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Volumn 338, Issue 1, 2004, Pages 99-109

Genomic organization of the Schistosoma mansoni aspartic protease gene, a platyhelminth orthologue of mammalian lysosomal cathepsin D

Author keywords

Aspartic protease; BAC; bacterial artificial chromosome; Cathepsin D; DIG; digoxygenin; EST; Exon; expressed sequence tag; Hemoglobin digestion; Intron; long terminal repeat; LTR; open reading frame; ORF; Orthologue; Parasite; Phylogeny; Retrotransposon; Schistosome

Indexed keywords

ASPARTIC PROTEINASE; CATHEPSIN D; COMPLEMENTARY DNA;

EID: 4143121384     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2004.05.017     Document Type: Article
Times cited : (20)

References (34)
  • 1
    • 0345181812 scopus 로고    scopus 로고
    • Importing statistical measures into Artemis enhances gene identification in Leishmania genome project
    • Aggarwal G., Worthey E.A., McDonagh P.D., Myler P.J. Importing statistical measures into Artemis enhances gene identification in Leishmania genome project. BMC Bioinformatics. 2003;4/23
    • (2003) BMC Bioinformatics
    • Aggarwal, G.1    Worthey, E.A.2    McDonagh, P.D.3    Myler, P.J.4
  • 2
    • 0037154180 scopus 로고    scopus 로고
    • Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine
    • Banerjee R., Liu J., Beatty W., Pelosof L., Klemba M., Goldberg D.E. Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine. Proc. Natl. Acad. Sci. U. S. A. 99:2002;990-995
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 990-995
    • Banerjee, R.1    Liu, J.2    Beatty, W.3    Pelosof, L.4    Klemba, M.5    Goldberg, D.E.6
  • 3
    • 0004582738 scopus 로고    scopus 로고
    • Chapter 270, Introduction: Aspartic peptidases and their clans
    • A.J. Barrett, N.D. Rawlings, & J.F. Woessner. San Diego: Academic Press
    • Barrett A.J., Rawlings N.D., Woessner J.F. Chapter 270, Introduction: aspartic peptidases and their clans. Barrett A.J., Rawlings N.D., Woessner J.F. Handbook of Proteolytic Enzymes. 1998;801 Academic Press, San Diego
    • (1998) Handbook of Proteolytic Enzymes , pp. 801
    • Barrett, A.J.1    Rawlings, N.D.2    Woessner, J.F.3
  • 4
    • 0028866913 scopus 로고
    • Cloning and characterization of the Schistosoma japonicum aspartic proteinase involved in hemoglobin degradation
    • Becker M.M., Harrop S.A., Dalton J.P., Kalinna B.H., McManus D.P., Brindley P.J. Cloning and characterization of the Schistosoma japonicum aspartic proteinase involved in hemoglobin degradation. J. Biol. Chem. 270:1995;24496-24501
    • (1995) J. Biol. Chem. , vol.270 , pp. 24496-24501
    • Becker, M.M.1    Harrop, S.A.2    Dalton, J.P.3    Kalinna, B.H.4    McManus, D.P.5    Brindley, P.J.6
  • 5
    • 0141425540 scopus 로고    scopus 로고
    • Mapping and sequencing of acetylcholinesterase genes from the platyhelminth blood fluke Schistosoma
    • Bentley G.N., Jones A.K., Agnew A. Mapping and sequencing of acetylcholinesterase genes from the platyhelminth blood fluke Schistosoma. Gene. 314:2003;103-112
    • (2003) Gene , vol.314 , pp. 103-112
    • Bentley, G.N.1    Jones, A.K.2    Agnew, A.3
  • 7
    • 0037314466 scopus 로고    scopus 로고
    • Mobile genetic elements colonizing the genomes of metazoan parasites
    • Brindley P.J., Laha T., McManus D.P., Loukas A. Mobile genetic elements colonizing the genomes of metazoan parasites. Trends Parasitol. 19:2003;79-87
    • (2003) Trends Parasitol. , vol.19 , pp. 79-87
    • Brindley, P.J.1    Laha, T.2    McManus, D.P.3    Loukas, A.4
  • 8
    • 0035914328 scopus 로고    scopus 로고
    • Hemoglobin-degrading, aspartic proteases of blood-feeding parasites: Substrate specificity revealed by homology models
    • Brinkworth R.I., Prociv P., Loukas A., Brindley P.J. Hemoglobin- degrading, aspartic proteases of blood-feeding parasites: substrate specificity revealed by homology models. J. Biol. Chem. 276:2001;38844-38851
    • (2001) J. Biol. Chem. , vol.276 , pp. 38844-38851
    • Brinkworth, R.I.1    Prociv, P.2    Loukas, A.3    Brindley, P.J.4
  • 9
    • 0035201828 scopus 로고    scopus 로고
    • Phylogenetic inferences from molecular sequences: Review and critique
    • Brocchieri L. Phylogenetic inferences from molecular sequences: review and critique. Theor. Popul. Biol. 59:2001;27-40
    • (2001) Theor. Popul. Biol. , vol.59 , pp. 27-40
    • Brocchieri, L.1
  • 10
    • 0031457314 scopus 로고    scopus 로고
    • Molecular organization of a gene in barley which encodes a protein similar to aspartic protease and its specific expression in nucellar cells during degeneration
    • Chen F., Foolad M.R. Molecular organization of a gene in barley which encodes a protein similar to aspartic protease and its specific expression in nucellar cells during degeneration. Plant Mol. Biol. 35:1997;821-831
    • (1997) Plant Mol. Biol. , vol.35 , pp. 821-831
    • Chen, F.1    Foolad, M.R.2
  • 11
    • 0002553476 scopus 로고    scopus 로고
    • Cathepsin D
    • A.J. Barrett, N.D. Rawlings, & J.F. Woessner. San Diego: Academic Press
    • Conner G.E. Cathepsin D. Barrett A.J., Rawlings N.D., Woessner J.F. Handbook of Proteolytic Enzymes. 1998;828-836 Academic Press, San Diego
    • (1998) Handbook of Proteolytic Enzymes , pp. 828-836
    • Conner, G.E.1
  • 12
    • 0024504280 scopus 로고
    • Evidence for a class of very small introns in the gene for hypoxanthine-guanine phosphoribosyltransferase in Schistosoma mansoni
    • Craig S.P. III, Muralidhar M.G., McKerrow J.H., Wang C.C. Evidence for a class of very small introns in the gene for hypoxanthine-guanine phosphoribosyltransferase in Schistosoma mansoni. Nucleic Acids Res. 17:1989;1635-1647
    • (1989) Nucleic Acids Res. , vol.17 , pp. 1635-1647
    • Craig III, S.P.1    Muralidhar, M.G.2    McKerrow, J.H.3    Wang, C.C.4
  • 13
    • 0032819618 scopus 로고    scopus 로고
    • SR2, non-long terminal repeat retrotransposons of the RTE-1 lineage, from the human blood fluke Schistosoma mansoni
    • Drew A.C., Minchella D.J., King L.T., Rollinson D., Brindley P.J. SR2, non-long terminal repeat retrotransposons of the RTE-1 lineage, from the human blood fluke Schistosoma mansoni. Mol. Biol. Evol. 16:1999;1256-1269
    • (1999) Mol. Biol. Evol. , vol.16 , pp. 1256-1269
    • Drew, A.C.1    Minchella, D.J.2    King, L.T.3    Rollinson, D.4    Brindley, P.J.5
  • 14
    • 0031806709 scopus 로고    scopus 로고
    • Schistosome satellite DNA encodes active hammerhead ribozymes
    • Ferbeyre G., Smith J.M., Cedergren R. Schistosome satellite DNA encodes active hammerhead ribozymes. Mol. Cell. Biol. 18:1998;3880-3888
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3880-3888
    • Ferbeyre, G.1    Smith, J.M.2    Cedergren, R.3
  • 15
    • 0036829506 scopus 로고    scopus 로고
    • Adenylosuccinate lyase of Schistosoma mansoni: Gene structure, mRNA expression, and analysis of the predicted peptide structure of potential chemotherapeutic target
    • Foulk B.W., Pappas G., Hirai Y., Hirai H., Williams D.L. Adenylosuccinate lyase of Schistosoma mansoni: gene structure, mRNA expression, and analysis of the predicted peptide structure of potential chemotherapeutic target. Int. J. Parasitol. 32:2002;1487-1495
    • (2002) Int. J. Parasitol. , vol.32 , pp. 1487-1495
    • Foulk, B.W.1    Pappas, G.2    Hirai, Y.3    Hirai, H.4    Williams, D.L.5
  • 16
    • 0029791403 scopus 로고    scopus 로고
    • Splice site prediction in Arabidopsis thaliana DNA by combining local and global sequence information
    • Hebsgaard S.M., Korning P.G., Tolstrup N., Engelbrecht J., Rouze P., Brunak S. Splice site prediction in Arabidopsis thaliana DNA by combining local and global sequence information. Nucleic Acids Res. 24:1996;3439-3452
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3439-3452
    • Hebsgaard, S.M.1    Korning, P.G.2    Tolstrup, N.3    Engelbrecht, J.4    Rouze, P.5    Brunak, S.6
  • 17
    • 0021402417 scopus 로고
    • Evolution of aspartyl proteases by gene duplication: The mouse renin gene is organized by two homologous clusters of four exons
    • Holm I., Ollo R., Panthier J.J., Rougeon F. Evolution of aspartyl proteases by gene duplication: the mouse renin gene is organized by two homologous clusters of four exons. EMBO J. 3:1984;557-562
    • (1984) EMBO J. , vol.3 , pp. 557-562
    • Holm, I.1    Ollo, R.2    Panthier, J.J.3    Rougeon, F.4
  • 19
    • 0035479334 scopus 로고    scopus 로고
    • Aspartyl proteinase genes from apicomplexan parasites: Evidence for evolution of the gene structure
    • Jean L., Long M., Young J., Pery P., Tomley F. Aspartyl proteinase genes from apicomplexan parasites: evidence for evolution of the gene structure. Trends Parasitol. 17:2001;491-498
    • (2001) Trends Parasitol. , vol.17 , pp. 491-498
    • Jean, L.1    Long, M.2    Young, J.3    Pery, P.4    Tomley, F.5
  • 20
    • 0035834953 scopus 로고    scopus 로고
    • Genomic organisation and developmentally regulated expression of an apicomplexan aspartyl proteinase
    • Jean L., Pery P., Dunn P., Bumstead J., Billington K., Ryan R., Tomley F. Genomic organisation and developmentally regulated expression of an apicomplexan aspartyl proteinase. Gene. 262:2001;129-136
    • (2001) Gene , vol.262 , pp. 129-136
    • Jean, L.1    Pery, P.2    Dunn, P.3    Bumstead, J.4    Billington, K.5    Ryan, R.6    Tomley, F.7
  • 22
    • 0030875082 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of a putative aspartate proteinase associated with a gut membrane protein complex from adult Haemonchus contortus
    • Longbottom D., Redmond D.L., Russell M., Liddell S., Smith W.D., Knox D.P. Molecular cloning and characterisation of a putative aspartate proteinase associated with a gut membrane protein complex from adult Haemonchus contortus. Mol. Biochem. Parasitol. 88:1997;63-72
    • (1997) Mol. Biochem. Parasitol. , vol.88 , pp. 63-72
    • Longbottom, D.1    Redmond, D.L.2    Russell, M.3    Liddell, S.4    Smith, W.D.5    Knox, D.P.6
  • 25
    • 0029083689 scopus 로고
    • Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells
    • Saftig P., Hetman M., Schmahl W., Weber K., Heine L., Mossmann H., Koster A., Hess B., Evers M., von Figura K., et al. Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells. EMBO J. 14:1995;3599-3608
    • (1995) EMBO J. , vol.14 , pp. 3599-3608
    • Saftig, P.1    Hetman, M.2    Schmahl, W.3    Weber, K.4    Heine, L.5    Mossmann, H.6    Koster, A.7    Hess, B.8    Evers, M.9    Von Figura, K.10
  • 26
    • 0023375195 scopus 로고
    • The Neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N., Nei M. The Neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:1987;406-425
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 27
    • 0025321246 scopus 로고
    • Splice junctions, branch point sites and exons: Sequence statistics, identification, and applications to genome project
    • Senapathy P., Sharpiro M.B., Harris N.L. Splice junctions, branch point sites and exons: sequence statistics, identification, and applications to genome project. Methods Enzymol. 183:1990;252-278
    • (1990) Methods Enzymol , vol.183 , pp. 252-278
    • Senapathy, P.1    Sharpiro, M.B.2    Harris, N.L.3
  • 28
    • 0031574072 scopus 로고    scopus 로고
    • The Clustal X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeannmougin F., Higgins D.G. The Clustal X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 24:1997;4876-4882
    • (1997) Nucleic Acids Res. , vol.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeannmougin, F.4    Higgins, D.G.5
  • 29
    • 0017843307 scopus 로고
    • Structural evidence for gene duplication in evolution of acid proteases
    • Tang J., James M.N., Hsu I.N., Jenkins J.A., Blundell T.L. Structural evidence for gene duplication in evolution of acid proteases. Nature. 271:1978;618-621
    • (1978) Nature , vol.271 , pp. 618-621
    • Tang, J.1    James, M.N.2    Hsu, I.N.3    Jenkins, J.A.4    Blundell, T.L.5
  • 30
    • 0034714374 scopus 로고    scopus 로고
    • Aspartic proteases from the nematode Caenorhabditis elegans. Structural organization and developmental and cell-specific expression of asp-1
    • Tcherepanova I., Bhattacharyya L., Rubin C., Freedman J. Aspartic proteases from the nematode Caenorhabditis elegans. Structural organization and developmental and cell-specific expression of asp-1. J. Biol. Chem. 275:2000;26359-26369
    • (2000) J. Biol. Chem. , vol.275 , pp. 26359-26369
    • Tcherepanova, I.1    Bhattacharyya, L.2    Rubin, C.3    Freedman, J.4
  • 32
    • 0032746069 scopus 로고    scopus 로고
    • Developmental expression of the cathepsin D aspartic protease of Schistosoma japonicum
    • Verity C.K., McManus D.P., Brindley P.J. Developmental expression of the cathepsin D aspartic protease of Schistosoma japonicum. Int. J. Parasitol. 29:1999;1819-1824
    • (1999) Int. J. Parasitol. , vol.29 , pp. 1819-1824
    • Verity, C.K.1    McManus, D.P.2    Brindley, P.J.3


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