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Volumn 5, Issue 1, 2012, Pages

Spliced leader RNA silencing (SLS) - A programmed cell death pathway in Trypanosoma brucei that is induced upon ER stress

Author keywords

ER quality control; Programmed cell death; Spliced leader silencing; Translocation to the ER; Unfolded protein response

Indexed keywords

ALPHA MANNOSIDASE; BIM PROTEIN; CALNEXIN; CALRETICULIN; GLUCOSIDASE; GLUCOSYLTRANSFERASE; GLYCAN; PROTEIN BCL 2; RNA BINDING PROTEIN; SPLICED LEADER RNA; STRESS ACTIVATED PROTEIN KINASE; TRANSCRIPTION FACTOR; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; URIDINE DIPHOSPHATE GLUCOSE;

EID: 84861604014     PISSN: None     EISSN: 17563305     Source Type: Journal    
DOI: 10.1186/1756-3305-5-107     Document Type: Review
Times cited : (22)

References (83)
  • 1
    • 43249109174 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress responses
    • 10.1007/s00018-007-7383-5 18038217
    • Endoplasmic reticulum stress responses. Schroder M, Cell Mol Life Sci 2008 65 862 894 10.1007/s00018-007-7383-5 18038217
    • (2008) Cell Mol Life Sci , vol.65 , pp. 862-894
    • Schroder, M.1
  • 2
    • 34047155622 scopus 로고    scopus 로고
    • Spliced-leader RNA silencing: A novel stress-induced mechanism in Trypanosoma brucei
    • DOI 10.1038/sj.embor.7400930, PII 7400930
    • Spliced-leader RNA silencing: a novel stress-induced mechanism in Trypanosoma brucei. Lustig Y, Sheiner L, Vagima Y, Goldshmidt H, Das A, Bellofatto V, Michaeli S, EMBO Rep 2007 8 408 413 10.1038/sj.embor.7400930 17347669 (Pubitemid 46511043)
    • (2007) EMBO Reports , vol.8 , Issue.4 , pp. 408-413
    • Lustig, Y.1    Sheiner, L.2    Vagima, Y.3    Goldshmidt, H.4    Das, A.5    Bellofatto, V.6    Michaeli, S.7
  • 3
    • 0142247085 scopus 로고    scopus 로고
    • Trans and cis splicing in trypanosomatids: Mechanism, factors, and regulation
    • DOI 10.1128/EC.2.5.830-840.2003
    • trans and cis splicing in Trypanosomatids: mechanism, factors, and regulation. Liang XH, Haritan A, Uliel S, Michaeli S, Eukaryot Cell 2003 2 830 840 10.1128/EC.2.5.830-840.2003 14555465 (Pubitemid 37298696)
    • (2003) Eukaryotic Cell , vol.2 , Issue.5 , pp. 830-840
    • Liang, X.-H.1    Haritan, A.2    Uliel, S.3    Michaeli, S.4
  • 4
    • 78149292214 scopus 로고    scopus 로고
    • The transcriptome of the human pathogen Trypanosoma brucei at single-nucleotide resolution
    • 10.1371/journal.ppat.1001090 20838601
    • The transcriptome of the human pathogen Trypanosoma brucei at single-nucleotide resolution. Kolev NG, Franklin JB, Carmi S, Shi H, Michaeli S, Tschudi C, PLoS Pathog 2010 6 9 1001090 10.1371/journal.ppat.1001090 20838601
    • (2010) PLoS Pathog , vol.6 , Issue.9 , pp. 51001090
    • Kolev, N.G.1    Franklin, J.B.2    Carmi, S.3    Shi, H.4    Michaeli, S.5    Tschudi, C.6
  • 5
    • 79955619183 scopus 로고    scopus 로고
    • Trans-splicing in trypanosomes: Machinery and its impact on the parasite transcriptome
    • 10.2217/fmb.11.20 21526946
    • Trans-splicing in trypanosomes: machinery and its impact on the parasite transcriptome. Michaeli S, Future Microbiol 2011 6 459 474 10.2217/fmb.11.20 21526946
    • (2011) Future Microbiol , vol.6 , pp. 459-474
    • Michaeli, S.1
  • 6
    • 77956841596 scopus 로고    scopus 로고
    • The pre-mRNA splicing machinery of trypanosomes: Complex or simplified?
    • 10.1128/EC.00113-10 20581293
    • The pre-mRNA splicing machinery of trypanosomes: complex or simplified? Gunzl A, Eukaryot Cell 2010 9 1159 1170 10.1128/EC.00113-10 20581293
    • (2010) Eukaryot Cell , vol.9 , pp. 1159-1170
    • Gunzl, A.1
  • 7
    • 40949097695 scopus 로고    scopus 로고
    • RNA polymerase transcription machinery in trypanosomes
    • DOI 10.1128/EC.00297-07
    • RNA polymerase transcription machinery in trypanosomes. Das A, Banday M, Bellofatto V, Eukaryot Cell 2008 7 429 434 10.1128/EC.00297-07 17951525 (Pubitemid 351959670)
    • (2008) Eukaryotic Cell , vol.7 , Issue.3 , pp. 429-434
    • Das, A.1    Banday, M.2    Bellofatto, V.3
  • 8
    • 57649137959 scopus 로고    scopus 로고
    • Role of protein translocation pathways across the ER in Trypanosoma brucei
    • 10.1074/jbc.M801499200 18768469
    • Role of protein translocation pathways across the ER in Trypanosoma brucei. Goldshmidt H, Sheiner L, Butikofer P, Roditi I, Uliel S, Gunzel M, Engstler M, Michaeli S, J Biol Chem 2008 283 46 32085 32098 10.1074/jbc. M801499200 18768469
    • (2008) J Biol Chem , vol.283 , Issue.46 , pp. 32085-32098
    • Goldshmidt, H.1    Sheiner, L.2    Butikofer, P.3    Roditi, I.4    Uliel, S.5    Gunzel, M.6    Engstler, M.7    Michaeli, S.8
  • 9
    • 77649219141 scopus 로고    scopus 로고
    • Persistent ER stress induces the spliced leader RNA silencing pathway (SLS), leading to programmed cell death in Trypanosoma brucei
    • 10.1371/journal.ppat.1000731 20107599
    • Persistent ER stress induces the spliced leader RNA silencing pathway (SLS), leading to programmed cell death in Trypanosoma brucei. Goldshmidt H, Matas D, Kabi A, Carmi S, Hope R, Michaeli S, PLoS Pathog 2010 6 1000731 10.1371/journal.ppat.1000731 20107599
    • (2010) PLoS Pathog , vol.6 , pp. 51000731
    • Goldshmidt, H.1    Matas, D.2    Kabi, A.3    Carmi, S.4    Hope, R.5    Michaeli, S.6
  • 11
    • 33845480131 scopus 로고    scopus 로고
    • Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response
    • DOI 10.1371/journal.pbio.0040423
    • Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response. Bernales S, McDonald KL, Walter P, PLoS Biol 2006 4 423 10.1371/journal.pbio.0040423 17132049 (Pubitemid 44917620)
    • (2006) PLoS Biology , vol.4 , Issue.12 , pp. 2311-2324
    • Bernales, S.1    McDonald, K.L.2    Walter, P.3
  • 12
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • DOI 10.1038/nrm2199, PII NRM2199
    • Signal integration in the endoplasmic reticulum unfolded protein response. Ron D, Walter P, Nat Rev Mol Cell Biol 2007 8 519 529 10.1038/nrm2199 17565364 (Pubitemid 46985379)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.7 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 13
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: Controlling cell fate decisions under ER stress and beyond
    • 22251901
    • The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Hetz C, Nat Rev Mol Cell Biol 2012 13 89 102 22251901
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 89-102
    • Hetz, C.1
  • 14
    • 80054026314 scopus 로고    scopus 로고
    • A review of the mammalian unfolded protein response
    • 10.1002/bit.23282 21809331
    • A review of the mammalian unfolded protein response. Chakrabarti A, Chen AW, Varner JD, Biotechnol Bioeng 2011 108 2777 2793 10.1002/bit.23282 21809331
    • (2011) Biotechnol Bioeng , vol.108 , pp. 2777-2793
    • Chakrabarti, A.1    Chen, A.W.2    Varner, J.D.3
  • 15
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • DOI 10.1038/nrm1052
    • Quality control in the endoplasmic reticulum. Ellgaard L, Helenius A, Nat Rev Mol Cell Biol 2003 4 181 191 12612637 (Pubitemid 36288040)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.3 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 16
    • 21744447192 scopus 로고    scopus 로고
    • The glycan code of the endoplasmic reticulum: Asparagine-linked carbohydrates as protein maturation and quality-control tags
    • DOI 10.1016/j.tcb.2005.05.007, PII S0962892405001327
    • The glycan code of the endoplasmic reticulum: asparagine-linked carbohydrates as protein maturation and quality-control tags. Hebert DN, Garman SC, Molinari M, Trends Cell Biol 2005 15 364 370 10.1016/j.tcb.2005.05.007 15939591 (Pubitemid 40943525)
    • (2005) Trends in Cell Biology , vol.15 , Issue.7 , pp. 364-370
    • Hebert, D.N.1    Garman, S.C.2    Molinari, M.3
  • 17
    • 0029934119 scopus 로고    scopus 로고
    • Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes
    • Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. Hebert DN, Foellmer B, Helenius A, EMBO J 1996 15 2961 2968 8670797 (Pubitemid 26187744)
    • (1996) EMBO Journal , vol.15 , Issue.12 , pp. 2961-2968
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 19
    • 0038080911 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors. Role of ATP binding site in suppression of caspase-7 activation
    • DOI 10.1074/jbc.M212328200
    • Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: role of ATP binding site in suppression of caspase-7 activation. Reddy RK, Mao C, Baumeister P, Austin RC, Kaufman RJ, Lee AS, J Biol Chem 2003 278 20915 20924 10.1074/jbc.M212328200 12665508 (Pubitemid 36806399)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.23 , pp. 20915-20924
    • Reddy, R.K.1    Mao, C.2    Baumeister, P.3    Austin, R.C.4    Kaufman, R.J.5    Lee, A.S.6
  • 20
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • 10.1038/35014014 10854322
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Bertolotti A, Zhang Y, Hendershot LM, Harding HP, Ron D, Nat Cell Biol 2000 2 326 332 10.1038/35014014 10854322
    • (2000) Nat Cell Biol , vol.2 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 21
    • 34250794495 scopus 로고    scopus 로고
    • XBP1 controls diverse cell type- and condition-specific transcriptional regulatory networks
    • DOI 10.1016/j.molcel.2007.06.011, PII S1097276507004005
    • XBP1 controls diverse cell type- and condition-specific transcriptional regulatory networks. Acosta-Alvear D, Zhou Y, Blais A, Tsikitis M, Lents NH, Arias C, Lennon CJ, Kluger Y, Dynlacht BD, Mol Cell 2007 27 53 66 10.1016/j.molcel.2007.06.011 17612490 (Pubitemid 46991391)
    • (2007) Molecular Cell , vol.27 , Issue.1 , pp. 53-66
    • Acosta-Alvear, D.1    Zhou, Y.2    Blais, A.3    Tsikitis, M.4    Lents, N.H.5    Arias, C.6    Lennon, C.J.7    Kluger, Y.8    Dynlacht, B.D.9
  • 22
    • 33745893809 scopus 로고    scopus 로고
    • Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response
    • DOI 10.1126/science.1129631
    • Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response. Hollien J, Weissman JS, Science 2006 313 104 107 10.1126/science.1129631 16825573 (Pubitemid 44051264)
    • (2006) Science , vol.313 , Issue.5783 , pp. 104-107
    • Hollien, J.1    Weissman, J.S.2
  • 23
    • 68549092781 scopus 로고    scopus 로고
    • Regulated Ire1-dependent decay of messenger RNAs in mammalian cells
    • 10.1083/jcb.200903014 19651891
    • Regulated Ire1-dependent decay of messenger RNAs in mammalian cells. Hollien J, Lin JH, Li H, Stevens N, Walter P, Weissman JS, J Cell Biol 2009 186 323 331 10.1083/jcb.200903014 19651891
    • (2009) J Cell Biol , vol.186 , pp. 323-331
    • Hollien, J.1    Lin, J.H.2    Li, H.3    Stevens, N.4    Walter, P.5    Weissman, J.S.6
  • 24
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of golgi localization signals
    • DOI 10.1016/S1534-5807(02)00203-4
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Shen J, Chen X, Hendershot L, Prywes R, Dev Cell 2002 3 99 111 10.1016/S1534-5807(02)00203-4 12110171 (Pubitemid 34778399)
    • (2002) Developmental Cell , vol.3 , Issue.1 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 25
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • 10.1016/S0092-8674(00)80835-1 10847680
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Travers KJ, Patil CK, Wodicka L, Lockhart DJ, Weissman JS, Walter P, Cell 2000 101 249 258 10.1016/S0092-8674(00)80835-1 10847680
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3    Lockhart, D.J.4    Weissman, J.S.5    Walter, P.6
  • 26
    • 34548172495 scopus 로고    scopus 로고
    • Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1
    • DOI 10.1016/j.devcel.2007.07.018, PII S1534580707003000
    • Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1. Yamamoto K, Sato T, Matsui T, Sato M, Okada T, Yoshida H, Harada A, Mori K, Dev Cell 2007 13 365 376 10.1016/j.devcel.2007.07.018 17765680 (Pubitemid 47308680)
    • (2007) Developmental Cell , vol.13 , Issue.3 , pp. 365-376
    • Yamamoto, K.1    Sato, T.2    Matsui, T.3    Sato, M.4    Okada, T.5    Yoshida, H.6    Harada, A.7    Mori, K.8
  • 27
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic- reticulum-resident kinase
    • DOI 10.1038/16729
    • Protein translation and folding are coupled by an endoplasmic-reticulum- resident kinase. Harding HP, Zhang Y, Ron D, Nature 1999 397 271 274 10.1038/16729 9930704 (Pubitemid 29051178)
    • (1999) Nature , vol.397 , Issue.6716 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 28
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • DOI 10.1146/annurev.biochem.73.011303.074134
    • The mammalian unfolded protein response. Schroder M, Kaufman RJ, Annu Rev Biochem 2005 74 739 789 10.1146/annurev.biochem.73.011303.074134 15952902 (Pubitemid 40995523)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 30
    • 0034808081 scopus 로고    scopus 로고
    • Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1
    • DOI 10.1128/MCB.21.20.6841-6850.2001
    • Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1. Connor JH, Weiser DC, Li S, Hallenbeck JM, Shenolikar S, Mol Cell Biol 2001 21 6841 6850 10.1128/MCB.21.20.6841-6850.2001 11564868 (Pubitemid 32911245)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.20 , pp. 6841-6850
    • Connor, J.H.1    Weiser, D.C.2    Li, S.3    Hallenbeck, J.M.4    Shenolikar, S.5
  • 31
    • 33749579383 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress triggers autophagy
    • DOI 10.1074/jbc.M607007200
    • Endoplasmic reticulum stress triggers autophagy. Yorimitsu T, Nair U, Yang Z, Klionsky DJ, J Biol Chem 2006 281 30299 30304 10.1074/jbc.M607007200 16901900 (Pubitemid 44537037)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.40 , pp. 30299-30304
    • Yorimitsu, T.1    Nair, U.2    Yang, Z.3    Klionsky, D.J.4
  • 32
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • DOI 10.1126/science.287.5453.664
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Urano F, Wang X, Bertolotti A, Zhang Y, Chung P, Harding HP, Ron D, Science 2000 287 664 666 10.1126/science.287.5453.664 10650002 (Pubitemid 30070916)
    • (2000) Science , vol.287 , Issue.5453 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, H.P.6    Ron, D.7
  • 35
    • 44949237240 scopus 로고    scopus 로고
    • JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy
    • DOI 10.1016/j.molcel.2008.06.001, PII S1097276508003894
    • JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy. Wei Y, Pattingre S, Sinha S, Bassik M, Levine B, Mol Cell 2008 30 678 688 10.1016/j.molcel.2008.06.001 18570871 (Pubitemid 351818252)
    • (2008) Molecular Cell , vol.30 , Issue.6 , pp. 678-688
    • Wei, Y.1    Pattingre, S.2    Sinha, S.3    Bassik, M.4    Levine, B.5
  • 37
    • 0031993255 scopus 로고    scopus 로고
    • Bax inhibitor-1, a mammalian apoptosis suppressor identified by functional screening in yeast
    • Bax inhibitor-1, a mammalian apoptosis suppressor identified by functional screening in yeast. Xu Q, Reed JC, Mol Cell 1998 1 337 346 10.1016/S1097-2765(00)80034-9 9660918 (Pubitemid 128378882)
    • (1998) Molecular Cell , vol.1 , Issue.3 , pp. 337-346
    • Xu, Q.1    Reed, J.C.2
  • 39
    • 62549154503 scopus 로고    scopus 로고
    • Intricate links between ER stress and apoptosis
    • 10.1016/j.molcel.2009.03.002 19328058
    • Intricate links between ER stress and apoptosis. Madeo F, Kroemer G, Mol Cell 2009 33 669 670 10.1016/j.molcel.2009.03.002 19328058
    • (2009) Mol Cell , vol.33 , pp. 669-670
    • Madeo, F.1    Kroemer, G.2
  • 41
    • 0035947778 scopus 로고    scopus 로고
    • Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2α
    • DOI 10.1083/jcb.153.5.1011
    • Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha. Novoa I, Zeng H, Harding HP, Ron D, J Cell Biol 2001 153 1011 1022 10.1083/jcb.153.5.1011 11381086 (Pubitemid 34289240)
    • (2001) Journal of Cell Biology , vol.153 , Issue.5 , pp. 1011-1021
    • Novoa, I.1    Zeng, H.2    Harding, H.P.3    Ron, D.4
  • 43
    • 33751069967 scopus 로고    scopus 로고
    • Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins
    • DOI 10.1371/journal.pbio.0040374
    • Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins. Rutkowski DT, Arnold SM, Miller CN, Wu J, Li J, Gunnison KM, Mori K, Sadighi Akha AA, Raden D, Kaufman RJ, PLoS Biol 2006 4 374 10.1371/journal.pbio.0040374 17090218 (Pubitemid 44760017)
    • (2006) PLoS Biology , vol.4 , Issue.11 , pp. 2024-2041
    • Rutkowski, D.T.1    Arnold, S.M.2    Miller, C.N.3    Wu, J.4    Li, J.5    Gunnison, K.M.6    Mori, K.7    Akha, A.A.S.8    Raden, D.9    Kaufman, R.J.10
  • 44
    • 79952264011 scopus 로고    scopus 로고
    • Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress
    • 10.1038/ncb0311-184 21364565
    • Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress. Tabas I, Ron D, Nat Cell Biol 2011 13 184 190 10.1038/ncb0311-184 21364565
    • (2011) Nat Cell Biol , vol.13 , pp. 184-190
    • Tabas, I.1    Ron, D.2
  • 45
  • 46
    • 35349012982 scopus 로고    scopus 로고
    • Post-transcriptional regulation of gene expression in trypanosomes and leishmanias
    • DOI 10.1016/j.molbiopara.2007.07.007, PII S0166685107002101
    • Post-transcriptional regulation of gene expression in trypanosomes and leishmanias. Clayton C, Shapira M, Mol Biochem Parasitol 2007 156 93 101 10.1016/j.molbiopara.2007.07.007 17765983 (Pubitemid 47600362)
    • (2007) Molecular and Biochemical Parasitology , vol.156 , Issue.2 , pp. 93-101
    • Clayton, C.1    Shapira, M.2
  • 47
    • 78650533544 scopus 로고    scopus 로고
    • Trans-acting proteins regulating mRNA maturation, stability and translation in trypanosomatids
    • 10.1016/j.pt.2010.06.011 20609625
    • Trans-acting proteins regulating mRNA maturation, stability and translation in trypanosomatids. Kramer S, Carrington M, Trends Parasitol 2011 27 23 30 10.1016/j.pt.2010.06.011 20609625
    • (2011) Trends Parasitol , vol.27 , pp. 23-30
    • Kramer, S.1    Carrington, M.2
  • 48
    • 77958123318 scopus 로고    scopus 로고
    • Spliced leader trapping reveals widespread alternative splicing patterns in the highly dynamic transcriptome of Trypanosoma brucei
    • 10.1371/journal.ppat.1001037 20700444
    • Spliced leader trapping reveals widespread alternative splicing patterns in the highly dynamic transcriptome of Trypanosoma brucei. Nilsson D, Gunasekera K, Mani J, Osteras M, Farinelli L, Baerlocher L, Roditi I, Ochsenreiter T, PLoS Pathog 2010 6 8 1001037 10.1371/journal.ppat.1001037 20700444
    • (2010) PLoS Pathog , vol.6 , Issue.8 , pp. 51001037
    • Nilsson, D.1    Gunasekera, K.2    Mani, J.3    Osteras, M.4    Farinelli, L.5    Baerlocher, L.6    Roditi, I.7    Ochsenreiter, T.8
  • 49
    • 80052924614 scopus 로고    scopus 로고
    • Gene expression in Trypanosoma brucei: Lessons from high-throughput RNA sequencing
    • 10.1016/j.pt.2011.05.006 21737348
    • Gene expression in Trypanosoma brucei: lessons from high-throughput RNA sequencing. Siegel TN, Gunasekera K, Cross GA, Ochsenreiter T, Trends Parasitol 2011 27 10 434 441 10.1016/j.pt.2011.05.006 21737348
    • (2011) Trends Parasitol , vol.27 , Issue.10 , pp. 434-441
    • Siegel, T.N.1    Gunasekera, K.2    Cross, G.A.3    Ochsenreiter, T.4
  • 50
    • 47149105277 scopus 로고    scopus 로고
    • The trypanosome transcriptome is remodelled during differentiation but displays limited responsiveness within life stages
    • DOI 10.1186/1471-2164-9-298
    • The trypanosome transcriptome is remodelled during differentiation but displays limited responsiveness within life stages. Koumandou VL, Natesan SK, Sergeenko T, Field MC, BMC Genomics 2008 9 298 10.1186/1471-2164-9-298 18573209 (Pubitemid 351974290)
    • (2008) BMC Genomics , vol.9 , pp. 298
    • Koumando, V.L.1    Natesan, S.K.A.2    Sergeenko, T.3    Field, M.C.4
  • 51
    • 63649161943 scopus 로고    scopus 로고
    • The ubiquitylation machinery of the endoplasmic reticulum
    • 10.1038/nature07962 19325625
    • The ubiquitylation machinery of the endoplasmic reticulum. Hirsch C, Gauss R, Horn SC, Neuber O, Sommer T, Nature 2009 458 453 460 10.1038/nature07962 19325625
    • (2009) Nature , vol.458 , pp. 453-460
    • Hirsch, C.1    Gauss, R.2    Horn, S.C.3    Neuber, O.4    Sommer, T.5
  • 52
    • 0032065335 scopus 로고    scopus 로고
    • The quality control of glycoprotein folding in the endoplasmic reticulum, a trip from trypanosomes to mammals
    • The quality control of glycoprotein folding in the endoplasmic reticulum, a trip from trypanosomes to mammals. Parodi AJ, Braz J Med Biol Res 1998 31 601 614 9698764 (Pubitemid 128526520)
    • (1998) Brazilian Journal of Medical and Biological Research , vol.31 , Issue.5 , pp. 601-614
    • Parodi, A.J.1
  • 53
    • 34447537881 scopus 로고    scopus 로고
    • Intracellular transport systems in trypanosomes: Function, evolution and virulence
    • Horizon Scientific Press, Wymondham, UK. Barry JD, Mottram J, McCulloch R, Acosta-Serrano A Chapter 9
    • Intracellular transport systems in trypanosomes: function, evolution and virulence. Engstler M, Bangs JD, Field MC, Trypanosomes-after the genome Horizon Scientific Press, Wymondham, UK., Barry JD, Mottram J, McCulloch R, Acosta-Serrano A, 2006 281 317 Chapter 9
    • (2006) Trypanosomes - After the Genome , pp. 281-317
    • Engstler, M.1    Bangs, J.D.2    Field, M.C.3
  • 54
    • 77649088404 scopus 로고    scopus 로고
    • Chaperone requirements for biosynthesis of the trypanosome variant surface glycoprotein
    • 10.1371/journal.pone.0008468 20052285
    • Chaperone requirements for biosynthesis of the trypanosome variant surface glycoprotein. Field MC, Sergeenko T, Wang YN, Bohm S, Carrington M, PLoS One 2010 5 8468 10.1371/journal.pone.0008468 20052285
    • (2010) PLoS One , vol.5 , pp. 58468
    • Field, M.C.1    Sergeenko, T.2    Wang, Y.N.3    Bohm, S.4    Carrington, M.5
  • 55
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • DOI 10.1038/nature06384, PII NATURE06384
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Rapoport TA, Nature 2007 450 663 669 10.1038/nature06384 18046402 (Pubitemid 350207698)
    • (2007) Nature , vol.450 , Issue.7170 , pp. 663-669
    • Rapoport, T.A.1
  • 56
    • 35348872673 scopus 로고    scopus 로고
    • Down-regulation of the trypanosomatid signal recognition particle affects the biogenesis of polytopic membrane proteins but not of signal peptide-containing proteins
    • DOI 10.1128/EC.00134-07
    • Down-regulation of the trypanosomatid signal recognition particle affects the biogenesis of polytopic membrane proteins but not of signal peptide-containing proteins. Lustig Y, Vagima Y, Goldshmidt H, Erlanger A, Ozeri V, Vince J, McConville MJ, Dwyer DM, Landfear SM, Michaeli S, Eukaryot Cell 2007 6 1865 1875 10.1128/EC.00134-07 17715370 (Pubitemid 47585575)
    • (2007) Eukaryotic Cell , vol.6 , Issue.10 , pp. 1865-1875
    • Lustig, Y.1    Vagima, Y.2    Goldshmidt, H.3    Erlanger, A.4    Ozeri, V.5    Vince, J.6    McConville, M.J.7    Dwyer, D.M.8    Landfear, S.M.9    Michaeli, S.10
  • 57
    • 0037033097 scopus 로고    scopus 로고
    • RNA interference of signal peptide-binding protein SRP54 elicits deleterious effects and protein sorting defects in trypanosomes
    • DOI 10.1074/jbc.M207736200
    • RNA interference of signal peptide-binding protein SRP54 elicits deleterious effects and protein sorting defects in trypanosomes. Liu L, Liang XH, Uliel S, Unger R, Ullu E, Michaeli S, J Biol Chem 2002 277 47348 47357 10.1074/jbc.M207736200 12244113 (Pubitemid 36159249)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.49 , pp. 47348-47357
    • Liu, L.1    Liang, X.-H.2    Uliel, S.3    Unger, R.4    Ullu, E.5    Michaeli, S.6
  • 58
    • 27644589630 scopus 로고    scopus 로고
    • The Trypanosoma brucei signal recognition particle lacks the Alu-domain-binding proteins: Purification and functional analysis of its binding proteins by RNAi
    • DOI 10.1242/jcs.02578
    • The Trypanosoma brucei signal recognition particle lacks the Alu-domain-binding proteins: purification and functional analysis of its binding proteins by RNAi. Lustig Y, Goldshmidt H, Uliel S, Michaeli S, J Cell Sci 2005 118 4551 4562 10.1242/jcs.02578 16179612 (Pubitemid 41556351)
    • (2005) Journal of Cell Science , vol.118 , Issue.19 , pp. 4551-4562
    • Lustig, Y.1    Goldshmidt, H.2    Uliel, S.3    Michaeli, S.4
  • 59
    • 62549158711 scopus 로고    scopus 로고
    • Multiple roles for polypyrimidine tract binding (PTB) proteins in trypanosome RNA metabolism
    • 10.1261/rna.1230209 19218552
    • Multiple roles for polypyrimidine tract binding (PTB) proteins in trypanosome RNA metabolism. Stern MZ, Gupta SK, Salmon-Divon M, Haham T, Barda O, Levi S, Wachtel C, Nilsen TW, Michaeli S, RNA 2009 15 648 665 10.1261/rna.1230209 19218552
    • (2009) RNA , vol.15 , pp. 648-665
    • Stern, M.Z.1    Gupta, S.K.2    Salmon-Divon, M.3    Haham, T.4    Barda, O.5    Levi, S.6    Wachtel, C.7    Nilsen, T.W.8    Michaeli, S.9
  • 63
    • 0037330831 scopus 로고    scopus 로고
    • Necrosis: A specific form of programmed cell death?
    • DOI 10.1016/S0014-4827(02)00027-7
    • Necrosis: a specific form of programmed cell death? Proskuryakov SY, Konoplyannikov AG, Gabai VL, Exp Cell Res 2003 283 1 16 10.1016/S0014-4827(02) 00027-7 12565815 (Pubitemid 36259891)
    • (2003) Experimental Cell Research , vol.283 , Issue.1 , pp. 1-16
    • Proskuryakov, S.Ya.1    Konoplyannikov, A.G.2    Gabai, V.L.3
  • 64
    • 0034801843 scopus 로고    scopus 로고
    • Caspase-independent apoptotic pathways in T lymphocytes: A minireview
    • DOI 10.1023/A:1011390103783
    • Caspase-independent apoptotic pathways in T lymphocytes: a minireview. Bidere N, Senik A, Apoptosis 2001 6 371 375 10.1023/A:1011390103783 11483861 (Pubitemid 32910878)
    • (2001) Apoptosis , vol.6 , Issue.5 , pp. 371-375
    • Bidere, N.1    Senik, A.2
  • 65
    • 33749074492 scopus 로고    scopus 로고
    • Death of a trypanosome: A selfish altruism
    • DOI 10.1016/j.pt.2006.08.010, PII S1471492206002157
    • Death of a trypanosome: a selfish altruism. Duszenko M, Figarella K, Macleod ET, Welburn SC, Trends Parasitol 2006 22 536 542 10.1016/j.pt.2006.08. 010 16942915 (Pubitemid 44466530)
    • (2006) Trends in Parasitology , vol.22 , Issue.11 , pp. 536-542
    • Duszenko, M.1    Figarella, K.2    Macleod, E.T.3    Welburn, S.C.4
  • 66
    • 77956882084 scopus 로고    scopus 로고
    • Programmed cell death in unicellular parasites: A prerequisite for sustained infection?
    • 10.1016/j.pt.2010.06.008 20591738
    • Programmed cell death in unicellular parasites: a prerequisite for sustained infection? van Zandbergen G, Luder CG, Heussler V, Duszenko M, Trends Parasitol 2010 26 477 483 10.1016/j.pt.2010.06.008 20591738
    • (2010) Trends Parasitol , vol.26 , pp. 477-483
    • Van Zandbergen, G.1    Luder, C.G.2    Heussler, V.3    Duszenko, M.4
  • 68
    • 78349249826 scopus 로고    scopus 로고
    • Targeting essential pathways in trypanosomatids gives insights into protozoan mechanisms of cell death
    • 10.1186/1756-3305-3-107 21083891
    • Targeting essential pathways in trypanosomatids gives insights into protozoan mechanisms of cell death. Smirlis D, Duszenko M, Ruiz AJ, Scoulica E, Bastien P, Fasel N, Soteriadou K, Parasit Vectors 2010 3 107 10.1186/1756-3305-3-107 21083891
    • (2010) Parasit Vectors , vol.3 , pp. 107
    • Smirlis, D.1    Duszenko, M.2    Ruiz, A.J.3    Scoulica, E.4    Bastien, P.5    Fasel, N.6    Soteriadou, K.7
  • 69
    • 33748697633 scopus 로고    scopus 로고
    • Prostaglandin-induced programmed cell death in Trypanosoma brucei involves oxidative stress
    • DOI 10.1038/sj.cdd.4401862, PII 4401862
    • Prostaglandin-induced programmed cell death in Trypanosoma brucei involves oxidative stress. Figarella K, Uzcategui NL, Beck A, Schoenfeld C, Kubata BK, Lang F, Duszenko M, Cell Death Differ 2006 13 1802 1814 10.1038/sj.cdd.4401862 16456581 (Pubitemid 44390866)
    • (2006) Cell Death and Differentiation , vol.13 , Issue.10 , pp. 1802-1814
    • Figarella, K.1    Uzcategui, N.L.2    Beck, A.3    Schoenfeld, C.4    Kubata, B.K.5    Lang, F.6    Duszenko, M.7
  • 71
    • 0034987789 scopus 로고    scopus 로고
    • The acidocalcisome
    • DOI 10.1016/S0166-6851(01)00246-8, PII S0166685101002468
    • The acidocalcisome. Docampo R, Moreno SN, Mol Biochem Parasitol 2001 114 151 159 10.1016/S0166-6851(01)00246-8 11378195 (Pubitemid 32510752)
    • (2001) Molecular and Biochemical Parasitology , vol.114 , Issue.2 , pp. 151-159
    • Docampo, R.1    Moreno, S.N.J.2
  • 72
    • 54949110895 scopus 로고    scopus 로고
    • Calcium and apoptosis: ER-mitochondria Ca2+ transfer in the control of apoptosis
    • 10.1038/onc.2008.308 18955969
    • Calcium and apoptosis: ER-mitochondria Ca2+ transfer in the control of apoptosis. Pinton P, Giorgi C, Siviero R, Zecchini E, Rizzuto R, Oncogene 2008 27 6407 6418 10.1038/onc.2008.308 18955969
    • (2008) Oncogene , vol.27 , pp. 6407-6418
    • Pinton, P.1    Giorgi, C.2    Siviero, R.3    Zecchini, E.4    Rizzuto, R.5
  • 73
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • DOI 10.1038/20959
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Shimizu S, Narita M, Tsujimoto Y, Nature 1999 399 483 487 10.1038/20959 10365962 (Pubitemid 29258855)
    • (1999) Nature , vol.399 , Issue.6735 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 74
    • 39049149816 scopus 로고    scopus 로고
    • The role of mitochondria in apoptosis
    • 10.5483/BMBRep.2008.41.1.011 18304445
    • The role of mitochondria in apoptosis. Jeong SY, Seol DW, BMB Rep 2008 41 11 22 10.5483/BMBRep.2008.41.1.011 18304445
    • (2008) BMB Rep , vol.41 , pp. 11-22
    • Jeong, S.Y.1    Seol, D.W.2
  • 75
    • 79959213375 scopus 로고    scopus 로고
    • Promastigote to amastigote differentiation of Leishmania is markedly delayed in the absence of PERK eIF2alpha kinase-dependent eIF2alpha phosphorylation
    • 10.1111/j.1462-5822.2011.01602.x 21624030
    • Promastigote to amastigote differentiation of Leishmania is markedly delayed in the absence of PERK eIF2alpha kinase-dependent eIF2alpha phosphorylation. Chow C, Cloutier S, Dumas C, Chou MN, Papadopoulou B, Cell Microbiol 2011 13 1059 1077 10.1111/j.1462-5822.2011.01602.x 21624030
    • (2011) Cell Microbiol , vol.13 , pp. 1059-1077
    • Chow, C.1    Cloutier, S.2    Dumas, C.3    Chou, M.N.4    Papadopoulou, B.5
  • 76
    • 81155137356 scopus 로고    scopus 로고
    • Protein synthesis attenuation by phosphorylation of eIF2alpha is required for the differentiation of Trypanosoma cruzi into infective forms
    • 10.1371/journal.pone.0027904 22114724
    • Protein synthesis attenuation by phosphorylation of eIF2alpha is required for the differentiation of Trypanosoma cruzi into infective forms. Tonelli RR, Augusto Lda S, Castilho BA, Schenkman S, PLoS One 2011 6 11 27904 10.1371/journal.pone.0027904 22114724
    • (2011) PLoS One , vol.6 , Issue.11 , pp. 527904
    • Tonelli, R.R.1    Augusto Lda, S.2    Castilho, B.A.3    Schenkman, S.4
  • 77
    • 55049098755 scopus 로고    scopus 로고
    • Heat shock causes a decrease in polysomes and the appearance of stress granules in trypanosomes independently of eIF2{alpha} phosphorylation at Thr169
    • 10.1242/jcs.031823 18713834
    • Heat shock causes a decrease in polysomes and the appearance of stress granules in trypanosomes independently of eIF2{alpha} phosphorylation at Thr169. Kramer S, Queiroz R, Ellis L, Webb H, Hoheisel JD, Clayton C, Carrington M, J Cell Sci 2008 121 3002 3014 10.1242/jcs.031823 18713834
    • (2008) J Cell Sci , vol.121 , pp. 3002-3014
    • Kramer, S.1    Queiroz, R.2    Ellis, L.3    Webb, H.4    Hoheisel, J.D.5    Clayton, C.6    Carrington, M.7
  • 78
    • 27644484061 scopus 로고    scopus 로고
    • Autophagy: Molecular machinery for self-eating
    • DOI 10.1038/sj.cdd.4401765, PII 4401765
    • Autophagy: molecular machinery for self-eating. Yorimitsu T, Klionsky DJ, Cell Death Differ 2005 12 Suppl 2 1542 1552 16247502 (Pubitemid 41553991)
    • (2005) Cell Death and Differentiation , vol.12 , Issue.SUPPL. 2 , pp. 1542-1552
    • Yorimitsu, T.1    Klionsky, D.J.2
  • 79
    • 41449083862 scopus 로고    scopus 로고
    • Turnover of glycosomes during life-cycle differentiation of Trypanosoma brucei
    • Turnover of glycosomes during life-cycle differentiation of Trypanosoma brucei. Herman M, Perez-Morga D, Schtickzelle N, Michels PA, Autophagy 2008 4 294 308 18365344 (Pubitemid 351458090)
    • (2008) Autophagy , vol.4 , Issue.3 , pp. 294-308
    • Herman, M.1    Perez-Morga, D.2    Schtickzelle, N.3    Michels, P.A.M.4
  • 81
    • 61649127283 scopus 로고    scopus 로고
    • Characterization of unusual families of ATG8-like proteins and ATG12 in the protozoan parasite Leishmania major
    • 10.4161/auto.5.2.7328 19066473
    • Characterization of unusual families of ATG8-like proteins and ATG12 in the protozoan parasite Leishmania major. Williams RA, Woods KL, Juliano L, Mottram JC, Coombs GH, Autophagy 2009 5 159 172 10.4161/auto.5.2.7328 19066473
    • (2009) Autophagy , vol.5 , pp. 159-172
    • Williams, R.A.1    Woods, K.L.2    Juliano, L.3    Mottram, J.C.4    Coombs, G.H.5
  • 82
    • 55749100531 scopus 로고    scopus 로고
    • Rapamycin inhibits trypanosome cell growth by preventing TOR complex 2 formation
    • 10.1073/pnas.0802668105 18796613
    • Rapamycin inhibits trypanosome cell growth by preventing TOR complex 2 formation. Barquilla A, Crespo JL, Navarro M, Proc Natl Acad Sci USA 2008 105 14579 14584 10.1073/pnas.0802668105 18796613
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14579-14584
    • Barquilla, A.1    Crespo, J.L.2    Navarro, M.3
  • 83
    • 61649084207 scopus 로고    scopus 로고
    • Trypanosome TOR as a major regulator of cell growth and autophagy
    • 10.4161/auto.5.2.7591 19139627
    • Trypanosome TOR as a major regulator of cell growth and autophagy. Barquilla A, Navarro M, Autophagy 2009 5 256 258 10.4161/auto.5.2.7591 19139627
    • (2009) Autophagy , vol.5 , pp. 256-258
    • Barquilla, A.1    Navarro, M.2


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