메뉴 건너뛰기




Volumn 8, Issue 8, 2013, Pages

Food Vacuole Associated Enolase in Plasmodium Undergoes Multiple Post-Translational Modifications: Evidence for Atypical Ubiquitination

Author keywords

[No Author keywords available]

Indexed keywords

ENOLASE; HEMOZOIN; UBIQUITIN; UBIQUITIN 1; UBIQUITIN 2; UBIQUITIN 3; UNCLASSIFIED DRUG;

EID: 84883037305     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0072687     Document Type: Article
Times cited : (10)

References (62)
  • 1
    • 0034947535 scopus 로고    scopus 로고
    • Multifunctional alpha-enolase: its role in diseases
    • doi: 10.1007/PL00000910
    • Pancholi V, (2001) Multifunctional alpha-enolase: its role in diseases. Cell Mol Life Sci 58: 902-920. doi:10.1007/PL00000910. PubMed: 11497239.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 902-920
    • Pancholi, V.1
  • 2
    • 0032486286 scopus 로고    scopus 로고
    • alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci
    • doi: 10.1074/jbc.273.23.14503
    • Pancholi V, Fischetti VA, (1998) alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci. J Biol Chem 273: 14503-14515. doi:10.1074/jbc.273.23.14503. PubMed: 9603964.
    • (1998) J Biol Chem , vol.273 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 3
    • 65549164868 scopus 로고    scopus 로고
    • Surface-expressed enolase contributes to the pathogenesis of clinical isolate SSU of Aeromonas hydrophila
    • doi: 10.1128/JB.00005-09
    • Sha J, Erova TE, Alyea RA, Wang S, Olano JP, et al. (2009) Surface-expressed enolase contributes to the pathogenesis of clinical isolate SSU of Aeromonas hydrophila. J Bacteriol 191: 3095-3107. doi:10.1128/JB.00005-09. PubMed: 19270100.
    • (2009) J Bacteriol , vol.191 , pp. 3095-3107
    • Sha, J.1    Erova, T.E.2    Alyea, R.A.3    Wang, S.4    Olano, J.P.5
  • 4
    • 34247870811 scopus 로고    scopus 로고
    • Genetic and proteomic evidences support the localization of yeast enolase in the cell surface
    • doi: 10.1002/pmic.200500479
    • López-Villar E, Monteoliva L, Larsen MR, Sachon E, Shabaz M, et al. (2006) Genetic and proteomic evidences support the localization of yeast enolase in the cell surface. Proteomics 6 (Suppl 1):: S107-S118. doi:10.1002/pmic.200500479. PubMed: 16544286.
    • (2006) Proteomics , vol.6 , Issue.SUPPL. 1
    • López-Villar, E.1    Monteoliva, L.2    Larsen, M.R.3    Sachon, E.4    Shabaz, M.5
  • 5
    • 69449107551 scopus 로고    scopus 로고
    • Plasmodium falciparum enolase: stage-specific expression and sub-cellular localization
    • doi: 10.1186/1475-2875-8-179
    • Bhowmick IP, Kumar N, Sharma S, Coppens I, Jarori GK, (2009) Plasmodium falciparum enolase: stage-specific expression and sub-cellular localization. Malar J 8: 179. doi:10.1186/1475-2875-8-179. PubMed: 19642995.
    • (2009) Malar J , vol.8 , pp. 179
    • Bhowmick, I.P.1    Kumar, N.2    Sharma, S.3    Coppens, I.4    Jarori, G.K.5
  • 6
    • 38549150292 scopus 로고    scopus 로고
    • [Role of neuron specific enolase and S100 protein in evaluation of brain damage in patients resuscitated from cardiac arrest]
    • PubMed: 18093437
    • Miao WL, Li HL, Wang HD, Wang J, Liu H, et al. (2007) [Role of neuron specific enolase and S100 protein in evaluation of brain damage in patients resuscitated from cardiac arrest]. Zhongguo Wei Zhong Bing Ji Jiu Yi Xue 19: 749-752. PubMed: 18093437.
    • (2007) Zhongguo Wei Zhong Bing Ji Jiu Yi Xue , vol.19 , pp. 749-752
    • Miao, W.L.1    Li, H.L.2    Wang, H.D.3    Wang, J.4    Liu, H.5
  • 7
    • 77649263299 scopus 로고    scopus 로고
    • A new nuclear function of the Entamoeba histolytica glycolytic enzyme enolase: the metabolic regulation of cytosine-5 methyltransferase 2 (Dnmt2) activity
    • PubMed: 20174608
    • Tovy A, Siman Tov R, Gaentzsch R, Helm M, Ankri S, (2010) A new nuclear function of the Entamoeba histolytica glycolytic enzyme enolase: the metabolic regulation of cytosine-5 methyltransferase 2 (Dnmt2) activity. PLOS Pathog 6: e1000775. PubMed: 20174608.
    • (2010) PLOS Pathog , vol.6
    • Tovy, A.1    Siman Tov, R.2    Gaentzsch, R.3    Helm, M.4    Ankri, S.5
  • 8
    • 0037013865 scopus 로고    scopus 로고
    • LOS2, a genetic locus required for cold-responsive gene transcription encodes a bi-functional enolase
    • doi: 10.1093/emboj/21.11.2692
    • Lee H, Guo Y, Ohta M, Xiong L, Stevenson B, et al. (2002) LOS2, a genetic locus required for cold-responsive gene transcription encodes a bi-functional enolase. EMBO J 21: 2692-2702. doi:10.1093/emboj/21.11.2692. PubMed: 12032082.
    • (2002) EMBO J , vol.21 , pp. 2692-2702
    • Lee, H.1    Guo, Y.2    Ohta, M.3    Xiong, L.4    Stevenson, B.5
  • 9
    • 0034604055 scopus 로고    scopus 로고
    • ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: relationship with Myc promoter-binding protein 1 (MBP-1)
    • doi: 10.1016/S0014-5793(00)01494-0
    • Feo S, Arcuri D, Piddini E, Passantino R, Giallongo A, (2000) ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: relationship with Myc promoter-binding protein 1 (MBP-1). FEBS Lett 473: 47-52. doi:10.1016/S0014-5793(00)01494-0. PubMed: 10802057.
    • (2000) FEBS Lett , vol.473 , pp. 47-52
    • Feo, S.1    Arcuri, D.2    Piddini, E.3    Passantino, R.4    Giallongo, A.5
  • 10
    • 0036803087 scopus 로고    scopus 로고
    • Evidence for nuclear localisation of two stage-specific isoenzymes of enolase in Toxoplasma gondii correlates with active parasite replication
    • doi: 10.1016/S0020-7519(02)00129-7
    • Ferguson DJ, Parmley SF, Tomavo S, (2002) Evidence for nuclear localisation of two stage-specific isoenzymes of enolase in Toxoplasma gondii correlates with active parasite replication. Int J Parasitol 32: 1399-1410. doi:10.1016/S0020-7519(02)00129-7. PubMed: 12350375.
    • (2002) Int J Parasitol , vol.32 , pp. 1399-1410
    • Ferguson, D.J.1    Parmley, S.F.2    Tomavo, S.3
  • 11
    • 34247547010 scopus 로고    scopus 로고
    • Sub-cellular localization and post-translational modifications of the Plasmodium yoelii enolase suggest moonlighting functions
    • doi: 10.1186/1475-2875-6-45
    • Pal-Bhowmick I, Vora HK, Jarori GK, (2007) Sub-cellular localization and post-translational modifications of the Plasmodium yoelii enolase suggest moonlighting functions. Malar J 6: 45. doi:10.1186/1475-2875-6-45. PubMed: 17437631.
    • (2007) Malar J , vol.6 , pp. 45
    • Pal-Bhowmick, I.1    Vora, H.K.2    Jarori, G.K.3
  • 12
    • 33744916797 scopus 로고    scopus 로고
    • Enolase activates homotypic vacuole fusion and protein transport to the vacuole in yeast
    • doi: 10.1074/jbc.M600911200
    • Decker BL, Wickner WT, (2006) Enolase activates homotypic vacuole fusion and protein transport to the vacuole in yeast. J Biol Chem 281: 14523-14528. doi:10.1074/jbc.M600911200. PubMed: 16565073.
    • (2006) J Biol Chem , vol.281 , pp. 14523-14528
    • Decker, B.L.1    Wickner, W.T.2
  • 13
    • 79959767781 scopus 로고    scopus 로고
    • Plasmodium falciparum enolase complements yeast enolase functions and associates with the parasite food vacuole
    • doi: 10.1016/j.molbiopara.2011.05.001
    • Das S, Shevade S, Lacount DJ, Jarori GK, (2011) Plasmodium falciparum enolase complements yeast enolase functions and associates with the parasite food vacuole. Mol Biochem Parasitol 179: 8-17. doi:10.1016/j.molbiopara.2011.05.001. PubMed: 21600245.
    • (2011) Mol Biochem Parasitol , vol.179 , pp. 8-17
    • Das, S.1    Shevade, S.2    Lacount, D.J.3    Jarori, G.K.4
  • 14
    • 36549046777 scopus 로고    scopus 로고
    • The Role of Enolase in Tissue Invasion and Metastasis of Pathogens and Tumor Cells
    • Liu K-J, Shih N-Y, (2007) The Role of Enolase in Tissue Invasion and Metastasis of Pathogens and Tumor Cells. J Cancer Mol 3: 45-48.
    • (2007) J Cancer Mol , vol.3 , pp. 45-48
    • Liu, K.-J.1    Shih, N.-Y.2
  • 15
    • 80054723119 scopus 로고    scopus 로고
    • Plasmodium ookinetes coopt mammalian plasminogen to invade the mosquito midgut
    • doi: 10.1073/pnas.1103657108
    • Ghosh AK, Coppens I, Gårdsvoll H, Ploug M, Jacobs-Lorena M, (2011) Plasmodium ookinetes coopt mammalian plasminogen to invade the mosquito midgut. Proc Natl Acad Sci U S A 108: 17153-17158. doi:10.1073/pnas.1103657108. PubMed: 21949403.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 17153-17158
    • Ghosh, A.K.1    Coppens, I.2    Gårdsvoll, H.3    Ploug, M.4    Jacobs-Lorena, M.5
  • 16
    • 80053059117 scopus 로고    scopus 로고
    • Conserved peptide sequences bind to actin and enolase on the surface of Plasmodium berghei ookinetes
    • doi: 10.1017/S0031182011001296
    • Hernández-Romano J, Rodríguez MH, Pando V, Torres-Monzón JA, Alvarado-Delgado A, et al. (2011) Conserved peptide sequences bind to actin and enolase on the surface of Plasmodium berghei ookinetes. Parasitology 138: 1341-1353. doi:10.1017/S0031182011001296. PubMed: 21816124.
    • (2011) Parasitology , vol.138 , pp. 1341-1353
    • Hernández-Romano, J.1    Rodríguez, M.H.2    Pando, V.3    Torres-Monzón, J.A.4    Alvarado-Delgado, A.5
  • 17
    • 8544261105 scopus 로고    scopus 로고
    • Enolase in the RNA degradosome plays a crucial role in the rapid decay of glucose transporter mRNA in the response to phosphosugar stress in Escherichia coli
    • doi: 10.1111/j.1365-2958.2004.04329.x
    • Morita T, Kawamoto H, Mizota T, Inada T, Aiba H, (2004) Enolase in the RNA degradosome plays a crucial role in the rapid decay of glucose transporter mRNA in the response to phosphosugar stress in Escherichia coli. Mol Microbiol 54: 1063-1075. doi:10.1111/j.1365-2958.2004.04329.x. PubMed: 15522087.
    • (2004) Mol Microbiol , vol.54 , pp. 1063-1075
    • Morita, T.1    Kawamoto, H.2    Mizota, T.3    Inada, T.4    Aiba, H.5
  • 18
    • 0024252493 scopus 로고
    • Tau-crystallin/alpha-enolase: one gene encodes both an enzyme and a lens structural protein
    • doi: 10.1083/jcb.107.6.2729
    • Wistow GJ, Lietman T, Williams LA, Stapel SO, de Jong WW, et al. (1988) Tau-crystallin/alpha-enolase: one gene encodes both an enzyme and a lens structural protein. J Cell Biol 107: 2729-2736. doi:10.1083/jcb.107.6.2729. PubMed: 2462567.
    • (1988) J Cell Biol , vol.107 , pp. 2729-2736
    • Wistow, G.J.1    Lietman, T.2    Williams, L.A.3    Stapel, S.O.4    de Jong, W.W.5
  • 19
    • 0021984720 scopus 로고
    • Yeast heat-shock protein of Mr 48,000 is an isoprotein of enolase
    • doi: 10.1038/315688a0
    • Iida H, Yahara I, (1985) Yeast heat-shock protein of Mr 48,000 is an isoprotein of enolase. Nature 315: 688-690. doi:10.1038/315688a0.
    • (1985) Nature , vol.315 , pp. 688-690
    • Iida, H.1    Yahara, I.2
  • 20
    • 14744284637 scopus 로고    scopus 로고
    • Multifaceted roles of glycolytic enzymes
    • doi: 10.1016/j.tibs.2005.01.005
    • Kim JW, Dang CV, (2005) Multifaceted roles of glycolytic enzymes. Trends Biochem Sci 30: 142-150. doi:10.1016/j.tibs.2005.01.005. PubMed: 15752986.
    • (2005) Trends Biochem Sci , vol.30 , pp. 142-150
    • Kim, J.W.1    Dang, C.V.2
  • 21
    • 35648977084 scopus 로고    scopus 로고
    • Protective properties and surface localization of Plasmodium falciparum enolase
    • doi: 10.1128/IAI.00551-07
    • Pal-Bhowmick I, Mehta M, Coppens I, Sharma S, Jarori GK, (2007) Protective properties and surface localization of Plasmodium falciparum enolase. Infect Immun 75: 5500-5508. doi:10.1128/IAI.00551-07. PubMed: 17785475.
    • (2007) Infect Immun , vol.75 , pp. 5500-5508
    • Pal-Bhowmick, I.1    Mehta, M.2    Coppens, I.3    Sharma, S.4    Jarori, G.K.5
  • 22
    • 84856703405 scopus 로고    scopus 로고
    • Quantitative Proteomics Reveals New Insights into Erythrocyte Invasion by Plasmodium falciparum
    • PubMed: 22023809
    • Kuss C, Gan CS, Gunalan K, Bozdech Z, Sze SK, et al. (2012) Quantitative Proteomics Reveals New Insights into Erythrocyte Invasion by Plasmodium falciparum. Mol Cell Proteomics 11: 010645. PubMed: 22023809.
    • (2012) Mol Cell Proteomics , vol.11 , pp. 010645
    • Kuss, C.1    Gan, C.S.2    Gunalan, K.3    Bozdech, Z.4    Sze, S.K.5
  • 23
    • 33644555054 scopus 로고    scopus 로고
    • Proteome survey reveals modularity of the yeast cell machinery
    • doi: 10.1038/nature04532
    • Gavin AC, Aloy P, Grandi P, Krause R, Boesche M, et al. (2006) Proteome survey reveals modularity of the yeast cell machinery. Nature 440: 631-636. doi:10.1038/nature04532. PubMed: 16429126.
    • (2006) Nature , vol.440 , pp. 631-636
    • Gavin, A.C.1    Aloy, P.2    Grandi, P.3    Krause, R.4    Boesche, M.5
  • 24
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • doi: 10.1038/415141a
    • Gavin AC, Bösche M, Krause R, Grandi P, Marzioch M, et al. (2002) Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415: 141-147. doi:10.1038/415141a. PubMed: 11805826.
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.C.1    Bösche, M.2    Krause, R.3    Grandi, P.4    Marzioch, M.5
  • 25
    • 0030886261 scopus 로고    scopus 로고
    • The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole
    • doi: 10.1016/S0092-8674(01)80013-1
    • Cowles CR, Odorizzi G, Payne GS, Emr SD, (1997) The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole. Cell 91: 109-118. doi:10.1016/S0092-8674(01)80013-1. PubMed: 9335339.
    • (1997) Cell , vol.91 , pp. 109-118
    • Cowles, C.R.1    Odorizzi, G.2    Payne, G.S.3    Emr, S.D.4
  • 26
    • 0032404443 scopus 로고    scopus 로고
    • The AP-3 complex: a coat of many colours
    • doi: 10.1016/S0962-8924(98)01295-1
    • Odorizzi G, Cowles CR, Emr SD, (1998) The AP-3 complex: a coat of many colours. Trends Cell Biol 8: 282-288. doi:10.1016/S0962-8924(98)01295-1. PubMed: 9714600.
    • (1998) Trends Cell Biol , vol.8 , pp. 282-288
    • Odorizzi, G.1    Cowles, C.R.2    Emr, S.D.3
  • 27
    • 75649110055 scopus 로고    scopus 로고
    • Quantitative proteomics of the tonoplast reveals a role for glycolytic enzymes in salt tolerance
    • doi: 10.1105/tpc.109.069211
    • Barkla BJ, Vera-Estrella R, Hernández-Coronado M, Pantoja O, (2009) Quantitative proteomics of the tonoplast reveals a role for glycolytic enzymes in salt tolerance. Plant Cell 21: 4044-4058. doi:10.1105/tpc.109.069211. PubMed: 20028841.
    • (2009) Plant Cell , vol.21 , pp. 4044-4058
    • Barkla, B.J.1    Vera-Estrella, R.2    Hernández-Coronado, M.3    Pantoja, O.4
  • 28
    • 0033609934 scopus 로고    scopus 로고
    • The protozoan parasite Toxoplasma gondii expresses two functional plant-like glycolytic enzymes. Implications for evolutionary origin of apicomplexans
    • doi: 10.1074/jbc.274.35.24888
    • Dzierszinski F, Popescu O, Toursel C, Slomianny C, Yahiaoui B, et al. (1999) The protozoan parasite Toxoplasma gondii expresses two functional plant-like glycolytic enzymes. Implications for evolutionary origin of apicomplexans. J Biol Chem 274: 24888-24895. doi:10.1074/jbc.274.35.24888. PubMed: 10455162.
    • (1999) J Biol Chem , vol.274 , pp. 24888-24895
    • Dzierszinski, F.1    Popescu, O.2    Toursel, C.3    Slomianny, C.4    Yahiaoui, B.5
  • 29
    • 0028280998 scopus 로고
    • Molecular characterisation of the enolase gene from the human malaria parasite Plasmodium falciparum. Evidence for ancestry within a photosynthetic lineage
    • doi: 10.1111/j.1432-1033.1994.tb18650.x
    • Read M, Hicks KE, Sims PF, Hyde JE, (1994) Molecular characterisation of the enolase gene from the human malaria parasite Plasmodium falciparum. Evidence for ancestry within a photosynthetic lineage. Eur J Biochem 220: 513-520. doi:10.1111/j.1432-1033.1994.tb18650.x. PubMed: 8125109.
    • (1994) Eur J Biochem , vol.220 , pp. 513-520
    • Read, M.1    Hicks, K.E.2    Sims, P.F.3    Hyde, J.E.4
  • 30
    • 11244252155 scopus 로고    scopus 로고
    • Cloning, over-expression, purification and characterization of Plasmodium falciparum enolase
    • doi: 10.1111/j.1432-1033.2004.04450.x
    • Pal-Bhowmick I, Sadagopan K, Vora HK, Sehgal A, Sharma S, et al. (2004) Cloning, over-expression, purification and characterization of Plasmodium falciparum enolase. Eur J Biochem 271: 4845-4854. doi:10.1111/j.1432-1033.2004.04450.x. PubMed: 15606772.
    • (2004) Eur J Biochem , vol.271 , pp. 4845-4854
    • Pal-Bhowmick, I.1    Sadagopan, K.2    Vora, H.K.3    Sehgal, A.4    Sharma, S.5
  • 31
    • 0037458576 scopus 로고    scopus 로고
    • Acidification of the malaria parasite's digestive vacuole by a H+-ATPase and a H+-pyrophosphatase
    • doi: 10.1074/jbc.M208648200
    • Saliba KJ, Allen RJ, Zissis S, Bray PG, Ward SA, et al. (2003) Acidification of the malaria parasite's digestive vacuole by a H+-ATPase and a H+-pyrophosphatase. J Biol Chem 278: 5605-5612. doi:10.1074/jbc.M208648200. PubMed: 12427765.
    • (2003) J Biol Chem , vol.278 , pp. 5605-5612
    • Saliba, K.J.1    Allen, R.J.2    Zissis, S.3    Bray, P.G.4    Ward, S.A.5
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • doi: 10.1038/227680a0
    • Laemmli UK, (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685. doi:10.1038/227680a0. PubMed: 5432063.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 10544244161 scopus 로고    scopus 로고
    • Linking genome and proteome by mass spectrometry: large-scale identification of yeast proteins from two dimensional gels
    • doi: 10.1073/pnas.93.25.14440
    • Shevchenko A, Jensen ON, Podtelejnikov AV, Sagliocco F, Wilm M, et al. (1996) Linking genome and proteome by mass spectrometry: large-scale identification of yeast proteins from two dimensional gels. Proc Natl Acad Sci U S A 93: 14440-14445. doi:10.1073/pnas.93.25.14440. PubMed: 8962070.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 14440-14445
    • Shevchenko, A.1    Jensen, O.N.2    Podtelejnikov, A.V.3    Sagliocco, F.4    Wilm, M.5
  • 34
    • 33846520786 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system regulates membrane fusion of yeast vacuoles
    • doi: 10.1038/sj.emboj.7601486
    • Kleijnen MF, Kirkpatrick DS, Gygi SP, (2007) The ubiquitin-proteasome system regulates membrane fusion of yeast vacuoles. EMBO J 26: 275-287. doi:10.1038/sj.emboj.7601486. PubMed: 17183369.
    • (2007) EMBO J , vol.26 , pp. 275-287
    • Kleijnen, M.F.1    Kirkpatrick, D.S.2    Gygi, S.P.3
  • 35
    • 53549096785 scopus 로고    scopus 로고
    • Food vacuole proteome of the malarial parasite Plasmodium falciparum
    • doi: 10.1002/prca.200700112
    • Lamarque M, Tastet C, Poncet J, Demettre E, Jouin P, et al. (2008) Food vacuole proteome of the malarial parasite Plasmodium falciparum. Proteomics Clin Appl 2: 1361-1374. doi:10.1002/prca.200700112. PubMed: 21136929.
    • (2008) Proteomics Clin Appl , vol.2 , pp. 1361-1374
    • Lamarque, M.1    Tastet, C.2    Poncet, J.3    Demettre, E.4    Jouin, P.5
  • 36
    • 7044237455 scopus 로고    scopus 로고
    • Proteome analysis of rhoptry-enriched fractions isolated from Plasmodium merozoites
    • doi: 10.1021/pr049926m
    • Sam-Yellowe TY, Florens L, Wang T, Raine JD, Carucci DJ, et al. (2004) Proteome analysis of rhoptry-enriched fractions isolated from Plasmodium merozoites. J Proteome Res 3: 995-1001. doi:10.1021/pr049926m. PubMed: 15473688.
    • (2004) J Proteome Res , vol.3 , pp. 995-1001
    • Sam-Yellowe, T.Y.1    Florens, L.2    Wang, T.3    Raine, J.D.4    Carucci, D.J.5
  • 37
    • 44649101850 scopus 로고    scopus 로고
    • Atypical ubiquitin chains: new molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series
    • doi: 10.1038/embor.2008.93
    • Ikeda F, Dikic I, (2008) Atypical ubiquitin chains: new molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series. EMBO Rep 9: 536-542. doi:10.1038/embor.2008.93. PubMed: 18516089.
    • (2008) EMBO Rep , vol.9 , pp. 536-542
    • Ikeda, F.1    Dikic, I.2
  • 38
    • 67650064603 scopus 로고    scopus 로고
    • Linear polyubiquitination: a new regulator of NF-kappaB activation
    • doi: 10.1038/embor.2009.144
    • Iwai K, Tokunaga F, (2009) Linear polyubiquitination: a new regulator of NF-kappaB activation. EMBO Rep 10: 706-713. doi:10.1038/embor.2009.144. PubMed: 19543231.
    • (2009) EMBO Rep , vol.10 , pp. 706-713
    • Iwai, K.1    Tokunaga, F.2
  • 39
    • 33750219981 scopus 로고    scopus 로고
    • A ubiquitin ligase complex assembles linear polyubiquitin chains
    • doi: 10.1038/sj.emboj.7601360
    • Kirisako T, Kamei K, Murata S, Kato M, Fukumoto H, et al. (2006) A ubiquitin ligase complex assembles linear polyubiquitin chains. EMBO J 25: 4877-4887. doi:10.1038/sj.emboj.7601360. PubMed: 17006537.
    • (2006) EMBO J , vol.25 , pp. 4877-4887
    • Kirisako, T.1    Kamei, K.2    Murata, S.3    Kato, M.4    Fukumoto, H.5
  • 40
    • 80051654221 scopus 로고    scopus 로고
    • Quantitative time-course profiling of parasite and host cell proteins in the human malaria parasite Plasmodium falciparum
    • PubMed: 21558492
    • Foth BJ, Zhang N, Chaal BK, Sze SK, Preiser PR, et al. (2011) Quantitative time-course profiling of parasite and host cell proteins in the human malaria parasite Plasmodium falciparum. Mol Cell Proteomics 10M110: 006411. PubMed: 21558492.
    • (2011) Mol Cell Proteomics , vol.10 , pp. 006411
    • Foth, B.J.1    Zhang, N.2    Chaal, B.K.3    Sze, S.K.4    Preiser, P.R.5
  • 41
    • 58349118483 scopus 로고    scopus 로고
    • Quantitative protein expression profiling reveals extensive post-transcriptional regulation and post-translational modifications in schizont-stage malaria parasites
    • doi: 10.1186/gb-2008-9-12-r177
    • Foth BJ, Zhang N, Mok S, Preiser PR, Bozdech Z, (2008) Quantitative protein expression profiling reveals extensive post-transcriptional regulation and post-translational modifications in schizont-stage malaria parasites. Genome Biol 9: R177. doi:10.1186/gb-2008-9-12-r177. PubMed: 19091060.
    • (2008) Genome Biol , vol.9
    • Foth, B.J.1    Zhang, N.2    Mok, S.3    Preiser, P.R.4    Bozdech, Z.5
  • 42
    • 43049134137 scopus 로고    scopus 로고
    • HDP-a novel heme detoxification protein from the malaria parasite
    • PubMed: 18437218
    • Jani D, Nagarkatti R, Beatty W, Angel R, Slebodnick C, et al. (2008) HDP-a novel heme detoxification protein from the malaria parasite. PLOS Pathog 4: e1000053. PubMed: 18437218.
    • (2008) PLOS Pathog , vol.4
    • Jani, D.1    Nagarkatti, R.2    Beatty, W.3    Angel, R.4    Slebodnick, C.5
  • 43
    • 0029013807 scopus 로고
    • The plasmodium digestive vacuole: metabolic headquarters and choice drug target
    • doi: 10.1016/0169-4758(95)80042-5
    • Olliaro PL, Goldberg DE, (1995) The plasmodium digestive vacuole: metabolic headquarters and choice drug target. Parasitol Today 11: 294-297. doi:10.1016/0169-4758(95)80042-5. PubMed: 15275326.
    • (1995) Parasitol Today , vol.11 , pp. 294-297
    • Olliaro, P.L.1    Goldberg, D.E.2
  • 44
    • 52649134596 scopus 로고    scopus 로고
    • Formation of the food vacuole in Plasmodium falciparum: a potential role for the 19 kDa fragment of merozoite surface protein 1 (MSP1(19))
    • doi: 10.1371/journal.pone.0003085
    • Dluzewski AR, Ling IT, Hopkins JM, Grainger M, Margos G, et al. (2008) Formation of the food vacuole in Plasmodium falciparum: a potential role for the 19 kDa fragment of merozoite surface protein 1 (MSP1(19)). PLOS ONE 3: e3085. doi:10.1371/journal.pone.0003085. PubMed: 18769730.
    • (2008) PLOS ONE , vol.3
    • Dluzewski, A.R.1    Ling, I.T.2    Hopkins, J.M.3    Grainger, M.4    Margos, G.5
  • 45
    • 61949332590 scopus 로고    scopus 로고
    • Dual sorting of the Saccharomyces cerevisiae vacuolar protein Sna4p
    • doi: 10.1128/EC.00363-08
    • Pokrzywa W, Guerriat B, Dodzian J, Morsomme P, (2009) Dual sorting of the Saccharomyces cerevisiae vacuolar protein Sna4p. Eukaryot Cell 8: 278-286. doi:10.1128/EC.00363-08. PubMed: 19168755.
    • (2009) Eukaryot Cell , vol.8 , pp. 278-286
    • Pokrzywa, W.1    Guerriat, B.2    Dodzian, J.3    Morsomme, P.4
  • 46
    • 27644484749 scopus 로고    scopus 로고
    • A protein interaction network of the malaria parasite Plasmodium falciparum
    • doi: 10.1038/nature04104
    • LaCount DJ, Vignali M, Chettier R, Phansalkar A, Bell R, et al. (2005) A protein interaction network of the malaria parasite Plasmodium falciparum. Nature 438: 103-107. doi:10.1038/nature04104. PubMed: 16267556.
    • (2005) Nature , vol.438 , pp. 103-107
    • LaCount, D.J.1    Vignali, M.2    Chettier, R.3    Phansalkar, A.4    Bell, R.5
  • 47
    • 10744231179 scopus 로고    scopus 로고
    • The N'-terminal domain of glyceraldehyde-3-phosphate dehydrogenase of the apicomplexan Plasmodium falciparum mediates GTPase Rab2-dependent recruitment to membranes
    • PubMed: 12974391
    • Daubenberger CA, Tisdale EJ, Curcic M, Diaz D, Silvie O, et al. (2003) The N'-terminal domain of glyceraldehyde-3-phosphate dehydrogenase of the apicomplexan Plasmodium falciparum mediates GTPase Rab2-dependent recruitment to membranes. Biol Chem 384: 1227-1237. PubMed: 12974391.
    • (2003) Biol Chem , vol.384 , pp. 1227-1237
    • Daubenberger, C.A.1    Tisdale, E.J.2    Curcic, M.3    Diaz, D.4    Silvie, O.5
  • 48
    • 0032973950 scopus 로고    scopus 로고
    • New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
    • doi: 10.1016/S0167-4838(99)00119-3
    • Sirover MA, (1999) New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase. Biochim Biophys Acta 1432: 159-184. doi:10.1016/S0167-4838(99)00119-3. PubMed: 10407139.
    • (1999) Biochim Biophys Acta , vol.1432 , pp. 159-184
    • Sirover, M.A.1
  • 50
    • 79952830765 scopus 로고    scopus 로고
    • alpha-Enolase: a promising therapeutic and diagnostic tumor target
    • doi: 10.1111/j.1742-4658.2011.08025.x
    • Capello M, Ferri-Borgogno S, Cappello P, Novelli F, (2011) alpha-Enolase: a promising therapeutic and diagnostic tumor target. FEBS J 278: 1064-1074. doi:10.1111/j.1742-4658.2011.08025.x. PubMed: 21261815.
    • (2011) FEBS J , vol.278 , pp. 1064-1074
    • Capello, M.1    Ferri-Borgogno, S.2    Cappello, P.3    Novelli, F.4
  • 51
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • doi: 10.1146/annurev.cellbio.19.110701.154617
    • Hicke L, Dunn R, (2003) Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu Rev Cell Dev Biol 19: 141-172. doi:10.1146/annurev.cellbio.19.110701.154617. PubMed: 14570567.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 52
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • doi: 10.1126/science.2538923
    • Chau V, Tobias JW, Bachmair A, Marriott D, Ecker DJ, et al. (1989) A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science 243: 1576-1583. doi:10.1126/science.2538923. PubMed: 2538923.
    • (1989) Science , vol.243 , pp. 1576-1583
    • Chau, V.1    Tobias, J.W.2    Bachmair, A.3    Marriott, D.4    Ecker, D.J.5
  • 53
    • 0033525582 scopus 로고    scopus 로고
    • Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair
    • doi: 10.1016/S0092-8674(00)80575-9
    • Hofmann RM, Pickart CM, (1999) Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. Cell 96: 645-653. doi:10.1016/S0092-8674(00)80575-9. PubMed: 10089880.
    • (1999) Cell , vol.96 , pp. 645-653
    • Hofmann, R.M.1    Pickart, C.M.2
  • 54
    • 8844237615 scopus 로고    scopus 로고
    • Polyubiquitin chains: polymeric protein signals
    • doi: 10.1016/j.cbpa.2004.09.009
    • Pickart CM, Fushman D, (2004) Polyubiquitin chains: polymeric protein signals. Curr Opin Chem Biol 8: 610-616. doi:10.1016/j.cbpa.2004.09.009. PubMed: 15556404.
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 610-616
    • Pickart, C.M.1    Fushman, D.2
  • 55
    • 77956903406 scopus 로고    scopus 로고
    • Engineered diubiquitin synthesis reveals Lys29-isopeptide specificity of an OTU deubiquitinase
    • doi: 10.1038/nchembio.426
    • Virdee S, Ye Y, Nguyen DP, Komander D, Chin JW, (2010) Engineered diubiquitin synthesis reveals Lys29-isopeptide specificity of an OTU deubiquitinase. Nat Chem Biol 6: 750-757. doi:10.1038/nchembio.426. PubMed: 20802491.
    • (2010) Nat Chem Biol , vol.6 , pp. 750-757
    • Virdee, S.1    Ye, Y.2    Nguyen, D.P.3    Komander, D.4    Chin, J.W.5
  • 56
    • 10844221661 scopus 로고    scopus 로고
    • A genomic perspective of protein kinases in Plasmodium falciparum
    • PubMed: 15515182
    • Anamika, Srinivasan N, Krupa A, (2005) A genomic perspective of protein kinases in Plasmodium falciparum. Proteins 58: 180-189. PubMed: 15515182.
    • (2005) Proteins , vol.58 , pp. 180-189
    • Anamika1    Srinivasan, N.2    Krupa, A.3
  • 57
    • 9144258616 scopus 로고    scopus 로고
    • Protein kinases of the human malaria parasite Plasmodium falciparum: the kinome of a divergent eukaryote
    • doi: 10.1186/1471-2164-5-79
    • Ward P, Equinet L, Packer J, Doerig C, (2004) Protein kinases of the human malaria parasite Plasmodium falciparum: the kinome of a divergent eukaryote. BMC Genomics 5: 79. doi:10.1186/1471-2164-5-79. PubMed: 15479470.
    • (2004) BMC Genomics , vol.5 , pp. 79
    • Ward, P.1    Equinet, L.2    Packer, J.3    Doerig, C.4
  • 58
    • 70349293594 scopus 로고    scopus 로고
    • Post-translational modifications in Plasmodium: more than you think!
    • doi: 10.1016/j.molbiopara.2009.08.001
    • Chung DW, Ponts N, Cervantes S, Le Roch, (2009) Post-translational modifications in Plasmodium: more than you think! Mol Biochem Parasitol 168: 123-134. doi:10.1016/j.molbiopara.2009.08.001. PubMed: 19666057.
    • (2009) Mol Biochem Parasitol , vol.168 , pp. 123-134
    • Chung, D.W.1    Ponts, N.2    Cervantes, S.3    Roch, L.4
  • 59
    • 80054901700 scopus 로고    scopus 로고
    • The Phosphoproteomes of Plasmodium falciparum and Toxoplasma gondii Reveal Unusual Adaptations Within and Beyond the Parasites' Boundaries
    • doi: 10.1016/j.chom.2011.09.004
    • Treeck M, Sanders JL, Elias JE, Boothroyd JC, (2011) The Phosphoproteomes of Plasmodium falciparum and Toxoplasma gondii Reveal Unusual Adaptations Within and Beyond the Parasites' Boundaries. Cell Host Microbe 10: 410-419. doi:10.1016/j.chom.2011.09.004. PubMed: 22018241.
    • (2011) Cell Host Microbe , vol.10 , pp. 410-419
    • Treeck, M.1    Sanders, J.L.2    Elias, J.E.3    Boothroyd, J.C.4
  • 60
    • 24044547036 scopus 로고    scopus 로고
    • Regulating the regulators: control of protein ubiquitination and ubiquitin-like modifications by extracellular stimuli
    • doi: 10.1016/j.molcel.2005.08.017
    • Gao M, Karin M, (2005) Regulating the regulators: control of protein ubiquitination and ubiquitin-like modifications by extracellular stimuli. Mol Cell 19: 581-593. doi:10.1016/j.molcel.2005.08.017. PubMed: 16137616.
    • (2005) Mol Cell , vol.19 , pp. 581-593
    • Gao, M.1    Karin, M.2
  • 61
    • 0035812709 scopus 로고    scopus 로고
    • Phosphorylation-dependent ubiquitination of cyclin E by the SCFFbw7 ubiquitin ligase
    • doi: 10.1126/science.1065203
    • Koepp DM, Schaefer LK, Ye X, Keyomarsi K, Chu C, et al. (2001) Phosphorylation-dependent ubiquitination of cyclin E by the SCFFbw7 ubiquitin ligase. Science 294: 173-177. doi:10.1126/science.1065203. PubMed: 11533444.
    • (2001) Science , vol.294 , pp. 173-177
    • Koepp, D.M.1    Schaefer, L.K.2    Ye, X.3    Keyomarsi, K.4    Chu, C.5
  • 62
    • 12344310195 scopus 로고    scopus 로고
    • Preferred in vivo ubiquitination sites
    • doi: 10.1093/bioinformatics/bth407
    • Catic A, Collins C, Church GM, Ploegh HL, (2004) Preferred in vivo ubiquitination sites. Bioinformatics 20: 3302-3307. doi:10.1093/bioinformatics/bth407. PubMed: 15256413.
    • (2004) Bioinformatics , vol.20 , pp. 3302-3307
    • Catic, A.1    Collins, C.2    Church, G.M.3    Ploegh, H.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.