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Volumn 9, Issue 1, 2010, Pages

Chaperone expression profiles correlate with distinct physiological states of Plasmodium falciparum in malaria patients

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 90;

EID: 77955682353     PISSN: None     EISSN: 14752875     Source Type: Journal    
DOI: 10.1186/1475-2875-9-236     Document Type: Article
Times cited : (41)

References (38)
  • 1
    • 57149123666 scopus 로고    scopus 로고
    • Molecular chaperones in pathogen virulence: Emerging new targets for therapy
    • 10.1016/j.chom.2008.10.011. 19064253
    • Molecular chaperones in pathogen virulence: emerging new targets for therapy. L Neckers U Tatu, Cell Host Microbe 2008 4 519 527 10.1016/j.chom.2008. 10.011 19064253
    • (2008) Cell Host Microbe , vol.4 , pp. 519-527
    • Neckers, L.1    Tatu, U.2
  • 2
    • 8744228200 scopus 로고    scopus 로고
    • Recurrent fever promotes Plasmodium falciparum development in human erythrocytes
    • 10.1074/jbc.M409165200. 15339915
    • Recurrent fever promotes Plasmodium falciparum development in human erythrocytes. SR Pavithra G Banumathy O Joy V Singh U Tatu, J Biol Chem 2004 279 46692 46699 10.1074/jbc.M409165200 15339915
    • (2004) J Biol Chem , vol.279 , pp. 46692-46699
    • Pavithra, S.R.1    Banumathy, G.2    Joy, O.3    Singh, V.4    Tatu, U.5
  • 3
    • 0038381514 scopus 로고    scopus 로고
    • Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes
    • 10.1074/jbc.M211309200. 12584193
    • Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes. G Banumathy V Singh SR Pavithra U Tatu, J Biol Chem 2003 278 18336 18345 10.1074/jbc.M211309200 12584193
    • (2003) J Biol Chem , vol.278 , pp. 18336-18345
    • Banumathy, G.1    Singh, V.2    Pavithra, S.R.3    Tatu, U.4
  • 6
    • 70350548428 scopus 로고    scopus 로고
    • 17 AAG for HSP90 inhibition in cancer - From bench to bedside
    • 10.2174/156652409788488757. 19601813
    • SZ Usmani R Bona Z Li: 17 AAG for HSP90 inhibition in cancer - from bench to bedside. Curr Mol Med 2009 9 654 64 10.2174/156652409788488757 19601813
    • (2009) Curr Mol Med , vol.9 , pp. 654-664
    • Usmani, S.Z.1    Bona, R.2    Li, Z.3
  • 8
    • 34247513586 scopus 로고    scopus 로고
    • Chaperoning a cellular upheaval in malaria: Heat shock proteins in Plasmodium falciparum
    • 10.1016/j.molbiopara.2007.01.009. 17307260
    • Chaperoning a cellular upheaval in malaria: heat shock proteins in Plasmodium falciparum. P Acharya R Kumar U Tatu, Mol Biochem Parasitol 2007 153 85 94 10.1016/j.molbiopara.2007.01.009 17307260
    • (2007) Mol Biochem Parasitol , vol.153 , pp. 85-94
    • Acharya, P.1    Kumar, R.2    Tatu, U.3
  • 9
    • 34848844683 scopus 로고    scopus 로고
    • Systems analysis of chaperone networks in the malarial parasite Plasmodium falciparum
    • 10.1371/journal.pcbi.0030168. 17941702
    • Systems analysis of chaperone networks in the malarial parasite Plasmodium falciparum. SR Pavithra R Kumar U Tatu, PLoS Comput Biol 2007 3 1701 1715 10.1371/journal.pcbi.0030168 17941702
    • (2007) PLoS Comput Biol , vol.3 , pp. 1701-1715
    • Pavithra, S.R.1    Kumar, R.2    Tatu, U.3
  • 13
    • 4644278673 scopus 로고    scopus 로고
    • Hsp70 and Hsp90 - A relay team for protein folding
    • full-text. 14740253
    • Hsp70 and Hsp90 - a relay team for protein folding. H Wegele L Muller J Buchner, Rev Physiol Biochem Pharmacol 2004 151 1 44 full-text 14740253
    • (2004) Rev Physiol Biochem Pharmacol , vol.151 , pp. 1-44
    • Wegele, H.1    Muller, L.2    Buchner, J.3
  • 14
    • 0032941766 scopus 로고    scopus 로고
    • Characterization of protein Ser/Thr phosphatases of the malaria parasite, Plasmodium falciparum: Inhibition of the parasitic calcineurin by cyclophilin-cyclosporin complex
    • 10.1016/S0166-6851(99)00010-9. 10340482
    • Characterization of protein Ser/Thr phosphatases of the malaria parasite, Plasmodium falciparum: inhibition of the parasitic calcineurin by cyclophilin-cyclosporin complex. S Dobson T May M Berriman C Del Vecchio AH Fairlamb D Chakrabarti S Barik, Mol Biochem Parasitol 1999 99 167 181 10.1016/S0166-6851(99)00010-9 10340482
    • (1999) Mol Biochem Parasitol , vol.99 , pp. 167-181
    • Dobson, S.1    May, T.2    Berriman, M.3    Del Vecchio, C.4    Fairlamb, A.H.5    Chakrabarti, D.6    Barik, S.7
  • 15
    • 17844396246 scopus 로고    scopus 로고
    • The FK506-binding protein of the malaria parasite, Plasmodium falciparum, is a FK506-sensitive chaperone with FK506-independent calcineurin-inhibitory activity
    • 10.1016/j.molbiopara.2005.02.007. 15850699
    • The FK506-binding protein of the malaria parasite, Plasmodium falciparum, is a FK506-sensitive chaperone with FK506-independent calcineurin-inhibitory activity. R Kumar B Adams A Musiyenko O Shulyayeva S Barik, Mol Biochem Parasitol 2005 141 163 173 10.1016/j.molbiopara.2005.02.007 15850699
    • (2005) Mol Biochem Parasitol , vol.141 , pp. 163-173
    • Kumar, R.1    Adams, B.2    Musiyenko, A.3    Shulyayeva, O.4    Barik, S.5
  • 17
    • 0035575616 scopus 로고    scopus 로고
    • Rab GTPases: Specifying and deciphering organelle identity and function
    • 10.1016/S0962-8924(01)02147-X. 11719054
    • Rab GTPases: specifying and deciphering organelle identity and function. SR Pfeffer, Trends Cell Biol 2001 11 487 491 10.1016/S0962-8924(01)02147-X 11719054
    • (2001) Trends Cell Biol , vol.11 , pp. 487-491
    • Pfeffer, S.R.1
  • 18
    • 33746588172 scopus 로고    scopus 로고
    • The Hsp90 chaperone complex regulates GDI-dependent Rab recycling
    • 10.1091/mbc.E05-12-1096. 16687576
    • The Hsp90 chaperone complex regulates GDI-dependent Rab recycling. CY Chen WE Balch, Mol Biol Cell 2006 17 3494 3507 10.1091/mbc.E05-12-1096 16687576
    • (2006) Mol Biol Cell , vol.17 , pp. 3494-3507
    • Chen, C.Y.1    Balch, W.E.2
  • 19
    • 31944445649 scopus 로고    scopus 로고
    • Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradation
    • 10.1091/mbc.E05-08-0713. 16314389
    • Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradation. TS Kim CY Jang HD Kim JY Lee BY Ahn J Kim, Mol Biol Cell 2006 17 824 833 10.1091/mbc.E05-08-0713 16314389
    • (2006) Mol Biol Cell , vol.17 , pp. 824-833
    • Kim, T.S.1    Jang, C.Y.2    Kim, H.D.3    Lee, J.Y.4    Ahn, B.Y.5    Kim, J.6
  • 20
    • 18744382408 scopus 로고    scopus 로고
    • Heat shock protein 90 modulates the unfolded protein response by stabilizing IRE1alpha
    • 10.1128/MCB.22.24.8506-8513.2002. 12446770
    • Heat shock protein 90 modulates the unfolded protein response by stabilizing IRE1alpha. MG Marcu M Doyle A Bertolotti D Ron L Hendershot L Neckers, Mol Cell Biol 2002 22 8506 8513 10.1128/MCB.22.24.8506-8513.2002 12446770
    • (2002) Mol Cell Biol , vol.22 , pp. 8506-8513
    • Marcu, M.G.1    Doyle, M.2    Bertolotti, A.3    Ron, D.4    Hendershot, L.5    Neckers, L.6
  • 21
    • 0033512306 scopus 로고    scopus 로고
    • Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the alpha subunit of eukaryotic translation initiation factor 2 [corrected]
    • 10567567
    • Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the alpha subunit of eukaryotic translation initiation factor 2 [corrected]. O Donze D Picard, Mol Cell Biol 1999 19 8422 8432 10567567
    • (1999) Mol Cell Biol , vol.19 , pp. 8422-8432
    • Donze, O.1    Picard, D.2
  • 22
    • 0031009879 scopus 로고    scopus 로고
    • The role of the 90-kDa heat-shock protein and its associated cohorts in stabilizing the heme-regulated eIF-2alpha kinase in reticulocyte lysates during heat stress
    • 10.1111/j.1432-1033.1997.t01-1-00461.x. 9208939
    • The role of the 90-kDa heat-shock protein and its associated cohorts in stabilizing the heme-regulated eIF-2alpha kinase in reticulocyte lysates during heat stress. Z Xu JK Pal V Thulasiraman HP Hahn JJ Chen RL Matts, Eur J Biochem 1997 246 461 470 10.1111/j.1432-1033.1997.t01-1-00461.x 9208939
    • (1997) Eur J Biochem , vol.246 , pp. 461-470
    • Xu, Z.1    Pal, J.K.2    Thulasiraman, V.3    Hahn, H.P.4    Chen, J.J.5    Matts, R.L.6
  • 23
    • 0035166679 scopus 로고    scopus 로고
    • Translation initiation control by heme-regulated eukaryotic initiation factor 2alpha kinase in erythroid cells under cytoplasmic stresses
    • 10.1128/MCB.21.23.7971-7980.2001. 11689689
    • Translation initiation control by heme-regulated eukaryotic initiation factor 2alpha kinase in erythroid cells under cytoplasmic stresses. L Lu AP Han JJ Chen, Mol Cell Biol 2001 21 7971 7980 10.1128/MCB.21.23.7971-7980.2001 11689689
    • (2001) Mol Cell Biol , vol.21 , pp. 7971-7980
    • Lu, L.1    Han, A.P.2    Chen, J.J.3
  • 24
    • 0034718540 scopus 로고    scopus 로고
    • Modulation of Akt kinase activity by binding to Hsp90
    • 10.1073/pnas.170276797. 10995457
    • Modulation of Akt kinase activity by binding to Hsp90. S Sato N Fujita T Tsuruo, Proc Natl Acad Sci USA 2000 97 10832 10837 10.1073/pnas.170276797 10995457
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10832-10837
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 25
    • 0024416815 scopus 로고
    • A heat shock-like protein from the human malaria parasite Plasmodium falciparum induces autoantibodies
    • 10.1002/eji.1830191010. 2479563
    • A heat shock-like protein from the human malaria parasite Plasmodium falciparum induces autoantibodies. D.Mattei A Scherf O Bensaude LP da Silva, Eur J Immunol 1989 19 1823 1828 10.1002/eji.1830191010 2479563
    • (1989) Eur J Immunol , vol.19 , pp. 1823-1828
    • Mattei, D.1    Scherf, A.2    Bensaude, O.3    Da Silva, L.P.4
  • 26
    • 0023213575 scopus 로고
    • Changes in recognition of Plasmodium falciparum antigens by human sera depending on previous malaria exposure
    • 10.1016/S0769-2625(87)80050-8. 3307832
    • Changes in recognition of Plasmodium falciparum antigens by human sera depending on previous malaria exposure. P Dubois P Druilhe D Arriat M Jendoubi H Jouin, Ann Inst Pasteur Immunol 1987 138 383 396 10.1016/S0769-2625(87)80050-8 3307832
    • (1987) Ann Inst Pasteur Immunol , vol.138 , pp. 383-396
    • Dubois, P.1    Druilhe, P.2    Arriat, D.3    Jendoubi, M.4    Jouin, H.5
  • 27
    • 2542435778 scopus 로고    scopus 로고
    • The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family
    • 10.1074/jbc.M313739200. 15028727
    • The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family. L Shaner A Trott JL Goeckeler JL Brodsky KA Morano, J Biol Chem 2004 279 21992 22001 10.1074/jbc.M313739200 15028727
    • (2004) J Biol Chem , vol.279 , pp. 21992-22001
    • Shaner, L.1    Trott, A.2    Goeckeler, J.L.3    Brodsky, J.L.4    Morano, K.A.5
  • 28
    • 33745762927 scopus 로고    scopus 로고
    • Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s
    • 10.1038/sj.emboj.7601138. 16688212
    • Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. Z Dragovic SA Broadley Y Shomura A Bracher FU Hartl, EMBO J 2006 25 2519 2528 10.1038/sj.emboj.7601138 16688212
    • (2006) EMBO J , vol.25 , pp. 2519-2528
    • Dragovic, Z.1    Broadley, S.A.2    Shomura, Y.3    Bracher, A.4    Hartl, F.U.5
  • 29
    • 0033625965 scopus 로고    scopus 로고
    • The hsp110 and Grp170 stress proteins: Newly recognized relatives of the Hsp70s
    • 10.1379/1466-1268(2000)005< 0276:THAGSP>2.0.CO;2. 11048651
    • The hsp110 and Grp170 stress proteins: newly recognized relatives of the Hsp70s. DP Easton Y Kaneko JR Subjeck, Cell Stress Chaperones 2000 5 276 290 10.1379/1466-1268(2000)005<0276:THAGSP>2.0.CO;2 11048651
    • (2000) Cell Stress Chaperones , vol.5 , pp. 276-290
    • Easton, D.P.1    Kaneko, Y.2    Subjeck, J.R.3
  • 30
    • 23344432378 scopus 로고    scopus 로고
    • The molecular chaperone Sse1 and the growth control protein kinase Sch9 collaborate to regulate protein kinase A activity in Saccharomyces cerevisiae
    • 10.1534/genetics.105.043109. 15879503
    • The molecular chaperone Sse1 and the growth control protein kinase Sch9 collaborate to regulate protein kinase A activity in Saccharomyces cerevisiae. A Trott L Shaner KA Morano, Genetics 2005 170 1009 1021 10.1534/genetics.105. 043109 15879503
    • (2005) Genetics , vol.170 , pp. 1009-1021
    • Trott, A.1    Shaner, L.2    Morano, K.A.3
  • 31
    • 0033578875 scopus 로고    scopus 로고
    • The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone
    • 10.1074/jbc.274.38.26654. 10480867
    • The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone. XD Liu KA Morano DJ Thiele, J Biol Chem 1999 274 26654 26660 10.1074/jbc.274.38.26654 10480867
    • (1999) J Biol Chem , vol.274 , pp. 26654-26660
    • Liu, X.D.1    Morano, K.A.2    Thiele, D.J.3
  • 32
    • 10344245559 scopus 로고    scopus 로고
    • A host-targeting signal in virulence proteins reveals a secretome in malarial infection
    • 10.1126/science.1102737. 15591203
    • A host-targeting signal in virulence proteins reveals a secretome in malarial infection. NL Hiller S Bhattacharjee C van Ooij K Liolios T Harrison C Lopez-Estrano K Haldar, Science 2004 306 5703 1934 1937 10.1126/science.1102737 15591203
    • (2004) Science , vol.306 , Issue.5703 , pp. 1934-1937
    • Hiller, N.L.1    Bhattacharjee, S.2    Van Ooij, C.3    Liolios, K.4    Harrison, T.5    Lopez-Estrano, C.6    Haldar, K.7
  • 33
    • 4344590764 scopus 로고    scopus 로고
    • The J-protein family: Modulating protein assembly, disassembly and translocation
    • 10.1038/sj.embor.7400172. 15170475
    • The J-protein family: modulating protein assembly, disassembly and translocation. P Walsh D Bursac YC Law D Cyr T Lithgow, EMBO Rep 2004 5 6 567 571 10.1038/sj.embor.7400172 15170475
    • (2004) EMBO Rep , vol.5 , Issue.6 , pp. 567-571
    • Walsh, P.1    Bursac, D.2    Law, Y.C.3    Cyr, D.4    Lithgow, T.5
  • 34
    • 51249122014 scopus 로고    scopus 로고
    • The Plasmodium falciparum heat shock protein 40, Pfj4, associates with heat shock protein 70 and shows similar heat induction and localisation patterns
    • 10.1016/j.biocel.2008.06.011. 18674634
    • The Plasmodium falciparum heat shock protein 40, Pfj4, associates with heat shock protein 70 and shows similar heat induction and localisation patterns. ER Pesce P Acharya U Tatu WS Nicoll A Shonhai HC Hoppe GL Blatch, Int J Biochem Cell Biol 2008 40 12 2914 2926 10.1016/j.biocel.2008.06.011 18674634
    • (2008) Int J Biochem Cell Biol , vol.40 , Issue.12 , pp. 2914-2926
    • Pesce, E.R.1    Acharya, P.2    Tatu, U.3    Nicoll, W.S.4    Shonhai, A.5    Hoppe, H.C.6    Blatch, G.L.7
  • 37
    • 34548232285 scopus 로고    scopus 로고
    • The Hsp40 proteins of Plasmodium falciparum and other apicomplexa: Regulating chaperone power in the parasite and the host
    • 10.1016/j.biocel.2007.02.011. 17428722
    • The Hsp40 proteins of Plasmodium falciparum and other apicomplexa: regulating chaperone power in the parasite and the host. M Botha ER Pesce GL Blatch, Int J Biochem Cell Biol 2007 39 1781 1803 10.1016/j.biocel.2007.02.011 17428722
    • (2007) Int J Biochem Cell Biol , vol.39 , pp. 1781-1803
    • Botha, M.1    Pesce, E.R.2    Blatch, G.L.3
  • 38
    • 0028003611 scopus 로고
    • The Plasmodium falciparum protein RESA interacts with the erythrocyte cytoskeleton and modifies erythrocyte thermal stability
    • 10.1016/0166-6851(94)90036-1. 7984188
    • The Plasmodium falciparum protein RESA interacts with the erythrocyte cytoskeleton and modifies erythrocyte thermal stability. E Da Silva M Foley AR Dluzewski LJ Murray RF Anders L Tilley, Mol Biochem Parasitol 1994 66 59 69 10.1016/0166-6851(94)90036-1 7984188
    • (1994) Mol Biochem Parasitol , vol.66 , pp. 59-69
    • Da Silva, E.1    Foley, M.2    Dluzewski, A.R.3    Murray, L.J.4    Anders, R.F.5    Tilley, L.6


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