메뉴 건너뛰기




Volumn 73, Issue 5, 2010, Pages 845-867

Proteomics of trypanosomatids of human medical importance

Author keywords

Leishmania spp.; Proteome; Proteomics; Protozoa parasites; Trypanosoma brucei; Trypanosoma cruzi; Trypanosomatids

Indexed keywords

6 PHOSPHOFRUCTOKINASE; ACID PHOSPHATASE; ALPHA TUBULIN; AMPHOTERICIN B; BETA TUBULIN; CRUZIPAIN; FRUCTOSE BISPHOSPHATE ALDOLASE; GLUCOSE 6 PHOSPHATE ISOMERASE; GLUTAMATE DEHYDROGENASE; HEAT SHOCK PROTEIN 70; HEXOKINASE; ISOCITRATE DEHYDROGENASE; LEISHMANIA VACCINE; MEGLUMINE ANTIMONATE; MELARSOPROL; METHOTREXATE; METHYLMALONYL COENZYME A DECARBOXYLASE; MILTEFOSINE; MULTIDRUG RESISTANCE PROTEIN; NIFURTIMOX; PENTAMIDINE; PROTEOME; STIBOGLUCONATE SODIUM; SUPEROXIDE DISMUTASE; TRANSKETOLASE; TRIACYLGLYCEROL LIPASE; TRIOSEPHOSPHATE ISOMERASE; TRYPANOSOMA VACCINE; TRYPANOTHIONE; UNINDEXED DRUG;

EID: 77249169142     PISSN: 18743919     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jprot.2009.12.012     Document Type: Review
Times cited : (37)

References (250)
  • 2
    • 3042555141 scopus 로고    scopus 로고
    • Leishmaniasis: current situation and new perspectives
    • Desjeux P. Leishmaniasis: current situation and new perspectives. Comp Immunol Microbiol Infect Dis 27 (2004) 305-318
    • (2004) Comp Immunol Microbiol Infect Dis , vol.27 , pp. 305-318
    • Desjeux, P.1
  • 3
    • 0027317582 scopus 로고
    • Leishmaniases of the New World: current concepts and implications for future research
    • Grimaldi Jr. G., and Tesh R.B. Leishmaniases of the New World: current concepts and implications for future research. Clin Microbiol Rev 6 (1993) 230-250
    • (1993) Clin Microbiol Rev , vol.6 , pp. 230-250
    • Grimaldi Jr., G.1    Tesh, R.B.2
  • 4
    • 0028475399 scopus 로고
    • Taxonomy of the genus Leishmania: present and future trends and their implications
    • Shaw J.J. Taxonomy of the genus Leishmania: present and future trends and their implications. Mem Inst Oswaldo Cruz 89 (1994) 471-478
    • (1994) Mem Inst Oswaldo Cruz , vol.89 , pp. 471-478
    • Shaw, J.J.1
  • 5
    • 0033517487 scopus 로고    scopus 로고
    • Leishmaniasis
    • Herwaldt B.L. Leishmaniasis. Lancet 354 (1999) 1191-1199
    • (1999) Lancet , vol.354 , pp. 1191-1199
    • Herwaldt, B.L.1
  • 7
    • 1242347426 scopus 로고    scopus 로고
    • Control of Chagas disease
    • World Health Organization. Second report of the WHO Expert Committee, WHO
    • World Health Organization. Control of Chagas disease. Second report of the WHO Expert Committee. Technical Report Series 905, Geneva (2002), WHO
    • (2002) Technical Report Series 905, Geneva
  • 8
    • 0142197130 scopus 로고    scopus 로고
    • Chagas disease: current epidemiological trends after the interruption of vectorial and transfusional transmission in the Southern Cone countries
    • Moncayo A. Chagas disease: current epidemiological trends after the interruption of vectorial and transfusional transmission in the Southern Cone countries. Mem Inst Oswaldo Cruz 98 (2003) 577-591
    • (2003) Mem Inst Oswaldo Cruz , vol.98 , pp. 577-591
    • Moncayo, A.1
  • 10
    • 59349113671 scopus 로고    scopus 로고
    • Acute phase of Chagas disease in the Brazilian Amazon region: study of 233 cases from Pará, Amapá and Maranhão observed between 1988 and 2005
    • Pinto A.Y., Valente S.A., Valente Vda C., Ferreira Jr. A.G., and Coura J.R. Acute phase of Chagas disease in the Brazilian Amazon region: study of 233 cases from Pará, Amapá and Maranhão observed between 1988 and 2005. Rev Soc Bras Med Trop 41 (2008) 602-614
    • (2008) Rev Soc Bras Med Trop , vol.41 , pp. 602-614
    • Pinto, A.Y.1    Valente, S.A.2    Valente Vda, C.3    Ferreira Jr., A.G.4    Coura, J.R.5
  • 12
    • 70449513874 scopus 로고    scopus 로고
    • Neglected tropical diseases in sub-Saharan Africa: review of their prevalence, distribution, and disease burden
    • Hotez P.J., and Kamath A. Neglected tropical diseases in sub-Saharan Africa: review of their prevalence, distribution, and disease burden. PLoS Negl Trop Dis 3 (2009) e412
    • (2009) PLoS Negl Trop Dis , vol.3
    • Hotez, P.J.1    Kamath, A.2
  • 13
    • 51549108736 scopus 로고    scopus 로고
    • The continuing problem of human African trypanosomiasis (sleeping sickness)
    • Kennedy P.G. The continuing problem of human African trypanosomiasis (sleeping sickness). Ann Neurol 64 (2008) 116-126
    • (2008) Ann Neurol , vol.64 , pp. 116-126
    • Kennedy, P.G.1
  • 14
  • 15
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira P.T. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J Biol Chem 262 (1987) 10035-10038
    • (1987) J Biol Chem , vol.262 , pp. 10035-10038
    • Matsudaira, P.T.1
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell P.H. High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250 (1975) 4007-4021
    • (1975) J Biol Chem , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 18
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10000 kDa
    • Karas M., and Hillemkamp F. Laser desorption ionization of proteins with molecular masses exceeding 10000 kDa. Anal.Chem 60 (1988) 2299-2301
    • (1988) Anal.Chem , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillemkamp, F.2
  • 19
    • 0000732594 scopus 로고
    • Detection of high mass molecules by laser desorption ionization time-of-flight mass spectrometry
    • Masuda H., and Xiao-tian L. (Eds), Osaka, Japan
    • Tanaka K., Ido Y., Akita S., Yoshida Y., and Yoshida T. Detection of high mass molecules by laser desorption ionization time-of-flight mass spectrometry. In: Masuda H., and Xiao-tian L. (Eds). Proc. 2nd Japan-China join symp. mass spectrom (1987), Osaka, Japan 185-188
    • (1987) Proc. 2nd Japan-China join symp. mass spectrom , pp. 185-188
    • Tanaka, K.1    Ido, Y.2    Akita, S.3    Yoshida, Y.4    Yoshida, T.5
  • 20
    • 84984042980 scopus 로고
    • Protein and polymer analyses up to m/z 100 000 by laser ionization time-of-flight mass spectrometry
    • Tanaka K., Waki H., Ido Y., Akita S., Yoshida Y., Yoshida T., et al. Protein and polymer analyses up to m/z 100 000 by laser ionization time-of-flight mass spectrometry. Rapid Commun Mass Spectrom 2 (1988) 151-153
    • (1988) Rapid Commun Mass Spectrom , vol.2 , pp. 151-153
    • Tanaka, K.1    Waki, H.2    Ido, Y.3    Akita, S.4    Yoshida, Y.5    Yoshida, T.6
  • 21
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn J., Mann M., Meng C.K., Wong S.F., and Whitehouse C.M. Electrospray ionization for mass spectrometry of large biomolecules. Science 246 (1989) 64-71
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 22
    • 0027608882 scopus 로고
    • Use of mass spectrometric molecular weight information to identify proteins in sequence databases
    • Mann M., Hojrup P., and Roepstorff P. Use of mass spectrometric molecular weight information to identify proteins in sequence databases. Biol Mass Spectrom 22 (1993) 338-345
    • (1993) Biol Mass Spectrom , vol.22 , pp. 338-345
    • Mann, M.1    Hojrup, P.2    Roepstorff, P.3
  • 23
    • 0027198862 scopus 로고
    • Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases
    • Henzel W.J., Billeci T.M., Stults J.T., Wong S.C., Grimley C., and Watanabe C. Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases. Proc Natl Acad Sci USA 90 (1993) 5011-5015
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5011-5015
    • Henzel, W.J.1    Billeci, T.M.2    Stults, J.T.3    Wong, S.C.4    Grimley, C.5    Watanabe, C.6
  • 24
    • 0027375364 scopus 로고
    • Peptide mass maps: a highly informative approach to protein identification
    • Yates III J.R., Speicher S., Griffin P.R., and Hunkapiller T. Peptide mass maps: a highly informative approach to protein identification. Anal Biochem 214 (1993) 397-408
    • (1993) Anal Biochem , vol.214 , pp. 397-408
    • Yates III, J.R.1    Speicher, S.2    Griffin, P.R.3    Hunkapiller, T.4
  • 26
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng J.K., McCormack A.L., and Yates III J.R. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrom 5 (1994) 976-989
    • (1994) J Am Soc Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 27
    • 0037370373 scopus 로고    scopus 로고
    • Proteomics: the first decade and beyond
    • Aebersold R.H.., and Patterson S.D. Proteomics: the first decade and beyond. Nat Genet 33 Suppl (2003) 311-323
    • (2003) Nat Genet , vol.33 , Issue.SUPPL , pp. 311-323
    • Aebersold, R.H..1    Patterson, S.D.2
  • 29
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters D.A., Washburn M.P., and Yates III J.R. An automated multidimensional protein identification technology for shotgun proteomics. Anal Chem 73 (2001) 5683-5690
    • (2001) Anal Chem , vol.73 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates III, J.R.3
  • 30
    • 0034158441 scopus 로고    scopus 로고
    • Mass spectrometric identification of proteins and characterization of their post-translational modifications in proteome analysis
    • Larsen M.R., and Roepstorff P. Mass spectrometric identification of proteins and characterization of their post-translational modifications in proteome analysis. Fresenius J Anal Chem 366 (2000) 677-690
    • (2000) Fresenius J Anal Chem , vol.366 , pp. 677-690
    • Larsen, M.R.1    Roepstorff, P.2
  • 31
    • 0035260294 scopus 로고    scopus 로고
    • Identification of protein-bound carbohydrates by mass spectrometry
    • Harvey D.J. Identification of protein-bound carbohydrates by mass spectrometry. Proteomics 1 (2001) 311-328
    • (2001) Proteomics , vol.1 , pp. 311-328
    • Harvey, D.J.1
  • 32
    • 65549109927 scopus 로고    scopus 로고
    • Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: an update for 2003-2004
    • Harvey D.J. Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: an update for 2003-2004. Mass Spectrom Rev 28 (2009) 273-361
    • (2009) Mass Spectrom Rev , vol.28 , pp. 273-361
    • Harvey, D.J.1
  • 34
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • Mann M., and Jensen O.N. Proteomic analysis of post-translational modifications. Nat Biotechnol 21 (2003) 255-261
    • (2003) Nat Biotechnol , vol.21 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 35
    • 13244249515 scopus 로고    scopus 로고
    • Deamidation: differentiation of aspartyl from isoaspartyl products in peptides by electron capture dissociation
    • Cournoyer J.J., Pittman J.L., Ivleva V.B., Fallows E., Waskell L., Costello C.E., et al. Deamidation: differentiation of aspartyl from isoaspartyl products in peptides by electron capture dissociation. Protein Sci 14 (2005) 452-463
    • (2005) Protein Sci , vol.14 , pp. 452-463
    • Cournoyer, J.J.1    Pittman, J.L.2    Ivleva, V.B.3    Fallows, E.4    Waskell, L.5    Costello, C.E.6
  • 36
    • 34248184647 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation in the regions of consecutive serine/threonine residues by negative ion electrospray collision-induced dissociation. Approach to pinpointing of phosphorylation sites
    • Edelson-Averbukh M., Pipkorn R., and Lehmann W.D. Analysis of protein phosphorylation in the regions of consecutive serine/threonine residues by negative ion electrospray collision-induced dissociation. Approach to pinpointing of phosphorylation sites. Anal Chem 79 (2007) 3476-3486
    • (2007) Anal Chem , vol.79 , pp. 3476-3486
    • Edelson-Averbukh, M.1    Pipkorn, R.2    Lehmann, W.D.3
  • 37
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi S.P., Rist B., Gerber S.A., Turecek F., Gelb M.H., and Aebersold R. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol 17 (1999) 994-999
    • (1999) Nat Biotechnol , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 38
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong S.E., Blagoev B., Kratchmarova I., Kristensen D.B., Steen H., Pandey A., et al. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1 (2002) 376-386
    • (2002) Mol Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6
  • 39
    • 0036428393 scopus 로고    scopus 로고
    • Amino acid residue specific stable isotope labeling for quantitative proteomics
    • Zhu H., Pan S., Gu S., Bradbury E.M., and Chen X. Amino acid residue specific stable isotope labeling for quantitative proteomics. Rapid Commun Mass Spectrom 16 (2002) 2115-2123
    • (2002) Rapid Commun Mass Spectrom , vol.16 , pp. 2115-2123
    • Zhu, H.1    Pan, S.2    Gu, S.3    Bradbury, E.M.4    Chen, X.5
  • 40
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross P.L., Huang Y.N., Marchese J.N., Williamson B., Parker K., Hattten S., et al. Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol Cell Proteomics 3 (2004) 1154-1169
    • (2004) Mol Cell Proteomics , vol.3 , pp. 1154-1169
    • Ross, P.L.1    Huang, Y.N.2    Marchese, J.N.3    Williamson, B.4    Parker, K.5    Hattten, S.6
  • 41
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • Ishihama Y., Oda Y., Tabata T., Sato T., Nagasu T., Rappsilber J., et al. Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein. Mol Cell Proteomics 4 (2005) 1265-1272
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4    Nagasu, T.5    Rappsilber, J.6
  • 42
    • 33847179916 scopus 로고    scopus 로고
    • Multiplexed absolute quantification for proteomics using concatenated signature peptides encoded by QconCAT genes
    • Pratt J.M., Simpson D.M., Doherty M.K., Rivers J., Gaskell S.J., and Beynon R.J. Multiplexed absolute quantification for proteomics using concatenated signature peptides encoded by QconCAT genes. Nat Protoc 1 (2006) 1029-1043
    • (2006) Nat Protoc , vol.1 , pp. 1029-1043
    • Pratt, J.M.1    Simpson, D.M.2    Doherty, M.K.3    Rivers, J.4    Gaskell, S.J.5    Beynon, R.J.6
  • 43
    • 33646564676 scopus 로고    scopus 로고
    • Label-free protein quantification using LC-coupled ion trap or FT mass spectrometry: reproducibility, linearity, and application with complex proteomes
    • Wang G., Wu W., Zeng W., Chou C., and Shen R. Label-free protein quantification using LC-coupled ion trap or FT mass spectrometry: reproducibility, linearity, and application with complex proteomes. J Proteome Res 5 (2006) 1214-1223
    • (2006) J Proteome Res , vol.5 , pp. 1214-1223
    • Wang, G.1    Wu, W.2    Zeng, W.3    Chou, C.4    Shen, R.5
  • 48
    • 0019514840 scopus 로고
    • Identification and characterization of protein antigens of Leishmania tropica isolates
    • Handman E., Mitchell G.F., and Goding J.W. Identification and characterization of protein antigens of Leishmania tropica isolates. J Immunol 126 (1981) 508-512
    • (1981) J Immunol , vol.126 , pp. 508-512
    • Handman, E.1    Mitchell, G.F.2    Goding, J.W.3
  • 49
    • 0021637305 scopus 로고
    • Two-dimensional electrophoresis used to differentiate the causal agents of American tegumentary leishmaniasis
    • Saravia N.G., Gemmell M.A., Nance S.L., and Anderson N.L. Two-dimensional electrophoresis used to differentiate the causal agents of American tegumentary leishmaniasis. Clin Chem 30 (1984) 2048-2052
    • (1984) Clin Chem , vol.30 , pp. 2048-2052
    • Saravia, N.G.1    Gemmell, M.A.2    Nance, S.L.3    Anderson, N.L.4
  • 50
    • 0022178279 scopus 로고
    • Comparison of African trypanosomes of different antigenic phenotypes, subspecies and life cycle stages by two-dimensional gel electrophoresis
    • Anderson N.L., Parish N.M., Richardson J.P., and Pearson T.W. Comparison of African trypanosomes of different antigenic phenotypes, subspecies and life cycle stages by two-dimensional gel electrophoresis. Mol Biochem Parasitol 16 (1985) 299-314
    • (1985) Mol Biochem Parasitol , vol.16 , pp. 299-314
    • Anderson, N.L.1    Parish, N.M.2    Richardson, J.P.3    Pearson, T.W.4
  • 51
    • 0035171001 scopus 로고    scopus 로고
    • Comparative proteome analysis of Leishmania donovani at different stages of transformation from promastigotes to amastigotes
    • Thiel M., and Bruchhaus I. Comparative proteome analysis of Leishmania donovani at different stages of transformation from promastigotes to amastigotes. Med Microbiol Immunol 190 (2001) 33-36
    • (2001) Med Microbiol Immunol , vol.190 , pp. 33-36
    • Thiel, M.1    Bruchhaus, I.2
  • 52
  • 53
    • 0036668518 scopus 로고    scopus 로고
    • A proteomic approach to identify developmentally regulated proteins in Leishmania infantum
    • El Fakhry Y., Ouellette M., and Papadopoulou B. A proteomic approach to identify developmentally regulated proteins in Leishmania infantum. Proteomics 2 (2002) 1007-1017
    • (2002) Proteomics , vol.2 , pp. 1007-1017
    • El Fakhry, Y.1    Ouellette, M.2    Papadopoulou, B.3
  • 54
    • 0142030010 scopus 로고    scopus 로고
    • Mapping the proteome of Leishmania Viannia parasites using two-dimensional polyacrylamide gel electrophoresis and associated technologies
    • Gongora R., Acestor N., Quadroni M., Fasel N., Saravia N.G., and Walker J. Mapping the proteome of Leishmania Viannia parasites using two-dimensional polyacrylamide gel electrophoresis and associated technologies. Biomedica 23 (2003) 153-160
    • (2003) Biomedica , vol.23 , pp. 153-160
    • Gongora, R.1    Acestor, N.2    Quadroni, M.3    Fasel, N.4    Saravia, N.G.5    Walker, J.6
  • 55
    • 0141520538 scopus 로고    scopus 로고
    • Developmentally induced changes of the proteome in the protozoan parasite Leishmania donovani
    • Bente M., Harder S., Wiesgigl M., Heukeshoven J., Gelhaus C., Krause E., et al. Developmentally induced changes of the proteome in the protozoan parasite Leishmania donovani. Proteomics 3 (2003) 1811-1829
    • (2003) Proteomics , vol.3 , pp. 1811-1829
    • Bente, M.1    Harder, S.2    Wiesgigl, M.3    Heukeshoven, J.4    Gelhaus, C.5    Krause, E.6
  • 56
    • 0141909066 scopus 로고    scopus 로고
    • Proteome mapping of the protozoan parasite Leishmania and application to the study of drug targets and resistance mechanisms
    • Drummelsmith J., Brochu V., Girard I., Messier N., and Ouellette M. Proteome mapping of the protozoan parasite Leishmania and application to the study of drug targets and resistance mechanisms. Mol Cell Proteomics 2 (2003) 146-155
    • (2003) Mol Cell Proteomics , vol.2 , pp. 146-155
    • Drummelsmith, J.1    Brochu, V.2    Girard, I.3    Messier, N.4    Ouellette, M.5
  • 58
    • 33645847251 scopus 로고    scopus 로고
    • Identification of developmentally-regulated proteins in Leishmania panamensis by proteome profiling of promastigotes and axenic amastigotes
    • Walker J., Vasquez J.J., Gomez M.A., Drummelsmith J., Burchmore R., Girard I., and Ouellette M. Identification of developmentally-regulated proteins in Leishmania panamensis by proteome profiling of promastigotes and axenic amastigotes. Mol Biochem Parasitol 147 (2006) 64-73
    • (2006) Mol Biochem Parasitol , vol.147 , pp. 64-73
    • Walker, J.1    Vasquez, J.J.2    Gomez, M.A.3    Drummelsmith, J.4    Burchmore, R.5    Girard, I.6    Ouellette, M.7
  • 59
    • 33745065761 scopus 로고    scopus 로고
    • Comparative two-dimensional gel electrophoresis maps for promastigotes of Leishmania amazonensis and Leishmania major
    • Brobey R.K., Mei F.C., Cheng X., and Soong L. Comparative two-dimensional gel electrophoresis maps for promastigotes of Leishmania amazonensis and Leishmania major. Braz J Infect Dis 10 (2006) 1-6
    • (2006) Braz J Infect Dis , vol.10 , pp. 1-6
    • Brobey, R.K.1    Mei, F.C.2    Cheng, X.3    Soong, L.4
  • 60
    • 33846568874 scopus 로고    scopus 로고
    • Establishing a liquid-phase IEF in combination with 2-DE for the analysis of Leishmania proteins
    • Brobey R.K., and Soong L. Establishing a liquid-phase IEF in combination with 2-DE for the analysis of Leishmania proteins. Proteomics 7 (2007) 116-120
    • (2007) Proteomics , vol.7 , pp. 116-120
    • Brobey, R.K.1    Soong, L.2
  • 65
    • 34247217300 scopus 로고    scopus 로고
    • Investigation of a protein expression profile by high-resolution bidimensional electrophoresis of Trypanosoma cruzi epimastigotes
    • Souza R.A., Henriques C., Alves-Ferreira M., Mendonça-Lima L., and Degrave W.M. Investigation of a protein expression profile by high-resolution bidimensional electrophoresis of Trypanosoma cruzi epimastigotes. Anal Biochem 365 (2007) 144-146
    • (2007) Anal Biochem , vol.365 , pp. 144-146
    • Souza, R.A.1    Henriques, C.2    Alves-Ferreira, M.3    Mendonça-Lima, L.4    Degrave, W.M.5
  • 66
    • 53149125159 scopus 로고    scopus 로고
    • Trypanosoma cruzi alkaline 2-DE: optimization and application to comparative proteome analysis of flagellate life stages
    • Magalhães A.D., Charneau S., Paba J., Guércio R.A., Teixeira A.R., Santana J.M., et al. Trypanosoma cruzi alkaline 2-DE: optimization and application to comparative proteome analysis of flagellate life stages. Proteome Sci 6 (2008) 24
    • (2008) Proteome Sci , vol.6 , pp. 24
    • Magalhães, A.D.1    Charneau, S.2    Paba, J.3    Guércio, R.A.4    Teixeira, A.R.5    Santana, J.M.6
  • 68
    • 0037466374 scopus 로고    scopus 로고
    • A reproducible protocol for analysis of the proteome of Trypanosoma brucei by 2-dimensional gel electrophoresis
    • van Deursen F.J., Thornton D.J., and Matthews K.R. A reproducible protocol for analysis of the proteome of Trypanosoma brucei by 2-dimensional gel electrophoresis. Mol Biochem Parasitol 128 (2003) 107-110
    • (2003) Mol Biochem Parasitol , vol.128 , pp. 107-110
    • van Deursen, F.J.1    Thornton, D.J.2    Matthews, K.R.3
  • 69
    • 31344479863 scopus 로고    scopus 로고
    • Visualisation and analysis of proteomic data from the procyclic form of Trypanosoma brucei
    • Jones A., Faldas A., Foucher A., Hunt E., Tait A., Wastling J.M., et al. Visualisation and analysis of proteomic data from the procyclic form of Trypanosoma brucei. Proteomics 6 (2006) 259-267
    • (2006) Proteomics , vol.6 , pp. 259-267
    • Jones, A.1    Faldas, A.2    Foucher, A.3    Hunt, E.4    Tait, A.5    Wastling, J.M.6
  • 70
    • 0017707814 scopus 로고
    • Leishmania in phlebotomid sandflies: VI. Importance of hindgut development in distinguishing between parasites of the Leishmania mexicana and L. braziliensis complexes
    • Lainson R., Ward R.D., and Shaw J.J. Leishmania in phlebotomid sandflies: VI. Importance of hindgut development in distinguishing between parasites of the Leishmania mexicana and L. braziliensis complexes. Proc R Soc Lond B 199 (1977) 309-320
    • (1977) Proc R Soc Lond B , vol.199 , pp. 309-320
    • Lainson, R.1    Ward, R.D.2    Shaw, J.J.3
  • 71
    • 34447264232 scopus 로고    scopus 로고
    • Transmission of Leishmania metacyclic promastigotes by phlebotomine sand flies
    • Bates P.A. Transmission of Leishmania metacyclic promastigotes by phlebotomine sand flies. Int J Parasitol 37 (2007) 1097-1106
    • (2007) Int J Parasitol , vol.37 , pp. 1097-1106
    • Bates, P.A.1
  • 72
    • 34347339518 scopus 로고    scopus 로고
    • Comparative genomic analysis of three Leishmania species that cause diverse human disease
    • Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A., et al. Comparative genomic analysis of three Leishmania species that cause diverse human disease. Nat Genet 39 (2007) 839-847
    • (2007) Nat Genet , vol.39 , pp. 839-847
    • Peacock, C.S.1    Seeger, K.2    Harris, D.3    Murphy, L.4    Ruiz, J.C.5    Quail, M.A.6
  • 73
    • 34447625535 scopus 로고    scopus 로고
    • Comparative genomics: from genotype to disease phenotype in the leishmaniases
    • Smith D.F., Peacock C.S., and Cruz A.K. Comparative genomics: from genotype to disease phenotype in the leishmaniases. Int J Parasitol 37 (2007) 1173-1186
    • (2007) Int J Parasitol , vol.37 , pp. 1173-1186
    • Smith, D.F.1    Peacock, C.S.2    Cruz, A.K.3
  • 74
    • 33745725868 scopus 로고    scopus 로고
    • A combined proteomic and transcriptomic approach to the study of stage differentiation in Leishmania infantum
    • McNicoll F., Drummelsmith J., Müller M., Madore E., Boilard N., Ouellette M., et al. A combined proteomic and transcriptomic approach to the study of stage differentiation in Leishmania infantum. Proteomics 6 (2006) 3567-3581
    • (2006) Proteomics , vol.6 , pp. 3567-3581
    • McNicoll, F.1    Drummelsmith, J.2    Müller, M.3    Madore, E.4    Boilard, N.5    Ouellette, M.6
  • 75
    • 33745862409 scopus 로고    scopus 로고
    • Prefractionation by digitonin extraction increases representation of the cytosolic and intracellular proteome of Leishmania infantum
    • Foucher A.L., Papadopoulou B., and Ouellette M. Prefractionation by digitonin extraction increases representation of the cytosolic and intracellular proteome of Leishmania infantum. J Proteome Res 5 (2006) 1741-1750
    • (2006) J Proteome Res , vol.5 , pp. 1741-1750
    • Foucher, A.L.1    Papadopoulou, B.2    Ouellette, M.3
  • 76
    • 33846202033 scopus 로고    scopus 로고
    • Genomic and proteomic expression analysis of Leishmania promastigote and amastigote life stages: the Leishmania genome is constitutively expressed
    • Leifso K., Cohen-Freue G., Dogra N., Murray A., and McMaster W.R. Genomic and proteomic expression analysis of Leishmania promastigote and amastigote life stages: the Leishmania genome is constitutively expressed. Mol Biochem Parasitol 152 (2007) 35-46
    • (2007) Mol Biochem Parasitol , vol.152 , pp. 35-46
    • Leifso, K.1    Cohen-Freue, G.2    Dogra, N.3    Murray, A.4    McMaster, W.R.5
  • 79
    • 44249089014 scopus 로고    scopus 로고
    • Leishmania major: identification of developmentally regulated proteins in procyclic and metacyclic promastigotes
    • Mojtahedi Z., Clos J., and Kamali-Sarvestani E. Leishmania major: identification of developmentally regulated proteins in procyclic and metacyclic promastigotes. Exp Parasitol 119 (2008) 422-429
    • (2008) Exp Parasitol , vol.119 , pp. 422-429
    • Mojtahedi, Z.1    Clos, J.2    Kamali-Sarvestani, E.3
  • 80
    • 43549096649 scopus 로고    scopus 로고
    • Post-translational modification of cellular proteins during Leishmania donovani differentiation
    • Rosenzweig D., Smith D., Myler P.J., Olafson R.W., and Zilberstein D. Post-translational modification of cellular proteins during Leishmania donovani differentiation. Proteomics 8 (2008) 1843-1850
    • (2008) Proteomics , vol.8 , pp. 1843-1850
    • Rosenzweig, D.1    Smith, D.2    Myler, P.J.3    Olafson, R.W.4    Zilberstein, D.5
  • 81
    • 0020103971 scopus 로고
    • A comparative study of Leishmania mexicana amastigotes and promastigotes. Enzyme activities and subcellular locations
    • Coombs G.H., Craft J.A., and Hart D.T. A comparative study of Leishmania mexicana amastigotes and promastigotes. Enzyme activities and subcellular locations. Mol Biochem Parasitol 5 (1982) 199-211
    • (1982) Mol Biochem Parasitol , vol.5 , pp. 199-211
    • Coombs, G.H.1    Craft, J.A.2    Hart, D.T.3
  • 82
    • 0020353207 scopus 로고
    • Leishmania mexicana: energy metabolism of amastigotes and promastigotes
    • Hart D.T., and Coombs G.H. Leishmania mexicana: energy metabolism of amastigotes and promastigotes. Exp Parasitol 54 (1982) 397-409
    • (1982) Exp Parasitol , vol.54 , pp. 397-409
    • Hart, D.T.1    Coombs, G.H.2
  • 83
    • 0037090528 scopus 로고    scopus 로고
    • Developmental regulation without transcriptional control? From fly to man and back again
    • Clayton C.E. Developmental regulation without transcriptional control? From fly to man and back again. EMBO J 21 (2002) 1881-1888
    • (2002) EMBO J , vol.21 , pp. 1881-1888
    • Clayton, C.E.1
  • 84
    • 35349012982 scopus 로고    scopus 로고
    • Post-transcriptional regulation of gene expression in trypanosomes and leishmanias
    • Clayton C., and Shapira M. Post-transcriptional regulation of gene expression in trypanosomes and leishmanias. Mol Biochem Parasitol 156 (2007) 93-101
    • (2007) Mol Biochem Parasitol , vol.156 , pp. 93-101
    • Clayton, C.1    Shapira, M.2
  • 86
    • 0030035450 scopus 로고    scopus 로고
    • The developmental expression of Leishmania donovani A2 amastigote-specific genes is post-transcriptionally mediated and involves elements located in the 3′-untranslated region
    • Charest H., Zhang W.W., and Matlashewski G. The developmental expression of Leishmania donovani A2 amastigote-specific genes is post-transcriptionally mediated and involves elements located in the 3′-untranslated region. J Biol Chem 271 (1996) 17081-17090
    • (1996) J Biol Chem , vol.271 , pp. 17081-17090
    • Charest, H.1    Zhang, W.W.2    Matlashewski, G.3
  • 87
    • 0035861634 scopus 로고    scopus 로고
    • The stage-regulated expression of Leishmania mexicana CPB cysteine proteases is mediated by an intercistronic sequence element
    • Brooks D.R., Denise H., Westrop G.D., Coombs G.H., and Mottram J.C. The stage-regulated expression of Leishmania mexicana CPB cysteine proteases is mediated by an intercistronic sequence element. J Biol Chem 276 (2001) 47061-47069
    • (2001) J Biol Chem , vol.276 , pp. 47061-47069
    • Brooks, D.R.1    Denise, H.2    Westrop, G.D.3    Coombs, G.H.4    Mottram, J.C.5
  • 88
    • 0034895706 scopus 로고    scopus 로고
    • Stage-specific expression in Leishmania conferred by 3′ untranslated regions of L. major leishmanolysin genes (GP63)
    • Kelly B.L., Nelson T.N., and McMaster W.R. Stage-specific expression in Leishmania conferred by 3′ untranslated regions of L. major leishmanolysin genes (GP63). Mol Biochem Parasitol 116 (2001) 101-104
    • (2001) Mol Biochem Parasitol , vol.116 , pp. 101-104
    • Kelly, B.L.1    Nelson, T.N.2    McMaster, W.R.3
  • 89
    • 26444522312 scopus 로고    scopus 로고
    • The expression of HSP83 genes in Leishmania infantum is affected by temperature and by stage-differentiation and is regulated at the levels of mRNA stability and translation
    • Larreta R., Soto M., Quijada L., Folgueira C., Abanades D.R., Alonso C., et al. The expression of HSP83 genes in Leishmania infantum is affected by temperature and by stage-differentiation and is regulated at the levels of mRNA stability and translation. BMC Mol Biol 5 (2004) 3
    • (2004) BMC Mol Biol , vol.5 , pp. 3
    • Larreta, R.1    Soto, M.2    Quijada, L.3    Folgueira, C.4    Abanades, D.R.5    Alonso, C.6
  • 90
    • 19344371567 scopus 로고    scopus 로고
    • Regulation of genes encoding the major surface protease of Leishmania chagasi via mRNA stability
    • Purdy J.E., Donelson J.E., and Wilson M.E. Regulation of genes encoding the major surface protease of Leishmania chagasi via mRNA stability. Mol Biochem Parasitol 142 (2005) 88-97
    • (2005) Mol Biochem Parasitol , vol.142 , pp. 88-97
    • Purdy, J.E.1    Donelson, J.E.2    Wilson, M.E.3
  • 91
    • 0027563564 scopus 로고
    • Developmental life cycle of Leishmania-cultivation and characterization of cultured extracellular amastigotes
    • Pan A.A., Duboise S.M., Eperon S., Rivas L., Hodgkinson V., Traub-Cseko Y., et al. Developmental life cycle of Leishmania-cultivation and characterization of cultured extracellular amastigotes. J Eukaryot Microbiol 40 (1993) 213-223
    • (1993) J Eukaryot Microbiol , vol.40 , pp. 213-223
    • Pan, A.A.1    Duboise, S.M.2    Eperon, S.3    Rivas, L.4    Hodgkinson, V.5    Traub-Cseko, Y.6
  • 92
    • 0030902239 scopus 로고    scopus 로고
    • Axenically cultured amastigote forms as an in vitro model for investigation of antileishmanial agents
    • Sereno D., and Lemesre J.-L. Axenically cultured amastigote forms as an in vitro model for investigation of antileishmanial agents. Antimicrob Agents Chemother 41 (1997) 972-976
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 972-976
    • Sereno, D.1    Lemesre, J.-L.2
  • 93
    • 0034441836 scopus 로고    scopus 로고
    • Cultivation and characterization of stable Leishmania guyanensis complex axenic amastigotes derived from infected U937 cells
    • Puentes F., Diaz D., Hoya R.D., Gutíerrez J.A., Lozano J.M., Patarroyo M.E., et al. Cultivation and characterization of stable Leishmania guyanensis complex axenic amastigotes derived from infected U937 cells. Am J Trop Med Hyg 63 (2000) 102-110
    • (2000) Am J Trop Med Hyg , vol.63 , pp. 102-110
    • Puentes, F.1    Diaz, D.2    Hoya, R.D.3    Gutíerrez, J.A.4    Lozano, J.M.5    Patarroyo, M.E.6
  • 94
    • 0035005951 scopus 로고    scopus 로고
    • In vitro cultivation and characterization of axenic amastigotes of Leishmania
    • Gupta N., Goyal N., and Rastogi A.K. In vitro cultivation and characterization of axenic amastigotes of Leishmania. Trends Parasitol 17 (2001) 150-153
    • (2001) Trends Parasitol , vol.17 , pp. 150-153
    • Gupta, N.1    Goyal, N.2    Rastogi, A.K.3
  • 96
    • 1242294372 scopus 로고    scopus 로고
    • Generation of Leishmania donovani axenic amastigotes: their growth and biological characteristics
    • Debrabant A., Joshi M.B., Pimenta P.F., and Dwyer D.M. Generation of Leishmania donovani axenic amastigotes: their growth and biological characteristics. Int J Parasitol 34 (2004) 205-217
    • (2004) Int J Parasitol , vol.34 , pp. 205-217
    • Debrabant, A.1    Joshi, M.B.2    Pimenta, P.F.3    Dwyer, D.M.4
  • 97
    • 52649088373 scopus 로고    scopus 로고
    • Transgenic, fluorescent Leishmania mexicana allow direct analysis of the proteome of intracellular amastigotes
    • Paape D., Lippuner C., Schmid M., Ackermann R., Barrios-Llerena M.E., Zimny-Arndt U., et al. Transgenic, fluorescent Leishmania mexicana allow direct analysis of the proteome of intracellular amastigotes. Mol Cell Proteomics 7 (2008) 1688-1701
    • (2008) Mol Cell Proteomics , vol.7 , pp. 1688-1701
    • Paape, D.1    Lippuner, C.2    Schmid, M.3    Ackermann, R.4    Barrios-Llerena, M.E.5    Zimny-Arndt, U.6
  • 98
    • 0025925012 scopus 로고
    • Metastatic capability of Leishmania (Viannia) panamensis and Leishmania (Viannia) guyanensis in golden hamsters
    • Martinez J.E., Travi B.L., Valencia A.Z., and Saravia N.G. Metastatic capability of Leishmania (Viannia) panamensis and Leishmania (Viannia) guyanensis in golden hamsters. J Parasitol 77 (1991) 762-768
    • (1991) J Parasitol , vol.77 , pp. 762-768
    • Martinez, J.E.1    Travi, B.L.2    Valencia, A.Z.3    Saravia, N.G.4
  • 99
    • 0031778351 scopus 로고    scopus 로고
    • Mucosal leishmaniasis due to Leishmania (Viannia) panamensis: clinical characteristics
    • Osorio L., Castillo C.M., and Ochoa M.T. Mucosal leishmaniasis due to Leishmania (Viannia) panamensis: clinical characteristics. Am J Trop Med Hyg 59 (1998) 49-52
    • (1998) Am J Trop Med Hyg , vol.59 , pp. 49-52
    • Osorio, L.1    Castillo, C.M.2    Ochoa, M.T.3
  • 100
    • 4444270867 scopus 로고    scopus 로고
    • Proteomic analysis of Trypanosoma cruzi developmental stages using isotope-coded affinity tag reagents
    • Paba J., Santana J.M., Teixeira A.R., Fontes W., Sousa M.V., and Ricart C.A. Proteomic analysis of Trypanosoma cruzi developmental stages using isotope-coded affinity tag reagents. J Proteome Res 3 (2004) 517-524
    • (2004) J Proteome Res , vol.3 , pp. 517-524
    • Paba, J.1    Santana, J.M.2    Teixeira, A.R.3    Fontes, W.4    Sousa, M.V.5    Ricart, C.A.6
  • 101
  • 102
    • 34347376906 scopus 로고    scopus 로고
    • The relationships between the isoelectric point and: length of proteins, taxonomy and ecology of organisms
    • Kiraga J., Mackiewicz P., Mackiewicz D., Kowalczuk M., Biecek P., Polak N., et al. The relationships between the isoelectric point and: length of proteins, taxonomy and ecology of organisms. BMC Genomics 8 (2007) 163
    • (2007) BMC Genomics , vol.8 , pp. 163
    • Kiraga, J.1    Mackiewicz, P.2    Mackiewicz, D.3    Kowalczuk, M.4    Biecek, P.5    Polak, N.6
  • 103
    • 14044264288 scopus 로고    scopus 로고
    • The developmental cell biology of Trypanosoma brucei
    • Matthews K.R. The developmental cell biology of Trypanosoma brucei. J Cell Sci 118 (2005) 283-290
    • (2005) J Cell Sci , vol.118 , pp. 283-290
    • Matthews, K.R.1
  • 104
    • 0023137641 scopus 로고
    • Differential protein synthesis during the life cycle of the protozoan parasite Trypanosoma brucei
    • Shapiro S.Z., and Kimmel B.E. Differential protein synthesis during the life cycle of the protozoan parasite Trypanosoma brucei. J Protozool 34 (1987) 58-62
    • (1987) J Protozool , vol.34 , pp. 58-62
    • Shapiro, S.Z.1    Kimmel, B.E.2
  • 105
    • 0023464501 scopus 로고
    • Compartmentation of carbohydrate metabolism in trypanosomes
    • Opperdoes F.R. Compartmentation of carbohydrate metabolism in trypanosomes. Annu Rev Microbiol 41 (1987) 127-151
    • (1987) Annu Rev Microbiol , vol.41 , pp. 127-151
    • Opperdoes, F.R.1
  • 107
    • 0025375818 scopus 로고
    • Trypanosoma brucei: two-dimensional gel analysis of the major glycosomal proteins during the life cycle
    • Parsons M., and Nielsen B. Trypanosoma brucei: two-dimensional gel analysis of the major glycosomal proteins during the life cycle. Exp Parasitol 70 (1990) 276-285
    • (1990) Exp Parasitol , vol.70 , pp. 276-285
    • Parsons, M.1    Nielsen, B.2
  • 108
    • 39049118320 scopus 로고    scopus 로고
    • Differential expression of glycosomal and mitochondrial proteins in the two major life-cycle stages of Trypanosoma brucei
    • Vertommen D., Van Roy J., Szikora J.P., Rider M.H., Michels P.A., and Opperdoes F.R. Differential expression of glycosomal and mitochondrial proteins in the two major life-cycle stages of Trypanosoma brucei. Mol Biochem Parasitol 158 (2008) 189-201
    • (2008) Mol Biochem Parasitol , vol.158 , pp. 189-201
    • Vertommen, D.1    Van Roy, J.2    Szikora, J.P.3    Rider, M.H.4    Michels, P.A.5    Opperdoes, F.R.6
  • 109
    • 33745060757 scopus 로고    scopus 로고
    • Comparative proteomics of glycosomes from bloodstream form and procyclic culture form Trypanosoma brucei brucei
    • Colasante C., Ellis M., Ruppert T., and Voncken F. Comparative proteomics of glycosomes from bloodstream form and procyclic culture form Trypanosoma brucei brucei. Proteomics. 6 11 (2006 Jun) 3275-3293
    • (2006) Proteomics. , vol.6 , Issue.11 , pp. 3275-3293
    • Colasante, C.1    Ellis, M.2    Ruppert, T.3    Voncken, F.4
  • 110
    • 0024497978 scopus 로고
    • The enzymes of the classical pentose phosphate pathway display differential activities in procyclic and bloodstream forms of Trypanosoma brucei
    • Cronín C.N., Nolan D.P., and Voorheis H.P. The enzymes of the classical pentose phosphate pathway display differential activities in procyclic and bloodstream forms of Trypanosoma brucei. FEBS Lett 244 (1989) 26-30
    • (1989) FEBS Lett , vol.244 , pp. 26-30
    • Cronín, C.N.1    Nolan, D.P.2    Voorheis, H.P.3
  • 111
    • 0037934549 scopus 로고    scopus 로고
    • Subcellular proteomics
    • Dreger M. Subcellular proteomics. Mass Spectrom Rev 22 (2003) 27-56
    • (2003) Mass Spectrom Rev , vol.22 , pp. 27-56
    • Dreger, M.1
  • 112
    • 0022555868 scopus 로고
    • Discontinuous transcription and antigenic variation in trypanosomes
    • Borst P. Discontinuous transcription and antigenic variation in trypanosomes. Annu Rev Biochem 55 (1986) 701-732
    • (1986) Annu Rev Biochem , vol.55 , pp. 701-732
    • Borst, P.1
  • 113
    • 0023038870 scopus 로고
    • Discontinuous transcription and splicing in trypanosomes
    • Van der Ploeg L.H. Discontinuous transcription and splicing in trypanosomes. Cell 47 (1986) 479-480
    • (1986) Cell , vol.47 , pp. 479-480
    • Van der Ploeg, L.H.1
  • 114
    • 0037922159 scopus 로고    scopus 로고
    • Uridine insertion/deletion RNA editing in trypanosome mitochondria - a review
    • Estevez A.M., and Simpson L. Uridine insertion/deletion RNA editing in trypanosome mitochondria - a review. Gene 240 (1999) 247-260
    • (1999) Gene , vol.240 , pp. 247-260
    • Estevez, A.M.1    Simpson, L.2
  • 115
    • 0033534532 scopus 로고    scopus 로고
    • Novel organization and sequences of five genes encoding all six enzymes for de novo pyrimidine biosynthesis in Trypanosoma cruzi
    • Gao G., Nara T., Nakajima-Shimada J., and Aoki T. Novel organization and sequences of five genes encoding all six enzymes for de novo pyrimidine biosynthesis in Trypanosoma cruzi. J Mol Biol 285 (1999) 149-161
    • (1999) J Mol Biol , vol.285 , pp. 149-161
    • Gao, G.1    Nara, T.2    Nakajima-Shimada, J.3    Aoki, T.4
  • 117
    • 34548317153 scopus 로고    scopus 로고
    • Alternative transsplicing of the Trypanosoma cruzi LYT1 gene transcript results in compartmental and functional switch for the encoded protein
    • Benabdellah K., Gonzalez-Rey E., and Gonzalez A. Alternative transsplicing of the Trypanosoma cruzi LYT1 gene transcript results in compartmental and functional switch for the encoded protein. Mol Microbiol 65 (2007) 1559-1567
    • (2007) Mol Microbiol , vol.65 , pp. 1559-1567
    • Benabdellah, K.1    Gonzalez-Rey, E.2    Gonzalez, A.3
  • 118
    • 0025771198 scopus 로고
    • Subcellular localization of glutamate dehydrogenases and alanine aminotransferase in epimastigotes of Trypanosoma cruzi
    • Duschak V.G., and Cazzulo J.J. Subcellular localization of glutamate dehydrogenases and alanine aminotransferase in epimastigotes of Trypanosoma cruzi. FEMS Microbiol Lett 67 (1991) 131-135
    • (1991) FEMS Microbiol Lett , vol.67 , pp. 131-135
    • Duschak, V.G.1    Cazzulo, J.J.2
  • 119
    • 0030034571 scopus 로고    scopus 로고
    • Import of a DHFR hybrid protein into glycosomes in vivo is not inhibited by the folate-analogue aminopterin
    • Hausler T., Stierhof Y.D., Wirtz E., and Clayton C. Import of a DHFR hybrid protein into glycosomes in vivo is not inhibited by the folate-analogue aminopterin. J Cell Biol 132 (1996) 311-324
    • (1996) J Cell Biol , vol.132 , pp. 311-324
    • Hausler, T.1    Stierhof, Y.D.2    Wirtz, E.3    Clayton, C.4
  • 120
    • 0034723361 scopus 로고    scopus 로고
    • A developmentally regulated aconitase related to iron-regulatory protein-1 is localized in the cytoplasm and in the mitochondrion of Trypanosoma brucei
    • Saas J., Ziegelbauer K., von Haeseler A., Fast B., and Boshart M. A developmentally regulated aconitase related to iron-regulatory protein-1 is localized in the cytoplasm and in the mitochondrion of Trypanosoma brucei. J Biol Chem 275 (2000) 2745-2755
    • (2000) J Biol Chem , vol.275 , pp. 2745-2755
    • Saas, J.1    Ziegelbauer, K.2    von Haeseler, A.3    Fast, B.4    Boshart, M.5
  • 121
    • 2942562566 scopus 로고    scopus 로고
    • Two linked genes of Leishmania infantum encode tryparedoxins localised to cytosol and mitochondrion
    • Castro H., Sousa C., Novais M., Santos M., Budde H., Cordeiro-da-Silva A., et al. Two linked genes of Leishmania infantum encode tryparedoxins localised to cytosol and mitochondrion. Mol Biochem Parasitol 136 (2004) 137-147
    • (2004) Mol Biochem Parasitol , vol.136 , pp. 137-147
    • Castro, H.1    Sousa, C.2    Novais, M.3    Santos, M.4    Budde, H.5    Cordeiro-da-Silva, A.6
  • 122
    • 4544269846 scopus 로고    scopus 로고
    • Transketolase from Leishmania mexicana has a dual subcellular localization
    • Veitch N.J., Maugeri D.A., Cazzulo J.J., Lindqvist Y., and Barrett M.P. Transketolase from Leishmania mexicana has a dual subcellular localization. Biochem J 382 (2004) 759-767
    • (2004) Biochem J , vol.382 , pp. 759-767
    • Veitch, N.J.1    Maugeri, D.A.2    Cazzulo, J.J.3    Lindqvist, Y.4    Barrett, M.P.5
  • 123
    • 48349095097 scopus 로고    scopus 로고
    • Leishmania infantum: tuning digitonin fractionation for comparative proteomic of the mitochondrial protein content
    • Hide M., Ritleng A.S., Brizard J.P., Monte-Allegre A., and Sereno D. Leishmania infantum: tuning digitonin fractionation for comparative proteomic of the mitochondrial protein content. Parasitol Res 103 (2008) 989-992
    • (2008) Parasitol Res , vol.103 , pp. 989-992
    • Hide, M.1    Ritleng, A.S.2    Brizard, J.P.3    Monte-Allegre, A.4    Sereno, D.5
  • 125
    • 0033647396 scopus 로고    scopus 로고
    • Trypanosoma cruzi epimastigote endocytic pathway: cargo enters the cytostome and passes through an early endosomal network before storage in reservosomes
    • Porto-Carreiro I., Attias M., Miranda K., De Souza W., and Cunha-e-Silva N. Trypanosoma cruzi epimastigote endocytic pathway: cargo enters the cytostome and passes through an early endosomal network before storage in reservosomes. Eur J Cell Biol 79 (2000) 858-869
    • (2000) Eur J Cell Biol , vol.79 , pp. 858-869
    • Porto-Carreiro, I.1    Attias, M.2    Miranda, K.3    De Souza, W.4    Cunha-e-Silva, N.5
  • 127
    • 47249134299 scopus 로고    scopus 로고
    • Proteomics in Trypanosoma cruzi-localization of novel proteins to various organelles
    • Ferella M., Nilsson D., Darban H., Rodrigues C., Bontempi E.J., Docampo R., et al. Proteomics in Trypanosoma cruzi-localization of novel proteins to various organelles. Proteomics 8 (2008) 2735-2749
    • (2008) Proteomics , vol.8 , pp. 2735-2749
    • Ferella, M.1    Nilsson, D.2    Darban, H.3    Rodrigues, C.4    Bontempi, E.J.5    Docampo, R.6
  • 128
    • 67649908740 scopus 로고    scopus 로고
    • Proteomic and network analysis characterize stage-specific metabolism in Trypanosoma cruzi
    • Roberts S.B., Robichaux J.L., Chavali A.K., Manque P.A., Lee V., Lara A.M., et al. Proteomic and network analysis characterize stage-specific metabolism in Trypanosoma cruzi. BMC Syst Biol 3 (2009) 52
    • (2009) BMC Syst Biol , vol.3 , pp. 52
    • Roberts, S.B.1    Robichaux, J.L.2    Chavali, A.K.3    Manque, P.A.4    Lee, V.5    Lara, A.M.6
  • 132
    • 0026691797 scopus 로고
    • Identification of a large prelysosomal compartment in the pathogenic protozoon Trypanosoma cruzi
    • Soares M.J., Souto-Padron T., and De Souza W. Identification of a large prelysosomal compartment in the pathogenic protozoon Trypanosoma cruzi. J Cell Sci 102 (1992) 157-167
    • (1992) J Cell Sci , vol.102 , pp. 157-167
    • Soares, M.J.1    Souto-Padron, T.2    De Souza, W.3
  • 134
    • 7644222414 scopus 로고    scopus 로고
    • Characterization of an ABCA-like transporter involved in vesicular trafficking in the protozoan parasite Trypanosoma cruzi
    • Torres C., Perez-Victoria F.J., Parodi-Talice A., Castanys S., and Gamarro F. Characterization of an ABCA-like transporter involved in vesicular trafficking in the protozoan parasite Trypanosoma cruzi. Mol Microbiol 54 (2004) 632-646
    • (2004) Mol Microbiol , vol.54 , pp. 632-646
    • Torres, C.1    Perez-Victoria, F.J.2    Parodi-Talice, A.3    Castanys, S.4    Gamarro, F.5
  • 135
    • 25144479943 scopus 로고    scopus 로고
    • Characterization of farnesylated protein tyrosine phosphatase TcPRL-1 from Trypanosoma cruzi
    • Cuevas I.C., Rohloff P., Sanchez D.O., and Docampo R. Characterization of farnesylated protein tyrosine phosphatase TcPRL-1 from Trypanosoma cruzi. Eukaryot Cell 4 (2005) 1550-1561
    • (2005) Eukaryot Cell , vol.4 , pp. 1550-1561
    • Cuevas, I.C.1    Rohloff, P.2    Sanchez, D.O.3    Docampo, R.4
  • 136
    • 29644436501 scopus 로고    scopus 로고
    • Role for a P-type H1-ATPase in the acidification of the endocytic pathway of Trypanosoma cruzi
    • Vieira M., Rohloff P., Luo S., Cunha-e-Silva N.L., de Souza W., and Docampo R. Role for a P-type H1-ATPase in the acidification of the endocytic pathway of Trypanosoma cruzi. Biochem J 392 (2005) 467-474
    • (2005) Biochem J , vol.392 , pp. 467-474
    • Vieira, M.1    Rohloff, P.2    Luo, S.3    Cunha-e-Silva, N.L.4    de Souza, W.5    Docampo, R.6
  • 138
    • 22544453281 scopus 로고    scopus 로고
    • The structure of the 80S ribosome from Trypanosoma cruzi reveals unique rRNA components
    • Gao H., Ayub M.J., Levin M.J., and Frank J. The structure of the 80S ribosome from Trypanosoma cruzi reveals unique rRNA components. Proc Natl Acad Sci U S A 102 (2005) 10206-10211
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 10206-10211
    • Gao, H.1    Ayub, M.J.2    Levin, M.J.3    Frank, J.4
  • 139
    • 67650367143 scopus 로고    scopus 로고
    • Proteomic analysis of detergent-solubilized membrane proteins from insect-developmental forms of Trypanosoma cruzi
    • Cordero E.M., Nakayasu E.S., Gentil L.G., Yoshida N., Almeida I.C., and da Silveira J.F. Proteomic analysis of detergent-solubilized membrane proteins from insect-developmental forms of Trypanosoma cruzi. J Proteome Res 8 (2009) 3642-3652
    • (2009) J Proteome Res , vol.8 , pp. 3642-3652
    • Cordero, E.M.1    Nakayasu, E.S.2    Gentil, L.G.3    Yoshida, N.4    Almeida, I.C.5    da Silveira, J.F.6
  • 140
    • 2442436725 scopus 로고    scopus 로고
    • RNA interference in protozoan parasites
    • Ullu E., Tschudi C., and Chakraborty T. RNA interference in protozoan parasites. Cell Microbiol 6 (2004) 509-519
    • (2004) Cell Microbiol , vol.6 , pp. 509-519
    • Ullu, E.1    Tschudi, C.2    Chakraborty, T.3
  • 141
    • 33644858832 scopus 로고    scopus 로고
    • Flagellar motility is required for the viability of the bloodstream trypanosome
    • Broadhead R., Dawe H.R., Farr H., Griffiths S., Hart S.R., Portman N., et al. Flagellar motility is required for the viability of the bloodstream trypanosome. Nature 440 (2006) 224-227
    • (2006) Nature , vol.440 , pp. 224-227
    • Broadhead, R.1    Dawe, H.R.2    Farr, H.3    Griffiths, S.4    Hart, S.R.5    Portman, N.6
  • 142
    • 0035164020 scopus 로고    scopus 로고
    • Association of two novel proteins, TbMP52 and TbMP48, with the Trypanosoma brucei RNA editing complex
    • Panigrahi A.K., Gygi S., Ernst N., Igo Jr. R.P., Palazzo S.S., and Schnaufer A. Association of two novel proteins, TbMP52 and TbMP48, with the Trypanosoma brucei RNA editing complex. Mol Cell Biol 21 (2001) 380-389
    • (2001) Mol Cell Biol , vol.21 , pp. 380-389
    • Panigrahi, A.K.1    Gygi, S.2    Ernst, N.3    Igo Jr., R.P.4    Palazzo, S.S.5    Schnaufer, A.6
  • 143
    • 0038488182 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the editosome and other multiprotein complexes in Trypanosoma brucei
    • Panigrahi A.K., Allen T.E., Stuart K., Haynes P.A., and Gygi S.P. Mass spectrometric analysis of the editosome and other multiprotein complexes in Trypanosoma brucei. J Am Soc Mass Spectrom 14 (2003) 728-735
    • (2003) J Am Soc Mass Spectrom , vol.14 , pp. 728-735
    • Panigrahi, A.K.1    Allen, T.E.2    Stuart, K.3    Haynes, P.A.4    Gygi, S.P.5
  • 144
    • 74049121769 scopus 로고    scopus 로고
    • Isolation and compositional analysis of trypanosomatid editosomes
    • Panigrahi A.K., Schnaufer A., and Stuart K.D. Isolation and compositional analysis of trypanosomatid editosomes. Methods Enzymol 424 (2007) 3-24
    • (2007) Methods Enzymol , vol.424 , pp. 3-24
    • Panigrahi, A.K.1    Schnaufer, A.2    Stuart, K.D.3
  • 145
    • 41549134681 scopus 로고    scopus 로고
    • Mitochondrial complexes in Trypanosoma brucei: a novel complex and a unique oxidoreductase complex
    • Panigrahi A.K., Zíková A., Dalley R.A., Acestor N., Ogata Y., Anupama A., et al. Mitochondrial complexes in Trypanosoma brucei: a novel complex and a unique oxidoreductase complex. Mol Cell Proteomics 7 (2008) 534-545
    • (2008) Mol Cell Proteomics , vol.7 , pp. 534-545
    • Panigrahi, A.K.1    Zíková, A.2    Dalley, R.A.3    Acestor, N.4    Ogata, Y.5    Anupama, A.6
  • 146
    • 47849100472 scopus 로고    scopus 로고
    • Trypanosoma brucei mitochondrial ribosomes: affinity purification and component identification by mass spectrometry
    • Zíková A., Panigrahi A.K., Dalley R.A., Acestor N., Anupama A., Ogata Y., et al. Trypanosoma brucei mitochondrial ribosomes: affinity purification and component identification by mass spectrometry. Mol Cell Proteomics 7 (2008) 1286-1296
    • (2008) Mol Cell Proteomics , vol.7 , pp. 1286-1296
    • Zíková, A.1    Panigrahi, A.K.2    Dalley, R.A.3    Acestor, N.4    Anupama, A.5    Ogata, Y.6
  • 148
    • 33646870148 scopus 로고    scopus 로고
    • Compositionally and functionally distinct editosomes in Trypanosoma brucei
    • Panigrahi A.K., Ernst N.L., Domingo G.J., Fleck M., Salavati R., and Stuart K.D. Compositionally and functionally distinct editosomes in Trypanosoma brucei. RNA 12 (2006) 1038-1049
    • (2006) RNA , vol.12 , pp. 1038-1049
    • Panigrahi, A.K.1    Ernst, N.L.2    Domingo, G.J.3    Fleck, M.4    Salavati, R.5    Stuart, K.D.6
  • 149
    • 71049191352 scopus 로고    scopus 로고
    • Evidence for a shared nuclear pore complex architecture that is conserved from the last common eukaryotic ancestor
    • DeGrasse J.A., DuBois K.N., Devos D., Siegel T.N., Sali A., Field M.C., et al. Evidence for a shared nuclear pore complex architecture that is conserved from the last common eukaryotic ancestor. Mol Cell Proteomics 8 (2009) 2119-2130
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2119-2130
    • DeGrasse, J.A.1    DuBois, K.N.2    Devos, D.3    Siegel, T.N.4    Sali, A.5    Field, M.C.6
  • 150
    • 0035851114 scopus 로고    scopus 로고
    • Isolation and characterization of subnuclear compartments from Trypanosoma brucei. Identification of a major repetitive nuclear lamina component
    • Field M.C., and Rout M.P. Isolation and characterization of subnuclear compartments from Trypanosoma brucei. Identification of a major repetitive nuclear lamina component. J Biol Chem 276 (2001) 38261-38267
    • (2001) J Biol Chem , vol.276 , pp. 38261-38267
    • Field, M.C.1    Rout, M.P.2
  • 151
    • 85052549634 scopus 로고    scopus 로고
    • High-yield isolation and subcellular proteomic characterization of nuclear and subnuclear structures from trypanosomes
    • Degrasse J.A., Chait B.T., Field M.C., and Rout M.P. High-yield isolation and subcellular proteomic characterization of nuclear and subnuclear structures from trypanosomes. Methods Mol Biol 463 (2008) 77-92
    • (2008) Methods Mol Biol , vol.463 , pp. 77-92
    • Degrasse, J.A.1    Chait, B.T.2    Field, M.C.3    Rout, M.P.4
  • 152
    • 0023663094 scopus 로고
    • Inactivation of transcription by UV irradiation of T. brucei provides evidence for a multicistronic transcription unit including a VSG gene
    • Johnson P.J., Kooter J.M., and Borst P. Inactivation of transcription by UV irradiation of T. brucei provides evidence for a multicistronic transcription unit including a VSG gene. Cell 51 (1987) 273-281
    • (1987) Cell , vol.51 , pp. 273-281
    • Johnson, P.J.1    Kooter, J.M.2    Borst, P.3
  • 153
    • 0027193605 scopus 로고
    • Coupling of poly(A) site selection and trans-splicing in Leishmania
    • LeBowitz J.H., Smith H.Q., Rusche L., and Beverley S.M. Coupling of poly(A) site selection and trans-splicing in Leishmania. Genes Dev 7 (1993) 996-1007
    • (1993) Genes Dev , vol.7 , pp. 996-1007
    • LeBowitz, J.H.1    Smith, H.Q.2    Rusche, L.3    Beverley, S.M.4
  • 154
    • 0142247085 scopus 로고    scopus 로고
    • trans and cis splicing in trypanosomatids: mechanism, factors, and regulation
    • Liang X.H., Haritan A., Uliel S., and Michaeli S. trans and cis splicing in trypanosomatids: mechanism, factors, and regulation. Eukaryot Cell 2 (2003) 830-840
    • (2003) Eukaryot Cell , vol.2 , pp. 830-840
    • Liang, X.H.1    Haritan, A.2    Uliel, S.3    Michaeli, S.4
  • 158
    • 58249088149 scopus 로고    scopus 로고
    • Analysis of the trypanosome flagellar proteome using a combined electron transfer/collisionally activated dissociation strategy
    • Hart S.R., Lau K.W., Hao Z., Broadhead R., Portman N., Hühmer A., et al. Analysis of the trypanosome flagellar proteome using a combined electron transfer/collisionally activated dissociation strategy. J Am Soc Mass Spectrom 20 (2009) 167-175
    • (2009) J Am Soc Mass Spectrom , vol.20 , pp. 167-175
    • Hart, S.R.1    Lau, K.W.2    Hao, Z.3    Broadhead, R.4    Portman, N.5    Hühmer, A.6
  • 159
    • 65549110811 scopus 로고    scopus 로고
    • Combining RNA interference mutants and comparative proteomics to identify protein components and dependences in a eukaryotic flagellum
    • Portman N., Lacomble S., Thomas B., McKean P.G., and Gull K. Combining RNA interference mutants and comparative proteomics to identify protein components and dependences in a eukaryotic flagellum. J Biol Chem 284 (2009) 5610-5619
    • (2009) J Biol Chem , vol.284 , pp. 5610-5619
    • Portman, N.1    Lacomble, S.2    Thomas, B.3    McKean, P.G.4    Gull, K.5
  • 160
    • 38149099329 scopus 로고    scopus 로고
    • Characterisation of the plasma membrane subproteome of bloodstream form Trypanosoma brucei
    • Bridges D.J., Pitt A.R., Hanrahan O., Brennan K., Voorheis H.P., Herzyk P., et al. Characterisation of the plasma membrane subproteome of bloodstream form Trypanosoma brucei. Proteomics 8 (2008) 83-99
    • (2008) Proteomics , vol.8 , pp. 83-99
    • Bridges, D.J.1    Pitt, A.R.2    Hanrahan, O.3    Brennan, K.4    Voorheis, H.P.5    Herzyk, P.6
  • 162
    • 70349988784 scopus 로고    scopus 로고
    • Proteomic characterization of the released/secreted proteins of Leishmania (Viannia) braziliensis promastigotes
    • Cuervo P., De Jesus J.B., Saboia-Vahia L., Mendonça-Lima L., Domont G.B., and Cupolillo E. Proteomic characterization of the released/secreted proteins of Leishmania (Viannia) braziliensis promastigotes. J Proteomics 73 (2009) 79-92
    • (2009) J Proteomics , vol.73 , pp. 79-92
    • Cuervo, P.1    De Jesus, J.B.2    Saboia-Vahia, L.3    Mendonça-Lima, L.4    Domont, G.B.5    Cupolillo, E.6
  • 163
    • 39049129358 scopus 로고    scopus 로고
    • Virulence and pathogenicity patterns of Trypanosoma brucei gambiense field isolates in experimentally infected mouse: differences in host immune response modulation by secretome and proteomics
    • Holzmuller P., Biron D.G., Courtois P., Koffi M., Bras-Gonçalves R., Daulouède S., et al. Virulence and pathogenicity patterns of Trypanosoma brucei gambiense field isolates in experimentally infected mouse: differences in host immune response modulation by secretome and proteomics. Microbes Infect 10 (2008) 79-86
    • (2008) Microbes Infect , vol.10 , pp. 79-86
    • Holzmuller, P.1    Biron, D.G.2    Courtois, P.3    Koffi, M.4    Bras-Gonçalves, R.5    Daulouède, S.6
  • 164
    • 67649669741 scopus 로고    scopus 로고
    • Identification of total and differentially expressed excreted-secreted proteins from Trypanosoma congolense strains exhibiting different virulence and pathogenicity
    • Grébaut P., Chuchana P., Brizard J.P., Demettre E., Seveno M., Bossard G., et al. Identification of total and differentially expressed excreted-secreted proteins from Trypanosoma congolense strains exhibiting different virulence and pathogenicity. Int J Parasitol 39 (2009) 1137-1150
    • (2009) Int J Parasitol , vol.39 , pp. 1137-1150
    • Grébaut, P.1    Chuchana, P.2    Brizard, J.P.3    Demettre, E.4    Seveno, M.5    Bossard, G.6
  • 165
    • 0034060128 scopus 로고    scopus 로고
    • Analysis of missed cleavage sites, tryptophan oxidation and N-terminal pyroglutamylation after in-gel tryptic digestion
    • Thiede B., Lamer S., Mattow J., Siejak F., Dimmler C., Rudel T., et al. Analysis of missed cleavage sites, tryptophan oxidation and N-terminal pyroglutamylation after in-gel tryptic digestion. Rapid Commun Mass Spectrom 14 (2000) 496-502
    • (2000) Rapid Commun Mass Spectrom , vol.14 , pp. 496-502
    • Thiede, B.1    Lamer, S.2    Mattow, J.3    Siejak, F.4    Dimmler, C.5    Rudel, T.6
  • 166
    • 85047698600 scopus 로고    scopus 로고
    • Archived polyacrylamide gels as a resource for proteome characterization by mass spectrometry
    • Shevchenko A., Loboda A., Ens W., Schraven B., Standing K.G., and Shevchenko A. Archived polyacrylamide gels as a resource for proteome characterization by mass spectrometry. Electrophoresis 22 (2001) 1194-1203
    • (2001) Electrophoresis , vol.22 , pp. 1194-1203
    • Shevchenko, A.1    Loboda, A.2    Ens, W.3    Schraven, B.4    Standing, K.G.5    Shevchenko, A.6
  • 167
    • 0034607086 scopus 로고    scopus 로고
    • Acetylation at the N-terminus of actin strengthens weak interaction between actin and myosin
    • Abe A., Saeki K., Yasunaga T., and Wakabayashi T. Acetylation at the N-terminus of actin strengthens weak interaction between actin and myosin. Biochem Biophys Res Commun 268 (2000) 14-19
    • (2000) Biochem Biophys Res Commun , vol.268 , pp. 14-19
    • Abe, A.1    Saeki, K.2    Yasunaga, T.3    Wakabayashi, T.4
  • 168
    • 0034711184 scopus 로고    scopus 로고
    • Nα-terminal acetylation of eukaryotic proteins
    • Polevoda B., and Sherman F. Nα-terminal acetylation of eukaryotic proteins. J Biol Chem 275 (2000) 36479-36482
    • (2000) J Biol Chem , vol.275 , pp. 36479-36482
    • Polevoda, B.1    Sherman, F.2
  • 169
    • 0033613196 scopus 로고    scopus 로고
    • The catalytic sites of 20S proteasomes and their role in subunit maturation: a mutational and crystallographic study
    • Groll M., Heinemeyer W., Jager S., Ullrich T., Bochtler M., Wolf D.H., et al. The catalytic sites of 20S proteasomes and their role in subunit maturation: a mutational and crystallographic study. Proc Natl Acad Sci USA 96 (1999) 10976-10983
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10976-10983
    • Groll, M.1    Heinemeyer, W.2    Jager, S.3    Ullrich, T.4    Bochtler, M.5    Wolf, D.H.6
  • 170
    • 0032424256 scopus 로고    scopus 로고
    • Pyroglutamyl peptidase: an overview of the three known enzymatic forms
    • Cummins P.M., and O'Connor B. Pyroglutamyl peptidase: an overview of the three known enzymatic forms. Biochim Biophys Acta 1429 (1998) 1-17
    • (1998) Biochim Biophys Acta , vol.1429 , pp. 1-17
    • Cummins, P.M.1    O'Connor, B.2
  • 172
    • 1842525890 scopus 로고    scopus 로고
    • Asparagine deamidation: a regulatory hourglass
    • Weintraub S.J., and Manson S.R. Asparagine deamidation: a regulatory hourglass. Mech Age Dev 125 (2004) 255-257
    • (2004) Mech Age Dev , vol.125 , pp. 255-257
    • Weintraub, S.J.1    Manson, S.R.2
  • 174
    • 33845400905 scopus 로고    scopus 로고
    • Glycoproteomics of Trypanosoma cruzi trypomastigotes using subcellular fractionation, lectin affinity, and stable isotope labeling
    • Atwood III J.A., Minning T., Ludolf F., Nuccio A., Weatherly D.B., Alvarez-Manilla G., et al. Glycoproteomics of Trypanosoma cruzi trypomastigotes using subcellular fractionation, lectin affinity, and stable isotope labeling. J Proteome Res 5 (2006) 3376-3384
    • (2006) J Proteome Res , vol.5 , pp. 3376-3384
    • Atwood III, J.A.1    Minning, T.2    Ludolf, F.3    Nuccio, A.4    Weatherly, D.B.5    Alvarez-Manilla, G.6
  • 175
    • 67651233460 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of the human pathogen Trypanosoma cruzi at the epimastigote stage
    • Nakayasu E.S., Gaynor M.R., Sobreira T.J., Ross J.A., and Almeida I.C. Phosphoproteomic analysis of the human pathogen Trypanosoma cruzi at the epimastigote stage. Proteomics 9 (2009) 3489-3506
    • (2009) Proteomics , vol.9 , pp. 3489-3506
    • Nakayasu, E.S.1    Gaynor, M.R.2    Sobreira, T.J.3    Ross, J.A.4    Almeida, I.C.5
  • 176
    • 0030013633 scopus 로고    scopus 로고
    • A major tyrosine-phosphorylated protein of Trypanosoma brucei is a nucleolar RNA-binding protein
    • Das A., Peterson G.C., Kanner S.B., Frevert U., and Parsons M. A major tyrosine-phosphorylated protein of Trypanosoma brucei is a nucleolar RNA-binding protein. J Biol Chem 271 (1996) 15675-15681
    • (1996) J Biol Chem , vol.271 , pp. 15675-15681
    • Das, A.1    Peterson, G.C.2    Kanner, S.B.3    Frevert, U.4    Parsons, M.5
  • 177
    • 64749093072 scopus 로고    scopus 로고
    • Identification and specific localization of tyrosine-phosphorylated proteins in Trypanosoma brucei
    • Nett I.R., Davidson L., Lamont D., and Ferguson M.A. Identification and specific localization of tyrosine-phosphorylated proteins in Trypanosoma brucei. Eukaryot Cell 8 (2009) 617-626
    • (2009) Eukaryot Cell , vol.8 , pp. 617-626
    • Nett, I.R.1    Davidson, L.2    Lamont, D.3    Ferguson, M.A.4
  • 179
    • 0032856010 scopus 로고    scopus 로고
    • An unambiguous nomenclature for the major surface glycoproteins of the procyclic form of Trypanosoma brucei
    • Roditi I., and Clayton C. An unambiguous nomenclature for the major surface glycoproteins of the procyclic form of Trypanosoma brucei. Mol Biochem Parasitol 103 (1999) 99-100
    • (1999) Mol Biochem Parasitol , vol.103 , pp. 99-100
    • Roditi, I.1    Clayton, C.2
  • 180
    • 0032981742 scopus 로고    scopus 로고
    • Trypanosoma brucei GPEET-PARP is phosphorylated on six out of seven threonine residues
    • Mehlert A., Treumann A., and Ferguson M.A. Trypanosoma brucei GPEET-PARP is phosphorylated on six out of seven threonine residues. Mol Biochem Parasitol 98 (1999) 291-296
    • (1999) Mol Biochem Parasitol , vol.98 , pp. 291-296
    • Mehlert, A.1    Treumann, A.2    Ferguson, M.A.3
  • 181
    • 70049114411 scopus 로고    scopus 로고
    • The phosphoproteome of bloodstream form Trypanosoma brucei, causative agent of African sleeping sickness
    • Nett I.R., Martin D.M., Miranda-Saavedra D., Lamont D., Barber J.D., Mehlert A., et al. The phosphoproteome of bloodstream form Trypanosoma brucei, causative agent of African sleeping sickness. Mol Cell Proteomics 8 (2009) 1527-1538
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1527-1538
    • Nett, I.R.1    Martin, D.M.2    Miranda-Saavedra, D.3    Lamont, D.4    Barber, J.D.5    Mehlert, A.6
  • 182
    • 0022386153 scopus 로고
    • Mucocutaneous leishmaniasis in Colombia: Leishmania braziliensis subspecies diversity
    • Saravia N.G., Holguin A.F., McMahon-Pratt D., and D'Alessandro A. Mucocutaneous leishmaniasis in Colombia: Leishmania braziliensis subspecies diversity. Am J Trop Med Hyg 34 (1985) 714-720
    • (1985) Am J Trop Med Hyg , vol.34 , pp. 714-720
    • Saravia, N.G.1    Holguin, A.F.2    McMahon-Pratt, D.3    D'Alessandro, A.4
  • 183
  • 184
    • 0022836755 scopus 로고
    • Mucosal leishmaniasis ("espundia" escomel, 1911)
    • Marsden P.D. Mucosal leishmaniasis ("espundia" escomel, 1911). Trans R Soc Trop Med Hyg 80 (1986) 859-876
    • (1986) Trans R Soc Trop Med Hyg , vol.80 , pp. 859-876
    • Marsden, P.D.1
  • 185
    • 0033867594 scopus 로고    scopus 로고
    • American tegumentary leishmaniosis (ATL) in Rio de Janeiro state, Brazil: main clinical and epidemiologic characteristics
    • Oliveira-Neto M., Mattos M., Perez M., Da-Cruz A., Fernandes O., Moreira J., et al. American tegumentary leishmaniosis (ATL) in Rio de Janeiro state, Brazil: main clinical and epidemiologic characteristics. Int J Dermatol 39 (2000) 506-514
    • (2000) Int J Dermatol , vol.39 , pp. 506-514
    • Oliveira-Neto, M.1    Mattos, M.2    Perez, M.3    Da-Cruz, A.4    Fernandes, O.5    Moreira, J.6
  • 186
    • 69149101972 scopus 로고    scopus 로고
    • Detection of Leishmania in unaffected mucosal tissues of patients with cutaneous leishmaniasis caused by Leishmania (Viannia) species
    • Figueroa R.A., Lozano L.E., Romero I.C., Cardona M.T., Prager M., Pacheco R., et al. Detection of Leishmania in unaffected mucosal tissues of patients with cutaneous leishmaniasis caused by Leishmania (Viannia) species. J Infect Dis 200 (2009) 638-646
    • (2009) J Infect Dis , vol.200 , pp. 638-646
    • Figueroa, R.A.1    Lozano, L.E.2    Romero, I.C.3    Cardona, M.T.4    Prager, M.5    Pacheco, R.6
  • 187
    • 30544434167 scopus 로고    scopus 로고
    • Comparative protein profiling identifies elongation factor-1beta and tryparedoxin peroxidase as factors associated with metastasis in Leishmania guyanensis
    • Walker J., Acestor N., Gongora R., Quadroni M., Segura I., Fasel N., et al. Comparative protein profiling identifies elongation factor-1beta and tryparedoxin peroxidase as factors associated with metastasis in Leishmania guyanensis. Mol Biochem Parasitol 145 (2006) 254-264
    • (2006) Mol Biochem Parasitol , vol.145 , pp. 254-264
    • Walker, J.1    Acestor, N.2    Gongora, R.3    Quadroni, M.4    Segura, I.5    Fasel, N.6
  • 188
    • 3042641848 scopus 로고    scopus 로고
    • Trypanothione S-transferase activity in a trypanosomatid ribosomal elongation factor1B
    • Vickers T.J., and Fairlamb A.H. Trypanothione S-transferase activity in a trypanosomatid ribosomal elongation factor1B. J Biol Chem 279 (2004) 27246-27256
    • (2004) J Biol Chem , vol.279 , pp. 27246-27256
    • Vickers, T.J.1    Fairlamb, A.H.2
  • 189
    • 10444255569 scopus 로고    scopus 로고
    • Leishmania major elongation factor 1B complex has trypanothione S-transferase and peroxidase activity
    • Vickers T.J., Wylie S.H., and Fairlamb A.H. Leishmania major elongation factor 1B complex has trypanothione S-transferase and peroxidase activity. J Biol Chem 279 (2004) 49003-49009
    • (2004) J Biol Chem , vol.279 , pp. 49003-49009
    • Vickers, T.J.1    Wylie, S.H.2    Fairlamb, A.H.3
  • 190
    • 33750115294 scopus 로고    scopus 로고
    • Proteomic analysis of antigens from Leishmania infantum promastigotes
    • Dea-Ayuela M.A., Rama-Iñiguez S., and Bolás-Fernández F. Proteomic analysis of antigens from Leishmania infantum promastigotes. Proteomics 6 (2006) 4187-4194
    • (2006) Proteomics , vol.6 , pp. 4187-4194
    • Dea-Ayuela, M.A.1    Rama-Iñiguez, S.2    Bolás-Fernández, F.3
  • 191
    • 39649085703 scopus 로고    scopus 로고
    • Mapping the antigenicity of the parasites in Leishmania donovani infection by proteome serology
    • Forgber M., Basu R., Roychoudhury K., Theinert S., Roy S., Sundar S., et al. Mapping the antigenicity of the parasites in Leishmania donovani infection by proteome serology. PLoS One 1 (2006) e40
    • (2006) PLoS One , vol.1
    • Forgber, M.1    Basu, R.2    Roychoudhury, K.3    Theinert, S.4    Roy, S.5    Sundar, S.6
  • 192
    • 33947368687 scopus 로고    scopus 로고
    • Proteomic approach for identification and characterization of novel immunostimulatory proteins from soluble antigens of Leishmania donovani promastigotes
    • Gupta S.K., Sisodia B.S., Sinha S., Hajela K., Naik S., Shasany A.K., et al. Proteomic approach for identification and characterization of novel immunostimulatory proteins from soluble antigens of Leishmania donovani promastigotes. Proteomics 7 (2007) 816-823
    • (2007) Proteomics , vol.7 , pp. 816-823
    • Gupta, S.K.1    Sisodia, B.S.2    Sinha, S.3    Hajela, K.4    Naik, S.5    Shasany, A.K.6
  • 194
    • 61349152342 scopus 로고    scopus 로고
    • Changes in the proteome and infectivity of Leishmania infantum induced by in vitro exposure to a nitric oxide donor
    • Dea-Ayuela M.A., Ordoñez-Gutierrez L., and Bolás-Fernández F. Changes in the proteome and infectivity of Leishmania infantum induced by in vitro exposure to a nitric oxide donor. Int J Med Microbiol 299 (2009) 221-232
    • (2009) Int J Med Microbiol , vol.299 , pp. 221-232
    • Dea-Ayuela, M.A.1    Ordoñez-Gutierrez, L.2    Bolás-Fernández, F.3
  • 195
    • 53849129597 scopus 로고    scopus 로고
    • Heat-shock proteins as powerful weapons in vaccine development
    • Bolhassani A., and Rafati S. Heat-shock proteins as powerful weapons in vaccine development. Expert Rev Vaccines 7 (2008) 1185-1199
    • (2008) Expert Rev Vaccines , vol.7 , pp. 1185-1199
    • Bolhassani, A.1    Rafati, S.2
  • 196
    • 51349110109 scopus 로고    scopus 로고
    • Enhanced nitrosative stress during Trypanosoma cruzi infection causes nitrotyrosine modification of host proteins: implications in Chagas' disease
    • Dhiman M., Nakayasu E.S., Madaiah Y.H., Reynolds B.K., Wen J.J., Almeida I.C., et al. Enhanced nitrosative stress during Trypanosoma cruzi infection causes nitrotyrosine modification of host proteins: implications in Chagas' disease. Am J Pathol 173 (2008) 728-740
    • (2008) Am J Pathol , vol.173 , pp. 728-740
    • Dhiman, M.1    Nakayasu, E.S.2    Madaiah, Y.H.3    Reynolds, B.K.4    Wen, J.J.5    Almeida, I.C.6
  • 197
    • 33847636324 scopus 로고    scopus 로고
    • Proteomic inventory of myocardial proteins from patients with chronic Chagas' cardiomyopathy
    • Teixeira P.C., Iwai L.K., Kuramoto A.C., Honorato R., Fiorelli A., Stolf N., et al. Proteomic inventory of myocardial proteins from patients with chronic Chagas' cardiomyopathy. Braz J Med Biol Res 39 (2006) 1549-1562
    • (2006) Braz J Med Biol Res , vol.39 , pp. 1549-1562
    • Teixeira, P.C.1    Iwai, L.K.2    Kuramoto, A.C.3    Honorato, R.4    Fiorelli, A.5    Stolf, N.6
  • 198
    • 48749121390 scopus 로고    scopus 로고
    • Distinct outcomes of Trypanosoma cruzi infection in hamsters are related to myocardial parasitism, cytokine/chemokine gene expression, and protein expression profile
    • Bilate A.M., Teixeira P.C., Ribeiro S.P., Brito T., Silva A.M., Russo M., et al. Distinct outcomes of Trypanosoma cruzi infection in hamsters are related to myocardial parasitism, cytokine/chemokine gene expression, and protein expression profile. J Infect Dis 198 (2008) 614-623
    • (2008) J Infect Dis , vol.198 , pp. 614-623
    • Bilate, A.M.1    Teixeira, P.C.2    Ribeiro, S.P.3    Brito, T.4    Silva, A.M.5    Russo, M.6
  • 199
    • 0035852641 scopus 로고    scopus 로고
    • The surface coat of procyclic Trypanosoma brucei: programmed expression and proteolytic cleavage of procyclin in the tsetse fly
    • Acosta-Serrano A., Vassella E., Liniger M., Kunz Renggli C., Brun R., Roditi I., et al. The surface coat of procyclic Trypanosoma brucei: programmed expression and proteolytic cleavage of procyclin in the tsetse fly. Proc Natl Acad Sci U S A 98 (2001) 1513-1518
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 1513-1518
    • Acosta-Serrano, A.1    Vassella, E.2    Liniger, M.3    Kunz Renggli, C.4    Brun, R.5    Roditi, I.6
  • 200
    • 0033569874 scopus 로고    scopus 로고
    • The procyclin repertoire of Trypanosoma brucei. Identification and structural characterization of the Glu-Pro-rich polypeptides
    • Acosta-Serrano A., Cole R.N., Mehlert A., Lee M.G., Ferguson M.A., and Englund P.T. The procyclin repertoire of Trypanosoma brucei. Identification and structural characterization of the Glu-Pro-rich polypeptides. J Biol Chem 274 (1999) 29763-29771
    • (1999) J Biol Chem , vol.274 , pp. 29763-29771
    • Acosta-Serrano, A.1    Cole, R.N.2    Mehlert, A.3    Lee, M.G.4    Ferguson, M.A.5    Englund, P.T.6
  • 201
    • 0034624085 scopus 로고    scopus 로고
    • Killing of Trypanosoma brucei by concanavalin A: structural basis of resistance in glycosylation mutants
    • Acosta-Serrano A., Cole R.N., and Englund P.T. Killing of Trypanosoma brucei by concanavalin A: structural basis of resistance in glycosylation mutants. J Mol Biol 304 (2000) 633-644
    • (2000) J Mol Biol , vol.304 , pp. 633-644
    • Acosta-Serrano, A.1    Cole, R.N.2    Englund, P.T.3
  • 202
    • 11144357641 scopus 로고    scopus 로고
    • A novel and accurate diagnostic test for human African trypanosomiasis
    • Papadopoulos M.C., Abel P.M., Agranoff D., Stich A., Tarelli E., Bell B.A., et al. A novel and accurate diagnostic test for human African trypanosomiasis. Lancet 363 (2004) 1358-1363
    • (2004) Lancet , vol.363 , pp. 1358-1363
    • Papadopoulos, M.C.1    Abel, P.M.2    Agranoff, D.3    Stich, A.4    Tarelli, E.5    Bell, B.A.6
  • 204
    • 0036791428 scopus 로고    scopus 로고
    • Boosted decision tree analysis of surface-enhanced laser desorption/ionization mass spectral serum profiles discriminates prostate cancer from noncancer patients
    • Qu Y., Adam B.L., Yasui Y., Ward M.D., Cazares L.H., Schellhammer P.F., et al. Boosted decision tree analysis of surface-enhanced laser desorption/ionization mass spectral serum profiles discriminates prostate cancer from noncancer patients. Clin Chem 48 (2002) 1835-1843
    • (2002) Clin Chem , vol.48 , pp. 1835-1843
    • Qu, Y.1    Adam, B.L.2    Yasui, Y.3    Ward, M.D.4    Cazares, L.H.5    Schellhammer, P.F.6
  • 205
    • 0036324715 scopus 로고    scopus 로고
    • Proteomics and bioinformatics approaches for identification of serum biomarkers to detect breast cancer
    • Li J., Zhang Z., Rosenzweig J., Wang Y.Y., and Chan D.W. Proteomics and bioinformatics approaches for identification of serum biomarkers to detect breast cancer. Clin Chem 48 (2002) 1296-1304
    • (2002) Clin Chem , vol.48 , pp. 1296-1304
    • Li, J.1    Zhang, Z.2    Rosenzweig, J.3    Wang, Y.Y.4    Chan, D.W.5
  • 207
    • 64149120224 scopus 로고    scopus 로고
    • Rapid identification of Staphylococcus aureus by surface enhanced laser desorption and ionization time of flight mass spectrometry
    • Yang Y.C., Yu H., Xiao D.W., Liu H., Hu Q., Huang B., et al. Rapid identification of Staphylococcus aureus by surface enhanced laser desorption and ionization time of flight mass spectrometry. J Microbiol Methods 77 (2009) 202-206
    • (2009) J Microbiol Methods , vol.77 , pp. 202-206
    • Yang, Y.C.1    Yu, H.2    Xiao, D.W.3    Liu, H.4    Hu, Q.5    Huang, B.6
  • 208
    • 51149113993 scopus 로고    scopus 로고
    • Kinetoplastida: new therapeutic strategies
    • Croft S.L. Kinetoplastida: new therapeutic strategies. Parasite 15 (2008) 522-527
    • (2008) Parasite , vol.15 , pp. 522-527
    • Croft, S.L.1
  • 210
    • 0030997216 scopus 로고    scopus 로고
    • In vitro and in vivo resistance of Leishmania infantum to meglumine antimoniate: a study of 37 strains collected from patients with visceral leishmaniasis
    • Faraut-Gambarelli F., Piarroux R., Deniau M., Giusiano B., Marty P., Michel G., et al. In vitro and in vivo resistance of Leishmania infantum to meglumine antimoniate: a study of 37 strains collected from patients with visceral leishmaniasis. Antimicrob Agents Chemother 41 (1997) 827-830
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 827-830
    • Faraut-Gambarelli, F.1    Piarroux, R.2    Deniau, M.3    Giusiano, B.4    Marty, P.5    Michel, G.6
  • 211
    • 0033509735 scopus 로고    scopus 로고
    • Evidence that the high incidence of treatment failures in Indian kalaazar is due to the emergence of antimony-resistant strains of Leishmania donovani
    • Lira R., Sundar S., Makharia A., Kenney R., Gam A., Saraiva E., et al. Evidence that the high incidence of treatment failures in Indian kalaazar is due to the emergence of antimony-resistant strains of Leishmania donovani. J Infect Dis 180 (1999) 564-567
    • (1999) J Infect Dis , vol.180 , pp. 564-567
    • Lira, R.1    Sundar, S.2    Makharia, A.3    Kenney, R.4    Gam, A.5    Saraiva, E.6
  • 212
    • 0034968735 scopus 로고    scopus 로고
    • Treatment failure in children in a randomized clinical trial with 10 and 20 days of meglumine antimonate for cutaneous leishmaniasis due to Leishmania viannia species
    • Palacios R., Osorio L.E., Grajalew L.F., and Ochoa M.T. Treatment failure in children in a randomized clinical trial with 10 and 20 days of meglumine antimonate for cutaneous leishmaniasis due to Leishmania viannia species. Am J Trop Med Hyg 64 (2001) 187-193
    • (2001) Am J Trop Med Hyg , vol.64 , pp. 187-193
    • Palacios, R.1    Osorio, L.E.2    Grajalew, L.F.3    Ochoa, M.T.4
  • 213
    • 0034780949 scopus 로고    scopus 로고
    • Drug resistance in Indian visceral leishmaniasis
    • Sundar S. Drug resistance in Indian visceral leishmaniasis. Trop. Med. Int. Health 6 (2001) 849-854
    • (2001) Trop. Med. Int. Health , vol.6 , pp. 849-854
    • Sundar, S.1
  • 214
    • 16844369135 scopus 로고    scopus 로고
    • Antimony-resistant Leishmania Donovani in eastern Sudan: incidence and in vitro correlation
    • Abdo M.G., Elamin W.M., Khalil E.A., and Mukhtar M.M. Antimony-resistant Leishmania Donovani in eastern Sudan: incidence and in vitro correlation. East Mediterr Health J 9 (2003) 837-843
    • (2003) East Mediterr Health J , vol.9 , pp. 837-843
    • Abdo, M.G.1    Elamin, W.M.2    Khalil, E.A.3    Mukhtar, M.M.4
  • 215
    • 23844433812 scopus 로고    scopus 로고
    • Magnitude of unresponsiveness to sodium stibogluconate in the treatment of visceral leishmaniasis in Bihar
    • Das V.N., Ranjan A., Bimal S., Siddique N.A., Pandey K., Kumar N., et al. Magnitude of unresponsiveness to sodium stibogluconate in the treatment of visceral leishmaniasis in Bihar. Natl Med J India 18 (2005) 131-133
    • (2005) Natl Med J India , vol.18 , pp. 131-133
    • Das, V.N.1    Ranjan, A.2    Bimal, S.3    Siddique, N.A.4    Pandey, K.5    Kumar, N.6
  • 216
    • 33744464744 scopus 로고    scopus 로고
    • Unresponsiveness to Glucantime treatment in Iranian cutaneous leishmaniasis due to drug-resistant Leishmania tropica parasites
    • Hadighi R., Mohebali M., Boucher P., Hajjaran H., Khamesipour A., and Ouellette M. Unresponsiveness to Glucantime treatment in Iranian cutaneous leishmaniasis due to drug-resistant Leishmania tropica parasites. PLoS Med 3 (2006) e162
    • (2006) PLoS Med , vol.3
    • Hadighi, R.1    Mohebali, M.2    Boucher, P.3    Hajjaran, H.4    Khamesipour, A.5    Ouellette, M.6
  • 219
    • 34547337720 scopus 로고    scopus 로고
    • Inactivation of the miltefosine transporter, LdMT, causes miltefosine resistance that is conferred to the amastigote stage of Leishmania donovani and persists in vivo
    • Seifert K., Pérez-Victoria F.J., Stettler M., Sánchez-Cañete M.P., Castanys S., Gamarro F., et al. Inactivation of the miltefosine transporter, LdMT, causes miltefosine resistance that is conferred to the amastigote stage of Leishmania donovani and persists in vivo. Int J Antimicrob Agents 30 (2007) 229-235
    • (2007) Int J Antimicrob Agents , vol.30 , pp. 229-235
    • Seifert, K.1    Pérez-Victoria, F.J.2    Stettler, M.3    Sánchez-Cañete, M.P.4    Castanys, S.5    Gamarro, F.6
  • 220
    • 59749105928 scopus 로고    scopus 로고
    • In vitro susceptibility of field isolates of Leishmania donovani to Miltefosine and amphotericin B: correlation with sodium antimony gluconate susceptibility and implications for treatment in areas of endemicity
    • Kumar D., Kulshrestha A., Singh R., and Salotra P. In vitro susceptibility of field isolates of Leishmania donovani to Miltefosine and amphotericin B: correlation with sodium antimony gluconate susceptibility and implications for treatment in areas of endemicity. Antimicrob Agents Chemother 53 (2009) 835-838
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 835-838
    • Kumar, D.1    Kulshrestha, A.2    Singh, R.3    Salotra, P.4
  • 221
    • 58149339918 scopus 로고    scopus 로고
    • Large-scale differential proteome analysis in Plasmodium falciparum under drug treatment
    • Prieto J.H., Koncarevic S., Park S.K., Yates III J., and Becker K. Large-scale differential proteome analysis in Plasmodium falciparum under drug treatment. PLoS One 3 (2008) e4098
    • (2008) PLoS One , vol.3
    • Prieto, J.H.1    Koncarevic, S.2    Park, S.K.3    Yates III, J.4    Becker, K.5
  • 222
    • 64149123281 scopus 로고    scopus 로고
    • Trichomonas vaginalis: metronidazole and other nitroimidazole drugs are reduced by the flavin enzyme thioredoxin reductase and disrupt the cellular redox system. Implications for nitroimidazole toxicity and resistance
    • Leitsch D., Kolarich D., Binder M., Stadlmann J., Altmann F., and Duchêne M. Trichomonas vaginalis: metronidazole and other nitroimidazole drugs are reduced by the flavin enzyme thioredoxin reductase and disrupt the cellular redox system. Implications for nitroimidazole toxicity and resistance. Mol Microbiol 72 (2009) 518-536
    • (2009) Mol Microbiol , vol.72 , pp. 518-536
    • Leitsch, D.1    Kolarich, D.2    Binder, M.3    Stadlmann, J.4    Altmann, F.5    Duchêne, M.6
  • 223
    • 1642565125 scopus 로고    scopus 로고
    • Proteomic approaches to studying drug targets and resistance in Plasmodium
    • Cooper R.A., and Carucci D.J. Proteomic approaches to studying drug targets and resistance in Plasmodium. Curr Drug Targets Infect Disord 4 (2004) 41-51
    • (2004) Curr Drug Targets Infect Disord , vol.4 , pp. 41-51
    • Cooper, R.A.1    Carucci, D.J.2
  • 224
    • 33947415767 scopus 로고    scopus 로고
    • SELDI-TOF-MS analysis of chloroquine resistant and sensitive Plasmodium falciparum strains
    • Koncarevic S., Bogumil R., and Becker K. SELDI-TOF-MS analysis of chloroquine resistant and sensitive Plasmodium falciparum strains. Proteomics 7 (2007) 711-721
    • (2007) Proteomics , vol.7 , pp. 711-721
    • Koncarevic, S.1    Bogumil, R.2    Becker, K.3
  • 226
    • 33847132229 scopus 로고    scopus 로고
    • Chemotherapeutic strategies against Trypanosoma brucei: drug targets vs. drug targeting
    • Lüscher A., de Koning H.P., and Mäser P. Chemotherapeutic strategies against Trypanosoma brucei: drug targets vs. drug targeting. Curr Pharm Des 13 (2007) 555-567
    • (2007) Curr Pharm Des , vol.13 , pp. 555-567
    • Lüscher, A.1    de Koning, H.P.2    Mäser, P.3
  • 227
    • 59049092938 scopus 로고    scopus 로고
    • Discovery of novel vaccine candidates and drug targets against visceral leishmaniasis using proteomics and transcriptomics
    • Kumari S., Kumar A., Samant M., Singh N., and Dube A. Discovery of novel vaccine candidates and drug targets against visceral leishmaniasis using proteomics and transcriptomics. Curr Drug Targets 9 (2008) 938-947
    • (2008) Curr Drug Targets , vol.9 , pp. 938-947
    • Kumari, S.1    Kumar, A.2    Samant, M.3    Singh, N.4    Dube, A.5
  • 228
    • 41149091679 scopus 로고    scopus 로고
    • Proteomic approaches for discovery of new targets for vaccine and therapeutics against visceral leishmaniasis
    • Kumari S., Kumar A., Samant M., Sundar S., Singh N., and Dube A. Proteomic approaches for discovery of new targets for vaccine and therapeutics against visceral leishmaniasis. Proteomics 2 (2008) 372-386
    • (2008) Proteomics , vol.2 , pp. 372-386
    • Kumari, S.1    Kumar, A.2    Samant, M.3    Sundar, S.4    Singh, N.5    Dube, A.6
  • 229
    • 0026779424 scopus 로고
    • A novel antifolate resistance gene on the amplified H circle of Leishmania
    • Papadopoulou B., Roy G., and Ouellette M. A novel antifolate resistance gene on the amplified H circle of Leishmania. EMBO J 11 (1992) 3601-3608
    • (1992) EMBO J , vol.11 , pp. 3601-3608
    • Papadopoulou, B.1    Roy, G.2    Ouellette, M.3
  • 230
    • 0026459643 scopus 로고
    • A member of the aldoketo reductase family confers methotrexate resistance in Leishmania
    • Callahan H.L., and Beverley S.M. A member of the aldoketo reductase family confers methotrexate resistance in Leishmania. J Biol Chem 267 (1992) 24165-24168
    • (1992) J Biol Chem , vol.267 , pp. 24165-24168
    • Callahan, H.L.1    Beverley, S.M.2
  • 231
    • 4043094169 scopus 로고    scopus 로고
    • Differential protein expression analysis of Leishmania major reveals novel roles for methionine adenosyltransferase and S-adenosylmethionine in methotrexate resistance
    • Drummelsmith J., Girard I., Trudel N., and Ouellette M. Differential protein expression analysis of Leishmania major reveals novel roles for methionine adenosyltransferase and S-adenosylmethionine in methotrexate resistance. J Biol Chem 279 (2004) 33273-33280
    • (2004) J Biol Chem , vol.279 , pp. 33273-33280
    • Drummelsmith, J.1    Girard, I.2    Trudel, N.3    Ouellette, M.4
  • 232
    • 7944237421 scopus 로고    scopus 로고
    • Leishmaniasis: drugs in the clinic, resistance and new developments
    • Ouellette M., Drummelsmith J., and Papadopoulou B. Leishmaniasis: drugs in the clinic, resistance and new developments. Drug Resist Updat 7 (2004) 257-266
    • (2004) Drug Resist Updat , vol.7 , pp. 257-266
    • Ouellette, M.1    Drummelsmith, J.2    Papadopoulou, B.3
  • 235
    • 0042090390 scopus 로고    scopus 로고
    • 2+ through non-selective cation channels in the host and the parasite is responsible for apoptosis of intracellular Leishmania donovani amastigotes
    • 2+ through non-selective cation channels in the host and the parasite is responsible for apoptosis of intracellular Leishmania donovani amastigotes. J Biol Chem 278 (2003) 25120-25132
    • (2003) J Biol Chem , vol.278 , pp. 25120-25132
    • Sudhandiran, G.1    Shaha, C.2
  • 236
    • 33846554383 scopus 로고    scopus 로고
    • A proteomics screen implicates HSP83 and a small kinetoplastid calpain-related protein in drug resistance in Leishmania donovani clinical field isolates by modulating drug-induced programmed cell death
    • Vergnes B., Gourbal B., Girard I., Sundar S., Drummelsmith J., and Ouellette M. A proteomics screen implicates HSP83 and a small kinetoplastid calpain-related protein in drug resistance in Leishmania donovani clinical field isolates by modulating drug-induced programmed cell death. Mol Cell Proteomics 6 (2007) 88-101
    • (2007) Mol Cell Proteomics , vol.6 , pp. 88-101
    • Vergnes, B.1    Gourbal, B.2    Girard, I.3    Sundar, S.4    Drummelsmith, J.5    Ouellette, M.6
  • 237
    • 68049132858 scopus 로고    scopus 로고
    • Down regulation of KMP-11 in Leishmania infantum axenic antimony resistant amastigotes as revealed by a proteomic screen
    • El Fadili K., Drummelsmith J., Roy G., Jardim A., and Ouellette M. Down regulation of KMP-11 in Leishmania infantum axenic antimony resistant amastigotes as revealed by a proteomic screen. Exp Parasitol 123 (2009) 51-57
    • (2009) Exp Parasitol , vol.123 , pp. 51-57
    • El Fadili, K.1    Drummelsmith, J.2    Roy, G.3    Jardim, A.4    Ouellette, M.5
  • 238
    • 0033256630 scopus 로고    scopus 로고
    • Parasitological cure of Chagas disease: is it possible? Is it relevant?
    • Urbina J.A. Parasitological cure of Chagas disease: is it possible? Is it relevant?. Mem Inst Oswaldo Cruz 94 (1999) 34-35
    • (1999) Mem Inst Oswaldo Cruz , vol.94 , pp. 34-35
    • Urbina, J.A.1
  • 240
    • 17544400692 scopus 로고    scopus 로고
    • Long term evaluation of etiological treatment of Chagas disease with benznidazole
    • Cancado J.R. Long term evaluation of etiological treatment of Chagas disease with benznidazole. Rev Inst Med Trop Sao Paulo 44 (2002) 29-37
    • (2002) Rev Inst Med Trop Sao Paulo , vol.44 , pp. 29-37
    • Cancado, J.R.1
  • 241
    • 17344379918 scopus 로고    scopus 로고
    • Molecular characterization of susceptible and naturally resistant strains of Trypanosoma cruzi to benznidazole and nifurtimox
    • Murta S.M., Gazzinelli R.T., Brener Z., and Romanha A.J. Molecular characterization of susceptible and naturally resistant strains of Trypanosoma cruzi to benznidazole and nifurtimox. Mol Biochem Parasitol 93 (1998) 203-214
    • (1998) Mol Biochem Parasitol , vol.93 , pp. 203-214
    • Murta, S.M.1    Gazzinelli, R.T.2    Brener, Z.3    Romanha, A.J.4
  • 243
    • 0034777039 scopus 로고    scopus 로고
    • The phenomenon of treatment failures in Human African Trypanosomiasis
    • Brun R., Schumacher R., Schmid C., Kunz C., and Burri C. The phenomenon of treatment failures in Human African Trypanosomiasis. Trop Med Int Health 6 (2001) 906-914
    • (2001) Trop Med Int Health , vol.6 , pp. 906-914
    • Brun, R.1    Schumacher, R.2    Schmid, C.3    Kunz, C.4    Burri, C.5
  • 244
    • 0034990047 scopus 로고    scopus 로고
    • The situation of sleeping sickness in Angola: a calamity
    • Stanghellini A., and Josenando T. The situation of sleeping sickness in Angola: a calamity. Trop Med Int Health 6 (2001) 330-334
    • (2001) Trop Med Int Health , vol.6 , pp. 330-334
    • Stanghellini, A.1    Josenando, T.2
  • 245
    • 0034852287 scopus 로고    scopus 로고
    • Genetic variants of the TbAT1 adenosine transporter from African trypanosomes in relapse infections following melarsoprol therapy
    • Matovu E., Geiser F., Schneider V., Mäser P., Enyaru J.C., Kaminsky R., et al. Genetic variants of the TbAT1 adenosine transporter from African trypanosomes in relapse infections following melarsoprol therapy. Mol Biochem Parasitol 117 (2001) 73-81
    • (2001) Mol Biochem Parasitol , vol.117 , pp. 73-81
    • Matovu, E.1    Geiser, F.2    Schneider, V.3    Mäser, P.4    Enyaru, J.C.5    Kaminsky, R.6
  • 246
    • 10744226397 scopus 로고    scopus 로고
    • Mechanisms of arsenical and diamidine uptake and resistance in Trypanosoma brucei
    • Matovu E., Stewart M.L., Geiser F., Brun R., Mäser P., Wallace L.J., et al. Mechanisms of arsenical and diamidine uptake and resistance in Trypanosoma brucei. Eukaryot Cell 2 (2003) 1003-1008
    • (2003) Eukaryot Cell , vol.2 , pp. 1003-1008
    • Matovu, E.1    Stewart, M.L.2    Geiser, F.3    Brun, R.4    Mäser, P.5    Wallace, L.J.6
  • 247
    • 54049122193 scopus 로고    scopus 로고
    • Development of drug resistance in Trypanosoma brucei rhodesiense and Trypanosoma brucei gambiense. Treatment of human African trypanosomiasis with natural products
    • Gehrig S., and Efferth T. Development of drug resistance in Trypanosoma brucei rhodesiense and Trypanosoma brucei gambiense. Treatment of human African trypanosomiasis with natural products. Int J Mol Med 22 (2008) 411-419
    • (2008) Int J Mol Med , vol.22 , pp. 411-419
    • Gehrig, S.1    Efferth, T.2
  • 248
    • 0027500261 scopus 로고
    • Arsenical-resistant trypanosomes lack an unusual adenosine transporter
    • Carter N.S., and Fairlamb A.H. Arsenical-resistant trypanosomes lack an unusual adenosine transporter. Nature 361 (1993) 173-175
    • (1993) Nature , vol.361 , pp. 173-175
    • Carter, N.S.1    Fairlamb, A.H.2
  • 249
    • 0036223214 scopus 로고    scopus 로고
    • Overexpression of the putative thiol conjugate transporter TbMRPA causes melarsoprol resistance in Trypanosoma brucei
    • Shahi S.K., Krauth-Siegel R.L., and Clayton C.E. Overexpression of the putative thiol conjugate transporter TbMRPA causes melarsoprol resistance in Trypanosoma brucei. Mol Microbiol 43 (2002) 1129-1138
    • (2002) Mol Microbiol , vol.43 , pp. 1129-1138
    • Shahi, S.K.1    Krauth-Siegel, R.L.2    Clayton, C.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.