메뉴 건너뛰기




Volumn 24, Issue 4, 2012, Pages 273-280

The cytoplasmic AID complex

Author keywords

Activation induced deaminase; AID; Antibody diversification; Chaperone; Cytoplasmic complex; EEF1A; Nuclear:cytoplasmic traffic; Translation elongation factor 1

Indexed keywords

CYTOPLASM PROTEIN; ELONGATION FACTOR 1ALPHA; HEAT SHOCK PROTEIN 90; MESSENGER RNA; PROTEIN AID; UNCLASSIFIED DRUG;

EID: 84865167294     PISSN: 10445323     EISSN: 10963618     Source Type: Journal    
DOI: 10.1016/j.smim.2012.05.004     Document Type: Review
Times cited : (16)

References (86)
  • 5
    • 43049173617 scopus 로고    scopus 로고
    • MicroRNA-155 suppresses activation-induced cytidine deaminase-mediated Myc-Igh translocation
    • Dorsett Y., McBride K.M., Jankovic M., Gazumyan A., Thai T.H., Robbiani D.F., et al. MicroRNA-155 suppresses activation-induced cytidine deaminase-mediated Myc-Igh translocation. Immunity 2008, 28(5):630-638.
    • (2008) Immunity , vol.28 , Issue.5 , pp. 630-638
    • Dorsett, Y.1    McBride, K.M.2    Jankovic, M.3    Gazumyan, A.4    Thai, T.H.5    Robbiani, D.F.6
  • 6
    • 43049178852 scopus 로고    scopus 로고
    • MicroRNA-155 is a negative regulator of activation-induced cytidine deaminase
    • Teng G., Hakimpour P., Landgraf P., Rice A., Tuschl T., Casellas R., et al. MicroRNA-155 is a negative regulator of activation-induced cytidine deaminase. Immunity 2008, 28(5):621-629.
    • (2008) Immunity , vol.28 , Issue.5 , pp. 621-629
    • Teng, G.1    Hakimpour, P.2    Landgraf, P.3    Rice, A.4    Tuschl, T.5    Casellas, R.6
  • 8
    • 28544438261 scopus 로고    scopus 로고
    • AID antibody diversification enzyme is regulated by protein kinase A phosphorylation
    • Basu U., Chaudhuri J., Alpert C., Dutt S., Ranganath S., Li G., et al. AID antibody diversification enzyme is regulated by protein kinase A phosphorylation. Nature 2005, 438(7067):508-511.
    • (2005) Nature , vol.438 , Issue.7067 , pp. 508-511
    • Basu, U.1    Chaudhuri, J.2    Alpert, C.3    Dutt, S.4    Ranganath, S.5    Li, G.6
  • 10
    • 2942722486 scopus 로고    scopus 로고
    • Activation-induced cytosine deaminase (AID) is actively exported out of the nucleus but retained by the induction of DNA breaks
    • Brar S.S., Watson M., Diaz M. Activation-induced cytosine deaminase (AID) is actively exported out of the nucleus but retained by the induction of DNA breaks. Journal of Biological Chemistry 2004, 279(25):26395-26401.
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.25 , pp. 26395-26401
    • Brar, S.S.1    Watson, M.2    Diaz, M.3
  • 13
    • 84855509602 scopus 로고    scopus 로고
    • REG-gamma associates with and modulates the abundance of nuclear activation-induced deaminase
    • Uchimura Y., Barton L.F., Rada C., Neuberger M.S. REG-gamma associates with and modulates the abundance of nuclear activation-induced deaminase. Journal of Experimental Medicine 2011, 208(12):2385-2391.
    • (2011) Journal of Experimental Medicine , vol.208 , Issue.12 , pp. 2385-2391
    • Uchimura, Y.1    Barton, L.F.2    Rada, C.3    Neuberger, M.S.4
  • 15
    • 79959336838 scopus 로고    scopus 로고
    • The mechanisms regulating the subcellular localization of AID
    • Patenaude A.M., Di Noia J.M. The mechanisms regulating the subcellular localization of AID. Nucleus 2010, 1(4):325-331.
    • (2010) Nucleus , vol.1 , Issue.4 , pp. 325-331
    • Patenaude, A.M.1    Di Noia, J.M.2
  • 17
    • 33646596305 scopus 로고    scopus 로고
    • Nuclear and cytoplasmic AID in extrafollicular and germinal center B cells
    • Cattoretti G., Buttner M., Shaknovich R., Kremmer E., Alobeid B., Niedobitek G. Nuclear and cytoplasmic AID in extrafollicular and germinal center B cells. Blood 2006, 107(10):3967-3975.
    • (2006) Blood , vol.107 , Issue.10 , pp. 3967-3975
    • Cattoretti, G.1    Buttner, M.2    Shaknovich, R.3    Kremmer, E.4    Alobeid, B.5    Niedobitek, G.6
  • 19
    • 17144391393 scopus 로고    scopus 로고
    • Differential expression of activation-induced cytidine deaminase (AID) in nodular lymphocyte-predominant and classical Hodgkin lymphoma
    • Greiner A., Tobollik S., Buettner M., Jungnickel B., Herrmann K., Kremmer E., et al. Differential expression of activation-induced cytidine deaminase (AID) in nodular lymphocyte-predominant and classical Hodgkin lymphoma. Journal of Pathology 2005, 205(5):541-547.
    • (2005) Journal of Pathology , vol.205 , Issue.5 , pp. 541-547
    • Greiner, A.1    Tobollik, S.2    Buettner, M.3    Jungnickel, B.4    Herrmann, K.5    Kremmer, E.6
  • 20
    • 70449715730 scopus 로고    scopus 로고
    • Temporal regulation of Ig gene diversification revealed by single-cell imaging
    • Ordinario E.C., Yabuki M., Larson R.P., Maizels N. Temporal regulation of Ig gene diversification revealed by single-cell imaging. Journal of Immunology 2009, 183(7):4545-4553.
    • (2009) Journal of Immunology , vol.183 , Issue.7 , pp. 4545-4553
    • Ordinario, E.C.1    Yabuki, M.2    Larson, R.P.3    Maizels, N.4
  • 22
    • 0037452080 scopus 로고    scopus 로고
    • Transcription-targeted DNA deamination by the AID antibody diversification enzyme
    • Chaudhuri J., Tian M., Khuong C., Chua K., Pinaud E., Alt F.W. Transcription-targeted DNA deamination by the AID antibody diversification enzyme. Nature 2003, 422(6933):726-730.
    • (2003) Nature , vol.422 , Issue.6933 , pp. 726-730
    • Chaudhuri, J.1    Tian, M.2    Khuong, C.3    Chua, K.4    Pinaud, E.5    Alt, F.W.6
  • 24
    • 81055141344 scopus 로고    scopus 로고
    • Cytoplasmic activation-induced cytidine deaminase (AID) exists in stoichiometric complex with translation elongation factor 1alpha (eEF1A)
    • Hasler J., Rada C., Neuberger M.S. Cytoplasmic activation-induced cytidine deaminase (AID) exists in stoichiometric complex with translation elongation factor 1alpha (eEF1A). Proceedings of the National Academy of Sciences of the United States of America 2011, 108(45):18366-18371.
    • (2011) Proceedings of the National Academy of Sciences of the United States of America , vol.108 , Issue.45 , pp. 18366-18371
    • Hasler, J.1    Rada, C.2    Neuberger, M.S.3
  • 25
    • 0009499348 scopus 로고
    • Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum
    • Walter P., Blobel G. Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum. Proceedings of the National Academy of Sciences of the United States of America 1980, 77(12):7112-7116.
    • (1980) Proceedings of the National Academy of Sciences of the United States of America , vol.77 , Issue.12 , pp. 7112-7116
    • Walter, P.1    Blobel, G.2
  • 27
    • 18344372631 scopus 로고    scopus 로고
    • Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells
    • Chiu Y.L., Soros V.B., Kreisberg J.F., Stopak K., Yonemoto W., Greene W.C. Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells. Nature 2005, 435(7038):108-114.
    • (2005) Nature , vol.435 , Issue.7038 , pp. 108-114
    • Chiu, Y.L.1    Soros, V.B.2    Kreisberg, J.F.3    Stopak, K.4    Yonemoto, W.5    Greene, W.C.6
  • 28
    • 33847246310 scopus 로고    scopus 로고
    • Newly synthesized APOBEC3G is incorporated into HIV virions, inhibited by HIV RNA, and subsequently activated by RNase H
    • Soros V.B., Yonemoto W., Greene W.C. Newly synthesized APOBEC3G is incorporated into HIV virions, inhibited by HIV RNA, and subsequently activated by RNase H. PLoS Pathogens 2007, 3(2):e15.
    • (2007) PLoS Pathogens , vol.3 , Issue.2
    • Soros, V.B.1    Yonemoto, W.2    Greene, W.C.3
  • 29
    • 33845972280 scopus 로고    scopus 로고
    • Nanostructures of APOBEC3G support a hierarchical assembly model of high molecular mass ribonucleoprotein particles from dimeric subunits
    • Wedekind J.E., Gillilan R., Janda A., Krucinska J., Salter J.D., Bennett R.P., et al. Nanostructures of APOBEC3G support a hierarchical assembly model of high molecular mass ribonucleoprotein particles from dimeric subunits. Journal of Biological Chemistry 2006, 281(50):38122-38126.
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.50 , pp. 38122-38126
    • Wedekind, J.E.1    Gillilan, R.2    Janda, A.3    Krucinska, J.4    Salter, J.D.5    Bennett, R.P.6
  • 30
    • 58249114897 scopus 로고    scopus 로고
    • Sole copy of Z2-type human cytidine deaminase APOBEC3H has inhibitory activity against retrotransposons and HIV-1
    • Tan L., Sarkis P.T., Wang T., Tian C., Yu X.F. Sole copy of Z2-type human cytidine deaminase APOBEC3H has inhibitory activity against retrotransposons and HIV-1. FASEB Journal 2009, 23(1):279-287.
    • (2009) FASEB Journal , vol.23 , Issue.1 , pp. 279-287
    • Tan, L.1    Sarkis, P.T.2    Wang, T.3    Tian, C.4    Yu, X.F.5
  • 31
    • 77955474540 scopus 로고    scopus 로고
    • Cellular APOBEC3G restricts HIV-1 infection in resting CD4(+) T cells
    • Chiu Y.L., Soros V.B., Kreisberg J.F., Stopak K., Yonemoto W., Greene W.C., et al. Cellular APOBEC3G restricts HIV-1 infection in resting CD4(+) T cells. Nature 2010, 466(7303):276.
    • (2010) Nature , vol.466 , Issue.7303 , pp. 276
    • Chiu, Y.L.1    Soros, V.B.2    Kreisberg, J.F.3    Stopak, K.4    Yonemoto, W.5    Greene, W.C.6
  • 33
    • 33745853463 scopus 로고    scopus 로고
    • Identification of a specific domain required for dimerization of activation-induced cytidine deaminase
    • Wang J., Shinkura R., Muramatsu M., Nagaoka H., Kinoshita K., Honjo T. Identification of a specific domain required for dimerization of activation-induced cytidine deaminase. Journal of Biological Chemistry 2006, 281(28):19115-19123.
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.28 , pp. 19115-19123
    • Wang, J.1    Shinkura, R.2    Muramatsu, M.3    Nagaoka, H.4    Kinoshita, K.5    Honjo, T.6
  • 35
    • 36649006227 scopus 로고    scopus 로고
    • Activation-induced deaminase, AID, is catalytically active as a monomer on single-stranded DNA
    • Brar S.S., Sacho E.J., Tessmer I., Croteau D.L., Erie D.A., Diaz M. Activation-induced deaminase, AID, is catalytically active as a monomer on single-stranded DNA. DNA Repair (Amst) 2008, 7(1):77-87.
    • (2008) DNA Repair (Amst) , vol.7 , Issue.1 , pp. 77-87
    • Brar, S.S.1    Sacho, E.J.2    Tessmer, I.3    Croteau, D.L.4    Erie, D.A.5    Diaz, M.6
  • 37
    • 0037926476 scopus 로고    scopus 로고
    • Processive AID-catalysed cytosine deamination on single-stranded DNA simulates somatic hypermutation
    • Pham P., Bransteitter R., Petruska J., Goodman M.F. Processive AID-catalysed cytosine deamination on single-stranded DNA simulates somatic hypermutation. Nature 2003, 424(6944):103-107.
    • (2003) Nature , vol.424 , Issue.6944 , pp. 103-107
    • Pham, P.1    Bransteitter, R.2    Petruska, J.3    Goodman, M.F.4
  • 40
    • 27944508215 scopus 로고    scopus 로고
    • CLIP: a method for identifying protein-RNA interaction sites in living cells
    • Ule J., Jensen K., Mele A., Darnell R.B. CLIP: a method for identifying protein-RNA interaction sites in living cells. Methods 2005, 37(4):376-386.
    • (2005) Methods , vol.37 , Issue.4 , pp. 376-386
    • Ule, J.1    Jensen, K.2    Mele, A.3    Darnell, R.B.4
  • 41
    • 77952497487 scopus 로고    scopus 로고
    • Two forms of activation-induced cytidine deaminase differing in their ability to bind agarose
    • Metzner M., Schuh W., Roth E., Jack H.M., Wabl M. Two forms of activation-induced cytidine deaminase differing in their ability to bind agarose. PLoS One 2010, 5(1):e8883.
    • (2010) PLoS One , vol.5 , Issue.1
    • Metzner, M.1    Schuh, W.2    Roth, E.3    Jack, H.M.4    Wabl, M.5
  • 42
    • 4344700569 scopus 로고    scopus 로고
    • Replication protein A interacts with AID to promote deamination of somatic hypermutation targets
    • Chaudhuri J., Khuong C., Alt F.W. Replication protein A interacts with AID to promote deamination of somatic hypermutation targets. Nature 2004, 430(7003):992-998.
    • (2004) Nature , vol.430 , Issue.7003 , pp. 992-998
    • Chaudhuri, J.1    Khuong, C.2    Alt, F.W.3
  • 44
    • 77957239251 scopus 로고    scopus 로고
    • Activation-induced cytidine deaminase targets DNA at sites of RNA polymerase II stalling by interaction with Spt5
    • Pavri R., Gazumyan A., Jankovic M., Di Virgilio M., Klein I., Ansarah-Sobrinho C., et al. Activation-induced cytidine deaminase targets DNA at sites of RNA polymerase II stalling by interaction with Spt5. Cell 2010, 143(1):122-133.
    • (2010) Cell , vol.143 , Issue.1 , pp. 122-133
    • Pavri, R.1    Gazumyan, A.2    Jankovic, M.3    Di Virgilio, M.4    Klein, I.5    Ansarah-Sobrinho, C.6
  • 45
    • 77956345401 scopus 로고    scopus 로고
    • 14-3-3 adaptor proteins recruit AID to 5'-AGCT-3'-rich switch regions for class switch recombination
    • Xu Z., Fulop Z., Wu G., Pone E.J., Zhang J., Mai T., et al. 14-3-3 adaptor proteins recruit AID to 5'-AGCT-3'-rich switch regions for class switch recombination. Nature Structural & Molecular Biology 2010, 17(9):1124-1135.
    • (2010) Nature Structural & Molecular Biology , vol.17 , Issue.9 , pp. 1124-1135
    • Xu, Z.1    Fulop, Z.2    Wu, G.3    Pone, E.J.4    Zhang, J.5    Mai, T.6
  • 46
    • 49349112190 scopus 로고    scopus 로고
    • Interaction between antibody-diversification enzyme AID and spliceosome-associated factor CTNNBL1
    • Conticello S.G., Ganesh K., Xue K., Lu M., Rada C., Neuberger M.S. Interaction between antibody-diversification enzyme AID and spliceosome-associated factor CTNNBL1. Molecular Cell 2008, 31(4):474-484.
    • (2008) Molecular Cell , vol.31 , Issue.4 , pp. 474-484
    • Conticello, S.G.1    Ganesh, K.2    Xue, K.3    Lu, M.4    Rada, C.5    Neuberger, M.S.6
  • 47
    • 78751608734 scopus 로고    scopus 로고
    • The splicing regulator PTBP2 interacts with the cytidine deaminase AID and promotes binding of AID to switch-region DNA
    • Nowak U., Matthews A.J., Zheng S., Chaudhuri J. The splicing regulator PTBP2 interacts with the cytidine deaminase AID and promotes binding of AID to switch-region DNA. Nature Immunology 2011, 12(2):160-166.
    • (2011) Nature Immunology , vol.12 , Issue.2 , pp. 160-166
    • Nowak, U.1    Matthews, A.J.2    Zheng, S.3    Chaudhuri, J.4
  • 49
    • 77955385274 scopus 로고    scopus 로고
    • The interaction between AID and CIB1 is nonessential for antibody gene diversification by gene conversion or class switch recombination
    • Demorest Z.L., MacDuff D.A., Brown W.L., Morham S.G., Parise L.V., Harris R.S. The interaction between AID and CIB1 is nonessential for antibody gene diversification by gene conversion or class switch recombination. PLoS One 2010, 5(7):e11660.
    • (2010) PLoS One , vol.5 , Issue.7
    • Demorest, Z.L.1    MacDuff, D.A.2    Brown, W.L.3    Morham, S.G.4    Parise, L.V.5    Harris, R.S.6
  • 50
    • 77954901696 scopus 로고    scopus 로고
    • GANP-mediated recruitment of activation-induced cytidine deaminase to cell nuclei and to immunoglobulin variable region DNA
    • Maeda K., Singh S.K., Eda K., Kitabatake M., Pham P., Goodman M.F., et al. GANP-mediated recruitment of activation-induced cytidine deaminase to cell nuclei and to immunoglobulin variable region DNA. Journal of Biological Chemistry 2010, 285(31):23945-23953.
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.31 , pp. 23945-23953
    • Maeda, K.1    Singh, S.K.2    Eda, K.3    Kitabatake, M.4    Pham, P.5    Goodman, M.F.6
  • 51
    • 84865171411 scopus 로고    scopus 로고
    • YY1 controls immunoglobulin class switch recombination and nuclear AID levels
    • MCB 05989-11 [published ahead of print January 30, 2012]
    • Zaprazna K., Atchison M.L. YY1 controls immunoglobulin class switch recombination and nuclear AID levels. Molecular and Cellular Biology 2012, MCB 05989-11 [published ahead of print January 30, 2012].
    • (2012) Molecular and Cellular Biology
    • Zaprazna, K.1    Atchison, M.L.2
  • 53
    • 84856472936 scopus 로고    scopus 로고
    • Optimal functional levels of activation-induced deaminase specifically require the Hsp40 DnaJa1
    • Orthwein A., Zahn A., Methot S.P., Godin D., Conticello S.G., Terada K., et al. Optimal functional levels of activation-induced deaminase specifically require the Hsp40 DnaJa1. EMBO Journal 2011, 10.1038/emboj.2011.417.
    • (2011) EMBO Journal
    • Orthwein, A.1    Zahn, A.2    Methot, S.P.3    Godin, D.4    Conticello, S.G.5    Terada, K.6
  • 54
    • 0036359281 scopus 로고    scopus 로고
    • Moonlighting functions of polypeptide elongation factor 1: from actin bundling to zinc finger protein R1-associated nuclear localization
    • Ejiri S. Moonlighting functions of polypeptide elongation factor 1: from actin bundling to zinc finger protein R1-associated nuclear localization. Bioscience, Biotechnology, and Biochemistry 2002, 66(1):1-21.
    • (2002) Bioscience, Biotechnology, and Biochemistry , vol.66 , Issue.1 , pp. 1-21
    • Ejiri, S.1
  • 55
    • 4143091385 scopus 로고    scopus 로고
    • The translation elongation factor 1A in tumorigenesis, signal transduction and apoptosis: review article
    • Lamberti A., Caraglia M., Longo O., Marra M., Abbruzzese A., Arcari P. The translation elongation factor 1A in tumorigenesis, signal transduction and apoptosis: review article. Amino Acids 2004, 26(4):443-448.
    • (2004) Amino Acids , vol.26 , Issue.4 , pp. 443-448
    • Lamberti, A.1    Caraglia, M.2    Longo, O.3    Marra, M.4    Abbruzzese, A.5    Arcari, P.6
  • 57
    • 26944487335 scopus 로고    scopus 로고
    • Translation elongation factor 1A is essential for regulation of the actin cytoskeleton and cell morphology
    • Gross S.R., Kinzy T.G. Translation elongation factor 1A is essential for regulation of the actin cytoskeleton and cell morphology. Nature Structural & Molecular Biology 2005, 12(9):772-778.
    • (2005) Nature Structural & Molecular Biology , vol.12 , Issue.9 , pp. 772-778
    • Gross, S.R.1    Kinzy, T.G.2
  • 58
    • 63249124261 scopus 로고    scopus 로고
    • Coordination of eukaryotic translation elongation factor 1A (eEF1A) function in actin organization and translation elongation by the guanine nucleotide exchange factor eEF1Balpha
    • Pittman Y.R., Kandl K., Lewis M., Valente L., Kinzy T.G. Coordination of eukaryotic translation elongation factor 1A (eEF1A) function in actin organization and translation elongation by the guanine nucleotide exchange factor eEF1Balpha. Journal of Biological Chemistry 2009, 284(7):4739-4747.
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.7 , pp. 4739-4747
    • Pittman, Y.R.1    Kandl, K.2    Lewis, M.3    Valente, L.4    Kinzy, T.G.5
  • 59
    • 11144342006 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of cotranslationally damaged proteins involves translation elongation factor 1A
    • Chuang S.M., Chen L., Lambertson D., Anand M., Kinzy T.G., Madura K. Proteasome-mediated degradation of cotranslationally damaged proteins involves translation elongation factor 1A. Molecular and Cellular Biology 2005, 25(1):403-413.
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.1 , pp. 403-413
    • Chuang, S.M.1    Chen, L.2    Lambertson, D.3    Anand, M.4    Kinzy, T.G.5    Madura, K.6
  • 61
    • 33750695976 scopus 로고    scopus 로고
    • Tetrahymena eukaryotic translation elongation factor 1A (eEF1A) bundles filamentous actin through dimer formation
    • Bunai F., Ando K., Ueno H., Numata O. Tetrahymena eukaryotic translation elongation factor 1A (eEF1A) bundles filamentous actin through dimer formation. Journal of Biochemistry 2006, 140(3):393-399.
    • (2006) Journal of Biochemistry , vol.140 , Issue.3 , pp. 393-399
    • Bunai, F.1    Ando, K.2    Ueno, H.3    Numata, O.4
  • 62
    • 41149102857 scopus 로고    scopus 로고
    • Roles of three domains of tetrahymena eEF1A in bundling F-actin
    • Morita K., Bunai F., Numata O. Roles of three domains of tetrahymena eEF1A in bundling F-actin. Zoological Science 2008, 25(1):22-29.
    • (2008) Zoological Science , vol.25 , Issue.1 , pp. 22-29
    • Morita, K.1    Bunai, F.2    Numata, O.3
  • 64
    • 36849065315 scopus 로고    scopus 로고
    • Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer
    • Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., et al. Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell 2007, 131(6):1190-1203.
    • (2007) Cell , vol.131 , Issue.6 , pp. 1190-1203
    • Rikova, K.1    Guo, A.2    Zeng, Q.3    Possemato, A.4    Yu, J.5    Haack, H.6
  • 65
    • 21144458164 scopus 로고    scopus 로고
    • Immunoaffinity profiling of tyrosine phosphorylation in cancer cells
    • Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., et al. Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nature Biotechnology 2005, 23(1):94-101.
    • (2005) Nature Biotechnology , vol.23 , Issue.1 , pp. 94-101
    • Rush, J.1    Moritz, A.2    Lee, K.A.3    Guo, A.4    Goss, V.L.5    Spek, E.J.6
  • 66
    • 0030725392 scopus 로고    scopus 로고
    • Phosphorylation of elongation factor 1 and ribosomal protein S6 by multipotential S6 kinase and insulin stimulation of translational elongation
    • Chang Y.W., Traugh J.A. Phosphorylation of elongation factor 1 and ribosomal protein S6 by multipotential S6 kinase and insulin stimulation of translational elongation. Journal of Biological Chemistry 1997, 272(45):28252-28257.
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.45 , pp. 28252-28257
    • Chang, Y.W.1    Traugh, J.A.2
  • 67
    • 0032518567 scopus 로고    scopus 로고
    • Insulin stimulation of phosphorylation of elongation factor 1 (eEF-1) enhances elongation activity
    • Chang Y.W., Traugh J.A. Insulin stimulation of phosphorylation of elongation factor 1 (eEF-1) enhances elongation activity. European Journal of Biochemistry 1998, 251(1-2):201-207.
    • (1998) European Journal of Biochemistry , vol.251 , Issue.1-2 , pp. 201-207
    • Chang, Y.W.1    Traugh, J.A.2
  • 68
    • 77957230094 scopus 로고    scopus 로고
    • Phosphorylation of eEF1A1 at Ser300 by TbetaR-I results in inhibition of mRNA translation
    • Lin K.W., Yakymovych I., Jia M., Yakymovych M., Souchelnytskyi S. Phosphorylation of eEF1A1 at Ser300 by TbetaR-I results in inhibition of mRNA translation. Current Biology 2010, 20(18):1615-1625.
    • (2010) Current Biology , vol.20 , Issue.18 , pp. 1615-1625
    • Lin, K.W.1    Yakymovych, I.2    Jia, M.3    Yakymovych, M.4    Souchelnytskyi, S.5
  • 69
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., et al. Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 2009, 325(5942):834-840.
    • (2009) Science , vol.325 , Issue.5942 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3    Nielsen, M.L.4    Rehman, M.5    Walther, T.C.6
  • 70
    • 0024341194 scopus 로고
    • Location of seven post-translational modifications in rabbit elongation factor 1 alpha including dimethyllysine, trimethyllysine, and glycerylphosphorylethanolamine
    • Dever T.E., Costello C.E., Owens C.L., Rosenberry T.L., Merrick W.C. Location of seven post-translational modifications in rabbit elongation factor 1 alpha including dimethyllysine, trimethyllysine, and glycerylphosphorylethanolamine. Journal of Biological Chemistry 1989, 264(34):20518-20525.
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.34 , pp. 20518-20525
    • Dever, T.E.1    Costello, C.E.2    Owens, C.L.3    Rosenberry, T.L.4    Merrick, W.C.5
  • 71
    • 0024478177 scopus 로고
    • Biosynthetic incorporation of [3H]ethanolamine into protein synthesis elongation factor 1 alpha reveals a new post-translational protein modification
    • Rosenberry T.L., Krall J.A., Dever T.E., Haas R., Louvard D., Merrick W.C. Biosynthetic incorporation of [3H]ethanolamine into protein synthesis elongation factor 1 alpha reveals a new post-translational protein modification. Journal of Biological Chemistry 1989, 264(13):7096-7099.
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.13 , pp. 7096-7099
    • Rosenberry, T.L.1    Krall, J.A.2    Dever, T.E.3    Haas, R.4    Louvard, D.5    Merrick, W.C.6
  • 72
    • 0024414072 scopus 로고
    • Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha
    • Whiteheart S.W., Shenbagamurthi P., Chen L., Cotter R.J., Hart G.W. Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha. Journal of Biological Chemistry 1989, 264(24):14334-14341.
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.24 , pp. 14334-14341
    • Whiteheart, S.W.1    Shenbagamurthi, P.2    Chen, L.3    Cotter, R.J.4    Hart, G.W.5
  • 73
    • 77949712407 scopus 로고    scopus 로고
    • A structural domain mediates attachment of ethanolamine phosphoglycerol to eukaryotic elongation factor 1A in trypanosoma brucei
    • Greganova E., Heller M., Butikofer P. A structural domain mediates attachment of ethanolamine phosphoglycerol to eukaryotic elongation factor 1A in trypanosoma brucei. PLoS One 2010, 5(3):e9486.
    • (2010) PLoS One , vol.5 , Issue.3
    • Greganova, E.1    Heller, M.2    Butikofer, P.3
  • 74
    • 33744967284 scopus 로고    scopus 로고
    • A role for activation-induced cytidine deaminase in the host response against a transforming retrovirus
    • Gourzi P., Leonova T., Papavasiliou F.N. A role for activation-induced cytidine deaminase in the host response against a transforming retrovirus. Immunity 2006, 24(6):779-786.
    • (2006) Immunity , vol.24 , Issue.6 , pp. 779-786
    • Gourzi, P.1    Leonova, T.2    Papavasiliou, F.N.3
  • 75
    • 33847102791 scopus 로고    scopus 로고
    • Viral induction of AID is independent of the interferon and the toll-like receptor signaling pathways but requires NF-kappaB
    • Gourzi P., Leonova T., Papavasiliou F.N. Viral induction of AID is independent of the interferon and the toll-like receptor signaling pathways but requires NF-kappaB. Journal of Experimental Medicine 2007, 204(2):259-265.
    • (2007) Journal of Experimental Medicine , vol.204 , Issue.2 , pp. 259-265
    • Gourzi, P.1    Leonova, T.2    Papavasiliou, F.N.3
  • 76
    • 77950955761 scopus 로고    scopus 로고
    • Origin of chromosomal translocations in lymphoid cancer
    • Nussenzweig A., Nussenzweig M.C. Origin of chromosomal translocations in lymphoid cancer. Cell 2010, 141(1):27-38.
    • (2010) Cell , vol.141 , Issue.1 , pp. 27-38
    • Nussenzweig, A.1    Nussenzweig, M.C.2
  • 77
    • 0034825854 scopus 로고    scopus 로고
    • Generation and epitope mapping of high-affinity scFv to eukaryotic elongation factor 1A by dual application of phage display
    • Kjaer S., Wind T., Ravn P., Ostergaard M., Clark B.F., Nissim A. Generation and epitope mapping of high-affinity scFv to eukaryotic elongation factor 1A by dual application of phage display. European Journal of Biochemistry 2001, 268(12):3407-3415.
    • (2001) European Journal of Biochemistry , vol.268 , Issue.12 , pp. 3407-3415
    • Kjaer, S.1    Wind, T.2    Ravn, P.3    Ostergaard, M.4    Clark, B.F.5    Nissim, A.6
  • 78
    • 0037112790 scopus 로고    scopus 로고
    • Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm
    • Bohnsack M.T., Regener K., Schwappach B., Saffrich R., Paraskeva E., Hartmann E., et al. Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm. EMBO Journal 2002, 21(22):6205-6215.
    • (2002) EMBO Journal , vol.21 , Issue.22 , pp. 6205-6215
    • Bohnsack, M.T.1    Regener, K.2    Schwappach, B.3    Saffrich, R.4    Paraskeva, E.5    Hartmann, E.6
  • 79
    • 0037112842 scopus 로고    scopus 로고
    • Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNA
    • Calado A., Treichel N., Muller E.C., Otto A., Kutay U. Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNA. EMBO Journal 2002, 21(22):6216-6224.
    • (2002) EMBO Journal , vol.21 , Issue.22 , pp. 6216-6224
    • Calado, A.1    Treichel, N.2    Muller, E.C.3    Otto, A.4    Kutay, U.5
  • 80
    • 11844264903 scopus 로고    scopus 로고
    • The double-edged sword of activation-induced cytidine deaminase
    • Wu X., Geraldes P., Platt J.L., Cascalho M. The double-edged sword of activation-induced cytidine deaminase. Journal of Immunology 2005, 174(2):934-941.
    • (2005) Journal of Immunology , vol.174 , Issue.2 , pp. 934-941
    • Wu, X.1    Geraldes, P.2    Platt, J.L.3    Cascalho, M.4
  • 81
    • 0029020353 scopus 로고
    • PH regulation of the F-actin binding properties of Dictyostelium elongation factor 1 alpha
    • Edmonds B.T., Murray J., Condeelis J. pH regulation of the F-actin binding properties of Dictyostelium elongation factor 1 alpha. Journal of Biological Chemistry 1995, 270(25):15222-15230.
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.25 , pp. 15222-15230
    • Edmonds, B.T.1    Murray, J.2    Condeelis, J.3
  • 84
    • 30344463017 scopus 로고    scopus 로고
    • Evolution of class switch recombination function in fish activation-induced cytidine deaminase, AID
    • Wakae K., Magor B.G., Saunders H., Nagaoka H., Kawamura A., Kinoshita K., et al. Evolution of class switch recombination function in fish activation-induced cytidine deaminase, AID. International Immunology 2006, 18(1):41-47.
    • (2006) International Immunology , vol.18 , Issue.1 , pp. 41-47
    • Wakae, K.1    Magor, B.G.2    Saunders, H.3    Nagaoka, H.4    Kawamura, A.5    Kinoshita, K.6
  • 85
    • 78650308767 scopus 로고    scopus 로고
    • Deep-sequencing identification of the genomic targets of the cytidine deaminase AID and its cofactor RPA in B lymphocytes
    • Yamane A., Resch W., Kuo N., Kuchen S., Li Z., Sun H.W., et al. Deep-sequencing identification of the genomic targets of the cytidine deaminase AID and its cofactor RPA in B lymphocytes. Nature Immunology 2011, 12(1):62-69.
    • (2011) Nature Immunology , vol.12 , Issue.1 , pp. 62-69
    • Yamane, A.1    Resch, W.2    Kuo, N.3    Kuchen, S.4    Li, Z.5    Sun, H.W.6
  • 86
    • 67650330317 scopus 로고    scopus 로고
    • AID upmutants isolated using a high-throughput screen highlight the immunity/cancer balance limiting DNA deaminase activity
    • Wang M., Yang Z., Rada C., Neuberger M.S. AID upmutants isolated using a high-throughput screen highlight the immunity/cancer balance limiting DNA deaminase activity. Nature Structural & Molecular Biology 2009, 16(7):769-776.
    • (2009) Nature Structural & Molecular Biology , vol.16 , Issue.7 , pp. 769-776
    • Wang, M.1    Yang, Z.2    Rada, C.3    Neuberger, M.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.