메뉴 건너뛰기




Volumn 9, Issue 8, 2014, Pages 1869-1876

Assessing subunit dependency of the Plasmodium proteasome using small molecule inhibitors and active site probes

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMALARIAL AGENT; LU 102; PR 709A; PROTEASOME; PROTEASOME INHIBITOR; UBIQUITIN; UNCLASSIFIED DRUG; MOLECULAR PROBE; PROTEINASE INHIBITOR;

EID: 84906264786     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb5001263     Document Type: Article
Times cited : (44)

References (34)
  • 1
    • 84856408211 scopus 로고    scopus 로고
    • World Health Organization. World Health Organization: Geneva.
    • World Health Organization. World Malaria Report 2011; World Health Organization: Geneva; 2011.
    • (2011) World Malaria Report 2011
  • 4
    • 84861464856 scopus 로고    scopus 로고
    • The proteasome of malaria parasites: A multi-stage drug target for chemotherapeutic intervention?
    • Aminake, M. N., Arndt, H.-D., and Pradel, G. (2012) The proteasome of malaria parasites: A multi-stage drug target for chemotherapeutic intervention? Int. J. Parasitol.: Drugs and Drug Resistance 2, 1-10
    • (2012) Int. J. Parasitol.: Drugs and Drug Resistance , vol.2 , pp. 1-10
    • Aminake, M.N.1    Arndt, H.-D.2    Pradel, G.3
  • 5
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Voges, D., Zwickl, P., and Baumeister, W. (1999) The 26S proteasome: A molecular machine designed for controlled proteolysis Annu. Rev. Biochem. 68, 1015-1068
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 6
    • 0033613196 scopus 로고    scopus 로고
    • The catalytic sites of 20S proteasomes and their role in subunit maturation: A mutational and crystallographic study
    • Groll, M. (1999) The catalytic sites of 20S proteasomes and their role in subunit maturation: A mutational and crystallographic study Proc. Natl. Acad. Sci. U. S. A. 96, 10976-10983
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 10976-10983
    • Groll, M.1
  • 8
    • 0030595329 scopus 로고    scopus 로고
    • Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly
    • Chen, P. and Hochstrasser, M. (1996) Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly Cell 86, 961-972
    • (1996) Cell , vol.86 , pp. 961-972
    • Chen, P.1    Hochstrasser, M.2
  • 9
    • 0030774890 scopus 로고    scopus 로고
    • The active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing
    • Heinemeyer, W., Fischer, M., Krimmer, T., Stachon, U., and Wolf, D. H. (1997) The active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing J. Biol. Chem. 272, 25200-25209
    • (1997) J. Biol. Chem. , vol.272 , pp. 25200-25209
    • Heinemeyer, W.1    Fischer, M.2    Krimmer, T.3    Stachon, U.4    Wolf, D.H.5
  • 10
    • 0030737501 scopus 로고    scopus 로고
    • Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation
    • Arendt, C. S. and Hochstrasser, M. (1997) Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation Proc. Natl. Acad. Sci. U.S.A. 94, 7156-7161
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 7156-7161
    • Arendt, C.S.1    Hochstrasser, M.2
  • 13
    • 33646841837 scopus 로고    scopus 로고
    • Importance of the different proteolytic sites of the proteasome and the efficacy of inhibitors varies with the protein substrate
    • Kisselev, A. F. (2006) Importance of the different proteolytic sites of the proteasome and the efficacy of inhibitors varies with the protein substrate J. Biol. Chem. 281, 8582-8590
    • (2006) J. Biol. Chem. , vol.281 , pp. 8582-8590
    • Kisselev, A.F.1
  • 14
    • 0037821846 scopus 로고    scopus 로고
    • Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of mammalian proteasomes
    • Meiners, S., Heyken, D., Weller, A., Ludwig, A., Stangl, K., Kloetzel, P.-M., and Krüger, E. (2003) Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of mammalian proteasomes J. Biol. Chem. 278, 21517-21525
    • (2003) J. Biol. Chem. , vol.278 , pp. 21517-21525
    • Meiners, S.1    Heyken, D.2    Weller, A.3    Ludwig, A.4    Stangl, K.5    Kloetzel, P.-M.6    Krüger, E.7
  • 19
    • 0033230405 scopus 로고    scopus 로고
    • Towards subunit-specific proteasome inhibitors: Synthesis and evaluation of peptide α-, β-epoxyketones
    • Elofsson, M., Splittgerber, U., Myung, J., Mohan, R., and Crews, C. M. (1999) Towards subunit-specific proteasome inhibitors: Synthesis and evaluation of peptide α-, β-epoxyketones Chem. Biol. 6, 811-822
    • (1999) Chem. Biol. , vol.6 , pp. 811-822
    • Elofsson, M.1    Splittgerber, U.2    Myung, J.3    Mohan, R.4    Crews, C.M.5
  • 20
    • 84856373151 scopus 로고    scopus 로고
    • Proteasome inhibitors: An expanding army attacking a unique target
    • Kisselev, A. F., van der Linden, W. A., and Overkleeft, H. S. (2012) Proteasome inhibitors: An expanding army attacking a unique target Chem. Biol. 19, 99-115
    • (2012) Chem. Biol. , vol.19 , pp. 99-115
    • Kisselev, A.F.1    Van Der Linden, W.A.2    Overkleeft, H.S.3
  • 25
    • 84865405382 scopus 로고    scopus 로고
    • Inhibitors for the immuno- and constitutive proteasome: Current and future trends in drug development
    • Huber, E. M. and Groll, M. (2012) Inhibitors for the immuno- and constitutive proteasome: Current and future trends in drug development Angew. Chem., Int. Ed. Engl. 51, 8708-8720
    • (2012) Angew. Chem., Int. Ed. Engl. , vol.51 , pp. 8708-8720
    • Huber, E.M.1    Groll, M.2
  • 26
    • 13944258184 scopus 로고    scopus 로고
    • How many functional transport pathways does Plasmodium falciparum induce in the membrane of its host erythrocyte?
    • Ginsburg, H. and Stein, W. D. (2005) How many functional transport pathways does Plasmodium falciparum induce in the membrane of its host erythrocyte? Trends Parasitol. 21, 118-121
    • (2005) Trends Parasitol. , vol.21 , pp. 118-121
    • Ginsburg, H.1    Stein, W.D.2
  • 27
    • 38649139835 scopus 로고    scopus 로고
    • Antimalarial activity of the anticancer and proteasome inhibitor bortezomib and its analog ZL3B
    • Reynolds, J. M., Bissati, E. K., Brandenburg, J., Günzl, A., and Mamoun, C. B. (2007) Antimalarial activity of the anticancer and proteasome inhibitor bortezomib and its analog ZL3B BMC Clin. Pharmacol. 7, 13
    • (2007) BMC Clin. Pharmacol. , vol.7 , pp. 13
    • Reynolds, J.M.1    Bissati, E.K.2    Brandenburg, J.3    Günzl, A.4    Mamoun, C.B.5
  • 30
    • 84856282078 scopus 로고    scopus 로고
    • The contribution of Plasmodium chabaudi to our understanding of malaria
    • Stephens, R., Culleton, R. L., and Lamb, T. J. (2012) The contribution of Plasmodium chabaudi to our understanding of malaria Trends Parasitol. 28, 74-83
    • (2012) Trends Parasitol. , vol.28 , pp. 74-83
    • Stephens, R.1    Culleton, R.L.2    Lamb, T.J.3
  • 32
    • 4243071596 scopus 로고    scopus 로고
    • The transcriptome of the intraerythrocytic developmental cycle of Plasmodium falciparum
    • Bozdech, Z., Llinás, M., Pulliam, B. L., Wong, E. D., Zhu, J., and DeRisi, J. L. (2003) The transcriptome of the intraerythrocytic developmental cycle of Plasmodium falciparum PLoS Biol. 1, e5
    • (2003) PLoS Biol. , vol.1 , pp. 5
    • Bozdech, Z.1    Llinás, M.2    Pulliam, B.L.3    Wong, E.D.4    Zhu, J.5    Derisi, J.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.