메뉴 건너뛰기




Volumn 107, Issue 2, 2008, Pages 159-167

Purification and subcellular localization of a secreted 75 kDa Trypanosoma cruzi serine oligopeptidase

Author keywords

Extracellular serine peptidase; Purification; Reservosomes; Trypanosoma cruzi

Indexed keywords

1,10 PHENANTHROLINE; AGAROSE; ALPHA N 4 TOSYLARGININE METHYL ESTER; ANTISERUM; APROTININ; ARGININE; ARGININE DERIVATIVE; CALCIUM ION; DIMETHYL SULFOXIDE(N ALPHA TOSYLLYSYLCHLOROMETHYLKETONE); KETONE DERIVATIVE; NITROGEN DERIVATIVE; PEPTIDASE; POLYPEPTIDE; PROTEINASE INHIBITOR; SERINE OLIGOPEPTIDASE; TOSYLPHENYLALANYL CHLOROMETHYL KETONE; ZINC ION;

EID: 47549105099     PISSN: 0001706X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.actatropica.2008.05.016     Document Type: Article
Times cited : (18)

References (58)
  • 1
    • 0344625412 scopus 로고    scopus 로고
    • Leishmania (Leishmania) amazonensis: purification and enzyme characterization of a soluble serine oligopeptidase from promastigotes
    • Andrade A.R., Santoro M.M., Norma de Melo M., and Mares-Guia M. Leishmania (Leishmania) amazonensis: purification and enzyme characterization of a soluble serine oligopeptidase from promastigotes. Exp. Parasitol. 89 (1998) 153-160
    • (1998) Exp. Parasitol. , vol.89 , pp. 153-160
    • Andrade, A.R.1    Santoro, M.M.2    Norma de Melo, M.3    Mares-Guia, M.4
  • 2
    • 0023926827 scopus 로고
    • Extracellular nucleotide catabolism in human B and T lymphocytes
    • Barankiewicz J., Dosh H.M., and Cohen A. Extracellular nucleotide catabolism in human B and T lymphocytes. J. Biol. Chem. 263 (1988) 7094-7098
    • (1988) J. Biol. Chem. , vol.263 , pp. 7094-7098
    • Barankiewicz, J.1    Dosh, H.M.2    Cohen, A.3
  • 3
    • 23644461576 scopus 로고    scopus 로고
    • Structural analysis of the N-glycans of the major cysteine proteinase of Trypanosoma cruzi. Identification of sulfated high-mannose type oligosaccharides
    • Barboza M., Duschak V.G., Fukuyama Y., Nonami H., Erra-Balsells R., Cazzulo J.J., and Couto A.S. Structural analysis of the N-glycans of the major cysteine proteinase of Trypanosoma cruzi. Identification of sulfated high-mannose type oligosaccharides. FEBS J. 272 (2005) 3803-3815
    • (2005) FEBS J. , vol.272 , pp. 3803-3815
    • Barboza, M.1    Duschak, V.G.2    Fukuyama, Y.3    Nonami, H.4    Erra-Balsells, R.5    Cazzulo, J.J.6    Couto, A.S.7
  • 4
    • 0026892409 scopus 로고
    • Oligopeptidase and the emergence of the prolyl oligopeptidase family
    • Barrett A.J., and Rawling N.D. Oligopeptidase and the emergence of the prolyl oligopeptidase family. Biol. Chem. Hoppe-Seyler 373 (1992) 353-360
    • (1992) Biol. Chem. Hoppe-Seyler , vol.373 , pp. 353-360
    • Barrett, A.J.1    Rawling, N.D.2
  • 5
    • 0033083293 scopus 로고    scopus 로고
    • Recent advances in identifying and validating drug targets in trypanosomes and leishmanias
    • Barrett M.P., Mottram J.C., and Coombs G.H. Recent advances in identifying and validating drug targets in trypanosomes and leishmanias. Trends Microbiol. 7 (1999) 82-88
    • (1999) Trends Microbiol. , vol.7 , pp. 82-88
    • Barrett, M.P.1    Mottram, J.C.2    Coombs, G.H.3
  • 7
    • 0011451554 scopus 로고
    • Specificity of [alfa]-chymotrypsin
    • Berezin I., and Martinek K. Specificity of [alfa]-chymotrypsin. FEBS Lett. 8 (1970) 261-267
    • (1970) FEBS Lett. , vol.8 , pp. 261-267
    • Berezin, I.1    Martinek, K.2
  • 8
    • 0028900481 scopus 로고
    • 120-kDa alkaline peptidase from Trypanosoma cruzi is involved in the generation of a novel calcium-signaling factor for mammalian cells
    • Burleigh B.A., and Andrews N.A. 120-kDa alkaline peptidase from Trypanosoma cruzi is involved in the generation of a novel calcium-signaling factor for mammalian cells. J. Biol. Chem. 270 (1995) 5172-5180
    • (1995) J. Biol. Chem. , vol.270 , pp. 5172-5180
    • Burleigh, B.A.1    Andrews, N.A.2
  • 9
    • 0036855862 scopus 로고    scopus 로고
    • Cell signaling and Trypanosoma cruzi invasion
    • Burleigh B.A., and Woolsey A.M. Cell signaling and Trypanosoma cruzi invasion. Cell. Microbiol. 4 (2002) 701-711
    • (2002) Cell. Microbiol. , vol.4 , pp. 701-711
    • Burleigh, B.A.1    Woolsey, A.M.2
  • 10
    • 33645833054 scopus 로고    scopus 로고
    • Host cell signaling and Trypanosoma cruzi invasion: do all roads lead to lysosomes?
    • Burleigh B.A. Host cell signaling and Trypanosoma cruzi invasion: do all roads lead to lysosomes?. Sci. STKE 293 (2005) 36
    • (2005) Sci. STKE , vol.293 , pp. 36
    • Burleigh, B.A.1
  • 11
    • 0036835142 scopus 로고    scopus 로고
    • Proteinases of Trypanosoma cruzi: potential targets for the chemotherapy of Chagas disease
    • Cazzulo J.J. Proteinases of Trypanosoma cruzi: potential targets for the chemotherapy of Chagas disease. Curr. Top. Med. Chem. 2 (2002) 1257-1267
    • (2002) Curr. Top. Med. Chem. , vol.2 , pp. 1257-1267
    • Cazzulo, J.J.1
  • 12
    • 0037347019 scopus 로고    scopus 로고
    • Leishmania model for microbial virulence: the relevance of parasite multiplication and pathoantigenicity
    • Chang K.P., Reed S.G., McGwire B.S., and Soong G.L. Leishmania model for microbial virulence: the relevance of parasite multiplication and pathoantigenicity. Acta Trop. 85 (2003) 375-390
    • (2003) Acta Trop. , vol.85 , pp. 375-390
    • Chang, K.P.1    Reed, S.G.2    McGwire, B.S.3    Soong, G.L.4
  • 13
    • 3843056161 scopus 로고    scopus 로고
    • Proteases in trypanosomatids
    • Hide G., Mottram J.C., Coombs G.H., and Holmes P.H. (Eds), CAB International, London
    • Coombs G.H., and Mottram J.C. Proteases in trypanosomatids. In: Hide G., Mottram J.C., Coombs G.H., and Holmes P.H. (Eds). Trypanosomiasis and Leishmaniasis (1997), CAB International, London 176-197
    • (1997) Trypanosomiasis and Leishmaniasis , pp. 176-197
    • Coombs, G.H.1    Mottram, J.C.2
  • 14
    • 36348992108 scopus 로고    scopus 로고
    • Chagas disease: what is known and what is needed-a background article
    • Coura J.R. Chagas disease: what is known and what is needed-a background article. Mem. Inst. Oswaldo Cruz 102 (2007) 113-122
    • (2007) Mem. Inst. Oswaldo Cruz , vol.102 , pp. 113-122
    • Coura, J.R.1
  • 19
    • 0036155657 scopus 로고    scopus 로고
    • Pathogenesis of Chagas heart disease: role of autoimmunity
    • Engman D.M., and Leon J.S. Pathogenesis of Chagas heart disease: role of autoimmunity. Acta Trop. 81 (2002) 123-132
    • (2002) Acta Trop. , vol.81 , pp. 123-132
    • Engman, D.M.1    Leon, J.S.2
  • 20
    • 50549163362 scopus 로고
    • The preparation and properties of two new chromogenic substrates os trypsin
    • Erlanger B.F., Kokowsky N., and Cohen W. The preparation and properties of two new chromogenic substrates os trypsin. Arch. Biochem. Biophys. 95 (1961) 271-278
    • (1961) Arch. Biochem. Biophys. , vol.95 , pp. 271-278
    • Erlanger, B.F.1    Kokowsky, N.2    Cohen, W.3
  • 21
    • 29544446817 scopus 로고    scopus 로고
    • The serine carboxypeptidase like gene family of rice (Oryza sativa L. ssp. japonica)
    • Feng Y., and Xue Q. The serine carboxypeptidase like gene family of rice (Oryza sativa L. ssp. japonica). Funct. Integr. Genomics 6 (2006) 14-24
    • (2006) Funct. Integr. Genomics , vol.6 , pp. 14-24
    • Feng, Y.1    Xue, Q.2
  • 22
    • 5644295618 scopus 로고    scopus 로고
    • Reservosome: an endocytic compartment in epimastigote forms of the protozoan Trypanosoma cruzi (Kinetoplastida: Trypanosomatidae). Correlation between endocytosis of nutrients and cell differentiation
    • Figueiredo R.C.B., Rosa D.S., Gomes Y.M., Nakasawa M., and Soares M.J. Reservosome: an endocytic compartment in epimastigote forms of the protozoan Trypanosoma cruzi (Kinetoplastida: Trypanosomatidae). Correlation between endocytosis of nutrients and cell differentiation. Parasitology 129 (2004) 1-8
    • (2004) Parasitology , vol.129 , pp. 1-8
    • Figueiredo, R.C.B.1    Rosa, D.S.2    Gomes, Y.M.3    Nakasawa, M.4    Soares, M.J.5
  • 24
    • 33748660679 scopus 로고    scopus 로고
    • Inhibition of dipeptidylpeptidase IV activity as a therapy of type 2 diabetes
    • Green B.D., Flatt P.R., and Bailey C.J. Inhibition of dipeptidylpeptidase IV activity as a therapy of type 2 diabetes. Expert Opin. Emerg. Drugs 11 (2006) 525-539
    • (2006) Expert Opin. Emerg. Drugs , vol.11 , pp. 525-539
    • Green, B.D.1    Flatt, P.R.2    Bailey, C.J.3
  • 25
    • 0033385805 scopus 로고    scopus 로고
    • Cathepsin A/protective protein: an unusual lysosomal multifunctional protein
    • Hiraiwa M. Cathepsin A/protective protein: an unusual lysosomal multifunctional protein. Cell. Mol. Life Sci. 56 (1999) 894-907
    • (1999) Cell. Mol. Life Sci. , vol.56 , pp. 894-907
    • Hiraiwa, M.1
  • 26
    • 0035997361 scopus 로고    scopus 로고
    • Biological roles of proteases in parasitic protozoa
    • Klemba M., and Goldberg D.E. Biological roles of proteases in parasitic protozoa. Annu. Rev. Biochem. 71 (2002) 275-305
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 275-305
    • Klemba, M.1    Goldberg, D.E.2
  • 27
    • 38849143983 scopus 로고    scopus 로고
    • Neutrophil elastase, proteinase 3 and cathepsin G: physicochemical properties, activity and physiopathological functions
    • Korkmaz B., Moreau T., and Gauthier F. Neutrophil elastase, proteinase 3 and cathepsin G: physicochemical properties, activity and physiopathological functions. Biochimie 90 (2008) 227-242
    • (2008) Biochimie , vol.90 , pp. 227-242
    • Korkmaz, B.1    Moreau, T.2    Gauthier, F.3
  • 28
    • 33846293219 scopus 로고    scopus 로고
    • Cysteine proteinases of Trypanosoma cruzi: from digestive enzymes to programmed cell death mediators
    • Kosec G., Alvarez V., and Cazzulo J.J. Cysteine proteinases of Trypanosoma cruzi: from digestive enzymes to programmed cell death mediators. Biocell 30 (2006) 479-490
    • (2006) Biocell , vol.30 , pp. 479-490
    • Kosec, G.1    Alvarez, V.2    Cazzulo, J.J.3
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
  • 31
    • 0018873523 scopus 로고
    • Protein inhibitors of proteases
    • Laskowski M., and Kato I. Protein inhibitors of proteases. Ann. Rev. Biochem. 49 (1980) 593-626
    • (1980) Ann. Rev. Biochem. , vol.49 , pp. 593-626
    • Laskowski, M.1    Kato, I.2
  • 33
    • 0032781636 scopus 로고    scopus 로고
    • Purification and characterisation of a trypsin-like serine oligopeptidase from Trypanosoma congolense
    • Morty R.E., Authie E., Troeberg L., Lonsdale-Eccles J.D., and Coetzer T.H. Purification and characterisation of a trypsin-like serine oligopeptidase from Trypanosoma congolense. Mol. Biochem. Parasitol. 102 (1999) 145-155
    • (1999) Mol. Biochem. Parasitol. , vol.102 , pp. 145-155
    • Morty, R.E.1    Authie, E.2    Troeberg, L.3    Lonsdale-Eccles, J.D.4    Coetzer, T.H.5
  • 34
    • 0033543644 scopus 로고    scopus 로고
    • Oligopeptidase B from Trypanosoma brucei, a new member of an emerging subgroup of serine oligopeptidases
    • Morty R.E., Authié E., Troeberg L., Lonsdale-Eccles J.D., and Coetzer T.H.T. Oligopeptidase B from Trypanosoma brucei, a new member of an emerging subgroup of serine oligopeptidases. J. Biol. Chem. 274 (1999) 26149-26156
    • (1999) J. Biol. Chem. , vol.274 , pp. 26149-26156
    • Morty, R.E.1    Authié, E.2    Troeberg, L.3    Lonsdale-Eccles, J.D.4    Coetzer, T.H.T.5
  • 35
    • 0035082118 scopus 로고    scopus 로고
    • Trypanosome-derived oligopeptidase B is released into the plasma of infected rodents, where it persists and retains full catalytic activity
    • Morty R.E., Lonsdale-Eccles J.D., Mentele R., Auerswald E.A., and Coetzer T.H. Trypanosome-derived oligopeptidase B is released into the plasma of infected rodents, where it persists and retains full catalytic activity. Infect. Immun. 69 (2001) 2757-2761
    • (2001) Infect. Immun. , vol.69 , pp. 2757-2761
    • Morty, R.E.1    Lonsdale-Eccles, J.D.2    Mentele, R.3    Auerswald, E.A.4    Coetzer, T.H.5
  • 37
    • 33846466564 scopus 로고    scopus 로고
    • Two metallocarboxypeptidases from the protozoan Trypanosoma cruzi belong to the M32 family, found so far only in prokaryotes
    • Niemirowicz G., Parussini F., Aguero F., and Cazzulo J.J. Two metallocarboxypeptidases from the protozoan Trypanosoma cruzi belong to the M32 family, found so far only in prokaryotes. Biochem. J. 401 (2007) 399-410
    • (2007) Biochem. J. , vol.401 , pp. 399-410
    • Niemirowicz, G.1    Parussini, F.2    Aguero, F.3    Cazzulo, J.J.4
  • 38
    • 0031016286 scopus 로고    scopus 로고
    • Endocytosis and secretion in trypanosomatid parasites-tumultuous traffic in a pocket
    • Overath P., Stierhof Y.D., and Wiese M. Endocytosis and secretion in trypanosomatid parasites-tumultuous traffic in a pocket. Trends Cell Biol. 7 (1997) 27-33
    • (1997) Trends Cell Biol. , vol.7 , pp. 27-33
    • Overath, P.1    Stierhof, Y.D.2    Wiese, M.3
  • 40
    • 0031106627 scopus 로고    scopus 로고
    • Extracellular matrix: a tool for defining the extracorporeal function of parasite proteases
    • Rhoads M.L., and Fetterer R.H. Extracellular matrix: a tool for defining the extracorporeal function of parasite proteases. Parasitol. Today 13 (1997) 119-122
    • (1997) Parasitol. Today , vol.13 , pp. 119-122
    • Rhoads, M.L.1    Fetterer, R.H.2
  • 41
    • 0033042010 scopus 로고    scopus 로고
    • Proteases of protozoan parasites
    • Rosenthal P.J. Proteases of protozoan parasites. Adv. Parasitol. 43 (1999) 105-159
    • (1999) Adv. Parasitol. , vol.43 , pp. 105-159
    • Rosenthal, P.J.1
  • 42
    • 0030771205 scopus 로고    scopus 로고
    • A Trypanosoma cruzi-secreted 80 kDa protease with specificity for human collagen types I and IV
    • Santana J.M., Grellier P., Schrével J., and Teixeira A.R. A Trypanosoma cruzi-secreted 80 kDa protease with specificity for human collagen types I and IV. Biochem. J. 324 (1997) 129-137
    • (1997) Biochem. J. , vol.324 , pp. 129-137
    • Santana, J.M.1    Grellier, P.2    Schrével, J.3    Teixeira, A.R.4
  • 43
    • 36348949834 scopus 로고    scopus 로고
    • Epidemiology of Chagas disease in nonendemic countries: the role of international migration
    • Schmunis G.A. Epidemiology of Chagas disease in nonendemic countries: the role of international migration. Mem. Inst. Oswaldo Cruz 102 (2007) 75-86
    • (2007) Mem. Inst. Oswaldo Cruz , vol.102 , pp. 75-86
    • Schmunis, G.A.1
  • 44
    • 0026584008 scopus 로고
    • Autophagy and other vacuolar protein degradation mechanisms
    • Seglen P.O., and Bohley P. Autophagy and other vacuolar protein degradation mechanisms. Experientia 48 (1992) 158-172
    • (1992) Experientia , vol.48 , pp. 158-172
    • Seglen, P.O.1    Bohley, P.2
  • 46
    • 4143144193 scopus 로고    scopus 로고
    • A serine protease from a detergent soluble extract of Leishmania (Leishmania) amazonensis
    • Silva-Lopez R.E., and Giovanni De Simone S. A serine protease from a detergent soluble extract of Leishmania (Leishmania) amazonensis. Z. Naturforsch. 59c (2004) 590-598
    • (2004) Z. Naturforsch. , vol.59 c , pp. 590-598
    • Silva-Lopez, R.E.1    Giovanni De Simone, S.2
  • 47
    • 4444378997 scopus 로고    scopus 로고
    • Leishmania (Leishmania) amazonensis: purification and characterization of a promastigote serine protease
    • Silva-Lopez R.E., and Giovanni De Simone S. Leishmania (Leishmania) amazonensis: purification and characterization of a promastigote serine protease. Exp. Parasitol. 107 (2004) 173-182
    • (2004) Exp. Parasitol. , vol.107 , pp. 173-182
    • Silva-Lopez, R.E.1    Giovanni De Simone, S.2
  • 48
    • 22444447550 scopus 로고    scopus 로고
    • Characterization of an extracellular serine protease of Leishmania (Leishmania) amazonensis
    • Silva-Lopez R.E., and Giovanni De Simone S. Characterization of an extracellular serine protease of Leishmania (Leishmania) amazonensis. Parasitology 131 (2005) 85-96
    • (2005) Parasitology , vol.131 , pp. 85-96
    • Silva-Lopez, R.E.1    Giovanni De Simone, S.2
  • 49
    • 34948893961 scopus 로고    scopus 로고
    • Effects of serine protease inhibitors on viability and morphology of Leishmania (Leishmania) amazonensis promastigotes
    • Silva-Lopez R.E., Morgado-Díaz J.A., Cháves M.A., and Giovanni-De-Simone S. Effects of serine protease inhibitors on viability and morphology of Leishmania (Leishmania) amazonensis promastigotes. Parasitol. Res. 101 (2007) 1627-1635
    • (2007) Parasitol. Res. , vol.101 , pp. 1627-1635
    • Silva-Lopez, R.E.1    Morgado-Díaz, J.A.2    Cháves, M.A.3    Giovanni-De-Simone, S.4
  • 50
    • 0026691797 scopus 로고
    • Identification of a large pre-lysosomal compartment in the pathogenic protozoon Trypanosoma cruzi
    • Soares M.J., Souto-Padrón T., and De Souza W. Identification of a large pre-lysosomal compartment in the pathogenic protozoon Trypanosoma cruzi. J. Cell Sci. 102 (1991) 157-167
    • (1991) J. Cell Sci. , vol.102 , pp. 157-167
    • Soares, M.J.1    Souto-Padrón, T.2    De Souza, W.3
  • 51
    • 0036544578 scopus 로고    scopus 로고
    • Kinetic peculiarities of human tissue kallikrein. 1. Substrate activation in the catalyzed hydrolysis of H-d-valyl-leucyl-l-arginine 4-nitroanilide and H-d-valyl-leucyl-l-lysine 4-nitroanilide; 2. Substrate inhibition in the catalysed hydrolysis of N-ρ-tosyl-l-arginine methyl ester
    • Sousa M.O., Miranda T.S.L., Maia C.N., Santoro M.M., and Figueiredo A.F.S. Kinetic peculiarities of human tissue kallikrein. 1. Substrate activation in the catalyzed hydrolysis of H-d-valyl-leucyl-l-arginine 4-nitroanilide and H-d-valyl-leucyl-l-lysine 4-nitroanilide; 2. Substrate inhibition in the catalysed hydrolysis of N-ρ-tosyl-l-arginine methyl ester. Arch. Biochem. Biophys. 400 (2002) 7-14
    • (2002) Arch. Biochem. Biophys. , vol.400 , pp. 7-14
    • Sousa, M.O.1    Miranda, T.S.L.2    Maia, C.N.3    Santoro, M.M.4    Figueiredo, A.F.S.5
  • 53
    • 4644222305 scopus 로고    scopus 로고
    • Kluwer Academic Publishers, London, United Kingdom pp. 81-96
    • Tyler K., and Miles M.A. American Trypanosomiasis vol.7 (2003), Kluwer Academic Publishers, London, United Kingdom pp. 81-96
    • (2003) American Trypanosomiasis , vol.7
    • Tyler, K.1    Miles, M.A.2
  • 54
    • 0036409194 scopus 로고    scopus 로고
    • Expression and one-step purification of a developmentally regulated protein from Dictyostelium discoideum
    • Ubeidat M., and Rutherford C.L. Expression and one-step purification of a developmentally regulated protein from Dictyostelium discoideum. Protein Expr. Purif. 25 (2002) 472-480
    • (2002) Protein Expr. Purif. , vol.25 , pp. 472-480
    • Ubeidat, M.1    Rutherford, C.L.2
  • 55
    • 33745826249 scopus 로고    scopus 로고
    • Description of esterase and peptidase activities of acylaminoacyl peptidase from hyperthermophilic Aeropyrum pernix K1 by a single mutation
    • Wang Q., Yang G., Liu Y., and Feng Y. Description of esterase and peptidase activities of acylaminoacyl peptidase from hyperthermophilic Aeropyrum pernix K1 by a single mutation. J. Biol. Chem. 281 (2006) 18618-18625
    • (2006) J. Biol. Chem. , vol.281 , pp. 18618-18625
    • Wang, Q.1    Yang, G.2    Liu, Y.3    Feng, Y.4
  • 56
    • 47549100628 scopus 로고    scopus 로고
    • WHO, 2006. Strategic and technical meeting on intensified control of neglected tropical diseases. In: Proceedings of the Report of an International Workshop. Berlin, April 18-20, 2005, WHO/CDS/NTD/2006.1 http://www.who.int/neglected_diseases/en/acessed in December 2006.
    • WHO, 2006. Strategic and technical meeting on intensified control of neglected tropical diseases. In: Proceedings of the Report of an International Workshop. Berlin, April 18-20, 2005, WHO/CDS/NTD/2006.1 http://www.who.int/neglected_diseases/en/acessed in December 2006.
  • 57
    • 33644981279 scopus 로고    scopus 로고
    • Molecular basis of mammalian cell invasion by Trypanosoma cruzi
    • Yoshida N. Molecular basis of mammalian cell invasion by Trypanosoma cruzi. An. Acad. Bras. Cienc. 78 (2006) 87-111
    • (2006) An. Acad. Bras. Cienc. , vol.78 , pp. 87-111
    • Yoshida, N.1
  • 58
    • 0027314162 scopus 로고
    • Proteolytic release of cell surface protein during differentiation of Trypanosoma cruzi
    • Ziegelbauer K., Stahl B., Karas M., Stierhof Y.D., and Overath P. Proteolytic release of cell surface protein during differentiation of Trypanosoma cruzi. Biochemistry 32 (1993) 3737-3742
    • (1993) Biochemistry , vol.32 , pp. 3737-3742
    • Ziegelbauer, K.1    Stahl, B.2    Karas, M.3    Stierhof, Y.D.4    Overath, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.