메뉴 건너뛰기




Volumn 309, Issue 4, 2003, Pages 974-979

Stage-specific profiling of Plasmodium falciparum proteases using an internally quenched multispecificity protease substrate

Author keywords

Fluorescence resonance energy transfer; Fluorescent protease substrate; Malarial proteases; Mass spectrometry; Plasmodium falciparum; Hairpin peptide

Indexed keywords

4 (4 DIMETHYLAMINOPHENYLAZO)BENZOIC ACID; 5 (2 AMINOETHYLAMINO)NAPHTHALENE 1 SULFONIC ACID; BENZOIC ACID DERIVATIVE; PROTEINASE; SULFONIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0141453245     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.08.108     Document Type: Article
Times cited : (9)

References (41)
  • 1
    • 0035997361 scopus 로고    scopus 로고
    • Biological roles of proteases in parasitic protozoa
    • Klemba M., 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
  • 3
    • 0033004991 scopus 로고    scopus 로고
    • An overview of chemotherapeutic targets for antimalarial drug discovery
    • Olliaro P.L., Yuthavong Y. An overview of chemotherapeutic targets for antimalarial drug discovery. Pharmacol. Ther. 81:1999;91-110.
    • (1999) Pharmacol. Ther. , vol.81 , pp. 91-110
    • Olliaro, P.L.1    Yuthavong, Y.2
  • 5
    • 0034232515 scopus 로고    scopus 로고
    • Proteases involved in erythrocyte invasion by the malaria parasite: Function and potential as chemotherapeutic target
    • Blackman M.J. Proteases involved in erythrocyte invasion by the malaria parasite: function and potential as chemotherapeutic target. Curr. Drug Targets. 1:2000;59-83.
    • (2000) Curr. Drug Targets , vol.1 , pp. 59-83
    • Blackman, M.J.1
  • 7
    • 0026911104 scopus 로고
    • Plasmodial hemoglobin degradation: An ordered pathway in a specialized organelle
    • Goldberg D.E. Plasmodial hemoglobin degradation: an ordered pathway in a specialized organelle. Infect. Agents Dis. 1:1992;207-211.
    • (1992) Infect. Agents Dis. , vol.1 , pp. 207-211
    • Goldberg, D.E.1
  • 8
    • 0030200511 scopus 로고    scopus 로고
    • Kinetic analysis of plasmepsins I and II, aspartic proteases of the Plasmodium falciparum digestive vacuole
    • Luker K.E., Francis S.E., Gluzman I.Y., Goldberg D.E. Kinetic analysis of plasmepsins I and II, aspartic proteases of the Plasmodium falciparum digestive vacuole. Mol. Biochem. Parasitol. 79:1996;71-78.
    • (1996) Mol. Biochem. Parasitol. , vol.79 , pp. 71-78
    • Luker, K.E.1    Francis, S.E.2    Gluzman, I.Y.3    Goldberg, D.E.4
  • 10
    • 0037181136 scopus 로고    scopus 로고
    • Activity and inhibition of plasmepsin IV, a new aspartic proteinase from the malaria parasite, Plasmodium falciparum
    • Wayatt D.M., Berry C. Activity and inhibition of plasmepsin IV, a new aspartic proteinase from the malaria parasite, Plasmodium falciparum. FEBS Lett. 513:2002;159-162.
    • (2002) FEBS Lett. , vol.513 , pp. 159-162
    • Wayatt, D.M.1    Berry, C.2
  • 11
    • 0037154180 scopus 로고    scopus 로고
    • Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine
    • Banerjee R., Liu J., Beatty W., Pelosof L., Klemba M., Goldberg D.E. Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine. Proc. Natl. Acad. Sci. USA. 99:2002;990-995.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 990-995
    • Banerjee, R.1    Liu, J.2    Beatty, W.3    Pelosof, L.4    Klemba, M.5    Goldberg, D.E.6
  • 12
    • 0029057887 scopus 로고
    • Functional expression of falcipain, a Plasmodium falciparum cysteine proteinase, supports its role as a malarial hemoglobinase
    • Salas F., Fichmann J., Lee G.K., Scott M.D., Rosenthal P.J. Functional expression of falcipain, a Plasmodium falciparum cysteine proteinase, supports its role as a malarial hemoglobinase. Infect. Immun. 63:1995;2120-2125.
    • (1995) Infect. Immun. , vol.63 , pp. 2120-2125
    • Salas, F.1    Fichmann, J.2    Lee, G.K.3    Scott, M.D.4    Rosenthal, P.J.5
  • 13
    • 0034666133 scopus 로고    scopus 로고
    • Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum
    • Shenai B.R., Sijwali P.S., Singh A., Rosenthal P.J. Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum. J. Biol. Chem. 275:2000;29000-29010.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29000-29010
    • Shenai, B.R.1    Sijwali, P.S.2    Singh, A.3    Rosenthal, P.J.4
  • 14
    • 0035644195 scopus 로고    scopus 로고
    • Expression and characterization of the Plasmodium falciparum haemoglobinase falcipain-3
    • Sijwali P.S., Shenai B.R., Gut J., Singh A.J., Rosenthal P.J. Expression and characterization of the Plasmodium falciparum haemoglobinase falcipain-3. Biochem. J. 360:2001;481-489.
    • (2001) Biochem. J. , vol.360 , pp. 481-489
    • Sijwali, P.S.1    Shenai, B.R.2    Gut, J.3    Singh, A.J.4    Rosenthal, P.J.5
  • 15
    • 0033527572 scopus 로고    scopus 로고
    • Identification and characterization of falcilysin, a metallopeptidase involved in hemoglobin catabolism within the malaria parasite Plasmodium falciparum
    • Eggleson K.K., Duffin K.L., Goldberg D.E. Identification and characterization of falcilysin, a metallopeptidase involved in hemoglobin catabolism within the malaria parasite Plasmodium falciparum. J. Biol. Chem. 274:1999;32411-32417.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32411-32417
    • Eggleson, K.K.1    Duffin, K.L.2    Goldberg, D.E.3
  • 16
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • Trager W., Jensen J.B. Human malaria parasites in continuous culture. Science. 193:1976;673-675.
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 19
    • 0017795758 scopus 로고
    • Fluorescence energy transfer as a spectroscopic ruler
    • Stryer L. Fluorescence energy transfer as a spectroscopic ruler. Annu. Rev. Biochem. 47:1978;819-846.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 819-846
    • Stryer, L.1
  • 20
    • 0017917406 scopus 로고
    • The use of singlet-singlet energy transfer to study macromolecular assemblies
    • Fairclough R.H., Cantor C.R. The use of singlet-singlet energy transfer to study macromolecular assemblies. Methods Enzymol. 48:1978;347-379.
    • (1978) Methods Enzymol. , vol.48 , pp. 347-379
    • Fairclough, R.H.1    Cantor, C.R.2
  • 22
    • 0025099455 scopus 로고
    • Novel fluorogenic substrates for assaying retroviral proteases by resonance energy transfer
    • Matayoshi E.D., Wang G.T., Krafft G.A., Erickson J. Novel fluorogenic substrates for assaying retroviral proteases by resonance energy transfer. Science. 247:1990;954-958.
    • (1990) Science , vol.247 , pp. 954-958
    • Matayoshi, E.D.1    Wang, G.T.2    Krafft, G.A.3    Erickson, J.4
  • 25
    • 0028121382 scopus 로고
    • Synthesis of a fluorogenic interleukin-1 beta converting enzyme substrate based on resonance energy transfer
    • Pennington M.W., Thornberry N.A. Synthesis of a fluorogenic interleukin-1 beta converting enzyme substrate based on resonance energy transfer. Pept. Res. 7:1994;72-76.
    • (1994) Pept. Res. , vol.7 , pp. 72-76
    • Pennington, M.W.1    Thornberry, N.A.2
  • 26
    • 0027174845 scopus 로고
    • A fluorescent peptide substrate for the surface metalloprotease of Leishmania
    • Bouvier J., Schneider P., Malcolm B. A fluorescent peptide substrate for the surface metalloprotease of Leishmania. Exp. Parasitol. 76:1993;146-155.
    • (1993) Exp. Parasitol. , vol.76 , pp. 146-155
    • Bouvier, J.1    Schneider, P.2    Malcolm, B.3
  • 28
    • 0026680191 scopus 로고
    • Application of a fluorogenic substrate in the assay of proteolytic activity and in the discovery of a potent inhibitor of Candida albicans aspartic proteinase
    • Capobianco J.O., Lerner C.G., Goldman R.C. Application of a fluorogenic substrate in the assay of proteolytic activity and in the discovery of a potent inhibitor of Candida albicans aspartic proteinase. Anal. Biochem. 204:1992;96-102.
    • (1992) Anal. Biochem. , vol.204 , pp. 96-102
    • Capobianco, J.O.1    Lerner, C.G.2    Goldman, R.C.3
  • 29
    • 0026503894 scopus 로고
    • New intramolecularly quenched fluorogenic peptide substrates for the study of the kinetic specificity of papain
    • Garcia-Echeverria C., Rich D.H. New intramolecularly quenched fluorogenic peptide substrates for the study of the kinetic specificity of papain. FEBS Lett. 297:1992;100-102.
    • (1992) FEBS Lett. , vol.297 , pp. 100-102
    • Garcia-Echeverria, C.1    Rich, D.H.2
  • 31
    • 0037472666 scopus 로고    scopus 로고
    • Proteolytic stability of beta-peptide bonds probed using quenched fluorescent substrates incorporating a hemoglobin cleavage site
    • Gopi H.N., Ravindra G., Pal P.P., Pattanaik P., Balaram H., Balaram P. Proteolytic stability of beta-peptide bonds probed using quenched fluorescent substrates incorporating a hemoglobin cleavage site. FEBS Lett. 535:2003;175-178.
    • (2003) FEBS Lett. , vol.535 , pp. 175-178
    • Gopi, H.N.1    Ravindra, G.2    Pal, P.P.3    Pattanaik, P.4    Balaram, H.5    Balaram, P.6
  • 32
    • 0035793051 scopus 로고    scopus 로고
    • Malaria parasite exit from the host erythrocyte: A two-step process requiring extraerythrocytic proteolysis
    • Salmon B.L., Oksman A., Goldberg D.E. Malaria parasite exit from the host erythrocyte: a two-step process requiring extraerythrocytic proteolysis. Proc. Natl. Acad. Sci. USA. 98:2001;271-276.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 271-276
    • Salmon, B.L.1    Oksman, A.2    Goldberg, D.E.3
  • 34
    • 0034614404 scopus 로고    scopus 로고
    • Maturation and specificity of Plasmodium falciparum subtilisin-like protease-1, a malaria merozoite subtilisin like serine protease
    • Sajid M., Withers-Martinez C., Blackman M.J. Maturation and specificity of Plasmodium falciparum subtilisin-like protease-1, a malaria merozoite subtilisin like serine protease. J. Biol. Chem. 275:2000;631-641.
    • (2000) J. Biol. Chem. , vol.275 , pp. 631-641
    • Sajid, M.1    Withers-Martinez, C.2    Blackman, M.J.3
  • 36
    • 0023840713 scopus 로고
    • Induction of the proteolytic activity of a membrane protein in Plasmodium falciparum by phosphatidyl inositol-specific phospholipase C
    • Braun-Breton C., Rosenberry T.L., da Silva L.P. Induction of the proteolytic activity of a membrane protein in Plasmodium falciparum by phosphatidyl inositol-specific phospholipase C. Nature. 332:1988;457-459.
    • (1988) Nature , vol.332 , pp. 457-459
    • Braun-Breton, C.1    Rosenberry, T.L.2    Da Silva, L.P.3
  • 37
    • 0025754304 scopus 로고
    • Hemoglobin degradation in the human malaria pathogen Plasmodium falciparum: A catabolic pathway initiated by a specific aspartic protease
    • Goldberg D.E., Slater A.F., Beavis R., Chait B., Cerami A., Henderson G.B. Hemoglobin degradation in the human malaria pathogen Plasmodium falciparum: a catabolic pathway initiated by a specific aspartic protease. J. Exp. Med. 173:1991;961-969.
    • (1991) J. Exp. Med. , vol.173 , pp. 961-969
    • Goldberg, D.E.1    Slater, A.F.2    Beavis, R.3    Chait, B.4    Cerami, A.5    Henderson, G.B.6
  • 38
    • 0035174389 scopus 로고    scopus 로고
    • PlasmoDB: An integrative database of the Plasmodium falciparum genome
    • PlasmoDB: An integrative database of the Plasmodium falciparum genome, Nucleic Acids Res. 29 (2001) 66-69.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 66-69
  • 39
    • 0035521154 scopus 로고    scopus 로고
    • Aspartic proteases of Plasmodium falciparum and other parasitic protozoa as drug targets
    • Coombs G.H., Goldberg D.E., Klemba M., Berry C., Kay J., Mottram J.C. Aspartic proteases of Plasmodium falciparum and other parasitic protozoa as drug targets. Trends Parasitol. 17:2001;532-537.
    • (2001) Trends Parasitol. , vol.17 , pp. 532-537
    • Coombs, G.H.1    Goldberg, D.E.2    Klemba, M.3    Berry, C.4    Kay, J.5    Mottram, J.C.6
  • 40
    • 0033553410 scopus 로고    scopus 로고
    • Plasmepsin II, an acidic hemoglobinase from the Plasmodium falciparum food vacuole, is active at neutral pH on the host erythrocyte membrane skeleton
    • Le Bonniec S., Deregnaucourt C., Redeker V., Banerjee R., Grellier P., Goldberg D.E., Schrevel J. Plasmepsin II, an acidic hemoglobinase from the Plasmodium falciparum food vacuole, is active at neutral pH on the host erythrocyte membrane skeleton. J. Biol. Chem. 14:1999;14218-14223.
    • (1999) J. Biol. Chem. , vol.14 , pp. 14218-14223
    • Le Bonniec, S.1    Deregnaucourt, C.2    Redeker, V.3    Banerjee, R.4    Grellier, P.5    Goldberg, D.E.6    Schrevel, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.