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Volumn 103, Issue 1, 1999, Pages 49-60

The Leishmania mexicana proteasome

Author keywords

Inhibition; Lactacystin; Leishmania; Proteasome; Purification

Indexed keywords

ADENOSINE TRIPHOSPHATE; LACTACYSTIN; PROTEASOME;

EID: 0032821504     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(99)00110-3     Document Type: Article
Times cited : (65)

References (56)
  • 1
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC Class I molecules
    • Rock K.L., Gramm C., Rothstein L., Clark K., Stein R., Dick L., Hwang D., Goldberg A.L. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC Class I molecules. Cell. 78:1994;761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 2
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux O., Tanaka K., Goldberg A.L. Structure and functions of the 20S and 26S proteasomes. Annu Rev Biochem. 65:1996;801-847.
    • (1996) Annu Rev Biochem , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 3
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the Archaeon Thermplasma acidophilum at 3.4 Å resolution
    • Lowe J., Stock D., Jap B., Zwickl P., Baumeister W., Hubert R. Crystal structure of the 20S proteasome from the Archaeon Thermplasma acidophilum at 3.4 Å resolution. Science. 268:1995;533-539.
    • (1995) Science , vol.268 , pp. 533-539
    • Lowe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Hubert, R.6
  • 4
    • 0024972956 scopus 로고
    • The multicatalytic proteinase (prosome) is ubiquitous from Eukaryotes to Archaebacteria
    • Dahlmann B., Kopp F., Kuehn L., Niedel B., Pfeifer G., Hegerl R., Baumeister W. The multicatalytic proteinase (prosome) is ubiquitous from Eukaryotes to Archaebacteria. FEBS Lett. 251:1989;125-131.
    • (1989) FEBS Lett , vol.251 , pp. 125-131
    • Dahlmann, B.1    Kopp, F.2    Kuehn, L.3    Niedel, B.4    Pfeifer, G.5    Hegerl, R.6    Baumeister, W.7
  • 6
    • 0026669739 scopus 로고
    • Identification, purification and characterisation of a protein activator (PA28) of the 20S proteasome (macropain)
    • Chu-Ping M., Slaughter C.A., DeMartino G.N. Identification, purification and characterisation of a protein activator (PA28) of the 20S proteasome (macropain). J Biol Chem. 267:1992;10515-10523.
    • (1992) J Biol Chem , vol.267 , pp. 10515-10523
    • Chu-Ping, M.1    Slaughter, C.A.2    Demartino, G.N.3
  • 7
    • 0026498493 scopus 로고
    • Purification of an 11S regulator of the multicatalytic protease
    • Dubiel W., Pratt G., Ferrell K., Rechsteiner M. Purification of an 11S regulator of the multicatalytic protease. J Biol Chem. 267:1992;22369-22377.
    • (1992) J Biol Chem , vol.267 , pp. 22369-22377
    • Dubiel, W.1    Pratt, G.2    Ferrell, K.3    Rechsteiner, M.4
  • 8
  • 9
    • 0028970626 scopus 로고
    • The interferon-γ-inducible 11S regulator (PA28) and the LMP2/LMP7 subunits govern the peptide production by the 20S proteasome in vitro
    • Groettrup M., Ruppert T., Kuehn L., Seeger M., Standera S., Koszinowski U., Kloetzel P.M. The interferon-γ-inducible 11S regulator (PA28) and the LMP2/LMP7 subunits govern the peptide production by the 20S proteasome in vitro. J Biol Chem. 270:1995;23808-23815.
    • (1995) J Biol Chem , vol.270 , pp. 23808-23815
    • Groettrup, M.1    Ruppert, T.2    Kuehn, L.3    Seeger, M.4    Standera, S.5    Koszinowski, U.6    Kloetzel, P.M.7
  • 10
    • 0031058531 scopus 로고    scopus 로고
    • Identification and characterisation of an activated 20S proteasome in Trypanosoma brucei
    • To W.-Y., Wang C.C. Identification and characterisation of an activated 20S proteasome in Trypanosoma brucei. FEBS Lett. 404:1997;253-262.
    • (1997) FEBS Lett , vol.404 , pp. 253-262
    • To, W.-Y.1    Wang, C.C.2
  • 11
    • 0028025326 scopus 로고
    • Identification, purification and characterisation of a high molecular weight, ATP-dependent activator (PA700) of the 20S proteasome
    • Chu-Ping M., Vu J.H., Proske R.J., Slaughter C.A., DeMartino G.N. Identification, purification and characterisation of a high molecular weight, ATP-dependent activator (PA700) of the 20S proteasome. J Biol Chem. 269:1994;3539-3547.
    • (1994) J Biol Chem , vol.269 , pp. 3539-3547
    • Chu-Ping, M.1    Vu, J.H.2    Proske, R.J.3    Slaughter, C.A.4    Demartino, G.N.5
  • 12
    • 0028234770 scopus 로고
    • Distinct 19S and 20S subcomplexes of the 26S proteasome and their distribution in the nucleus and the cytoplasm
    • Peters J.-M., Franke W.W., Kleinschmidt J.A. Distinct 19S and 20S subcomplexes of the 26S proteasome and their distribution in the nucleus and the cytoplasm. J Biol Chem. 269:1994;7709-7718.
    • (1994) J Biol Chem , vol.269 , pp. 7709-7718
    • Peters, J.-M.1    Franke, W.W.2    Kleinschmidt, J.A.3
  • 13
    • 0031973716 scopus 로고    scopus 로고
    • The AAA team: Related ATPases with related functions
    • Patel S., Latterich M. The AAA team: Related ATPases with related functions. Trends Cell Biol. 8:1998;65-71.
    • (1998) Trends Cell Biol , vol.8 , pp. 65-71
    • Patel, S.1    Latterich, M.2
  • 14
    • 0028235965 scopus 로고
    • A 26S proteasome subunit that binds ubiquitin conjugates
    • Devereaux Q., Ustrell V., Pickart C., Rechsteiner M. A 26S proteasome subunit that binds ubiquitin conjugates. J Biol Chem. 269:1994;7059-7061.
    • (1994) J Biol Chem , vol.269 , pp. 7059-7061
    • Devereaux, Q.1    Ustrell, V.2    Pickart, C.3    Rechsteiner, M.4
  • 15
    • 0030033982 scopus 로고    scopus 로고
    • Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome
    • Van Nocker S., Devereaux Q., Rechsteiner M., Vierstra R.D. Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome. Proc Natl Acad Sci USA. 93:1996;856-860.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 856-860
    • Van Nocker, S.1    Devereaux, Q.2    Rechsteiner, M.3    Vierstra, R.D.4
  • 16
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko A., Ciechanover A. The ubiquitin system for protein degradation. Annu Rev Biochem. 61:1992;761-807.
    • (1992) Annu Rev Biochem , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 17
    • 0027053491 scopus 로고
    • The ubiquitin-conjugation system
    • Jentsch S. The ubiquitin-conjugation system. Annu Rev Genet. 26:1992;179-207.
    • (1992) Annu Rev Genet , vol.26 , pp. 179-207
    • Jentsch, S.1
  • 18
    • 0029365999 scopus 로고
    • The only way out of mitosis
    • Glotzer M. The only way out of mitosis. Curr Biol. 5:1995;970-972.
    • (1995) Curr Biol , vol.5 , pp. 970-972
    • Glotzer, M.1
  • 19
    • 0028828193 scopus 로고
    • The self-destructive personality of a cell cycle in transition
    • Deshaies R.J. The self-destructive personality of a cell cycle in transition. Curr Opin Cell Biol. 7:1995;781-789.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 781-789
    • Deshaies, R.J.1
  • 20
    • 0032101245 scopus 로고    scopus 로고
    • Proteolytic ratchets that control progression through mitosis
    • Townsley F.M., Ruderman J.V. Proteolytic ratchets that control progression through mitosis. Trends Cell Biol. 8:1998;238-244.
    • (1998) Trends Cell Biol , vol.8 , pp. 238-244
    • Townsley, F.M.1    Ruderman, J.V.2
  • 21
    • 0000413462 scopus 로고    scopus 로고
    • Regulation of interferon-γ-activated STAT1 by the ubiquitin-proteasome pathway
    • Kim T.K., Maniatis T. Regulation of interferon-γ-activated STAT1 by the ubiquitin-proteasome pathway. Science. 273:1996;1717-1719.
    • (1996) Science , vol.273 , pp. 1717-1719
    • Kim, T.K.1    Maniatis, T.2
  • 22
    • 0028815630 scopus 로고
    • Catabolite inactivation of fructose-1,6-bisphosphatase of Saccharomyces cerevisiae
    • Schork S.M., Thumm M., Wolf D.H. Catabolite inactivation of fructose-1,6-bisphosphatase of Saccharomyces cerevisiae. J Biol Chem. 270:1995;26446-26450.
    • (1995) J Biol Chem , vol.270 , pp. 26446-26450
    • Schork, S.M.1    Thumm, M.2    Wolf, D.H.3
  • 23
    • 0030905981 scopus 로고    scopus 로고
    • New insights into the mechanisms and importance of the proteasome in intracellular protein degradation
    • Goldberg A.L., Akopian T.N., Kisselev A.F., Lee D.H., Rohrwild M. New insights into the mechanisms and importance of the proteasome in intracellular protein degradation. Biol Chem. 378:1997;131-140.
    • (1997) Biol Chem , vol.378 , pp. 131-140
    • Goldberg, A.L.1    Akopian, T.N.2    Kisselev, A.F.3    Lee, D.H.4    Rohrwild, M.5
  • 24
    • 0025632969 scopus 로고
    • Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins
    • Seufert W., Jentsch S. Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. EMBO J. 9:1990;4535-4541.
    • (1990) EMBO J , vol.9 , pp. 4535-4541
    • Seufert, W.1    Jentsch, S.2
  • 25
    • 0029838640 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller M.M., Finger A., Schweiger M., Wolf D.H. Endoplasmic reticulum degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science. 273:1996;1725-1728.
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 26
    • 0010485332 scopus 로고
    • Genome organisation and control of gene expression in Trypanosomatids
    • P.M.A. Broda, S.G. Oliver, & P.F.G. Sims. Cambridge: Cambridge University Press
    • Pays E. Genome organisation and control of gene expression in Trypanosomatids. Broda P.M.A., Oliver S.G., Sims P.F.G. The Eukaryotic genome - organisation and regulation. 1993;Cambridge University Press, Cambridge.
    • (1993) The Eukaryotic Genome - Organisation and Regulation
    • Pays, E.1
  • 27
    • 0030982143 scopus 로고    scopus 로고
    • Degradation of oxidised proteins in mammalian cells
    • Grune T., Reinheckel T., Davies K.J. Degradation of oxidised proteins in mammalian cells. FASEB J. 11:1997;526-534.
    • (1997) FASEB J , vol.11 , pp. 526-534
    • Grune, T.1    Reinheckel, T.2    Davies, K.J.3
  • 28
    • 0019833316 scopus 로고
    • Transformation in vitro of Leishmania mexicana amastigotes to promastigotes: Nutritional requirements and the effect of drugs
    • Hart D.T., Vickerman K., Coombs G.H. Transformation in vitro of Leishmania mexicana amastigotes to promastigotes: nutritional requirements and the effect of drugs. Parasitology. 83:1981;529-541.
    • (1981) Parasitology , vol.83 , pp. 529-541
    • Hart, D.T.1    Vickerman, K.2    Coombs, G.H.3
  • 29
    • 0027175178 scopus 로고
    • Leishmania mexicana: Induction of metacyclogenesis by cultivation of promastigotes at acidic pH
    • Bates P.A., Tetley L. Leishmania mexicana: induction of metacyclogenesis by cultivation of promastigotes at acidic pH. Exp Parasitol. 76:1993;412-423.
    • (1993) Exp Parasitol , vol.76 , pp. 412-423
    • Bates, P.A.1    Tetley, L.2
  • 30
    • 0026674542 scopus 로고
    • Axenic cultivation and characterisation of Leishmania mexicana amastigote-like forms
    • Bates P.A., Robertson C.D., Tetley L., Coombs G.H. Axenic cultivation and characterisation of Leishmania mexicana amastigote-like forms. Parasitology. 105:1992;193-202.
    • (1992) Parasitology , vol.105 , pp. 193-202
    • Bates, P.A.1    Robertson, C.D.2    Tetley, L.3    Coombs, G.H.4
  • 31
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany G., Standaert R.F., Lane W.S., Choi E.J., Corey E.J., Schreiber S.L. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science. 268:1995;726-731.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, E.J.4    Corey, E.J.5    Schreiber, S.L.6
  • 32
    • 0001847422 scopus 로고
    • Buffer systems and transfer parameters for semi-dry electroblotting with a horizontal apparatus
    • In: Dunn MJ, editor Weinheim, Germany: VCH
    • Bjerrum OJ, Schafer-Nielsen C. Buffer systems and transfer parameters for semi-dry electroblotting with a horizontal apparatus. In: Dunn MJ, editor. Electrophoresis '86. Weinheim, Germany: VCH, 1986.
    • (1986) Electrophoresis '86
    • Bjerrum, O.J.1    Schafer-Nielsen, C.2
  • 33
    • 0023655017 scopus 로고
    • Purification of two high molecular weight proteases from rabbit reticulocyte lysate
    • Hough R., Pratt G., Rechsteiner M. Purification of two high molecular weight proteases from rabbit reticulocyte lysate. J Biol Chem. 262:1987;8303-8313.
    • (1987) J Biol Chem , vol.262 , pp. 8303-8313
    • Hough, R.1    Pratt, G.2    Rechsteiner, M.3
  • 34
    • 0343431431 scopus 로고    scopus 로고
    • Purification and characterisation of proteasomes from Trypanosoma brucei
    • Hua S., To W.-Y., Nguyen T.T., Wong M.-L., Wang C.C. Purification and characterisation of proteasomes from Trypanosoma brucei. Mol Biochem Parasitol. 78:1996;33-46.
    • (1996) Mol Biochem Parasitol , vol.78 , pp. 33-46
    • Hua, S.1    To, W.-Y.2    Nguyen, T.T.3    Wong, M.-L.4    Wang, C.C.5
  • 35
    • 0030008041 scopus 로고    scopus 로고
    • Evidence for the existence of both proteasomes and a novel high molecular weight peptidase in Entamoeba histolytica
    • Scholze H., Frey S., Cejka Z., Bakker-Grunwald T. Evidence for the existence of both proteasomes and a novel high molecular weight peptidase in Entamoeba histolytica. J Biol Chem. 271:1996;6212-6216.
    • (1996) J Biol Chem , vol.271 , pp. 6212-6216
    • Scholze, H.1    Frey, S.2    Cejka, Z.3    Bakker-Grunwald, T.4
  • 36
    • 0025113919 scopus 로고
    • Characterisation of three groups of cysteine proteinases in the amastigotes of Leishmania mexicana mexicana
    • Robertson C.D., Coombs G.H. Characterisation of three groups of cysteine proteinases in the amastigotes of Leishmania mexicana mexicana. Mol Biochem Parasitol. 42:1990;269-276.
    • (1990) Mol Biochem Parasitol , vol.42 , pp. 269-276
    • Robertson, C.D.1    Coombs, G.H.2
  • 37
    • 0023664012 scopus 로고
    • Demonstration of two distinct high molecular weight proteases in rabbit reticulocytes, one of which degrades ubiquitin conjugates
    • Waxman L., Fagan J.M., Goldberg A.L. Demonstration of two distinct high molecular weight proteases in rabbit reticulocytes, one of which degrades ubiquitin conjugates. J Biol Chem. 262:1987;2451-2457.
    • (1987) J Biol Chem , vol.262 , pp. 2451-2457
    • Waxman, L.1    Fagan, J.M.2    Goldberg, A.L.3
  • 38
    • 0025016911 scopus 로고
    • Characterisation of an alkaline peptidase of Trypanosoma cruzi and other Trypanosomatids
    • Ashall F. Characterisation of an alkaline peptidase of Trypanosoma cruzi and other Trypanosomatids. Mol Biochem Parasitol. 38:1990;77-88.
    • (1990) Mol Biochem Parasitol , vol.38 , pp. 77-88
    • Ashall, F.1
  • 40
    • 0027454436 scopus 로고
    • The ubiquitin-ligase system in Trypanosoma brucei brucei
    • Lowrie D.J., Giffin B.F., Ventullo R.M. The ubiquitin-ligase system in Trypanosoma brucei brucei. Am J Trop Med Hyg. 49:1993;545-551.
    • (1993) Am J Trop Med Hyg , vol.49 , pp. 545-551
    • Lowrie, D.J.1    Giffin, B.F.2    Ventullo, R.M.3
  • 41
    • 0030581661 scopus 로고    scopus 로고
    • Characterisation of ubiquitin genes and transcripts and demonstration of a ubiquitin-conjugating system in Entamoeba histolytica
    • Wostmann C., Liakopoulos D., Ciechanover A., Bakker-Grunwald T. Characterisation of ubiquitin genes and transcripts and demonstration of a ubiquitin-conjugating system in Entamoeba histolytica. Mol Biochem Parasitol. 82:1996;81-90.
    • (1996) Mol Biochem Parasitol , vol.82 , pp. 81-90
    • Wostmann, C.1    Liakopoulos, D.2    Ciechanover, A.3    Bakker-Grunwald, T.4
  • 42
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: Valuable new tools for cell biologists
    • Lee D.H., Goldberg A.L. Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol. 8:1998;397-403.
    • (1998) Trends Cell Biol , vol.8 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.L.2
  • 44
    • 0025255957 scopus 로고
    • Developing selective inhibitors of calpains
    • Wang K.K.W. Developing selective inhibitors of calpains. Trends Pharmacol Sci. 11:1990;139-142.
    • (1990) Trends Pharmacol Sci , vol.11 , pp. 139-142
    • Wang, K.K.W.1
  • 45
    • 0028314784 scopus 로고
    • Null mutants for the lmcpa cysteine proteinase gene in Leishmania mexicana
    • Souza A.E., Bates P.A., Coombs G.H., Mottram J.C. Null mutants for the lmcpa cysteine proteinase gene in Leishmania mexicana. Mol Biochem Parasitol. 63:1994;213-220.
    • (1994) Mol Biochem Parasitol , vol.63 , pp. 213-220
    • Souza, A.E.1    Bates, P.A.2    Coombs, G.H.3    Mottram, J.C.4
  • 46
    • 0029898541 scopus 로고    scopus 로고
    • Evidence from disruption of the lmcpb gene array of Leishmania mexicana that cysteine proteinases are virulence factors
    • Mottram J.C., Souza A.E., Hutchison J.E., Carter R., Frame M.J., Coombs G.H. Evidence from disruption of the lmcpb gene array of Leishmania mexicana that cysteine proteinases are virulence factors. Proc Natl Acad Sci USA. 93:1996;6008-6013.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6008-6013
    • Mottram, J.C.1    Souza, A.E.2    Hutchison, J.E.3    Carter, R.4    Frame, M.J.5    Coombs, G.H.6
  • 48
    • 0031574481 scopus 로고    scopus 로고
    • Inhibition of proteasome activity blocks cell cycle progression at specific phase boundaries in African Trypanosomes
    • Mutomba M.C., To W.-Y., Hyun W., Wang C.C. Inhibition of proteasome activity blocks cell cycle progression at specific phase boundaries in African Trypanosomes. Mol Biochem Parasitol. 90:1997;491-504.
    • (1997) Mol Biochem Parasitol , vol.90 , pp. 491-504
    • Mutomba, M.C.1    To, W.-Y.2    Hyun, W.3    Wang, C.C.4
  • 49
    • 0029937677 scopus 로고    scopus 로고
    • Mechanistic studies on the inactivation of the proteasome by lactacystin
    • Dick L.R., Cruikshank L.G., Melandri F.D., Nunes S.L., Stein R.L. Mechanistic studies on the inactivation of the proteasome by lactacystin. J Biol Chem. 271:1996;7273-7276.
    • (1996) J Biol Chem , vol.271 , pp. 7273-7276
    • Dick, L.R.1    Cruikshank, L.G.2    Melandri, F.D.3    Nunes, S.L.4    Stein, R.L.5
  • 51
    • 0026793462 scopus 로고
    • Metabolism and functions of trypanothione in the Kinetoplastida
    • Fairlamb A.H., Cerami A. Metabolism and functions of trypanothione in the Kinetoplastida. Annu Rev Microbiol. 46:1992;695-729.
    • (1992) Annu Rev Microbiol , vol.46 , pp. 695-729
    • Fairlamb, A.H.1    Cerami, A.2
  • 53
    • 0019512549 scopus 로고
    • Inhibition of glutathione synthesis as a chemotherapeutic strategy for Trypanosomiasis
    • Arrick B.A., Griffith O.W., Cerami A. Inhibition of glutathione synthesis as a chemotherapeutic strategy for Trypanosomiasis. J Exp Med. 153:1981;720-725.
    • (1981) J Exp Med , vol.153 , pp. 720-725
    • Arrick, B.A.1    Griffith, O.W.2    Cerami, A.3
  • 54
    • 0028156734 scopus 로고
    • Complete developmental cycle of Leishmania mexicana in axenic culture
    • Bates P.A. Complete developmental cycle of Leishmania mexicana in axenic culture. Parasitology. 108:1994;1-9.
    • (1994) Parasitology , vol.108 , pp. 1-9
    • Bates, P.A.1
  • 56
    • 0029033504 scopus 로고
    • Genes involved in sister chromatid separation are needed for B-type cyclin proteolysis in budding yeast
    • Irniger S., Piatti S., Michaelis C., Nasmyth K. Genes involved in sister chromatid separation are needed for B-type cyclin proteolysis in budding yeast. Cell. 81:1995;269-277.
    • (1995) Cell , vol.81 , pp. 269-277
    • Irniger, S.1    Piatti, S.2    Michaelis, C.3    Nasmyth, K.4


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