyl aminopeptidase from three pathogenic Leishmania species
    • R.E. Morty, and J. Morehead Cloning and characterization of a leucyl aminopeptidase from three pathogenic Leishmania species J. Biol. Chem. 277 2002 26057 26065
    • (2002) J. Biol. Chem. , vol.277 , pp. 26057-26065
    • Morty, R.E.1    Morehead, J.2
  • 21
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • H. Nielsen, J. Engelbrecht, S. Brunak, and G. von Heijne Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites Prot. Eng. 10 1997 1 6
    • (1997) Prot. Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 22
    • 0033057631 scopus 로고    scopus 로고
    • Antimalarial effects in mice of orally administered peptidyl cysteine protease inhibitors
    • J.E. Olson, G.K. Lee, A. Semenov, and P.J. Rosenthal Antimalarial effects in mice of orally administered peptidyl cysteine protease inhibitors Bioorg. Med. Chem. 7 1999 633 638
    • (1999) Bioorg. Med. Chem. , vol.7 , pp. 633-638
    • Olson, J.E.1    Lee, G.K.2    Semenov, A.3    Rosenthal, P.J.4
  • 23
  • 24
    • 0034987779 scopus 로고    scopus 로고
    • Male reproductive defects caused by puromycin-sensitive aminopeptidase deficiency in mice
    • T. Osada, G. Watanabe, S. Kondo, M. Toyoda, Y. Sakaki, and T. Takeuchi Male reproductive defects caused by puromycin-sensitive aminopeptidase deficiency in mice Mol. Endocrinol. 15 2001 960 971
    • (2001) Mol. Endocrinol. , vol.15 , pp. 960-971
    • Osada, T.1    Watanabe, G.2    Kondo, S.3    Toyoda, M.4    Sakaki, Y.5    Takeuchi, T.6
  • 25
    • 0034982609 scopus 로고    scopus 로고
    • Puromycin-sensitive aminopeptidase is essential for the maternal recognition of pregnancy in mice
    • T. Osada, G. Watanabe, Y. Sakaki, and T. Takeuchi Puromycin-sensitive aminopeptidase is essential for the maternal recognition of pregnancy in mice Mol. Endocrinol. 15 2001 882 893
    • (2001) Mol. Endocrinol. , vol.15 , pp. 882-893
    • Osada, T.1    Watanabe, G.2    Sakaki, Y.3    Takeuchi, T.4
  • 26
    • 0036153721 scopus 로고    scopus 로고
    • Molecular cloning and analysis of the Cryptosporidium parvum aminopeptidase N gene
    • R.S. Padda, A. Tsai, C.L. Chappell, and P.C. Okhuysen Molecular cloning and analysis of the Cryptosporidium parvum aminopeptidase N gene Int J. Parasitol. 32 2002 187 197
    • (2002) Int J. Parasitol. , vol.32 , pp. 187-197
    • Padda, R.S.1    Tsai, A.2    Chappell, C.L.3    Okhuysen, P.C.4
  • 27
    • 0033034097 scopus 로고    scopus 로고
    • Vaccination with cathepsin L proteinases and with leucine aminopeptidase induces high levels of protection against fascioliasis in sheep
    • L. Piacenza, D. Acosta, I. Basmadjian, J.P. Dalton, and C. Carmona Vaccination with cathepsin L proteinases and with leucine aminopeptidase induces high levels of protection against fascioliasis in sheep Infect. Immun. 67 1999 1954 1961
    • (1999) Infect. Immun. , vol.67 , pp. 1954-1961
    • Piacenza, L.1    Acosta, D.2    Basmadjian, I.3    Dalton, J.P.4    Carmona, C.5
  • 28
    • 0030949381 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of a developmentally regulated metallopeptidase present in a host protective extract of Haemonchus contortus
    • D.L. Redmond, D.P. Knox, G. Newland, and W.D. Smith Molecular cloning and characterisation of a developmentally regulated metallopeptidase present in a host protective extract of Haemonchus contortus Mol. Biochem. Parasitol. 85 1997 77 87
    • (1997) Mol. Biochem. Parasitol. , vol.85 , pp. 77-87
    • Redmond, D.L.1    Knox, D.P.2    Newland, G.3    Smith, W.D.4
  • 29
    • 0031846843 scopus 로고    scopus 로고
    • Effect of protease class-specific inhibitors on in vitro development of the third- to fourth-stage larvae of Ascaris suum
    • M.L. Rhoads, R.H. Fetterer, and J.F. Urban Effect of protease class-specific inhibitors on in vitro development of the third- to fourth-stage larvae of Ascaris suum J. Parasitol. 84 1998 686 690
    • (1998) J. Parasitol. , vol.84 , pp. 686-690
    • Rhoads, M.L.1    Fetterer, R.H.2    Urban, J.F.3
  • 30
    • 0026914848 scopus 로고
    • Dirofilaria immitis: Proteases produced by third and fourth stage larvae
    • J.K. Richer, J.A. Sakanari, G.R. Frank, and R.B. Grieve Dirofilaria immitis: proteases produced by third and fourth stage larvae Exp. Parasitol. 75 1992 213 222
    • (1992) Exp. Parasitol. , vol.75 , pp. 213-222
    • Richer, J.K.1    Sakanari, J.A.2    Frank, G.R.3    Grieve, R.B.4
  • 31
    • 0020391316 scopus 로고
    • Enzymes in the exsheathing fluid of nematodes and their biological significance
    • W.P. Rogers Enzymes in the exsheathing fluid of nematodes and their biological significance Int. J. Parasitol. 12 1982 495 502
    • (1982) Int. J. Parasitol. , vol.12 , pp. 495-502
    • Rogers, W.P.1
  • 32
    • 0030866762 scopus 로고    scopus 로고
    • Purification and properties of a membrane aminopeptidase from Ascaris suum muscle that degrades neuropeptides AF1 and AF2
    • M. Sajid, R.E. Isaac, and I.D. Harrow Purification and properties of a membrane aminopeptidase from Ascaris suum muscle that degrades neuropeptides AF1 and AF2 Mol. Biochem. Parasitol. 89 1997 225 234
    • (1997) Mol. Biochem. Parasitol. , vol.89 , pp. 225-234
    • Sajid, M.1    Isaac, R.E.2    Harrow, I.D.3
  • 35
    • 0034026513 scopus 로고    scopus 로고
    • Evaluation of immunization with gut membrane glycoproteins of Ostertagia ostertagi against homologous challenge in calves and against Haemonchus contortus in sheep
    • W.D. Smith, S.K. Smith, and D. Pettit Evaluation of immunization with gut membrane glycoproteins of Ostertagia ostertagi against homologous challenge in calves and against Haemonchus contortus in sheep Parasite Immunol. 22 2000 239 247
    • (2000) Parasite Immunol. , vol.22 , pp. 239-247
    • Smith, W.D.1    Smith, S.K.2    Pettit, D.3
  • 36
    • 0004291818 scopus 로고
    • W.B. Wood Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY
    • J. Sulston, and J. Hodgkin W.B. Wood The nematode Caenorhabditis elegans 1988 Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY 587 606
    • (1988) The Nematode Caenorhabditis Elegans , pp. 587-606
    • Sulston, J.1    Hodgkin, J.2
  • 37
    • 0027208935 scopus 로고
    • Aminopeptidases: Towards a mechanism of action
    • A. Taylor Aminopeptidases: towards a mechanism of action Trends Biochem. Sci. 18 1993 167 172
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 167-172
    • Taylor, A.1
  • 38
    • 2342547464 scopus 로고
    • Leucine aminopeptidase in eggs of the soybean cyst nematode Heterodera glycines
    • P.M. Tefft, and L.W. Bone Leucine aminopeptidase in eggs of the soybean cyst nematode Heterodera glycines J. Nematol. 17 1985 270 274
    • (1985) J. Nematol. , vol.17 , pp. 270-274
    • Tefft, P.M.1    Bone, L.W.2
  • 39
    • 0031214840 scopus 로고    scopus 로고
    • Resistance to both cyst and root knot nematodes conferred by transgenic Arabidopsis expressing a modified plant cystatin
    • P.E. Urwin, C.J. Lilley, M.J. McPherson, and H.J. Atkinson Resistance to both cyst and root knot nematodes conferred by transgenic Arabidopsis expressing a modified plant cystatin Plant J. 12 1997 455 461
    • (1997) Plant J. , vol.12 , pp. 455-461
    • Urwin, P.E.1    Lilley, C.J.2    McPherson, M.J.3    Atkinson, H.J.4
  • 40
    • 0030946213 scopus 로고    scopus 로고
    • Characterization of two cDNAs encoding cysteine proteinases from the soybean cyst nematode Heterodera glycines
    • P.E. Urwin, C.J. Lilley, M.J. McPherson, and H.J. Atkinson Characterization of two cDNAs encoding cysteine proteinases from the soybean cyst nematode Heterodera glycines Parasitology 114 1997 605 613
    • (1997) Parasitology , vol.114 , pp. 605-613
    • Urwin, P.E.1    Lilley, C.J.2    McPherson, M.J.3    Atkinson, H.J.4
  • 41
    • 0032055743 scopus 로고    scopus 로고
    • Enhanced transgenic plant resistance to nematodes by dual inhibitor constructs
    • P.E. Urwin, M.J. McPherson, and H.J. Atkinson Enhanced transgenic plant resistance to nematodes by dual inhibitor constructs Planta 204 1998 472 479
    • (1998) Planta , vol.204 , pp. 472-479
    • Urwin, P.E.1    McPherson, M.J.2    Atkinson, H.J.3
  • 42
    • 0036679383 scopus 로고    scopus 로고
    • Ingestion of double-stranded RNA by preparasitic juvenile cyst nematodes leads to RNA interference
    • P.E. Urwin, C.J. Lilley, and H.J. Atkinson Ingestion of double-stranded RNA by preparasitic juvenile cyst nematodes leads to RNA interference Mol. Plant-Microbe Interact. 15 2002 747 752
    • (2002) Mol. Plant-Microbe Interact. , vol.15 , pp. 747-752
    • Urwin, P.E.1    Lilley, C.J.2    Atkinson, H.J.3
  • 43
    • 0032168209 scopus 로고    scopus 로고
    • A glutamate residue contributes to the exopeptidase specificity in aminopeptidase a
    • G. Vaseux, X. Iturrioz, P. Corvol, and C. Llorens-Cortes A glutamate residue contributes to the exopeptidase specificity in aminopeptidase A Biochem. J. 334 1998 407 413
    • (1998) Biochem. J. , vol.334 , pp. 407-413
    • Vaseux, G.1    Iturrioz, X.2    Corvol, P.3    Llorens-Cortes, C.4
  • 44
    • 0030607410 scopus 로고    scopus 로고
    • Cysteine protease inhibitors block schistosome hemoglobin degradation in vitro and decrease worm burden and egg production in vivo
    • M.M. Wasilewski, K.C. Lim, J. Phillips, and J.H. McKerrow Cysteine protease inhibitors block schistosome hemoglobin degradation in vitro and decrease worm burden and egg production in vivo Mol. Biochem. Parasitol. 81 1996 179 189
    • (1996) Mol. Biochem. Parasitol. , vol.81 , pp. 179-189
    • Wasilewski, M.M.1    Lim, K.C.2    Phillips, J.3    McKerrow, J.H.4
  • 45
    • 0036160207 scopus 로고    scopus 로고
    • Characterisation of guanylyl cyclase genes in the soybean cyst nematode Heterodera glycines
    • Y. Yan, and E.L. Davis Characterisation of guanylyl cyclase genes in the soybean cyst nematode Heterodera glycines Int. J. Parasitol. 32 2002 65 72
    • (2002) Int. J. Parasitol. , vol.32 , pp. 65-72
    • Yan, Y.1    Davis, E.L.2


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