메뉴 건너뛰기




Volumn 132, Issue 1, 2003, Pages 1-16

The major surface protease (MSP or GP63) of Leishmania sp. Biosynthesis, regulation of expression, and function

Author keywords

Biosynthesis; Gene expression; GP63; Leishmania; Major surface protease

Indexed keywords

COMPLEMENTARY RNA; MAJOR SURFACE PROTEASE; MEMBRANE PROTEIN; MICROBIAL ENZYME; PROTOZOAL PROTEIN; UNCLASSIFIED DRUG;

EID: 0141888314     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(03)00211-1     Document Type: Review
Times cited : (245)

References (124)
  • 1
    • 0002549642 scopus 로고
    • Biology of Leishmania and leishmaniasis
    • Chang KP, Bray RS, editors. New York: Elsevier
    • Chang KP, Fong D, Bray RS. Biology of Leishmania and leishmaniasis. In: Chang KP, Bray RS, editors. Leishmaniasis. New York: Elsevier; 1985. p. 1-30.
    • (1985) Leishmaniasis , pp. 1-30
    • Chang, K.P.1    Fong, D.2    Bray, R.S.3
  • 3
    • 0030249268 scopus 로고    scopus 로고
    • Leishmaniasis. Public health aspects and control
    • Desjeux P. Leishmaniasis. Public health aspects and control. Clin. Dermatol. 14:1996;417-423.
    • (1996) Clin. Dermatol. , vol.14 , pp. 417-423
    • Desjeux, P.1
  • 4
    • 0035348374 scopus 로고    scopus 로고
    • The increase in risk factors for leishmaniasis worldwide
    • Desjeux P. The increase in risk factors for leishmaniasis worldwide. Trans. R. Soc. Trop. Med. Hyg. 95:2001;239-243.
    • (2001) Trans. R. Soc. Trop. Med. Hyg. , vol.95 , pp. 239-243
    • Desjeux, P.1
  • 5
    • 18644374832 scopus 로고    scopus 로고
    • Strategic emphasis for tropical diseases research: A TDR perspective
    • Remme J.H., Blas E., Chitsulo L.et al. Strategic emphasis for tropical diseases research: a TDR perspective. Trends Parasitol. 18:2002;421-426.
    • (2002) Trends Parasitol. , vol.18 , pp. 421-426
    • Remme, J.H.1    Blas, E.2    Chitsulo, L.3
  • 6
    • 0026592139 scopus 로고
    • Human leishmaniases: Epidemiology and public health aspects
    • Desjeux P. Human leishmaniases: epidemiology and public health aspects. World Health Stat. Q. 45:1992;267-275.
    • (1992) World Health Stat. Q , vol.45 , pp. 267-275
    • Desjeux, P.1
  • 7
    • 0027128081 scopus 로고
    • Viscerotropic leishmaniasis in persons returning from Operation Desert Storm - 1990-1991
    • Magill AJ, Gasser RA, Oster CN, Grogl M, Sun W. Viscerotropic leishmaniasis in persons returning from Operation Desert Storm - 1990-1991. MMWR Morb Mortal Weekly Rep 1992;41:131-4.
    • (1992) MMWR Morb Mortal Weekly Rep , vol.41 , pp. 131-134
    • Magill, A.J.1    Gasser, R.A.2    Oster, C.N.3    Grogl, M.4    Sun, W.5
  • 8
    • 0027122563 scopus 로고
    • From the centers for disease control. Viscerotropic leishmaniasis in persons returning from Operation Desert Storm - 1990-1991
    • Magill A.J., Gasser R.A., Oster C.N., Grogl M., Sun W. From the centers for disease control. Viscerotropic leishmaniasis in persons returning from Operation Desert Storm - 1990-1991. JAMA. 267:1992;1444-1446.
    • (1992) JAMA , vol.267 , pp. 1444-1446
    • Magill, A.J.1    Gasser, R.A.2    Oster, C.N.3    Grogl, M.4    Sun, W.5
  • 9
    • 0027241626 scopus 로고
    • Visceral infection caused by Leishmania tropica in veterans of Operation Desert Storm [see comments]
    • Magill A.J., Grogl M., Gasser R.A. Jr., Sun W., Oster C.N. Visceral infection caused by Leishmania tropica in veterans of Operation Desert Storm [see comments]. N. Engl. J. Med. 328:1993;1383-1387.
    • (1993) N. Engl. J. Med. , vol.328 , pp. 1383-1387
    • Magill, A.J.1    Grogl, M.2    Gasser R.A., Jr.3    Sun, W.4    Oster, C.N.5
  • 10
    • 0033709808 scopus 로고    scopus 로고
    • The leishmaniases as emerging and reemerging zoonoses
    • Ashford R.W. The leishmaniases as emerging and reemerging zoonoses. Int. J. Parasitol. 30:2000;1269-1281.
    • (2000) Int. J. Parasitol. , vol.30 , pp. 1269-1281
    • Ashford, R.W.1
  • 12
    • 0032583153 scopus 로고    scopus 로고
    • Genetic nomenclature for Trypanosoma and Leishmania
    • Clayton C., Adams M., Almeida R.et al. Genetic nomenclature for Trypanosoma and Leishmania. Mol. Biochem. Parasitol. 97:1998;221-224.
    • (1998) Mol. Biochem. Parasitol. , vol.97 , pp. 221-224
    • Clayton, C.1    Adams, M.2    Almeida, R.3
  • 13
    • 0032529002 scopus 로고    scopus 로고
    • The crystal structure of the Leishmania major surface proteinase leishmanolysin (gp63)
    • Schlagenhauf E., Etges R., Metcalf P. The crystal structure of the Leishmania major surface proteinase leishmanolysin (gp63). Structure. 6:1998;1035-1046.
    • (1998) Structure , vol.6 , pp. 1035-1046
    • Schlagenhauf, E.1    Etges, R.2    Metcalf, P.3
  • 14
    • 0036438912 scopus 로고    scopus 로고
    • Activation mechanism of pro-astacin: Role of the pro-peptide, tryptic and autoproteolytic cleavage and importance of precise amino-terminal processing
    • Yiallouros I., Kappelhoff R., Schilling O.et al. Activation mechanism of pro-astacin: role of the pro-peptide, tryptic and autoproteolytic cleavage and importance of precise amino-terminal processing. J. Mol. Biol. 324:2002;237-246.
    • (2002) J. Mol. Biol. , vol.324 , pp. 237-246
    • Yiallouros, I.1    Kappelhoff, R.2    Schilling, O.3
  • 15
    • 0032582674 scopus 로고    scopus 로고
    • Crystal structures of acutolysin A, a three-disulfide hemorrhagic zinc metalloproteinase from the snake venom of Agkistrodon acutus
    • Gong W., Zhu X., Liu S., Teng M., Niu L. Crystal structures of acutolysin A, a three-disulfide hemorrhagic zinc metalloproteinase from the snake venom of Agkistrodon acutus. J. Mol. Biol. 283:1998;657-668.
    • (1998) J. Mol. Biol. , vol.283 , pp. 657-668
    • Gong, W.1    Zhu, X.2    Liu, S.3    Teng, M.4    Niu, L.5
  • 16
    • 0023193846 scopus 로고
    • The promastigote surface protease of Leishmania
    • Bordier C. The promastigote surface protease of Leishmania. Parsitol. Today. 3:1987;151-153.
    • (1987) Parsitol. Today , vol.3 , pp. 151-153
    • Bordier, C.1
  • 17
    • 0027466501 scopus 로고
    • Evolution and expression of the Leishmania surface proteinase (gp63) gene locus
    • Medina-Acosta E., Beverley S.M., Russell D.G. Evolution and expression of the Leishmania surface proteinase (gp63) gene locus. Infect Agents Dis. 2:1993;25-34.
    • (1993) Infect Agents Dis. , vol.2 , pp. 25-34
    • Medina-Acosta, E.1    Beverley, S.M.2    Russell, D.G.3
  • 18
    • 0027982197 scopus 로고
    • Mutational and functional analysis of the Leishmania surface metalloproteinase GP63: Similarities to matrix metalloproteinases
    • McMaster W.R., Morrison C.J., MacDonald M.H., Joshi P.B. Mutational and functional analysis of the Leishmania surface metalloproteinase GP63: similarities to matrix metalloproteinases. Parasitology. 108:1994;S29-S36.
    • (1994) Parasitology , vol.108
    • McMaster, W.R.1    Morrison, C.J.2    MacDonald, M.H.3    Joshi, P.B.4
  • 19
    • 0027509513 scopus 로고
    • Expression of lipophosphoglycan, high-molecular weight phosphoglycan and glycoprotein 63 in promastigotes and amastigotes of Leishmania mexicana
    • Bahr V., Stierhof Y.D., Ilg T.et al. Expression of lipophosphoglycan, high-molecular weight phosphoglycan and glycoprotein 63 in promastigotes and amastigotes of Leishmania mexicana. Mol. Biochem. Parasitol. 58:1993;107-121.
    • (1993) Mol. Biochem. Parasitol. , vol.58 , pp. 107-121
    • Bahr, V.1    Stierhof, Y.D.2    Ilg, T.3
  • 20
    • 0022373133 scopus 로고
    • Identification and purification of membrane and soluble forms of the major surface protein of Leishmania promastigotes
    • Bouvier J., Etges R.J., Bordier C. Identification and purification of membrane and soluble forms of the major surface protein of Leishmania promastigotes. J. Biol. Chem. 260:1985;15504-15509.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15504-15509
    • Bouvier, J.1    Etges, R.J.2    Bordier, C.3
  • 21
    • 0025138718 scopus 로고
    • Leishmania gp63 molecule implicated in cellular adhesion lacks an Arg-Gly-Asp sequence
    • Miller R.A., Reed S.G., Parsons M. Leishmania gp63 molecule implicated in cellular adhesion lacks an Arg-Gly-Asp sequence. Mol. Biochem. Parasitol. 39:1990;267-274.
    • (1990) Mol. Biochem. Parasitol. , vol.39 , pp. 267-274
    • Miller, R.A.1    Reed, S.G.2    Parsons, M.3
  • 22
    • 0024509987 scopus 로고
    • Surface acid proteinase (gp63) of Leishmania mexicana. A metalloenzyme capable of protecting liposome-encapsulated proteins from phagolysosomal degradation by macrophages
    • Chaudhuri G., Chaudhuri M., Pan A., Chang K.P. Surface acid proteinase (gp63) of Leishmania mexicana. A metalloenzyme capable of protecting liposome-encapsulated proteins from phagolysosomal degradation by macrophages. J. Biol. Chem. 264:1989;7483-7489.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7483-7489
    • Chaudhuri, G.1    Chaudhuri, M.2    Pan, A.3    Chang, K.P.4
  • 23
    • 0024454057 scopus 로고
    • Characterization of the promastigote surface protease of Leishmania as a membrane-bound zinc endopeptidase
    • Bouvier J., Bordier C., Vogel H., Reichelt R., Etges R. Characterization of the promastigote surface protease of Leishmania as a membrane-bound zinc endopeptidase. Mol. Biochem. Parasitol. 37:1989;235-245.
    • (1989) Mol. Biochem. Parasitol. , vol.37 , pp. 235-245
    • Bouvier, J.1    Bordier, C.2    Vogel, H.3    Reichelt, R.4    Etges, R.5
  • 24
    • 0026598731 scopus 로고
    • Three distinct RNAs for the surface protease gp63 are differentially expressed during development of Leishmania donovani chagasi promastigotes to an infectious form
    • Ramamoorthy R., Donelson J.E., Paetz K.E.et al. Three distinct RNAs for the surface protease gp63 are differentially expressed during development of Leishmania donovani chagasi promastigotes to an infectious form. J. Biol. Chem. 267:1992;1888-1895.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1888-1895
    • Ramamoorthy, R.1    Donelson, J.E.2    Paetz, K.E.3
  • 25
    • 0032523872 scopus 로고    scopus 로고
    • Differentially expressed Leishmania major gp63 genes encode cell surface leishmanolysin with distinct signals for glycosylphosphatidylinositol attachment
    • Voth B.R., Kelly B.L., Joshi P.B., Ivens A.C., McMaster W.R. Differentially expressed Leishmania major gp63 genes encode cell surface leishmanolysin with distinct signals for glycosylphosphatidylinositol attachment. Mol. Biochem. Parasitol. 93:1998;31-41.
    • (1998) Mol. Biochem. Parasitol. , vol.93 , pp. 31-41
    • Voth, B.R.1    Kelly, B.L.2    Joshi, P.B.3    Ivens, A.C.4    McMaster, W.R.5
  • 26
    • 0027472098 scopus 로고
    • Structurally distinct genes for the surface protease of Leishmania mexicana are developmentally regulated
    • Medina-Acosta E., Karess R.E., Russell D.G. Structurally distinct genes for the surface protease of Leishmania mexicana are developmentally regulated. Mol. Biochem. Parasitol. 57:1993;31-45.
    • (1993) Mol. Biochem. Parasitol. , vol.57 , pp. 31-45
    • Medina-Acosta, E.1    Karess, R.E.2    Russell, D.G.3
  • 27
    • 0023837354 scopus 로고
    • Molecular cloning of the major surface antigen of Leishmania
    • Button L.L., McMaster W.R. Molecular cloning of the major surface antigen of Leishmania. J. Exp. Med. 167:1988;724-729.
    • (1988) J. Exp. Med. , vol.167 , pp. 724-729
    • Button, L.L.1    McMaster, W.R.2
  • 28
    • 0028972393 scopus 로고
    • Analysis of the active site and activation mechanism of the Leishmania surface metalloproteinase GP63
    • Macdonald M.H., Morrison C.J., McMaster W.R. Analysis of the active site and activation mechanism of the Leishmania surface metalloproteinase GP63. Biochim. Biophys. Acta. 1253:1995;199-207.
    • (1995) Biochim. Biophys. Acta , vol.1253 , pp. 199-207
    • Macdonald, M.H.1    Morrison, C.J.2    McMaster, W.R.3
  • 30
    • 0027732044 scopus 로고
    • Sequence heterogeneity and polymorphic gene arrangements of the Leishmania guyanensis gp63 genes
    • Steinkraus H.B., Greer J.M., Stephenson D.C., Langer P.J. Sequence heterogeneity and polymorphic gene arrangements of the Leishmania guyanensis gp63 genes. Mol. Biochem. Parasitol. 62:1993;173-185.
    • (1993) Mol. Biochem. Parasitol. , vol.62 , pp. 173-185
    • Steinkraus, H.B.1    Greer, J.M.2    Stephenson, D.C.3    Langer, P.J.4
  • 31
    • 0029873473 scopus 로고    scopus 로고
    • Posttranslational regulation of a Leishmania HEXXH metalloprotease (gp63). The effects of site-specific mutagenesis of catalytic, zinc binding, N-glycosylation, and glycosyl phosphatidylinositol addition sites on N-terminal end cleavage, intracellular stability, and extracellular exit
    • McGwire B.S., Chang K.P. Posttranslational regulation of a Leishmania HEXXH metalloprotease (gp63). The effects of site-specific mutagenesis of catalytic, zinc binding, N-glycosylation, and glycosyl phosphatidylinositol addition sites on N-terminal end cleavage, intracellular stability, and extracellular exit. J. Biol. Chem. 271:1996;7903-7909.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7903-7909
    • McGwire, B.S.1    Chang, K.P.2
  • 32
    • 0026602824 scopus 로고
    • The protein sequence predicted from a Leishmania guyanensis gp63 major surface glycoprotein gene is divergent as compared with other Leishmania species
    • Steinkraus H.B., Langer P.J. The protein sequence predicted from a Leishmania guyanensis gp63 major surface glycoprotein gene is divergent as compared with other Leishmania species. Mol. Biochem. Parasitol. 52:1992;141-144.
    • (1992) Mol. Biochem. Parasitol. , vol.52 , pp. 141-144
    • Steinkraus, H.B.1    Langer, P.J.2
  • 33
    • 0037084391 scopus 로고    scopus 로고
    • Mutational analysis of the variant surface glycoprotein GPI-anchor signal sequence in Trypanosoma brucei
    • Bohme U., Cross G.A. Mutational analysis of the variant surface glycoprotein GPI-anchor signal sequence in Trypanosoma brucei. J. Cell. Sci. 115:2002;805-816.
    • (2002) J. Cell. Sci. , vol.115 , pp. 805-816
    • Bohme, U.1    Cross, G.A.2
  • 34
    • 0035171871 scopus 로고    scopus 로고
    • The Leishmania genome project: New insights into gene organization and function
    • Myler P.J., Beverley S.M., Cruz A.K.et al. The Leishmania genome project: new insights into gene organization and function. Med. Microbiol. Immunol. (Berl). 190:2001;9-12.
    • (2001) Med. Microbiol. Immunol. (Berl) , vol.190 , pp. 9-12
    • Myler, P.J.1    Beverley, S.M.2    Cruz, A.K.3
  • 35
    • 0034305646 scopus 로고    scopus 로고
    • Genomic organization and gene function in Leishmania
    • Myler P.J., Sisk E., McDonagh P.D.et al. Genomic organization and gene function in Leishmania. Biochem. Soc. Trans. 28:2000;527-531.
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 527-531
    • Myler, P.J.1    Sisk, E.2    McDonagh, P.D.3
  • 36
    • 0034662283 scopus 로고    scopus 로고
    • The unusual gene organization of Leishmania major chromosome 1 may reflect novel transcription processes
    • McDonagh P.D., Myler P.J., Stuart K. The unusual gene organization of Leishmania major chromosome 1 may reflect novel transcription processes. Nucleic Acids Res. 28:2000;2800-2803.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2800-2803
    • McDonagh, P.D.1    Myler, P.J.2    Stuart, K.3
  • 37
    • 13044271011 scopus 로고    scopus 로고
    • Leishmania major Friedlin chromosome 1 has an unusual distribution of protein-coding genes
    • Myler P.J., Audleman L., deVos T.et al. Leishmania major Friedlin chromosome 1 has an unusual distribution of protein-coding genes. Proc. Natl. Acad. Sci. USA. 96:1999;2902-2906.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2902-2906
    • Myler, P.J.1    Audleman, L.2    DeVos, T.3
  • 38
    • 0034634621 scopus 로고    scopus 로고
    • Mutational analysis of 3′ splice site selection during trans-splicing
    • Hummel H.S., Gillespie R.D., Swindle J. Mutational analysis of 3′ splice site selection during trans-splicing. J. Biol. Chem. 275:2000; 35522-35531.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35522-35531
    • Hummel, H.S.1    Gillespie, R.D.2    Swindle, J.3
  • 39
    • 0028214539 scopus 로고
    • A common pyrimidine-rich motif governs trans-splicing and polyadenylation of tubulin polycistronic pre-mRNA in trypanosomes
    • Matthews K.R., Tschudi C., Ullu E. A common pyrimidine-rich motif governs trans-splicing and polyadenylation of tubulin polycistronic pre-mRNA in trypanosomes. Genes Dev. 8:1994;491-501.
    • (1994) Genes Dev. , vol.8 , pp. 491-501
    • Matthews, K.R.1    Tschudi, C.2    Ullu, E.3
  • 40
    • 0027193605 scopus 로고
    • Coupling of poly(A) site selection and trans-splicing in Leishmania
    • LeBowitz JH, Smith HQ, Rusche L, Beverley SM. Coupling of poly(A) site selection and trans-splicing in Leishmania. Genes Dev 1993;7:996-1007.
    • (1993) Genes Dev , vol.7 , pp. 996-1007
    • LeBowitz, J.H.1    Smith, H.Q.2    Rusche, L.3    Beverley, S.M.4
  • 41
  • 42
    • 0027772884 scopus 로고
    • Sequence diversity and organization of the msp gene family encoding gp63 of Leishmania chagasi
    • Roberts S.C., Swihart K.G., Agey M.W.et al. Sequence diversity and organization of the msp gene family encoding gp63 of Leishmania chagasi. Mol. Biochem. Parasitol. 62:1993;157-171.
    • (1993) Mol. Biochem. Parasitol. , vol.62 , pp. 157-171
    • Roberts, S.C.1    Swihart, K.G.2    Agey, M.W.3
  • 43
    • 0029969609 scopus 로고    scopus 로고
    • Developmental changes in the expression of Leishmania chagasi gp63 and heat shock protein in a human macrophage cell line
    • Streit J.A., Donelson J.E., Agey M.W., Wilson M.E. Developmental changes in the expression of Leishmania chagasi gp63 and heat shock protein in a human macrophage cell line. Infect Immun. 64:1996;1810-1818.
    • (1996) Infect Immun. , vol.64 , pp. 1810-1818
    • Streit, J.A.1    Donelson, J.E.2    Agey, M.W.3    Wilson, M.E.4
  • 44
    • 0036178528 scopus 로고    scopus 로고
    • Targeted gene deletion in Leishmania major identifies leishmanolysin (GP63) as a virulence factor
    • Joshi P.B., Kelly B.L., Kamhawi S., Sacks D.L., McMaster W.R. Targeted gene deletion in Leishmania major identifies leishmanolysin (GP63) as a virulence factor. Mol. Biochem. Parasitol. 120:2002;33-40.
    • (2002) Mol. Biochem. Parasitol. , vol.120 , pp. 33-40
    • Joshi, P.B.1    Kelly, B.L.2    Kamhawi, S.3    Sacks, D.L.4    McMaster, W.R.5
  • 45
    • 0025913501 scopus 로고
    • Heterogeneity of the genes encoding the major surface glycoprotein of Leishmania donovani
    • Webb J.R., Button L.L., McMaster W.R. Heterogeneity of the genes encoding the major surface glycoprotein of Leishmania donovani. Mol. Biochem. Parasitol. 48:1991;173-184.
    • (1991) Mol. Biochem. Parasitol. , vol.48 , pp. 173-184
    • Webb, J.R.1    Button, L.L.2    McMaster, W.R.3
  • 47
    • 0030664774 scopus 로고    scopus 로고
    • African trypanosomes have differentially expressed genes encoding homologues of the Leishmania GP63 surface protease
    • El-Sayed N.M., Donelson J.E. African trypanosomes have differentially expressed genes encoding homologues of the Leishmania GP63 surface protease. J. Biol. Chem. 272:1997;26742-26748.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26742-26748
    • El-Sayed, N.M.1    Donelson, J.E.2
  • 50
    • 0037192110 scopus 로고    scopus 로고
    • Putting the Leishmania genome to work: Functional genomics by transposon trapping and expression profiling
    • Beverley S.M., Akopyants N.S., Goyard S.et al. Putting the Leishmania genome to work: functional genomics by transposon trapping and expression profiling. Philos. Trans. R. Soc. Lond. B Biol. Sci. 357:2002;47-53.
    • (2002) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.357 , pp. 47-53
    • Beverley, S.M.1    Akopyants, N.S.2    Goyard, S.3
  • 52
    • 0035930556 scopus 로고    scopus 로고
    • Developmental regulation of heat shock protein 83 in Leishmania. 3′ Processing and mRNA stability control transcript abundance, and translation id directed by a determinant in the 3′-untranslated region
    • Zilka A., Garlapati S., Dahan E., Yaolsky V., Shapira M.et al. Developmental regulation of heat shock protein 83 in Leishmania. 3′ Processing and mRNA stability control transcript abundance, and translation id directed by a determinant in the 3′-untranslated region. J. Biol. Chem. 276:2001;47922-47929.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47922-47929
    • Zilka, A.1    Garlapati, S.2    Dahan, E.3    Yaolsky, V.4    Shapira, M.5
  • 53
  • 54
    • 0031984118 scopus 로고    scopus 로고
    • Targeted gene deletion of Leishmania major genes encoding developmental stage-specific leishmanolysin (GP63)
    • Joshi P.B., Sacks D.L., Modi G., McMaster W.R. Targeted gene deletion of Leishmania major genes encoding developmental stage-specific leishmanolysin (GP63). Mol. Microbiol. 27:1998;519-530.
    • (1998) Mol. Microbiol. , vol.27 , pp. 519-530
    • Joshi, P.B.1    Sacks, D.L.2    Modi, G.3    McMaster, W.R.4
  • 55
    • 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., 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
  • 56
    • 0029012720 scopus 로고
    • Intergenic regions between tandem gp63 genes influence the differential expression of gp63 RNAs in Leishmania chagasi promastigotes
    • Ramamoorthy R., Swihart K.G., McCoy J.J., Wilson M.E., Donelson J.E. Intergenic regions between tandem gp63 genes influence the differential expression of gp63 RNAs in Leishmania chagasi promastigotes. J. Biol. Chem. 270:1995;12133-12139.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12133-12139
    • Ramamoorthy, R.1    Swihart, K.G.2    McCoy, J.J.3    Wilson, M.E.4    Donelson, J.E.5
  • 57
    • 0027306112 scopus 로고
    • The effect of ongoing protein synthesis on the steady state levels of Gp63 RNAs in Leishmania chagasi
    • Wilson M.E., Paetz K.E., Ramamoorthy R., Donelson J.E. The effect of ongoing protein synthesis on the steady state levels of Gp63 RNAs in Leishmania chagasi. J. Biol. Chem. 268:1993;15731-15736.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15731-15736
    • Wilson, M.E.1    Paetz, K.E.2    Ramamoorthy, R.3    Donelson, J.E.4
  • 58
    • 0035862695 scopus 로고    scopus 로고
    • Regulation of GP63 mRNA stability in promastigotes of virulent and attenuated Leishmania chagasi
    • Brittingham A., Miller M.A., Donelson J.E., Wilson M.E. Regulation of GP63 mRNA stability in promastigotes of virulent and attenuated Leishmania chagasi. Mol. Biochem. Parasitol. 112:2001;51-59.
    • (2001) Mol. Biochem. Parasitol. , vol.112 , pp. 51-59
    • Brittingham, A.1    Miller, M.A.2    Donelson, J.E.3    Wilson, M.E.4
  • 59
    • 0037053296 scopus 로고    scopus 로고
    • Comparison of the post-transcriptional regulation of the mRNAs for the surface proteins PSA (GP46) and MSP (GP63) of Leishmania chagasi
    • Myung K.S., Beetham J.K., Wilson M.E., Donelson J.E. Comparison of the post-transcriptional regulation of the mRNAs for the surface proteins PSA (GP46) and MSP (GP63) of Leishmania chagasi. J. Biol. Chem. 277:2002;16489-16497.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16489-16497
    • Myung, K.S.1    Beetham, J.K.2    Wilson, M.E.3    Donelson, J.E.4
  • 60
    • 0024400047 scopus 로고
    • Development of metacyclic Leishmania promastigotes is associated with the increasing expression of GP65, the major surface antigen
    • Kweider M., Lemesre J.L., Santoro F.et al. Development of metacyclic Leishmania promastigotes is associated with the increasing expression of GP65, the major surface antigen. Parasite Immunol. 11:1989;197-209.
    • (1989) Parasite Immunol. , vol.11 , pp. 197-209
    • Kweider, M.1    Lemesre, J.L.2    Santoro, F.3
  • 61
    • 0023203647 scopus 로고
    • Infectivity of Leishmania braziliensis promastigotes is dependent on the increasing expression of a 65,000-dalton surface antigen
    • Kweider M., Lemesre J.L., Darcy F.et al. Infectivity of Leishmania braziliensis promastigotes is dependent on the increasing expression of a 65,000-dalton surface antigen. J. Immunol. 138:1987;299-305.
    • (1987) J. Immunol. , vol.138 , pp. 299-305
    • Kweider, M.1    Lemesre, J.L.2    Darcy, F.3
  • 62
    • 0025123260 scopus 로고
    • Developmental modification of the lipophosphoglycan from Leishmania major promastigotes during metacyclogenesis
    • Sacks D.L., Brodin T.N., Turco S.J. Developmental modification of the lipophosphoglycan from Leishmania major promastigotes during metacyclogenesis. Mol. Biochem. Parasitol. 42:1990;225-233.
    • (1990) Mol. Biochem. Parasitol. , vol.42 , pp. 225-233
    • Sacks, D.L.1    Brodin, T.N.2    Turco, S.J.3
  • 63
    • 0025598330 scopus 로고
    • Expression of LPG and GP63 by different developmental stages of Leishmania major in the sandfly Phlebotomus papatasi
    • Davies C.R., Cooper A.M., Peacock C., Lane R.P., Blackwell J.M. Expression of LPG and GP63 by different developmental stages of Leishmania major in the sandfly Phlebotomus papatasi. Parasitology. 101(Pt 3):1990;337-343.
    • (1990) Parasitology , vol.101 , Issue.3 PART , pp. 337-343
    • Davies, C.R.1    Cooper, A.M.2    Peacock, C.3    Lane, R.P.4    Blackwell, J.M.5
  • 64
    • 0028963375 scopus 로고
    • Stage-specific binding of Leishmania donovani to the sand fly vector midgut is regulated by conformational changes in the abundant surface lipophosphoglycan
    • Sacks D.L., Pimenta P.F., McConville M.J., Schneider P., Turco S.J. Stage-specific binding of Leishmania donovani to the sand fly vector midgut is regulated by conformational changes in the abundant surface lipophosphoglycan. J. Exp. Med. 181:1995;685-697.
    • (1995) J. Exp. Med. , vol.181 , pp. 685-697
    • Sacks, D.L.1    Pimenta, P.F.2    McConville, M.J.3    Schneider, P.4    Turco, S.J.5
  • 65
    • 0037197792 scopus 로고    scopus 로고
    • Biosynthesis of the major surface protease GP63 of Leishmania chagasi
    • Yao C., Leidal K.G., Brittingham A.et al. Biosynthesis of the major surface protease GP63 of Leishmania chagasi. Mol. Biochem. Parasitol. 121:2002;119-128.
    • (2002) Mol. Biochem. Parasitol. , vol.121 , pp. 119-128
    • Yao, C.1    Leidal, K.G.2    Brittingham, A.3
  • 66
    • 0032522375 scopus 로고    scopus 로고
    • Species-specificity in endoplasmic reticulum signal peptide utilization revealed by proteins from Trypanosoma brucei and Leishmania
    • Al-Qahtani A., Teilhet M., Mensa-Wilmot K. Species-specificity in endoplasmic reticulum signal peptide utilization revealed by proteins from Trypanosoma brucei and Leishmania. Biochem. J. 331:1998;521-529.
    • (1998) Biochem. J. , vol.331 , pp. 521-529
    • Al-Qahtani, A.1    Teilhet, M.2    Mensa-Wilmot, K.3
  • 67
    • 0037088686 scopus 로고    scopus 로고
    • Extracellular release of the glycosylphosphatidylinositol (GPI)-linked Leishmania surface metalloprotease, Gp63, is independent of GPI phospholipolysis: Implications for parasite virulence
    • McGwire B.S., O'Connell W.A., Chang K.P., Engman D.M. Extracellular release of the glycosylphosphatidylinositol (GPI)-linked Leishmania surface metalloprotease, Gp63, is independent of GPI phospholipolysis: implications for parasite virulence. J. Biol. Chem. 277:2002;8802-8809.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8802-8809
    • McGwire, B.S.1    O'Connell, W.A.2    Chang, K.P.3    Engman, D.M.4
  • 68
    • 0037008696 scopus 로고    scopus 로고
    • Processing and trafficking of Leishmania mexicana GP63: Analysis using GPI8 mutants deficient in glycosylphosphatidyl inositol protein anchoring
    • Ellis M., Sharma D.K., Hilley J.D., Coombs G.H., Mottram J.C. Processing and trafficking of Leishmania mexicana GP63: analysis using GPI8 mutants deficient in glycosylphosphatidyl inositol protein anchoring. J. Biol. Chem. 277:2002;27968-27974.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27968-27974
    • Ellis, M.1    Sharma, D.K.2    Hilley, J.D.3    Coombs, G.H.4    Mottram, J.C.5
  • 69
    • 0034496239 scopus 로고    scopus 로고
    • Distribution of GPI-anchored proteins in the protozoan parasite Leishmania, based on an improved ultrastructural description using high-pressure frozen cells
    • Weise F., Stierhof Y.D., Kuhn C., Wiese M., Overath P. Distribution of GPI-anchored proteins in the protozoan parasite Leishmania, based on an improved ultrastructural description using high-pressure frozen cells. J. Cell. Sci. 113(Pt 24):2000;4587-4603.
    • (2000) J. Cell. Sci. , vol.113 , Issue.24 PART , pp. 4587-4603
    • Weise, F.1    Stierhof, Y.D.2    Kuhn, C.3    Wiese, M.4    Overath, P.5
  • 70
    • 0037090631 scopus 로고    scopus 로고
    • Intracellular trafficking of glycosylphosphatidylinositol (GPI)-anchored proteins and free GPIs in Leishmania mexicana
    • Ralton J.E., Mullin K.A., McConville M.J. Intracellular trafficking of glycosylphosphatidylinositol (GPI)-anchored proteins and free GPIs in Leishmania mexicana. Biochem. J. 363:2002;365-375.
    • (2002) Biochem. J. , vol.363 , pp. 365-375
    • Ralton, J.E.1    Mullin, K.A.2    McConville, M.J.3
  • 71
    • 0035936850 scopus 로고    scopus 로고
    • GPI-anchored proteins and glycoconjugates segregate into lipid rafts in Kinetoplastida
    • Denny P.W., Field M.C., Smith D.F. GPI-anchored proteins and glycoconjugates segregate into lipid rafts in Kinetoplastida. FEBS Lett. 491:2001;148-153.
    • (2001) FEBS Lett. , vol.491 , pp. 148-153
    • Denny, P.W.1    Field, M.C.2    Smith, D.F.3
  • 72
    • 0033525077 scopus 로고    scopus 로고
    • Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated
    • Melkonian K.A., Ostermeyer A.G., Chen J.Z., Roth M.G., Brown D.A. Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated. J. Biol. Chem. 274:1999;3910-3917.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3910-3917
    • Melkonian, K.A.1    Ostermeyer, A.G.2    Chen, J.Z.3    Roth, M.G.4    Brown, D.A.5
  • 73
    • 0031229420 scopus 로고    scopus 로고
    • Robert Feulgen Lecture1997. Lipid microdomains and membrane trafficking in mammalian cells
    • Verkade P., Simons K. Robert Feulgen Lecture1997. Lipid microdomains and membrane trafficking in mammalian cells. Histochem. Cell. Biol. 108:1997;211-220.
    • (1997) Histochem. Cell. Biol. , vol.108 , pp. 211-220
    • Verkade, P.1    Simons, K.2
  • 75
    • 0025027149 scopus 로고
    • Peptide substrate specificity of the membrane-bound metalloprotease of Leishmania
    • Bouvier J., Schneider P., Etges R., Bordier C. Peptide substrate specificity of the membrane-bound metalloprotease of Leishmania. Biochemistry. 29:1990;10113-10119.
    • (1990) Biochemistry , vol.29 , pp. 10113-10119
    • Bouvier, J.1    Schneider, P.2    Etges, R.3    Bordier, C.4
  • 76
    • 0022606362 scopus 로고
    • Expression and size heterogeneity of a 63 kilodalton membrane glycoprotein during growth and transformation of Leishmania mexicana amazonensis
    • Chang C.S., Inserra T.J., Kink J.A., Fong D., Chang K.P. Expression and size heterogeneity of a 63 kilodalton membrane glycoprotein during growth and transformation of Leishmania mexicana amazonensis. Mol. Biochem. Parasitol. 18:1986;197-210.
    • (1986) Mol. Biochem. Parasitol. , vol.18 , pp. 197-210
    • Chang, C.S.1    Inserra, T.J.2    Kink, J.A.3    Fong, D.4    Chang, K.P.5
  • 77
    • 0024439986 scopus 로고
    • The promastigote surface protease (gp63) of Leishmania is expressed but differentially processed and localized in the amastigote stage
    • Medina-Acosta E., Karess R.E., Schwartz H., Russell D.G. The promastigote surface protease (gp63) of Leishmania is expressed but differentially processed and localized in the amastigote stage. Mol. Biochem. Parasitol. 37:1989;263-273.
    • (1989) Mol. Biochem. Parasitol. , vol.37 , pp. 263-273
    • Medina-Acosta, E.1    Karess, R.E.2    Schwartz, H.3    Russell, D.G.4
  • 78
    • 0026918044 scopus 로고
    • Leishmania major: Differential regulation of the surface metalloprotease in amastigote and promastigote stages
    • Schneider P., Rosat J.P., Bouvier J., Louis J., Bordier C. Leishmania major: differential regulation of the surface metalloprotease in amastigote and promastigote stages. Exp. Parasitol. 75:1992;196-206.
    • (1992) Exp. Parasitol. , vol.75 , pp. 196-206
    • Schneider, P.1    Rosat, J.P.2    Bouvier, J.3    Louis, J.4    Bordier, C.5
  • 79
    • 0026109543 scopus 로고
    • The comparative fine structure and surface glycoconjugate expression of three life stages of Leishmania major
    • Pimenta P.F., Saraiva E.M., Sacks D.L. The comparative fine structure and surface glycoconjugate expression of three life stages of Leishmania major. Exp. Parasitol. 72:1991;191-204.
    • (1991) Exp. Parasitol. , vol.72 , pp. 191-204
    • Pimenta, P.F.1    Saraiva, E.M.2    Sacks, D.L.3
  • 80
    • 0025055580 scopus 로고
    • The major surface glycoprotein (GP63) is present in both life stages of Leishmania
    • Frommel T.O., Button L.L., Fujikura Y., McMaster W.R. The major surface glycoprotein (GP63) is present in both life stages of Leishmania. Mol. Biochem. Parasitol. 38:1990;25-32.
    • (1990) Mol. Biochem. Parasitol. , vol.38 , pp. 25-32
    • Frommel, T.O.1    Button, L.L.2    Fujikura, Y.3    McMaster, W.R.4
  • 81
    • 0027279941 scopus 로고
    • The lysosomal gp63-related protein in Leishmania mexicana amastigotes is a soluble metalloproteinase with an acidic pH optimum
    • Ilg T., Harbecke D., Overath P. The lysosomal gp63-related protein in Leishmania mexicana amastigotes is a soluble metalloproteinase with an acidic pH optimum. FEBS Lett. 327:1993;103-107.
    • (1993) FEBS Lett. , vol.327 , pp. 103-107
    • Ilg, T.1    Harbecke, D.2    Overath, P.3
  • 82
    • 0027761911 scopus 로고
    • Characterisation of two soluble metalloexopeptidases in the protozoan parasite Leishmania major
    • Schneider P., Glaser T.A. Characterisation of two soluble metalloexopeptidases in the protozoan parasite Leishmania major. Mol. Biochem. Parasitol. 62:1993;223-231.
    • (1993) Mol. Biochem. Parasitol. , vol.62 , pp. 223-231
    • Schneider, P.1    Glaser, T.A.2
  • 83
    • 0025318914 scopus 로고
    • Leishmania mexicana mexicana gp63 is a site-specific neutral endopeptidase
    • Ip H.S., Orn A., Russell D.G., Cross G.A. Leishmania mexicana mexicana gp63 is a site-specific neutral endopeptidase. Mol. Biochem. Parasitol. 40:1990;163-172.
    • (1990) Mol. Biochem. Parasitol. , vol.40 , pp. 163-172
    • Ip, H.S.1    Orn, A.2    Russell, D.G.3    Cross, G.A.4
  • 84
    • 0023637628 scopus 로고
    • Acid protease activity of a major surface membrane glycoprotein (gp63) from Leishmania mexicana promastigotes
    • Chaudhuri G., Chang K.P. Acid protease activity of a major surface membrane glycoprotein (gp63) from Leishmania mexicana promastigotes. Mol. Biochem. Parasitol. 27:1988;43-52.
    • (1988) Mol. Biochem. Parasitol. , vol.27 , pp. 43-52
    • Chaudhuri, G.1    Chang, K.P.2
  • 85
    • 0142008057 scopus 로고
    • The promastigote surface protease of Leishmania: pH optimum and effects of protease inhibitors
    • Hart DT, editor. New York: Plenum Publishing Cooperation
    • Etges R, Bouvier J, Bordier C. The promastigote surface protease of Leishmania: pH optimum and effects of protease inhibitors. In: Hart DT, editor. Leishmaniasis. New York: Plenum Publishing Cooperation; 1989. p. 627-33.
    • (1989) Leishmaniasis , pp. 627-633
    • Etges, R.1    Bouvier, J.2    Bordier, C.3
  • 86
    • 0025810812 scopus 로고
    • Substrate-dependent pH optima of gp63 purified from seven strains of Leishmania
    • Tzinia A.K., Soteriadou K.P. Substrate-dependent pH optima of gp63 purified from seven strains of Leishmania. Mol. Biochem. Parasitol. 47:1991;83-89.
    • (1991) Mol. Biochem. Parasitol. , vol.47 , pp. 83-89
    • Tzinia, A.K.1    Soteriadou, K.P.2
  • 87
    • 0023146963 scopus 로고
    • The macrophage-attachment glycoprotein gp63 is the predominant C3-acceptor site on Leishmania mexicana promastigotes
    • Russell D.G. The macrophage-attachment glycoprotein gp63 is the predominant C3-acceptor site on Leishmania mexicana promastigotes. Eur. J. Biochem. 164:1987;213-221.
    • (1987) Eur. J. Biochem. , vol.164 , pp. 213-221
    • Russell, D.G.1
  • 88
    • 0029046678 scopus 로고
    • Role of the Leishmania surface protease gp63 in complement fixation, cell adhesion, and resistance to complement-mediated lysis
    • Brittingham A., Morrison C.J., McMaster W.R.et al. Role of the Leishmania surface protease gp63 in complement fixation, cell adhesion, and resistance to complement-mediated lysis. J. Immunol. 155:1995;3102-3111.
    • (1995) J. Immunol. , vol.155 , pp. 3102-3111
    • Brittingham, A.1    Morrison, C.J.2    McMaster, W.R.3
  • 89
    • 0022652645 scopus 로고
    • The involvement of the major surface glycoprotein (gp63) of Leishmania promastigotes in attachment to macrophages
    • Russell D.G., Wilhelm H. The involvement of the major surface glycoprotein (gp63) of Leishmania promastigotes in attachment to macrophages. J. Immunol. 136:1986;2613-2620.
    • (1986) J. Immunol. , vol.136 , pp. 2613-2620
    • Russell, D.G.1    Wilhelm, H.2
  • 90
    • 0023752833 scopus 로고
    • The major concanavalin A-binding surface glycoprotein of Leishmania donovani chagasi promastigotes is involved in attachment to human macrophages
    • Wilson M.E., Hardin K.K. The major concanavalin A-binding surface glycoprotein of Leishmania donovani chagasi promastigotes is involved in attachment to human macrophages. J. Immunol. 141:1988;265-272.
    • (1988) J. Immunol. , vol.141 , pp. 265-272
    • Wilson, M.E.1    Hardin, K.K.2
  • 91
    • 0022571570 scopus 로고
    • Monoclonal antibody affinity purification of a Leishmania membrane glycoprotein and its inhibition of leishmania-macrophage binding
    • Chang C.S., Chang K.P. Monoclonal antibody affinity purification of a Leishmania membrane glycoprotein and its inhibition of leishmania-macrophage binding. Proc. Natl. Acad. Sci. USA. 83:1986;100-104.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 100-104
    • Chang, C.S.1    Chang, K.P.2
  • 92
    • 0022413168 scopus 로고
    • The mouse macrophage receptor for C3bi (CR3) is a major mechanism in the phagocytosis of Leishmania promastigotes
    • Mosser D.M., Edelson P.J. The mouse macrophage receptor for C3bi (CR3) is a major mechanism in the phagocytosis of Leishmania promastigotes. J. Immunol. 135:1985;2785-2789.
    • (1985) J. Immunol. , vol.135 , pp. 2785-2789
    • Mosser, D.M.1    Edelson, P.J.2
  • 93
    • 0025371936 scopus 로고
    • The major Leishmania donovani chagasi surface glycoprotein in tunicamycin-resistant promastigotes
    • Wilson M.E., Hardin K.K. The major Leishmania donovani chagasi surface glycoprotein in tunicamycin-resistant promastigotes. J. Immunol. 144:1990;4825-4834.
    • (1990) J. Immunol. , vol.144 , pp. 4825-4834
    • Wilson, M.E.1    Hardin, K.K.2
  • 94
    • 0023118494 scopus 로고
    • Increased infectivity of stationary-phase promastigotes of Leishmania donovani: Correlation with enhanced C3 binding capacity and CR3-mediated attachment to host macrophages
    • Wozencraft A.O., Blackwell J.M. Increased infectivity of stationary-phase promastigotes of Leishmania donovani: correlation with enhanced C3 binding capacity and CR3-mediated attachment to host macrophages. Immunology. 60:1987;559-563.
    • (1987) Immunology , vol.60 , pp. 559-563
    • Wozencraft, A.O.1    Blackwell, J.M.2
  • 95
    • 0024340791 scopus 로고
    • CR1, the C3b receptor, mediates binding of infective Leishmania major metacyclic promastigotes to human macrophages
    • Da Silva R.P., Hall B.F., Joiner K.A., Sacks D.L. CR1, the C3b receptor, mediates binding of infective Leishmania major metacyclic promastigotes to human macrophages. J. Immunol. 143:1989;617-622.
    • (1989) J. Immunol. , vol.143 , pp. 617-622
    • Da Silva, R.P.1    Hall, B.F.2    Joiner, K.A.3    Sacks, D.L.4
  • 96
    • 0026628358 scopus 로고
    • The Ser-Arg-Tyr-Asp region of the major surface glycoprotein of Leishmania mimics the Arg-Gly-Asp-Ser cell attachment region of fibronectin
    • Soteriadou K.P., Remoundos M.S., Katsikas M.C.et al. The Ser-Arg-Tyr-Asp region of the major surface glycoprotein of Leishmania mimics the Arg-Gly-Asp-Ser cell attachment region of fibronectin. J. Biol. Chem. 267:1992;13980-13985.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13980-13985
    • Soteriadou, K.P.1    Remoundos, M.S.2    Katsikas, M.C.3
  • 97
    • 0033966027 scopus 로고    scopus 로고
    • Episomal expression of specific sense and antisense mRNAs in Leishmania amazonensis: Modulation of gp63 level in promastigotes and their infection of macrophages in vitro
    • Chen D.Q., Kolli B.K., Yadava N.et al. Episomal expression of specific sense and antisense mRNAs in Leishmania amazonensis: modulation of gp63 level in promastigotes and their infection of macrophages in vitro. Infect Immun. 68:2000;80-86.
    • (2000) Infect Immun. , vol.68 , pp. 80-86
    • Chen, D.Q.1    Kolli, B.K.2    Yadava, N.3
  • 98
    • 0029851699 scopus 로고    scopus 로고
    • Surface Zn-proteinase as a molecule for defense of Leishmania mexicana amazonensis promastigotes against cytolysis inside macrophage phagolysosomes
    • Seay M.B., Heard P.L., Chaudhuri G. Surface Zn-proteinase as a molecule for defense of Leishmania mexicana amazonensis promastigotes against cytolysis inside macrophage phagolysosomes. Infect Immun. 64:1996;5129-5137.
    • (1996) Infect Immun. , vol.64 , pp. 5129-5137
    • Seay, M.B.1    Heard, P.L.2    Chaudhuri, G.3
  • 99
    • 0034875876 scopus 로고    scopus 로고
    • Phenotypic changes associated with deletion and overexpression of a stage-regulated gene family in Leishmania
    • McKean P.G., Denny P.W., Knuepfer E., Keen J.K., Smith D.F. Phenotypic changes associated with deletion and overexpression of a stage-regulated gene family in Leishmania. Cell Microbiol. 3:2001;511-523.
    • (2001) Cell Microbiol. , vol.3 , pp. 511-523
    • McKean, P.G.1    Denny, P.W.2    Knuepfer, E.3    Keen, J.K.4    Smith, D.F.5
  • 100
    • 0025649097 scopus 로고
    • Serum resistance of metacyclic stage Leishmania major promastigotes is due to release of C5b-9
    • Puentes S.M., Da Silva R.P., Sacks D.L., Hammer C.H., Joiner K.A. Serum resistance of metacyclic stage Leishmania major promastigotes is due to release of C5b-9. J. Immunol. 145:1990;4311-4316.
    • (1990) J. Immunol. , vol.145 , pp. 4311-4316
    • Puentes, S.M.1    Da Silva, R.P.2    Sacks, D.L.3    Hammer, C.H.4    Joiner, K.A.5
  • 101
    • 0023898688 scopus 로고
    • Complement binding by two developmental stages of Leishmania major promastigotes varying in expression of a surface lipophosphoglycan
    • Puentes S.M., Sacks D.L., da Silva R.P., Joiner K.A. Complement binding by two developmental stages of Leishmania major promastigotes varying in expression of a surface lipophosphoglycan. J. Exp. Med. 167:1988;887-902.
    • (1988) J. Exp. Med. , vol.167 , pp. 887-902
    • Puentes, S.M.1    Sacks, D.L.2    Da Silva, R.P.3    Joiner, K.A.4
  • 102
    • 0034044991 scopus 로고    scopus 로고
    • Leishmania mexicana mutants lacking glycosylphosphatidylinositol (GPI): Protein transamidase provide insights into the biosynthesis and functions of GPI-anchored proteins
    • Hilley J.D., Zawadzki J.L., McConville M.J., Coombs G.H., Mottram J.C. Leishmania mexicana mutants lacking glycosylphosphatidylinositol (GPI): protein transamidase provide insights into the biosynthesis and functions of GPI-anchored proteins. Mol. Biol. Cell. 11:2000;1183-1195.
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 1183-1195
    • Hilley, J.D.1    Zawadzki, J.L.2    McConville, M.J.3    Coombs, G.H.4    Mottram, J.C.5
  • 103
    • 0028204129 scopus 로고
    • The major surface glycoprotein (gp63) from Leishmania major and Leishmania donovani cleaves CD4 molecules on human T cells
    • Hey A.S., Theander T.G., Hviid L.et al. The major surface glycoprotein (gp63) from Leishmania major and Leishmania donovani cleaves CD4 molecules on human T cells. J. Immunol. 152:1994;4542-4548.
    • (1994) J. Immunol. , vol.152 , pp. 4542-4548
    • Hey, A.S.1    Theander, T.G.2    Hviid, L.3
  • 104
    • 0031869589 scopus 로고    scopus 로고
    • In vitro Leishmania major promastigote-induced macrophage migration is modulated by sensory and autonomic neuropeptides
    • Ahmed A.A., Wahbi A., Nordlind K.et al. In vitro Leishmania major promastigote-induced macrophage migration is modulated by sensory and autonomic neuropeptides. Scand. J. Immunol. 48:1998;79-85.
    • (1998) Scand. J. Immunol. , vol.48 , pp. 79-85
    • Ahmed, A.A.1    Wahbi, A.2    Nordlind, K.3
  • 105
    • 0030905133 scopus 로고    scopus 로고
    • Epitope cleavage by Leishmania endopeptidase(s) limits the efficiency of the exogenous pathway of major histocompatibility complex class I-associated antigen presentation
    • Garcia M.R., Graham S., Harris R.A., Beverley S.M., Kaye P.M. Epitope cleavage by Leishmania endopeptidase(s) limits the efficiency of the exogenous pathway of major histocompatibility complex class I-associated antigen presentation. Eur. J. Immunol. 27:1997;1005-1013.
    • (1997) Eur. J. Immunol. , vol.27 , pp. 1005-1013
    • Garcia, M.R.1    Graham, S.2    Harris, R.A.3    Beverley, S.M.4    Kaye, P.M.5
  • 106
    • 0033520431 scopus 로고    scopus 로고
    • MARCKS-related protein (MRP) is a substrate for the Leishmania major surface protease leishmanolysin (gp63)
    • Corradin S., Ransijn A., Corradin G.et al. MARCKS-related protein (MRP) is a substrate for the Leishmania major surface protease leishmanolysin (gp63). J. Biol. Chem. 274:1999;25411-25418.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25411-25418
    • Corradin, S.1    Ransijn, A.2    Corradin, G.3
  • 107
    • 0033546336 scopus 로고    scopus 로고
    • Down-regulation of MARCKS-related protein (MRP) in macrophages infected with Leishmania
    • Corradin S., Mauel J., Ransijn A., Sturzinger C., Vergeres G. Down-regulation of MARCKS-related protein (MRP) in macrophages infected with Leishmania. J. Biol. Chem. 274:1999;16782-16787.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16782-16787
    • Corradin, S.1    Mauel, J.2    Ransijn, A.3    Sturzinger, C.4    Vergeres, G.5
  • 108
    • 0031793544 scopus 로고    scopus 로고
    • The biogenesis and properties of the parasitophorous vacuoles that harbour Leishmania in murine macrophages
    • Antoine J.C., Prina E., Lang T., Courret N. The biogenesis and properties of the parasitophorous vacuoles that harbour Leishmania in murine macrophages. Trends Microbiol. 6:1998;392-401.
    • (1998) Trends Microbiol. , vol.6 , pp. 392-401
    • Antoine, J.C.1    Prina, E.2    Lang, T.3    Courret, N.4
  • 109
    • 0031662362 scopus 로고    scopus 로고
    • Coiling phagocytosis of trypanosomatids and fungal cells
    • Rittig M.G., Schroppel K., Seack K.H.et al. Coiling phagocytosis of trypanosomatids and fungal cells. Infect Immun. 66:1998;4331-4339.
    • (1998) Infect Immun. , vol.66 , pp. 4331-4339
    • Rittig, M.G.1    Schroppel, K.2    Seack, K.H.3
  • 110
    • 0037305054 scopus 로고    scopus 로고
    • Migration through the extracellular matrix by the parasitic protozoan Leishmania is enhanced by surface metalloprotease gp63
    • McGwire B.S., Chang K.P., Engman D.M. Migration through the extracellular matrix by the parasitic protozoan Leishmania is enhanced by surface metalloprotease gp63. Infect Immun. 71:2003;1008-1010.
    • (2003) Infect Immun. , vol.71 , pp. 1008-1010
    • McGwire, B.S.1    Chang, K.P.2    Engman, D.M.3
  • 111
    • 0026516594 scopus 로고
    • Identification of a surface metalloproteinase on 13 species of Leishmania isolated from humans, Crithidia fasciculata, and Herpetomonas samuelpessoai
    • Etges R. Identification of a surface metalloproteinase on 13 species of Leishmania isolated from humans, Crithidia fasciculata, and Herpetomonas samuelpessoai. Acta Trop. 50:1992;205-217.
    • (1992) Acta Trop. , vol.50 , pp. 205-217
    • Etges, R.1
  • 112
    • 0043092063 scopus 로고    scopus 로고
    • Surface coat remodeling during differentiation of trypanosoma brucei
    • Gruszynski A.E., DeMaster A., Hooper N.M., Bangs J.D. Surface coat remodeling during differentiation of trypanosoma brucei. J. Biol. Chem. 278:2003;24665-24672.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24665-24672
    • Gruszynski, A.E.1    DeMaster, A.2    Hooper, N.M.3    Bangs, J.D.4
  • 113
    • 0030841734 scopus 로고    scopus 로고
    • Loss of virulence in Leishmania donovani deficient in an amastigote-specific protein, A2
    • Zhang W.W., Matlashewski G. Loss of virulence in Leishmania donovani deficient in an amastigote-specific protein, A2. Proc. Natl. Acad. Sci. USA. 94:1997;8807-8811.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8807-8811
    • Zhang, W.W.1    Matlashewski, G.2
  • 114
    • 0034655625 scopus 로고    scopus 로고
    • Analysis of antisense and double stranded RNA downregulation of A2 protein expression in Leishmania donovani
    • Zhang W.W., Matlashewski G. Analysis of antisense and double stranded RNA downregulation of A2 protein expression in Leishmania donovani. Mol. Biochem. Parasitol. 107:2000;315-319.
    • (2000) Mol. Biochem. Parasitol. , vol.107 , pp. 315-319
    • Zhang, W.W.1    Matlashewski, G.2
  • 115
    • 0037067762 scopus 로고    scopus 로고
    • Functional analysis of cathepsin B-like cysteine proteases from Leishmania donovani complex. Evidence for the activation of latent transforming growth factor beta
    • Somanna A., Mundodi V., Gedamu L. Functional analysis of cathepsin B-like cysteine proteases from Leishmania donovani complex. Evidence for the activation of latent transforming growth factor beta. J. Biol. Chem. 277:2002;25305-25312.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25305-25312
    • Somanna, A.1    Mundodi, V.2    Gedamu, L.3
  • 116
    • 0037884861 scopus 로고    scopus 로고
    • Improvements in transfection efficiency and tests of RNA interference (RNAi) approaches in the protozoan parasite Leishmania
    • Robinson K.A., Beverley S.M. Improvements in transfection efficiency and tests of RNA interference (RNAi) approaches in the protozoan parasite Leishmania. Mol. Biochem. Parasitol. 128:2003;217-228.
    • (2003) Mol. Biochem. Parasitol. , vol.128 , pp. 217-228
    • Robinson, K.A.1    Beverley, S.M.2
  • 117
    • 0033768371 scopus 로고    scopus 로고
    • Double-stranded RNA interference in Trypanosoma brucei using head-to-head promoters
    • LaCount D.J., Bruse S., Hill K.L., Donelson J.E. Double-stranded RNA interference in Trypanosoma brucei using head-to-head promoters. Mol. Biochem. Parasitol. 111:2000;67-76.
    • (2000) Mol. Biochem. Parasitol. , vol.111 , pp. 67-76
    • LaCount, D.J.1    Bruse, S.2    Hill, K.L.3    Donelson, J.E.4
  • 118
    • 0032410928 scopus 로고    scopus 로고
    • Double-stranded RNA induces mRNA degradation in Trypanosoma brucei
    • Ngo H., Tschudi C., Gull K., Ullu E. Double-stranded RNA induces mRNA degradation in Trypanosoma brucei. Proc. Natl. Acad. Sci. USA. 95:1998;14687-14692.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14687-14692
    • Ngo, H.1    Tschudi, C.2    Gull, K.3    Ullu, E.4
  • 119
    • 0037226127 scopus 로고    scopus 로고
    • Protozomics: Trypanosomatid parasite genetics comes of age
    • Beverley S.M. Protozomics: trypanosomatid parasite genetics comes of age. Nat Rev. Genet. 4:2003;11-19.
    • (2003) Nat Rev. Genet. , vol.4 , pp. 11-19
    • Beverley, S.M.1
  • 120
    • 0035946347 scopus 로고    scopus 로고
    • In vitro cytocidal effects on Trypanosoma brucei and inhibition of Leishmania major GP63 by peptidomimetic metalloprotease inhibitors
    • Bangs J.D., Ransom D.A., Nimick M., Christie G., Hooper N.M. In vitro cytocidal effects on Trypanosoma brucei and inhibition of Leishmania major GP63 by peptidomimetic metalloprotease inhibitors. Mol. Biochem. Parasitol. 114:2001;111-117.
    • (2001) Mol. Biochem. Parasitol. , vol.114 , pp. 111-117
    • Bangs, J.D.1    Ransom, D.A.2    Nimick, M.3    Christie, G.4    Hooper, N.M.5
  • 121
    • 0036847052 scopus 로고    scopus 로고
    • Novel peptide inhibitors of Leishmania gp63 based on the cleavage site of MARCKS (myristoylated alanine-rich C kinase substrate)-related protein
    • Corradin S., Ransijn A., Corradin G.et al. Novel peptide inhibitors of Leishmania gp63 based on the cleavage site of MARCKS (myristoylated alanine-rich C kinase substrate)-related protein. Biochem. J. 367:2002;761-769.
    • (2002) Biochem. J. , vol.367 , pp. 761-769
    • Corradin, S.1    Ransijn, A.2    Corradin, G.3
  • 122
    • 0031007891 scopus 로고    scopus 로고
    • Mapping of the antigenic determinants of the Leishmania infantum gp63 protein recognized by antibodies elicited during canine visceral leishmaniasis
    • Morales G., Carrillo G., Requena J.M.et al. Mapping of the antigenic determinants of the Leishmania infantum gp63 protein recognized by antibodies elicited during canine visceral leishmaniasis. Parasitology. 114:1997;507-516.
    • (1997) Parasitology , vol.114 , pp. 507-516
    • Morales, G.1    Carrillo, G.2    Requena, J.M.3
  • 123
    • 0342813029 scopus 로고    scopus 로고
    • Cloning of the gp63 surface protease of Leishmania infantum. Differential post-translational modifications correlated with different infective forms
    • Gonzalez-Aseguinolaza G., Almazan F., Rodriguez J.F., Marquet A., Larraga V. Cloning of the gp63 surface protease of Leishmania infantum. Differential post-translational modifications correlated with different infective forms. Biochim. Biophys. Acta. 1361:1997;92-102.
    • (1997) Biochim. Biophys. Acta , vol.1361 , pp. 92-102
    • Gonzalez-Aseguinolaza, G.1    Almazan, F.2    Rodriguez, J.F.3    Marquet, A.4    Larraga, V.5
  • 124
    • 0033192656 scopus 로고    scopus 로고
    • Leishmania panamensis: A 44bp deletion in gp63 gene is found in cDNA and genomic libraries
    • Hoya R., Trujillo C., Cardenas C.et al. Leishmania panamensis: a 44bp deletion in gp63 gene is found in cDNA and genomic libraries. Mem. Inst. Oswaldo Cruz. 94:1999;641-643.
    • (1999) Mem. Inst. Oswaldo Cruz. , vol.94 , pp. 641-643
    • Hoya, R.1    Trujillo, C.2    Cardenas, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.