메뉴 건너뛰기




Volumn 579, Issue 7, 2005, Pages 1573-1578

Identification of EhICP1, a chagasin-like cysteine protease inhibitor of Entamoeba histolytica

Author keywords

Amoebiasin; Chagasin; Cystatin; Cysteine protease inhibitor; Entamoeba histolytica

Indexed keywords

AMOEBAPAIN; AMOEBIASIN 1; CHAGASIN; CYSTEINE PROTEASE INHIBITOR; CYSTEINE PROTEINASE; ENZYME INHIBITOR; GLYCYLASPARAGINYLPROLYLTHREONYLTHREONYLGLYCYLPHENYLALANINE; PAPAIN; PEPTIDE; PROTEIN; PROTOZOAL PROTEIN; UNCLASSIFIED DRUG;

EID: 14844288892     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.01.067     Document Type: Article
Times cited : (45)

References (29)
  • 1
    • 0000602914 scopus 로고    scopus 로고
    • WHO/Pan America Health Organisation Expert Consultation on Amoebiasis
    • WHO/Pan America Health Organisation Expert Consultation on Amoebiasis (1997) WHO Weekly Epidemiol. Records 72, 97-100
    • (1997) WHO Weekly Epidemiol. Records , vol.72 , pp. 97-100
  • 4
    • 0028673207 scopus 로고
    • Cysteine endopeptidases of Entamoeba histolytica
    • H. Scholze, and E. Tannich Cysteine endopeptidases of Entamoeba histolytica Methods Enzymol. 244 1994 512 523
    • (1994) Methods Enzymol. , vol.244 , pp. 512-523
    • Scholze, H.1    Tannich, E.2
  • 5
    • 0034041714 scopus 로고    scopus 로고
    • Cysteine proteinases and the pathogenesis of amebiasis
    • X. Que, and S.L. Reed Cysteine proteinases and the pathogenesis of amebiasis Clin. Microbiol. Rev. 13 2000 196 206
    • (2000) Clin. Microbiol. Rev. , vol.13 , pp. 196-206
    • Que, X.1    Reed, S.L.2
  • 6
    • 0038482128 scopus 로고    scopus 로고
    • The intestinal protozoan parasite Entamoeba histolytica contains 20 cysteine protease genes, of which only a small subset is expressed during in vitro cultivation
    • I. Bruchhaus, B.J. Loftus, N. Hall, and E. Tannich The intestinal protozoan parasite Entamoeba histolytica contains 20 cysteine protease genes, of which only a small subset is expressed during in vitro cultivation Eukaryot. Cell 2 2003 501 509
    • (2003) Eukaryot. Cell , vol.2 , pp. 501-509
    • Bruchhaus, I.1    Loftus, B.J.2    Hall, N.3    Tannich, E.4
  • 7
    • 0030918546 scopus 로고    scopus 로고
    • Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors
    • B. Turk, V. Turk, and D. Turk Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors Biol. Chem. 378 1997 141 150
    • (1997) Biol. Chem. , vol.378 , pp. 141-150
    • Turk, B.1    Turk, V.2    Turk, D.3
  • 8
    • 0024066065 scopus 로고
    • The 2.0 a X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases
    • W. Bode, R. Engh, D. Musil, U. Thiele, R. Huber, A. Karshikov, J. Brzin, J. Kos, and V. Turk The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases EMBO J. 7 1988 2593 2599
    • (1988) EMBO J. , vol.7 , pp. 2593-2599
    • Bode, W.1    Engh, R.2    Musil, D.3    Thiele, U.4    Huber, R.5    Karshikov, A.6    Brzin, J.7    Kos, J.8    Turk, V.9
  • 9
    • 0030067774 scopus 로고    scopus 로고
    • A novel cysteine protease inhibitor of the egg of chum salmon, containing a cysteine-rich thyroglobulin-like motif
    • M. Yamashita, and S. Konagaya A novel cysteine protease inhibitor of the egg of chum salmon, containing a cysteine-rich thyroglobulin-like motif J. Biol. Chem. 271 1996 1282 1284
    • (1996) J. Biol. Chem. , vol.271 , pp. 1282-1284
    • Yamashita, M.1    Konagaya, S.2
  • 10
  • 11
    • 0035189728 scopus 로고    scopus 로고
    • Identification, characterization and localization of chagasin, a tight-binding cysteine protease inhibitor in Trypanosoma cruzi
    • A.C. Monteiro, M. Abrahamson, A.P. Lima, M.A. Vannier-Santos, and J. Scharfstein Identification, characterization and localization of chagasin, a tight-binding cysteine protease inhibitor in Trypanosoma cruzi J. Cell Sci. 114 2001 3933 3942
    • (2001) J. Cell Sci. , vol.114 , pp. 3933-3942
    • Monteiro, A.C.1    Abrahamson, M.2    Lima, A.P.3    Vannier-Santos, M.A.4    Scharfstein, J.5
  • 12
    • 0036076146 scopus 로고    scopus 로고
    • Sequence conservation in the chagasin family suggests a common trend in cysteine proteinase binding by unrelated protein inhibitors
    • D.J. Rigden, V.V. Mosolov, and M.Y. Galperin Sequence conservation in the chagasin family suggests a common trend in cysteine proteinase binding by unrelated protein inhibitors Protein Sci. 11 2002 1971 1977
    • (2002) Protein Sci. , vol.11 , pp. 1971-1977
    • Rigden, D.J.1    Mosolov, V.V.2    Galperin, M.Y.3
  • 13
    • 0038025678 scopus 로고    scopus 로고
    • Functional conservation of a natural cysteine peptidase inhibitor in protozoan and bacterial pathogens
    • S.J. Sanderson, G.D. Westrop, J. Scharfstein, J.C. Mottram, and G.H. Coombs Functional conservation of a natural cysteine peptidase inhibitor in protozoan and bacterial pathogens FEBS Lett. 542 2003 12 16
    • (2003) FEBS Lett. , vol.542 , pp. 12-16
    • Sanderson, S.J.1    Westrop, G.D.2    Scharfstein, J.3    Mottram, J.C.4    Coombs, G.H.5
  • 14
    • 0017846267 scopus 로고
    • A new medium for the axenic cultivation of Entamoeba histolytica and other Entamoeba
    • L.S Diamond, D.R. Harlow, and C.C. Cunnick A new medium for the axenic cultivation of Entamoeba histolytica and other Entamoeba Trans. R. Soc. Trop. Med. Hyg. 72 1978 431 432
    • (1978) Trans. R. Soc. Trop. Med. Hyg. , vol.72 , pp. 431-432
    • Diamond, L.S.1    Harlow, D.R.2    Cunnick, C.C.3
  • 16
    • 0027995077 scopus 로고
    • PJC20 and pJC40 - Two high-copy-number vectors for T7 RNA polymerase-dependent expression of recombinant genes in Escherichia coli
    • J. Clos, and S. Brandau pJC20 and pJC40 - two high-copy-number vectors for T7 RNA polymerase-dependent expression of recombinant genes in Escherichia coli Protein Expr. Purif. 5 1994 133 137
    • (1994) Protein Expr. Purif. , vol.5 , pp. 133-137
    • Clos, J.1    Brandau, S.2
  • 17
    • 0031962434 scopus 로고    scopus 로고
    • Isolation and molecular characterization of a surface-bound proteinase of Entamoeba histolytica
    • T. Jacobs, I. Bruchhaus, T. Dandekar, E. Tannich, and M. Leippe Isolation and molecular characterization of a surface-bound proteinase of Entamoeba histolytica Mol. Microbiol. 27 1998 269 276
    • (1998) Mol. Microbiol. , vol.27 , pp. 269-276
    • Jacobs, T.1    Bruchhaus, I.2    Dandekar, T.3    Tannich, E.4    Leippe, M.5
  • 19
    • 0015327378 scopus 로고
    • A linear equation that describes the steady-state kinetics of enzymes and subcellular particles interacting with tightly bound inhibitors
    • P.J. Henderson A linear equation that describes the steady-state kinetics of enzymes and subcellular particles interacting with tightly bound inhibitors Biochem. J. 127 1972 321 333
    • (1972) Biochem. J. , vol.127 , pp. 321-333
    • Henderson, P.J.1
  • 20
    • 0018370095 scopus 로고
    • Analysis of products of mitochondrial protein synthesis in yeast: Genetic and biochemical aspects
    • M. Douglas, D. Finkelstein, and R.A. Butow Analysis of products of mitochondrial protein synthesis in yeast: genetic and biochemical aspects Methods Enzymol. 56 1979 58 66
    • (1979) Methods Enzymol. , vol.56 , pp. 58-66
    • Douglas, M.1    Finkelstein, D.2    Butow, R.A.3
  • 21
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • P. Matsudaira 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.1
  • 22
    • 0024759464 scopus 로고
    • Action of the major protease from Entamoeba histolytica on proteins of the extracellular matrix
    • W. Schulte, and H. Scholze Action of the major protease from Entamoeba histolytica on proteins of the extracellular matrix J. Protozool. 36 1989 538 543
    • (1989) J. Protozool. , vol.36 , pp. 538-543
    • Schulte, W.1    Scholze, H.2
  • 24
    • 9644257515 scopus 로고    scopus 로고
    • A potential role for ICP, a Leishmanial inhibitor of cysteine peptidases, in the interaction between host and parasite
    • S Besteiro, G.H. Coombs, and J.C. Mottram A potential role for ICP, a Leishmanial inhibitor of cysteine peptidases, in the interaction between host and parasite Mol. Microbiol. 54 2004 1224 1236
    • (2004) Mol. Microbiol. , vol.54 , pp. 1224-1236
    • Besteiro, S.1    Coombs, G.H.2    Mottram, J.C.3
  • 25
    • 0025301658 scopus 로고
    • The refined 2.4 a X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: A novel type of proteinase inhibitor interaction
    • M.T. Stubbs, B. Laber, W. Bode, R. Huber, R. Jerala, B. Lenarcic, and V. Turk The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction EMBO J. 9 1990 1939 1947
    • (1990) EMBO J. , vol.9 , pp. 1939-1947
    • Stubbs, M.T.1    Laber, B.2    Bode, W.3    Huber, R.4    Jerala, R.5    Lenarcic, B.6    Turk, V.7
  • 26
    • 0022356775 scopus 로고
    • Primary structures of the mRNAs encoding the rat precursors for bradykinin and T-kinin. Structural relationship of kininogens with major acute phase protein and alpha 1-cysteine proteinase inhibitor
    • S. Furuto-Kato, A. Matsumoto, N. Kitamura, and S. Nakanishi Primary structures of the mRNAs encoding the rat precursors for bradykinin and T-kinin. Structural relationship of kininogens with major acute phase protein and alpha 1-cysteine proteinase inhibitor J. Biol. Chem. 260 1985 12054 12059
    • (1985) J. Biol. Chem. , vol.260 , pp. 12054-12059
    • Furuto-Kato, S.1    Matsumoto, A.2    Kitamura, N.3    Nakanishi, S.4
  • 27
    • 0035943517 scopus 로고    scopus 로고
    • The protease inhibitor chagasin of Trypanosoma cruzi adopts an immunoglobulin-type fold and may have arisen by horizontal gene transfer
    • D.J. Rigden, A.C. Monteiro, and M.F. Grossi de Sa The protease inhibitor chagasin of Trypanosoma cruzi adopts an immunoglobulin-type fold and may have arisen by horizontal gene transfer FEBS Lett. 504 2001 41 44
    • (2001) FEBS Lett. , vol.504 , pp. 41-44
    • Rigden, D.J.1    Monteiro, A.C.2    Grossi De Sa, M.F.3
  • 28
    • 0028902211 scopus 로고
    • Role of the Entamoeba histolytica cysteine proteinase in amebic liver abscess formation in severe combined immunodeficient mice
    • S.L. Stanley Jr., T. Zhang, D. Rubin, and E. Li Role of the Entamoeba histolytica cysteine proteinase in amebic liver abscess formation in severe combined immunodeficient mice Infect. Immun. 63 1995 1587 1590
    • (1995) Infect. Immun. , vol.63 , pp. 1587-1590
    • Stanley Jr., S.L.1    Zhang, T.2    Rubin, D.3    Li, E.4
  • 29
    • 1542495414 scopus 로고    scopus 로고
    • Papain-like lysosomal cysteine proteases and their inhibitors: Drug discovery targets?
    • D. Turk, B. Turk, and V. Turk Papain-like lysosomal cysteine proteases and their inhibitors: drug discovery targets? Biochem. Soc. Symp. 70 2003 15 30
    • (2003) Biochem. Soc. Symp. , vol.70 , pp. 15-30
    • Turk, D.1    Turk, B.2    Turk, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.