메뉴 건너뛰기




Volumn 2, Issue 1, 2008, Pages

Characterization of the Entamoeba histolytica ornithine decarboxylase-like enzyme

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; ASPARTIC ACID; EFLORNITHINE; HISTIDINE; ORNITHINE; ORNITHINE DECARBOXYLASE; PHENYLALANINE; PROTOZOAL DNA; RECOMBINANT PROTEIN; TYROSINE; POLYAMINE; PROTOZOAL PROTEIN;

EID: 48949117998     PISSN: None     EISSN: None     Source Type: Journal    
DOI: 10.1371/journal.pntd.0000115     Document Type: Article
Times cited : (15)

References (47)
  • 1
    • 0030940912 scopus 로고    scopus 로고
    • Identification of an epitope on the Entamoeba histolytica 170-kD lectin conferring antibody-mediated protection against invasive amebiasis
    • Lotter H, Zhang T, Seydel KB, Stanley SL Jr, Tannich E (1997) Identification of an epitope on the Entamoeba histolytica 170-kD lectin conferring antibody-mediated protection against invasive amebiasis. J Exp Med 185: 1793-1801.
    • (1997) J Exp Med , vol.185 , pp. 1793-1801
    • Lotter, H.1    Zhang, T.2    Seydel, K.B.3    Stanley Jr, S.L.4    Tannich, E.5
  • 2
    • 33750492287 scopus 로고    scopus 로고
    • In vitro activity of antiamoebic drugs against clinical isolates of Entamoeba histolytica and Entamoeba dispar
    • Bansal D, Sehgal R, Chawla Y, Mahajan RC, Malla N (2004) In vitro activity of antiamoebic drugs against clinical isolates of Entamoeba histolytica and Entamoeba dispar. Ann Clin Microbiol Antimicrob 3: 27.
    • (2004) Ann Clin Microbiol Antimicrob , vol.3 , pp. 27
    • Bansal, D.1    Sehgal, R.2    Chawla, Y.3    Mahajan, R.C.4    Malla, N.5
  • 3
    • 0029793132 scopus 로고    scopus 로고
    • Physiology and molecular biology of multidrug resistance in Entamoeba histolytica
    • Gomez MD, Perez DG, Ayala P, Samuelson J, Orozco E (1996) Physiology and molecular biology of multidrug resistance in Entamoeba histolytica. Arch Med Res 27: 421-425.
    • (1996) Arch Med Res , vol.27 , pp. 421-425
    • Gomez, M.D.1    Perez, D.G.2    Ayala, P.3    Samuelson, J.4    Orozco, E.5
  • 4
    • 0028956729 scopus 로고
    • Polyamines as targets for therapeutic intervention
    • Marton LJ, Pegg AE (1995) Polyamines as targets for therapeutic intervention. Annu Rev Pharmacol Toxicol 35: 55-91.
    • (1995) Annu Rev Pharmacol Toxicol , vol.35 , pp. 55-91
    • Marton, L.J.1    Pegg, A.E.2
  • 5
    • 0020215250 scopus 로고
    • Polyamine metabalism and function
    • Pegg AE, McCann PP (1982) Polyamine metabalism and function. Am J Physiol 243: C212-221.
    • (1982) Am J Physiol , vol.243
    • Pegg, A.E.1    McCann, P.P.2
  • 7
    • 0028233249 scopus 로고
    • Cell-specific translational regulation of S-adenosylmethionine decarboxylase mRNA. Influence of the structure of the 5′ transcript leader on regulation by the upstream open reading frame
    • Ruan H, Hill JR, Fatemie-Nainie S, Morris DR (1994) Cell-specific translational regulation of S-adenosylmethionine decarboxylase mRNA. Influence of the structure of the 5′ transcript leader on regulation by the upstream open reading frame. J Biol Chem 269: 17905-17910.
    • (1994) J Biol Chem , vol.269 , pp. 17905-17910
    • Ruan, H.1    Hill, J.R.2    Fatemie-Nainie, S.3    Morris, D.R.4
  • 8
    • 30144433680 scopus 로고    scopus 로고
    • Significance of targeting polyamine metabolism as an antineoplastic strategy: Unique targets for polyamine analogues
    • Casero RA Jr, Frydman B, Stewart TM, Woster PM (2005) Significance of targeting polyamine metabolism as an antineoplastic strategy: unique targets for polyamine analogues. Proc West Pharmacol Soc 48: 24-30.
    • (2005) Proc West Pharmacol Soc , vol.48 , pp. 24-30
    • Casero Jr, R.A.1    Frydman, B.2    Stewart, T.M.3    Woster, P.M.4
  • 9
    • 4944242891 scopus 로고    scopus 로고
    • Polyamines and cancer. old molecules, new understanding
    • Gerner EW, Meyskens FL Jr (2004) Polyamines and cancer. old molecules, new understanding. Nat Rev Cancer 4: 781-792.
    • (2004) Nat Rev Cancer , vol.4 , pp. 781-792
    • Gerner, E.W.1    Meyskens Jr, F.L.2
  • 10
    • 0022483087 scopus 로고
    • Interference with polyamine biosynthesis and/ or function by analogs of polyamines or methionine as a potential anticancer chemotherapeutic strategy
    • Porter CW, Sufrin JR (1986) Interference with polyamine biosynthesis and/ or function by analogs of polyamines or methionine as a potential anticancer chemotherapeutic strategy. Anticancer Res 6: 525-542.
    • (1986) Anticancer Res , vol.6 , pp. 525-542
    • Porter, C.W.1    Sufrin, J.R.2
  • 11
    • 0033083293 scopus 로고    scopus 로고
    • Recent advances in identifying and validating drug targets in trypanosomes and leishmanias
    • Barrett MP, Mottram JC, Coombs GH (1999) Recent advances in identifying and validating drug targets in trypanosomes and leishmanias. Trends Microbiol 7: 82-88.
    • (1999) Trends Microbiol , vol.7 , pp. 82-88
    • Barrett, M.P.1    Mottram, J.C.2    Coombs, G.H.3
  • 12
    • 0028819048 scopus 로고
    • Fluorinated analogues of L-ornithine are powerful inhibitors of ormithine decarboxylase and cell growth of Leishmania infantum promastigotes
    • Reguera RM, Fouce RB, Cubria JC, Bujidos ML, Ordonez D (1995) Fluorinated analogues of L-ornithine are powerful inhibitors of ormithine decarboxylase and cell growth of Leishmania infantum promastigotes. Life Sci 56: 223-230.
    • (1995) Life Sci , vol.56 , pp. 223-230
    • Reguera, R.M.1    Fouce, R.B.2    Cubria, J.C.3    Bujidos, M.L.4    Ordonez, D.5
  • 13
    • 0026671825 scopus 로고
    • Ornithine decarboxylase as an enzyme target for therapy
    • McCann PP, Pegg AE (1992) Ornithine decarboxylase as an enzyme target for therapy. Pharmacol Ther 54: 195-215.
    • (1992) Pharmacol Ther , vol.54 , pp. 195-215
    • McCann, P.P.1    Pegg, A.E.2
  • 14
    • 0035017334 scopus 로고    scopus 로고
    • Targeting polyamines of parasitic protozoa in chemotherapy
    • Muller S, Coombs GH, Walter RD (2001) Targeting polyamines of parasitic protozoa in chemotherapy. Trends Parasitol 17: 242-249.
    • (2001) Trends Parasitol , vol.17 , pp. 242-249
    • Muller, S.1    Coombs, G.H.2    Walter, R.D.3
  • 15
    • 0002116418 scopus 로고
    • The bacterial aminoacid decarboxylase
    • Gale E (1976) The bacterial aminoacid decarboxylase. Adv Enzymol 6: 1-32.
    • (1976) Adv Enzymol , vol.6 , pp. 1-32
    • Gale, E.1
  • 16
    • 48949121518 scopus 로고
    • Activity of polyamine biosynthetic enzymes in trypanosomatid protozoa
    • Dave C, Chang KP, Cheng YC (1976) Activity of polyamine biosynthetic enzymes in trypanosomatid protozoa. J Parasitol 62 (suppl): 33.
    • (1976) J Parasitol , vol.62 , Issue.SUPPL. , pp. 33
    • Dave, C.1    Chang, K.P.2    Cheng, Y.C.3
  • 17
    • 0025508969 scopus 로고
    • Polyamines in plant physiology
    • Galston AW, Sawhney RK (1990) Polyamines in plant physiology. Plant Physiol 94: 406-410.
    • (1990) Plant Physiol , vol.94 , pp. 406-410
    • Galston, A.W.1    Sawhney, R.K.2
  • 18
    • 0021333120 scopus 로고
    • Calcium stimulates ornithine decarboxylase activity in cultured mammalian epithelial cells
    • Langdon RC, Fleckman P, McGuire J (1984) Calcium stimulates ornithine decarboxylase activity in cultured mammalian epithelial cells. J Cell Physiol 118: 39-44.
    • (1984) J Cell Physiol , vol.118 , pp. 39-44
    • Langdon, R.C.1    Fleckman, P.2    McGuire, J.3
  • 19
    • 0033135202 scopus 로고    scopus 로고
    • Structure of mammalian ornithine decarboxylase at 1.6 A resolution: Stereochemical implications of PLP-dependent amino acid decarboxylases
    • Kern AD, Oliveira MA, Coffino P, Hackert MI, (1999) Structure of mammalian ornithine decarboxylase at 1.6 A resolution: stereochemical implications of PLP-dependent amino acid decarboxylases. Structure 7: 567-581.
    • (1999) Structure , vol.7 , pp. 567-581
    • Kern, A.D.1    Oliveira, M.A.2    Coffino, P.3    Hackert, M.I.4
  • 22
    • 0024447883 scopus 로고
    • Intestinal crytosporidiosis treated with eflornithine: A prospective study among patients with AIDS
    • Rolston KV, Fainstein V, Bodey GP (1989) Intestinal crytosporidiosis treated with eflornithine: a prospective study among patients with AIDS. J Acquir Immune Defic Syndr 2: 426-430.
    • (1989) J Acquir Immune Defic Syndr , vol.2 , pp. 426-430
    • Rolston, K.V.1    Fainstein, V.2    Bodey, G.P.3
  • 23
    • 0025197133 scopus 로고
    • Pneumocystis carinii pneumonia treated with eflornithine in AIDS patients resistant to conventional therapy
    • Smith D, Davies S, Nelson M, Youle M, Gleeson J. et al. (1990) Pneumocystis carinii pneumonia treated with eflornithine in AIDS patients resistant to conventional therapy. AIDS 4: 1019-1021.
    • (1990) AIDS , vol.4 , pp. 1019-1021
    • Smith, D.1    Davies, S.2    Nelson, M.3    Youle, M.4    Gleeson, J.5
  • 24
    • 0021249073 scopus 로고
    • Inhibition of growth of Giardia lamblia by difluoromethylornithine, a specific inhibitor of polyamine biosynthesis
    • Gillin FD, Reiner DS, McCann PP (1984) Inhibition of growth of Giardia lamblia by difluoromethylornithine, a specific inhibitor of polyamine biosynthesis. J Protozool 31: 161-163.
    • (1984) J Protozool , vol.31 , pp. 161-163
    • Gillin, F.D.1    Reiner, D.S.2    McCann, P.P.3
  • 25
    • 0023175739 scopus 로고
    • Pblyamine metabolism in Acanthamoeba: Polyamine content and synthesis of ornithine, putrescine, and diaminopropane
    • Kim BG, Sobota A, Bitonti AJ, McCann PP, Byers TJ (1987) Pblyamine metabolism in Acanthamoeba: polyamine content and synthesis of ornithine, putrescine, and diaminopropane. J Protozool 34: 278-284.
    • (1987) J Protozool , vol.34 , pp. 278-284
    • Kim, B.G.1    Sobota, A.2    Bitonti, A.J.3    McCann, P.P.4    Byers, T.J.5
  • 27
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25: 3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5
  • 28
    • 0032729376 scopus 로고    scopus 로고
    • Lack of a chromosomal copy of the circular rDNA plasmid of Entamoeba histolytica
    • Bagchi A, Bhattacharya A, Bhattacharya S (1999) Lack of a chromosomal copy of the circular rDNA plasmid of Entamoeba histolytica. Int J Parasitol 29: 1775-1783.
    • (1999) Int J Parasitol , vol.29 , pp. 1775-1783
    • Bagchi, A.1    Bhattacharya, A.2    Bhattacharya, S.3
  • 30
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 31
    • 0017851175 scopus 로고
    • Determination of di-and polyamines by high-performance liquid chromatographic separation of their 5-dimethylamino-naphthalene-1-sulfonyl derivatives
    • Seiler N, Knodgen B (1978) Determination of di-and polyamines by high-performance liquid chromatographic separation of their 5-dimethylamino-naphthalene-1-sulfonyl derivatives. J Chromatogr 145: 29-39.
    • (1978) J Chromatogr , vol.145 , pp. 29-39
    • Seiler, N.1    Knodgen, B.2
  • 32
    • 0033576286 scopus 로고    scopus 로고
    • X-ray structure of ornithine decarboxylase from Trypanosoma brucei: The native structure and the structure in complex with alpha-difluoromethylornithine
    • Grishin NV, Osterman AL, Brooks HB, Phillips MA, Goldsmith EJ (1999) X-ray structure of ornithine decarboxylase from Trypanosoma brucei: the native structure and the structure in complex with alpha-difluoromethylornithine. Biochemistry 38: 15174-15184.
    • (1999) Biochemistry , vol.38 , pp. 15174-15184
    • Grishin, N.V.1    Osterman, A.L.2    Brooks, H.B.3    Phillips, M.A.4    Goldsmith, E.J.5
  • 33
    • 0026743174 scopus 로고
    • Multiple protein sequence alignment from tertiary structure comparison: Assignment of global and residue confidence levels
    • Russell RB, Barton GJ (1992) Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels. Proteins 14: 309-323.
    • (1992) Proteins , vol.14 , pp. 309-323
    • Russell, R.B.1    Barton, G.J.2
  • 36
    • 0033810049 scopus 로고    scopus 로고
    • Modeling of loops in protein structures
    • Fiser A, Do RK, Sali A (2000) Modeling of loops in protein structures. Protein Sci 9: 1753-1773.
    • (2000) Protein Sci , vol.9 , pp. 1753-1773
    • Fiser, A.1    Do, R.K.2    Sali, A.3
  • 37
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234: 779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 38
    • 84986518863 scopus 로고
    • AMBER: Assisted Model Building with Energy Refinement. A General Program for Modeling Molecules and Their Interactions
    • Weiner PY, Kollman PA (1981) AMBER: Assisted Model Building with Energy Refinement. A General Program for Modeling Molecules and Their Interactions. J Comp Chem 2: 287-303.
    • (1981) J Comp Chem , vol.2 , pp. 287-303
    • Weiner, P.Y.1    Kollman, P.A.2
  • 39
    • 0025868504 scopus 로고
    • Identification of residues in ornithine decarboxylase essential for enzymic activity and for rapid protein turnover
    • Lu L, Stanley BA, Pegg AE (1991) Identification of residues in ornithine decarboxylase essential for enzymic activity and for rapid protein turnover. Biochem J 277 (Pt 3): 671-675.
    • (1991) Biochem J , vol.277 , Issue.PART 3 , pp. 671-675
    • Lu, L.1    Stanley, B.A.2    Pegg, A.E.3
  • 40
    • 0026599430 scopus 로고
    • Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by alpha-difluor-omethylornithine. Characterization of sequences at the inhibitor and coenzyme binding sites
    • Poulin R, Lu L, Ackermann B, Bey P, Pegg AE (1992) Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by alpha-difluor-omethylornithine. Characterization of sequences at the inhibitor and coenzyme binding sites. J Biol Chem 267: 150-158.
    • (1992) J Biol Chem , vol.267 , pp. 150-158
    • Poulin, R.1    Lu, L.2    Ackermann, B.3    Bey, P.4    Pegg, A.E.5
  • 41
    • 0027193354 scopus 로고
    • Intersubunit location of the active site of mammalian ornithine decarboxylase as determined by hybridization of site-directed mutants
    • Tobias KE, Kahana C (1993) Intersubunit location of the active site of mammalian ornithine decarboxylase as determined by hybridization of site-directed mutants. Biochemistry 32: 5842-5847.
    • (1993) Biochemistry , vol.32 , pp. 5842-5847
    • Tobias, K.E.1    Kahana, C.2
  • 42
    • 0027445189 scopus 로고
    • Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers
    • Tobias KE, Mamroud-Kidron E, Kahana C (1993) Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers. Eur J Biochem 218: 245-250.
    • (1993) Eur J Biochem , vol.218 , pp. 245-250
    • Tobias, K.E.1    Mamroud-Kidron, E.2    Kahana, C.3
  • 43
    • 0015239342 scopus 로고
    • On the purification of L-ornithine decarboxylase from rat prostate and effects of thiol compounds on the enzyme
    • Janne J, Williams-Ashman HG (1971) On the purification of L-ornithine decarboxylase from rat prostate and effects of thiol compounds on the enzyme. J Biol Chem 246: 1725-1732.
    • (1971) J Biol Chem , vol.246 , pp. 1725-1732
    • Janne, J.1    Williams-Ashman, H.G.2
  • 44
    • 0035818416 scopus 로고    scopus 로고
    • Long-range interactions in the dimer interface of ornithine decarboxylase are important for enzyme function
    • Myers DP, Jackson LK, Ipe VG, Murphy GE, Phillips MA (2001) Long-range interactions in the dimer interface of ornithine decarboxylase are important for enzyme function. Biochem 40: 13230-13236.
    • (2001) Biochem , vol.40 , pp. 13230-13236
    • Myers, D.P.1    Jackson, L.K.2    Ipe, V.G.3    Murphy, G.E.4    Phillips, M.A.5
  • 45
    • 4143113737 scopus 로고    scopus 로고
    • Paramecium bursaria chlorella virus encodes an unusual arginine decarboxylase that is close homolog of eukaryotic ornithine decarboxylases
    • Shah R, Coleman CS, Mir K, Baldwin J, Van Etten et al. (2004) Paramecium bursaria chlorella virus encodes an unusual arginine decarboxylase that is close homolog of eukaryotic ornithine decarboxylases. J Biol Chem 279: 35760-35767.
    • (2004) J Biol Chem , vol.279 , pp. 35760-35767
    • Shah, R.1    Coleman, C.S.2    Mir, K.3    Baldwin, J.4    Etten, V.5
  • 46
    • 0030020026 scopus 로고    scopus 로고
    • Cloning of antizyme inhibitor, a highly homologous protein to ornithine decarboxylase
    • Murakami Y, Ichiba T, Matsufuji S, Hayashi S (1996) Cloning of antizyme inhibitor, a highly homologous protein to ornithine decarboxylase. J Biol Chem 271: 3340-3342.
    • (1996) J Biol Chem , vol.271 , pp. 3340-3342
    • Murakami, Y.1    Ichiba, T.2    Matsufuji, S.3    Hayashi, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.