메뉴 건너뛰기




Volumn 103, Issue 2, 1999, Pages 183-195

PfSUB-2: A second subtilisin-like protein in Plasmodium falciparum merozoites

Author keywords

Malaria; Merozoite; Post translational processing; Protease; Subtilisin

Indexed keywords

INTEGRIN; PROTEIN PFSUB 2; PROTEINASE; SUBTILISIN; UNCLASSIFIED DRUG;

EID: 0032887161     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(99)00122-X     Document Type: Article
Times cited : (62)

References (36)
  • 1
    • 0020568103 scopus 로고
    • Plasmodium knowlesi: Studies on invasion of rhesus erythrocytes by merozoites in the presence of protease inhibitors
    • Hadley T., Aikawa M., Miller L.H. Plasmodium knowlesi: studies on invasion of rhesus erythrocytes by merozoites in the presence of protease inhibitors. Exp. Parasitol. 55:1983;306-311.
    • (1983) Exp. Parasitol. , vol.55 , pp. 306-311
    • Hadley, T.1    Aikawa, M.2    Miller, L.H.3
  • 2
    • 0019869482 scopus 로고
    • Involvement of malarial proteases in the interaction between the parasite and the host erythrocyte in Plasmodium knowlesi infections
    • Banyal H.S., Misra G.C., Gupta C.M., Dutta G.P. Involvement of malarial proteases in the interaction between the parasite and the host erythrocyte in Plasmodium knowlesi infections. J. Parasitol. 67:1981;623-626.
    • (1981) J. Parasitol. , vol.67 , pp. 623-626
    • Banyal, H.S.1    Misra, G.C.2    Gupta, C.M.3    Dutta, G.P.4
  • 3
    • 0019430775 scopus 로고
    • In vitro susceptibility of erythrocytes of Presbytis entellus (Indian Langur) to Plasmodium knowlesi and blocking of merozoite invasion process by certain protease inhibitors
    • Dutta G.P., Banyal H.S. In vitro susceptibility of erythrocytes of Presbytis entellus (Indian Langur) to Plasmodium knowlesi and blocking of merozoite invasion process by certain protease inhibitors. Indian J. Exp. Biol. 19:1981;9-11.
    • (1981) Indian J. Exp. Biol. , vol.19 , pp. 9-11
    • Dutta, G.P.1    Banyal, H.S.2
  • 4
    • 0020603367 scopus 로고
    • Requirement of malarial protease in the invasion of human red cells by merozoites of Plasmodium falciparum
    • Dejkriengkraikhul P., Wilairat P. Requirement of malarial protease in the invasion of human red cells by merozoites of Plasmodium falciparum. Z. Parasitenkd. 69:1983;313-317.
    • (1983) Z. Parasitenkd. , vol.69 , pp. 313-317
    • Dejkriengkraikhul, P.1    Wilairat, P.2
  • 5
    • 0023029999 scopus 로고
    • Plasmodium falciparum: Protease inhibitors and inhibition of erythrocyte invasion
    • Dluzewski A.R., Rangachari K., Wilson R.J.M. Plasmodium falciparum: protease inhibitors and inhibition of erythrocyte invasion. Exp. Parasitol. 62:1986;416-422.
    • (1986) Exp. Parasitol. , vol.62 , pp. 416-422
    • Dluzewski, A.R.1    Rangachari, K.2    Wilson, R.J.M.3
  • 6
    • 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., Pereira da Silva L. 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    Pereira Da Silva, L.3
  • 7
    • 0025903879 scopus 로고
    • Effect of calpain inhibitors on the invasion of human erythrocytes by the parasite Plasmodium falciparum
    • Olaya C., Wasserman M. Effect of calpain inhibitors on the invasion of human erythrocytes by the parasite Plasmodium falciparum. Biochim. Biophys. Acta. 1096:1991;217-221.
    • (1991) Biochim. Biophys. Acta , vol.1096 , pp. 217-221
    • Olaya, C.1    Wasserman, M.2
  • 9
    • 0027771176 scopus 로고
    • Proteolytic digestion of band 3 at an external site alters the erythrocyte membrane organisation and may facilitate malarial invasion
    • McPherson R.A., Donald D.R., Sawyer W.H., Tilley L. Proteolytic digestion of band 3 at an external site alters the erythrocyte membrane organisation and may facilitate malarial invasion. Mol. Biochem. Parasitol. 62:1993;233-242.
    • (1993) Mol. Biochem. Parasitol. , vol.62 , pp. 233-242
    • McPherson, R.A.1    Donald, D.R.2    Sawyer, W.H.3    Tilley, L.4
  • 10
    • 0030581703 scopus 로고    scopus 로고
    • A role for erythrocyte band 3 degradation by the parasite gp76 serine protease in the formation of the parasitophorous vacuole during invasion of erythrocytes by Plasmodium falciparum
    • Roggwiller E., Bétoulle M.E., Blisnick T., Braun-Breton C. A role for erythrocyte band 3 degradation by the parasite gp76 serine protease in the formation of the parasitophorous vacuole during invasion of erythrocytes by Plasmodium falciparum. Mol. Biochem. Parasitol. 82:1996;13-24.
    • (1996) Mol. Biochem. Parasitol. , vol.82 , pp. 13-24
    • Roggwiller, E.1    Bétoulle, M.E.2    Blisnick, T.3    Braun-Breton, C.4
  • 11
    • 0028145547 scopus 로고
    • Differential localization of full-length and processed forms of PF83/AMA-1 an apical membrane antigen of Plasmodium falciparum merozoites
    • Narum D.L., Thomas A.W. Differential localization of full-length and processed forms of PF83/AMA-1 an apical membrane antigen of Plasmodium falciparum merozoites. Mol. Biochem. Parasitol. 67:1994;59-68.
    • (1994) Mol. Biochem. Parasitol. , vol.67 , pp. 59-68
    • Narum, D.L.1    Thomas, A.W.2
  • 12
    • 0032053739 scopus 로고    scopus 로고
    • Analysis of the processing of Plasmodium falciparum rhoptry-associated protein 1 and localization of Pr86 to schizont rhoptries and p67 to free merozoites
    • Howard R.F., Narum D.L., Blackman M.J., Thurman J. Analysis of the processing of Plasmodium falciparum rhoptry-associated protein 1 and localization of Pr86 to schizont rhoptries and p67 to free merozoites. Mol. Biochem. Parasitol. 92:1998;111-122.
    • (1998) Mol. Biochem. Parasitol. , vol.92 , pp. 111-122
    • Howard, R.F.1    Narum, D.L.2    Blackman, M.J.3    Thurman, J.4
  • 14
    • 0024198184 scopus 로고
    • Activation of a Plasmodium falciparum protease correlated with merozoite maturation and erythrocyte invasion
    • Braun-Breton C., Pereira da Silva L. Activation of a Plasmodium falciparum protease correlated with merozoite maturation and erythrocyte invasion. Biol. Cell. 64:1988;223-231.
    • (1988) Biol. Cell , vol.64 , pp. 223-231
    • Braun-Breton, C.1    Pereira Da Silva, L.2
  • 15
    • 0024315151 scopus 로고
    • Purification and identification of a neutral endopeptidase in Plasmodium falciparum schizonts and merozoites
    • Grellier P., Picard I., Bernard F., Mayer R., Heidrich H.-G., Monsigny M., Schrevel J. Purification and identification of a neutral endopeptidase in Plasmodium falciparum schizonts and merozoites. Parasitol. Res. 75:1989;455-460.
    • (1989) Parasitol. Res. , vol.75 , pp. 455-460
    • Grellier, P.1    Picard, I.2    Bernard, F.3    Mayer, R.4    Heidrich, H.-G.5    Monsigny, M.6    Schrevel, J.7
  • 16
    • 0023597795 scopus 로고
    • Identification of three stage-specific proteinases of Plasmodium falciparum
    • Rosenthal P.J., Kim K., McKerrow J.H., Leech J.H. Identification of three stage-specific proteinases of Plasmodium falciparum. J. Exp. Med. 166:1987;816-821.
    • (1987) J. Exp. Med. , vol.166 , pp. 816-821
    • Rosenthal, P.J.1    Kim, K.2    McKerrow, J.H.3    Leech, J.H.4
  • 17
    • 0027451943 scopus 로고
    • A conserved parasite serine protease processes the Plasmodium falciparum merozoite surface protein-1
    • Blackman M.J., Chappel J.A., Shai S., Holder A.A. A conserved parasite serine protease processes the Plasmodium falciparum merozoite surface protein-1. Mol. Biochem. Parasitol. 62:1993;103-114.
    • (1993) Mol. Biochem. Parasitol. , vol.62 , pp. 103-114
    • Blackman, M.J.1    Chappel, J.A.2    Shai, S.3    Holder, A.A.4
  • 18
    • 17144445308 scopus 로고
    • Plasmodium falciparum proteinases: Cloning of the putative gene coding for the merozoite proteinase for erythrocyte invasion (MPEI) and determination of hydrolysis sites of spectrin by Pf37 proteinase
    • Florent I., Le Bonniec S., Carcy B. et al. Plasmodium falciparum proteinases: cloning of the putative gene coding for the merozoite proteinase for erythrocyte invasion (MPEI) and determination of hydrolysis sites of spectrin by Pf37 proteinase. Mem. Inst. Oswaldo Cruz. 89 Suppl. 2:1994;47-49.
    • (1994) Mem. Inst. Oswaldo Cruz. , vol.892 , pp. 47-49
    • Florent, I.1    Le Bonniec, S.2    Carcy, B.3
  • 19
    • 0032483369 scopus 로고    scopus 로고
    • A subtilisin-like protein in secretory organelles of Plasmodium falciparum merozoites
    • Blackman M.J., Fujioka H., Stafford W.H. et al. A subtilisin-like protein in secretory organelles of Plasmodium falciparum merozoites. J. Biol. Chem. 273:1998;23398-23409.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23398-23409
    • Blackman, M.J.1    Fujioka, H.2    Stafford, W.H.3
  • 20
    • 0025310377 scopus 로고
    • A single fragment of a malaria merozoite surface protein remains on the parasite during red cell invasion and is the target of invasion-inhibiting antibodies
    • Blackman M.J., Heidrich H.-G., Donachie S., McBride J.S., Holder A.A. A single fragment of a malaria merozoite surface protein remains on the parasite during red cell invasion and is the target of invasion-inhibiting antibodies. J. Exp. Med. 172:1990;379-382.
    • (1990) J. Exp. Med. , vol.172 , pp. 379-382
    • Blackman, M.J.1    Heidrich, H.-G.2    Donachie, S.3    McBride, J.S.4    Holder, A.A.5
  • 21
    • 0028709387 scopus 로고
    • Purification of Plasmodium falciparum merozoites for analysis of the processing of merozoite surface protein-1
    • Blackman M.J. Purification of Plasmodium falciparum merozoites for analysis of the processing of merozoite surface protein-1. Methods Cell. Biol. 45:1994;213-220.
    • (1994) Methods Cell. Biol. , vol.45 , pp. 213-220
    • Blackman, M.J.1
  • 24
    • 0027212498 scopus 로고
    • Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins
    • Frangioni J.V., Neel B.G. Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins. Anal. Biochem. 210:1993;179-187.
    • (1993) Anal. Biochem. , vol.210 , pp. 179-187
    • Frangioni, J.V.1    Neel, B.G.2
  • 25
    • 0025750756 scopus 로고
    • An efficient method to purify active eukaryotic proteins from the inclusion bodies in Escherichia coli
    • Lin K.H., Cheng S.Y. An efficient method to purify active eukaryotic proteins from the inclusion bodies in Escherichia coli. Biotechniques. 11:1991;748, 750, 752-753.
    • (1991) Biotechniques , vol.11 , pp. 748
    • Lin, K.H.1    Cheng, S.Y.2
  • 26
    • 0003448569 scopus 로고
    • Cold Spring Harbor: Cold Spring Harbour Laboratory Press
    • Harlow E., Lane D. Antibodies. A Laboratory Manual. 1988;1988 Cold Spring Harbour Laboratory Press, Cold Spring Harbor.
    • (1988) Antibodies. a Laboratory Manual , pp. 1988
    • Harlow, E.1    Lane, D.2
  • 27
    • 0026010023 scopus 로고
    • Processing of the Plasmodium falciparum merozoite surface protein-1: Identification of a 33-kilodalton secondary processing product which is shed prior to erythrocyte invasion
    • Blackman M.J., Whittle H., Holder A.A. Processing of the Plasmodium falciparum merozoite surface protein-1: identification of a 33-kilodalton secondary processing product which is shed prior to erythrocyte invasion. Mol. Biochem. Parasitol. 49:1991;35-44.
    • (1991) Mol. Biochem. Parasitol. , vol.49 , pp. 35-44
    • Blackman, M.J.1    Whittle, H.2    Holder, A.A.3
  • 28
    • 0028102510 scopus 로고
    • Analysis of expressed sequence tags from Plasmodium falciparum
    • Chakrabarti D., Reddy G.R., Dame J.B. et al. Analysis of expressed sequence tags from Plasmodium falciparum. Mol. Biochem. Parasitol. 66:1994;97-104.
    • (1994) Mol. Biochem. Parasitol. , vol.66 , pp. 97-104
    • Chakrabarti, D.1    Reddy, G.R.2    Dame, J.B.3
  • 29
    • 0030896832 scopus 로고    scopus 로고
    • Subtilases: The superfamily of subtilisin-like serine proteases
    • Siezen R.J., Leunissen J.A. Subtilases: the superfamily of subtilisin-like serine proteases. Protein Sci. 6:1997;501-523.
    • (1997) Protein Sci. , vol.6 , pp. 501-523
    • Siezen, R.J.1    Leunissen, J.A.2
  • 30
    • 0028277501 scopus 로고
    • Homology modelling of the catalytic domain of human furin. A model for the eukaryotic subtilisin-like proprotein convertases
    • Siezen R.J., Creemers J.W., Van de Ven W.J. Homology modelling of the catalytic domain of human furin. A model for the eukaryotic subtilisin-like proprotein convertases. Eur. J. Biochem. 222:1994;255-266.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 255-266
    • Siezen, R.J.1    Creemers, J.W.2    Van De Ven, W.J.3
  • 31
    • 0002529802 scopus 로고
    • Homology analysis of the propeptides of subtilisin-like serine proteases (subtilases)
    • U. Shinde, & M. Inouye. Austin, TX, USA: RG Landes
    • Siezen R.J., Leunisse J.A.M., Shinde U. Homology analysis of the propeptides of subtilisin-like serine proteases (subtilases). Shinde U., Inouye M. Intramolecular Chaperones and Protein Folding. 1995;233-256 RG Landes, Austin, TX, USA.
    • (1995) Intramolecular Chaperones and Protein Folding , pp. 233-256
    • Siezen, R.J.1    Leunisse, J.A.M.2    Shinde, U.3
  • 32
    • 0028067179 scopus 로고
    • Autoprocessing of prothiolsubtilisin E in which active-site serine 221 is altered to cysteine
    • Li Y., Inouye M. Autoprocessing of prothiolsubtilisin E in which active-site serine 221 is altered to cysteine. J. Biol. Chem. 269:1994;4169-4174.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4169-4174
    • Li, Y.1    Inouye, M.2
  • 33
    • 0030580110 scopus 로고    scopus 로고
    • Evidence for intramolecular processing of prosubtilisin sequestered on a solid support
    • Volkov A., Jordan F. Evidence for intramolecular processing of prosubtilisin sequestered on a solid support. J. Mol. Biol. 262:1996;595-599.
    • (1996) J. Mol. Biol. , vol.262 , pp. 595-599
    • Volkov, A.1    Jordan, F.2
  • 34
    • 0031001304 scopus 로고    scopus 로고
    • Activation of the furin endoprotease is a multiple-step process: Requirements for acidification and internal propeptide cleavage
    • Anderson E.D., VanSlyke J.K., Thulin C.D., Jean F., Thomas G. Activation of the furin endoprotease is a multiple-step process: requirements for acidification and internal propeptide cleavage. EMBO J. 16:1997;1508-1518.
    • (1997) EMBO J. , vol.16 , pp. 1508-1518
    • Anderson, E.D.1    Vanslyke, J.K.2    Thulin, C.D.3    Jean, F.4    Thomas, G.5
  • 35
    • 0002716411 scopus 로고
    • Propeptide mediated protein folding: Intramolecular chaperones
    • U. Shinde, & M. Inouye. Austin, TX, USA: RG Landes
    • Shinde U., Li Y., Inouye M. Propeptide mediated protein folding: intramolecular chaperones. Shinde U., Inouye M. Intramolecular Chaperones and Protein Folding. 1995;1-31 RG Landes, Austin, TX, USA.
    • (1995) Intramolecular Chaperones and Protein Folding , pp. 1-31
    • Shinde, U.1    Li, Y.2    Inouye, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.