메뉴 건너뛰기




Volumn 357, Issue , 2012, Pages 1-18

Interaction of ricin and Shiga toxins with ribosomes

Author keywords

Ribosomal stalk; Ribosome binding; Ribosome depurination; Ricin; Sarcin ricin loop; Shiga toxin; Translation inhibition

Indexed keywords

ALPHA SARCIN; CYTOPLASM PROTEIN; ELONGATION FACTOR 1; ELONGATION FACTOR 2; GUANOSINE TRIPHOSPHATASE; PROTEIN; PROTEIN P2; RIBOSOME INACTIVATING PROTEIN; RIBOSOME INACTIVATING PROTEIN 1; RIBOSOME PROTEIN; RICIN; RNA 23S; SHIGA TOXIN; STALK PROTEIN; UNCLASSIFIED DRUG; VEROTOXIN 1; VEROTOXIN 2;

EID: 84863285459     PISSN: 0070217X     EISSN: None     Source Type: Book Series    
DOI: 10.1007/82_2011_174     Document Type: Article
Times cited : (39)

References (114)
  • 4
    • 40849106335 scopus 로고    scopus 로고
    • The C-terminal end of P proteins mediates ribosome inactivation by trichosanthin but does not affect the pokeweed antiviral protein activity
    • Ayub MJ, Smulski CR, Ma KW, Levin MJ, Shaw PC, Wong KB (2008) The C-terminal end of P proteins mediates ribosome inactivation by trichosanthin but does not affect the pokeweed antiviral protein activity. Biochem Biophys Res Commun 369:314-319
    • (2008) Biochem Biophys Res Commun , vol.369 , pp. 314-319
    • Ayub, M.J.1    Smulski, C.R.2    Ma, K.W.3    Levin, M.J.4    Shaw, P.C.5    Wong, K.B.6
  • 5
    • 0029686290 scopus 로고    scopus 로고
    • The large ribosomal subunit stalk as a regulatory element of the eukaryotic translational machinery
    • Ballesta JP, Remacha M (1996) The large ribosomal subunit stalk as a regulatory element of the eukaryotic translational machinery. Prog Nucleic Acid Res Mol Biol 55:157-193
    • (1996) Prog Nucleic Acid Res Mol Biol , vol.55 , pp. 157-193
    • Ballesta, J.P.1    Remacha, M.2
  • 7
    • 84883598626 scopus 로고    scopus 로고
    • Structure and dynamics of ribosomal protein L12: An ensemble model based on SAXS and NMR relaxation
    • Bernado P, Modig K, Grela P, Svergun DI, Tchorzewski M, Pons M, Akke M (2010) Structure and dynamics of ribosomal protein L12: an ensemble model based on SAXS and NMR relaxation. Biophys J 98:2374-2382
    • (2010) Biophys J , vol.98 , pp. 2374-2382
    • Bernado, P.1    Modig, K.2    Grela, P.3    Svergun, D.I.4    Tchorzewski, M.5    Pons, M.6    Akke, M.7
  • 8
    • 80051804184 scopus 로고    scopus 로고
    • Characterisation of the Escherichia coli strain associated with an outbreak of haemolytic uraemic syndrome in Germany: A microbiological study
    • Bielaszewska M, Mellmann A, Zhang W, Kock R, Fruth A, Bauwens A, Peters G, Karch H (2011) Characterisation of the Escherichia coli strain associated with an outbreak of haemolytic uraemic syndrome in Germany: a microbiological study. Lancet Infect Dis 11:671-676
    • (2011) Lancet Infect Dis , vol.11 , pp. 671-676
    • Bielaszewska, M.1    Mellmann, A.2    Zhang, W.3    Kock, R.4    Fruth, A.5    Bauwens, A.6    Peters, G.7    Karch, H.8
  • 9
    • 0029119214 scopus 로고
    • Escherichia coli O157:H7 and the hemolyticuremic syndrome
    • Boyce TG, Swerdlow DL, Griffin PM (1995) Escherichia coli O157:H7 and the hemolyticuremic syndrome. N Engl J Med 333:364-368
    • (1995) N Engl J Med , vol.333 , pp. 364-368
    • Boyce, T.G.1    Swerdlow, D.L.2    Griffin, P.M.3
  • 10
    • 0024589101 scopus 로고
    • Effect of α-sarcin and ribosome-inactivating proteins on the interaction of elongation factors with ribosomes
    • Brigotti M, Rambelli F, Zamboni M, Montanaro L, Sperti S (1989) Effect of alpha-sarcin and ribosome-inactivating proteins on the interaction of elongation factors with ribosomes. Biochem J 257:723-727 (Pubitemid 19050129)
    • (1989) Biochemical Journal , vol.257 , Issue.3 , pp. 723-727
    • Brigotti, M.1    Rambelli, F.2    Zamboni, M.3    Montanaro, L.4    Sperti, S.5
  • 11
    • 0030721959 scopus 로고    scopus 로고
    • The RNA-N-glycosidase activity of Shiga-like toxin I: Kinetic parameters of the native and activated toxin
    • DOI 10.1016/S0041-0101(96)00225-5, PII S0041010196002255
    • Brigotti M, Carnicelli D, Alvergna P, Mazzaracchio R, Sperti S, Montanaro L (1997) The RNAN-glycosidase activity of Shiga-like toxin I: kinetic parameters of the native and activated toxin. Toxicon 35:1431-1437 (Pubitemid 27478849)
    • (1997) Toxicon , vol.35 , Issue.9 , pp. 1431-1437
    • Brigotti, M.1    Carnicelli, D.2    Alvergna, P.3    Mazzaracchio, R.4    Sperti, S.5    Montanaro, L.6
  • 12
    • 0018426962 scopus 로고
    • Protection and rescue of ribosomes from the action of ricin A chain
    • DOI 10.1021/bi00579a034
    • Cawley DB, Hedblom ML, Houston LL (1979) Protection and rescue of ribosomes from the action of ricin A chain. Biochemistry 18:2648-2654 (Pubitemid 9203288)
    • (1979) Biochemistry , vol.18 , Issue.12 , pp. 2648-2654
    • Cawley, D.B.1    Hedblom, M.L.2    Houston, L.L.3
  • 13
    • 0034854299 scopus 로고    scopus 로고
    • Trichosanthin interacts with acidic ribosomal proteins P0 and P1 and mitotic checkpoint protein MAD2B
    • DOI 10.1046/j.1432-1327.2001.02091.x
    • Chan SH, Hung FS, Chan DS, Shaw PC (2001) Trichosanthin interacts with acidic ribosomal proteins P0 and P1 and mitotic checkpoint protein MAD2B. Eur J Biochem 268:2107-2112 (Pubitemid 32852953)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.7 , pp. 2107-2112
    • Chan, S.-H.1    Hung, F.S.-J.2    Chan, D.S.-B.3    Shaw, P.-C.4
  • 14
    • 34247135324 scopus 로고    scopus 로고
    • Interaction between trichosanthin, a ribosome-inactivating protein, and the ribosomal stalk protein P2 by chemical shift perturbation and mutagenesis analyses
    • DOI 10.1093/nar/gkm065
    • Chan DS, Chu LO, Lee KM, Too PH, Ma KW, Sze KH, Zhu G, Shaw PC, Wong KB (2007) Interaction between trichosanthin, a ribosome-inactivating protein, and the ribosomal stalk protein P2 by chemical shift perturbation and mutagenesis analyses. Nucleic Acids Res 35:1660-1672 (Pubitemid 46592885)
    • (2007) Nucleic Acids Research , vol.35 , Issue.5 , pp. 1660-1672
    • Chan, D.S.B.1    Chu, L.-O.2    Lee, K.-M.3    Too, P.H.M.4    Ma, K.-W.5    Sze, K.-H.6    Zhu, G.7    Shaw, P.-C.8    Wong, K.-B.9
  • 16
    • 56749154533 scopus 로고    scopus 로고
    • The ribosomal stalk is required for ribosome binding, depurination of the rRNA and cytotoxicity of ricin A chain in Saccharomyces cerevisiae
    • Chiou JC, Li XP, Remacha M, Ballesta JP, Tumer NE (2008) The ribosomal stalk is required for ribosome binding, depurination of the rRNA and cytotoxicity of ricin A chain in Saccharomyces cerevisiae. Mol Microbiol 70:1441-1452
    • (2008) Mol Microbiol , vol.70 , pp. 1441-1452
    • Chiou, J.C.1    Li, X.P.2    Remacha, M.3    Ballesta, J.P.4    Tumer, N.E.5
  • 17
    • 80255123875 scopus 로고    scopus 로고
    • Shiga toxin 1 is more dependent on the P proteins of the ribosomal stalk for depurination activity than Shiga toxin 2
    • (In press)
    • Chiou JC, Li XP, Remacha M, Ballesta JP, Tumer NE (2011) Shiga toxin 1 is more dependent on the P proteins of the ribosomal stalk for depurination activity than Shiga toxin 2. Int. J Biochem Cell Biol (In press)
    • (2011) Int. J Biochem Cell Biol
    • Chiou, J.C.1    Li, X.P.2    Remacha, M.3    Ballesta, J.P.4    Tumer, N.E.5
  • 18
    • 77951297777 scopus 로고    scopus 로고
    • Atomic mutagenesis reveals A2660 of 23S ribosomal RNA as key to EF-G GTPase activation
    • Clementi N, Chirkova A, Puffer B, Micura R, Polacek N (2010) Atomic mutagenesis reveals A2660 of 23S ribosomal RNA as key to EF-G GTPase activation. Nat Chem Biol 6:344-351
    • (2010) Nat Chem Biol , vol.6 , pp. 344-351
    • Clementi, N.1    Chirkova, A.2    Puffer, B.3    Micura, R.4    Polacek, N.5
  • 21
    • 0033578939 scopus 로고    scopus 로고
    • The two faces of the Escherichia coli 23 S rRNA sarcin/ricin domain: The structure at 1.11 A resolution
    • DOI 10.1006/jmbi.1999.3072
    • Correll CC, Wool IG, Munishkin A (1999) The two faces of the Escherichia coli 23 S rRNA sarcin/ricin domain: the structure at 1.11 A resolution. J Mol Biol 292:275-287 (Pubitemid 29435766)
    • (1999) Journal of Molecular Biology , vol.292 , Issue.2 , pp. 275-287
    • Correll, C.C.1    Wool, I.G.2    Munishkin, A.3
  • 22
    • 0345531092 scopus 로고    scopus 로고
    • The common and the distinctive features of the bulged-G motif based on a 1.04 A resolution RNA structure
    • DOI 10.1093/nar/gkg908
    • Correll CC, Beneken J, Plantinga MJ, Lubbers M, Chan YL (2003) The common and the distinctive features of the bulged-G motif based on a 1.04 A resolution RNA structure. Nucleic Acids Res 31:6806-6818 (Pubitemid 37508788)
    • (2003) Nucleic Acids Research , vol.31 , Issue.23 , pp. 6806-6818
    • Correll, C.C.1    Beneken, J.2    Plantinga, M.J.3    Lubbers, M.4    Chan, Y.-L.5
  • 23
    • 23044506167 scopus 로고    scopus 로고
    • Expression of a truncated form of ribosomal protein L3 confers resistance to pokeweed antiviral protein and the Fusarium mycotoxin deoxynivalenol
    • DOI 10.1094/MPMI-18-0762
    • Di R, Tumer NE (2005) Expression of a truncated form of ribosomal protein L3 confers resistance to pokeweed antiviral protein and the Fusarium mycotoxin deoxynivalenol. Mol Plant Microbe Interact 18:762-770 (Pubitemid 41061474)
    • (2005) Molecular Plant-Microbe Interactions , vol.18 , Issue.8 , pp. 762-770
    • Di, R.1    Tumer, N.E.2
  • 24
    • 79952359595 scopus 로고    scopus 로고
    • Identification of amino acids critical for the cytotoxicity of Shiga toxin 1 and 2 in Saccharomyces cerevisiae
    • Di R, Kyu E, Shete V, Saidasan H, Kahn PC, Tumer NE (2011) Identification of amino acids critical for the cytotoxicity of Shiga toxin 1 and 2 in Saccharomyces cerevisiae. Toxicon 57:525-539
    • (2011) Toxicon , vol.57 , pp. 525-539
    • Di Kyu, R.E.1    Shete, V.2    Saidasan, H.3    Kahn, P.C.4    Tumer, N.E.5
  • 25
    • 21244465843 scopus 로고    scopus 로고
    • Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTpase activation
    • DOI 10.1016/j.cell.2005.04.015, PII S0092867405003958
    • Diaconu M, Kothe U, Schlunzen F, Fischer N, Harms JM, Tonevitsky AG, Stark H, Rodnina MV, Wahl MC (2005) Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activation. Cell 121:991-1004 (Pubitemid 40884392)
    • (2005) Cell , vol.121 , Issue.7 , pp. 991-1004
    • Diaconu, M.1    Kothe, U.2    Schlunzen, F.3    Fischer, N.4    Harms, J.M.5    Tonevitsky, A.G.6    Stark, H.7    Rodnina, M.V.8    Wahl, M.C.9
  • 26
    • 0023219950 scopus 로고
    • RNA N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes
    • Endo Y, Tsurugi K (1987) RNA N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes. J Biol Chem 262:8128-8130 (Pubitemid 17104265)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.17 , pp. 8128-8130
    • Endo, Y.1    Tsurugi, K.2
  • 27
    • 0024194659 scopus 로고
    • The RNA N-glycosidase activity of ricin A-chain
    • Endo Y, Tsurugi K (1988) The RNA N-glycosidase activity of ricin A-chain. Nucleic Acids Symp Ser 19:139-142
    • (1988) Nucleic Acids Symp ser , vol.19 , pp. 139-142
    • Endo, Y.1    Tsurugi, K.2
  • 28
    • 0023664263 scopus 로고
    • The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes: The site and the characteristics of the modification in 28 S ribosomal RNA caused by the toxins
    • Endo Y, Mitsui K, Motizuki M, Tsurugi K (1987) The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes: the site and the characteristics of the modification in 28 S ribosomal RNA caused by the toxins. J Biol Chem 262:5908-5912
    • (1987) J Biol Chem , vol.262 , pp. 5908-5912
    • Endo, Y.1    Mitsui, K.2    Motizuki, M.3    Tsurugi, K.4
  • 29
    • 0023917453 scopus 로고
    • The cytotoxins alpha-sarcin and ricin retain their specificity when tested on a synthetic oligoribonucleotide (35-mer) that mimics a region of 28 S ribosomal ribonucleic acid
    • Endo Y, Chan YL, Lin A, Tsurugi K, Wool IG (1988) The cytotoxins alpha-sarcin and ricin retain their specificity when tested on a synthetic oligoribonucleotide (35-mer) that mimics a region of 28 S ribosomal ribonucleic acid. J Biol Chem 263:7917-7920
    • (1988) J Biol Chem , vol.263 , pp. 7917-7920
    • Endo, Y.1    Chan, Y.L.2    Lin, A.3    Tsurugi, K.4    Wool, I.G.5
  • 30
    • 0033943684 scopus 로고    scopus 로고
    • Antiviral activity of Shiga toxin 1: Suppression of bovine leukemia virus-related spontaneous lymphocyte proliferation
    • DOI 10.1128/IAI.68.8.4462-4469.2000
    • Ferens WA, Hovde CJ (2000) Antiviral activity of shiga toxin 1: suppression of bovine leukemia virus-related spontaneous lymphocyte proliferation. Infect Immun 68:4462-4469 (Pubitemid 30497711)
    • (2000) Infection and Immunity , vol.68 , Issue.8 , pp. 4462-4469
    • Ferens, W.A.1    Hovde, C.J.2
  • 31
    • 33947110305 scopus 로고    scopus 로고
    • The non-toxic A subunit of Shiga toxin type 1 prevents replication of bovine immunodeficiency virus in infected cells
    • DOI 10.1016/j.virusres.2006.12.003, PII S0168170206003686
    • Ferens WA, Hovde CJ (2007) The non-toxic A subunit of Shiga toxin type 1 prevents replication of bovine immunodeficiency virus in infected cells. Virus Res 125:29-41 (Pubitemid 46413384)
    • (2007) Virus Research , vol.125 , Issue.1 , pp. 29-41
    • Ferens, W.A.1    Hovde, C.J.2
  • 32
    • 33646359171 scopus 로고    scopus 로고
    • Intestinal Shiga toxin-producing Escherichia coli bacteria mitigate bovine leukemia virus infection in experimentally infected sheep
    • DOI 10.1128/IAI.74.5.2906-2916.2006
    • Ferens WA, Cobbold R, Hovde CJ (2006) Intestinal Shiga toxin-producing Escherichia coli bacteria mitigate bovine leukemia virus infection in experimentally infected sheep. Infect Immun 74:2906-2916 (Pubitemid 43673001)
    • (2006) Infection and Immunity , vol.74 , Issue.5 , pp. 2906-2916
    • Ferens, W.A.1    Cobbold, R.2    Hovde, C.J.3
  • 33
    • 33947128513 scopus 로고    scopus 로고
    • Differential sensitivity of viruses to the antiviral activity of Shiga toxin 1 A subunit
    • DOI 10.1016/j.virusres.2006.12.002, PII S0168170206003674
    • Ferens WA, Halver M, Gustin KE, Ott T, Hovde CJ (2007) Differential sensitivity of viruses to the antiviral activity of Shiga toxin 1 A subunit. Virus Res 125:104-108 (Pubitemid 46413383)
    • (2007) Virus Research , vol.125 , Issue.1 , pp. 104-108
    • Ferens, W.A.1    Halver, M.2    Gustin, K.E.3    Ott, T.4    Hovde, C.J.5
  • 34
    • 0017405550 scopus 로고
    • Effects of some proteins that inactivate the eukaryotic ribosome
    • DOI 10.1016/0014-5793(77)80292-5
    • Fernandez-Puentes C, Vazquez D (1977) Effects of some proteins that inactivate the eukaryotic ribosome. FEBS Lett 78:143-146 (Pubitemid 8138615)
    • (1977) FEBS Letters , vol.78 , Issue.1 , pp. 143-146
    • Fernandez-Puentes1    Vazquez, D.2
  • 35
    • 0017187578 scopus 로고
    • Protective effect of elongation factor 2 on the inactivation of ribosomes by the toxic lectins abrin and ricin
    • Fernandez-Puentes C, Benson S, Olsnes S, Pihl A (1976) Protective effect of elongation factor 2 on the inactivation of ribosomes by the toxic lectins abrin and ricin. Eur J Biochem 64:437-443
    • (1976) Eur J Biochem , vol.64 , pp. 437-443
    • Fernandez-Puentes, C.1    Benson, S.2    Olsnes, S.3    Pihl, A.4
  • 36
    • 0028367338 scopus 로고
    • Crystal structure of the holotoxin from Shigella dysenteriae at 2.5 A resolution
    • Fraser ME, Chernaia MM, Kozlov YV, James MN (1994) Crystal structure of the holotoxin from Shigella dysenteriae at 2.5 A resolution. Nat Struct Biol 1:59-64 (Pubitemid 24974781)
    • (1994) Nature Structural Biology , vol.1 , Issue.1 , pp. 59-64
    • Fraser, M.E.1    Chernaia, M.M.2    Kozlov, Y.V.3    James, M.N.G.4
  • 40
    • 0028961149 scopus 로고
    • Furin-induced cleavage and activation of Shiga toxin
    • Garred O, van Deurs B, Sandvig K (1995) Furin-induced cleavage and activation of Shiga toxin. J Biol Chem 270:10817-10821
    • (1995) J Biol Chem , vol.270 , pp. 10817-10821
    • Garred, O.1    Van Deurs, B.2    Sandvig, K.3
  • 41
    • 0026704534 scopus 로고
    • Ribosomal RNA identity elements for ricin A-chain recognition and catalysis: Analysis with tetraloop mutants
    • Gluck A, Endo Y, Wool IG (1992) Ribosomal RNA identity elements for ricin A-chain recognition and catalysis: Analysis with tetraloop mutants. J Mol Biol 226:411-424
    • (1992) J Mol Biol , vol.226 , pp. 411-424
    • Gluck, A.1    Endo, Y.2    Wool, I.G.3
  • 42
    • 0037781517 scopus 로고    scopus 로고
    • The puzzling lateral flexible stalk of the ribosome
    • DOI 10.1016/S0248-4900(03)00034-0
    • Gonzalo P, Reboud JP (2003) The puzzling lateral flexible stalk of the ribosome. Biol Cell 95:179-193 (Pubitemid 36889220)
    • (2003) Biology of the Cell , vol.95 , Issue.3-4 , pp. 179-193
    • Gonzalo, P.1    Reboud, J.-P.2
  • 43
    • 0035827659 scopus 로고    scopus 로고
    • Pivotal role of the P1 N-terminal domain in the assembly of the mammalian ribosomal stalk and in the proteosynthetic activity
    • Gonzalo P, Lavergne JP, Reboud JP (2001) Pivotal role of the P1 N-terminal domain in the assembly of the mammalian ribosomal stalk and in the proteosynthetic activity. J Biol Chem 276:19762-19769
    • (2001) J Biol Chem , vol.276 , pp. 19762-19769
    • Gonzalo, P.1    Lavergne, J.P.2    Reboud, J.P.3
  • 45
    • 0035980142 scopus 로고    scopus 로고
    • Asymmetric interactions between the acidic P1 and P2 proteins in the Saccharomyces cerevisiae ribosomal stalk
    • Guarinos E, Remacha M, Ballesta JP (2001) Asymmetric interactions between the acidic P1 and P2 proteins in the Saccharomyces cerevisiae ribosomal stalk. J Biol Chem 276:32474-32479
    • (2001) J Biol Chem , vol.276 , pp. 32474-32479
    • Guarinos, E.1    Remacha, M.2    Ballesta, J.P.3
  • 46
    • 0142093587 scopus 로고    scopus 로고
    • Tag-mediated fractionation of yeast ribosome populations proves the monomeric organization of the eukaryotic ribosomal stalk structure
    • DOI 10.1046/j.1365-2958.2003.03733.x
    • Guarinos E, Santos C, Sanchez A, Qiu DY, Remacha M, Ballesta JP (2003) Tag-mediated fractionation of yeast ribosome populations proves the monomeric organization of the eukaryotic ribosomal stalk structure. Mol Microbiol 50:703-712 (Pubitemid 37297145)
    • (2003) Molecular Microbiology , vol.50 , Issue.2 , pp. 703-712
    • Guarinos, E.1    Santos, C.2    Sanchez, A.3    Qiu, D.-Y.4    Remacha, M.5    Ballesta, J.P.G.6
  • 48
    • 0025878152 scopus 로고
    • Preparation of VT1 and VT2 hybrid toxins from their purified dissociated subunits: Evidence for B subunit modulation of a subunit function
    • Head SC, Karmali MA, Lingwood CA (1991) Preparation of VT1 and VT2 hybrid toxins from their purified dissociated subunits: evidence for B subunit modulation of a subunit function. J Biol Chem 266:3617-3621 (Pubitemid 21909257)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.6 , pp. 3617-3621
    • Head, S.C.1    Karmali, M.A.2    Lingwood, C.A.3
  • 49
    • 0033524919 scopus 로고    scopus 로고
    • Pokeweed antiviral protein accesses ribosomes by binding to L3
    • DOI 10.1074/jbc.274.6.3859
    • Hudak KA, Dinman JD, Tumer NE (1999) Pokeweed antiviral protein accesses ribosomes by binding to L3. J Biol Chem 274:3859-3864 (Pubitemid 29077236)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.6 , pp. 3859-3864
    • Hudak, K.A.1    Dinman, J.D.2    Tumer, N.E.3
  • 50
    • 4043177111 scopus 로고    scopus 로고
    • Generation of pokeweed antiviral protein mutations in Saccharomyces cerevisiae: Evidence that ribosome depurination is not sufficient for cytotoxicity
    • DOI 10.1093/nar/gkh757
    • Hudak KA, Parikh BA, Di R, Baricevic M, Santana M, Seskar M, Tumer NE (2004) Generation of pokeweed antiviral protein mutations in Saccharomyces cerevisiae: evidence that ribosome depurination is not sufficient for cytotoxicity. Nucleic Acids Res 32:4244-4256 (Pubitemid 39232297)
    • (2004) Nucleic Acids Research , vol.32 , Issue.14 , pp. 4244-4256
    • Hudak, K.A.1    Parikh, B.A.2    Di, R.3    Baricevic, M.4    Santana, M.5    Seskar, M.6    Tumer, N.E.7
  • 51
    • 0022508584 scopus 로고
    • Pathogenesis of shigella diarrhea. XI. Isolation of a shigella toxin-binding glycolipid from rabbit jejunum and HeLa cells and its identification as globotriaosylceramide
    • Jacewicz M, Clausen H, Nudelman E, Donohue-Rolfe A, Keusch GT (1986) Pathogenesis of shigella diarrhea XI: Isolation of a shigella toxin-binding glycolipid from rabbit jejunum and HeLa cells and its identification as globotriaosylceramide. J Exp Med 163:1391-1404 (Pubitemid 16043460)
    • (1986) Journal of Experimental Medicine , vol.163 , Issue.6 , pp. 1391-1404
    • Jacewicz, M.1    Clausen, H.2    Nudelman, E.3
  • 55
    • 33745090478 scopus 로고    scopus 로고
    • The electrostatic character of the ribosomal surface enables extraordinarily rapid target location by ribotoxins
    • DOI 10.1038/nsmb1082, PII N1082
    • Korennykh AV, Piccirilli JA, Correll CC (2006) The electrostatic character of the ribosomal surface enables extraordinarily rapid target location by ribotoxins. Nat Struct Mol Biol 13:436-443 (Pubitemid 43881584)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.5 , pp. 436-443
    • Korennykh, A.V.1    Piccirilli, J.A.2    Correll, C.C.3
  • 56
    • 34548348189 scopus 로고    scopus 로고
    • Evidence for the importance of electrostatics in the function of two distinct families of ribosome inactivating toxins
    • DOI 10.1261/rna.619707
    • Korennykh AV, Correll CC, Piccirilli JA (2007) Evidence for the importance of electrostatics in the function of two distinct families of ribosome inactivating toxins. RNA 13:1391-1396 (Pubitemid 47347409)
    • (2007) RNA , vol.13 , Issue.9 , pp. 1391-1396
    • Korennykh, A.V.1    Correll, C.C.2    Piccirilli, J.A.3
  • 59
    • 77956123000 scopus 로고    scopus 로고
    • Solution structure of the dimerization domain of ribosomal protein P2 provides insights for the structural organization of eukaryotic stalk
    • Lee KM, Yu CW, Chan DS, Chiu TY, Zhu G, Sze KH, Shaw PC, Wong KB (2010) Solution structure of the dimerization domain of ribosomal protein P2 provides insights for the structural organization of eukaryotic stalk. Nucleic Acids Res 38:5206-5216
    • (2010) Nucleic Acids Res , vol.38 , pp. 5206-5216
    • Lee, K.M.1    Yu, C.W.2    Chan, D.S.3    Chiu, T.Y.4    Zhu, G.5    Sze, K.H.6    Shaw, P.C.7    Wong, K.B.8
  • 60
    • 33845976010 scopus 로고    scopus 로고
    • Ribosome depurination is not sufficient for ricin-mediated cell death in Saccharomyces cerevisiae
    • DOI 10.1128/IAI.01295-06
    • Li XP, Baricevic M, Saidasan H, Tumer NE (2007) Ribosome depurination is not sufficient for ricin-mediated cell death in Saccharomyces cerevisiae. Infect Immun 75:417-428 (Pubitemid 46047918)
    • (2007) Infection and Immunity , vol.75 , Issue.1 , pp. 417-428
    • Li, X.-P.1    Baricevic, M.2    Saidasan, H.3    Tumer, N.E.4
  • 61
    • 66149084818 scopus 로고    scopus 로고
    • A two-step binding model proposed for the electrostatic interactions of ricin a chain with ribosomes
    • Li XP, Chiou JC, Remacha M, Ballesta JP, Tumer NE (2009) A two-step binding model proposed for the electrostatic interactions of ricin a chain with ribosomes. Biochemistry 48:3853-3863
    • (2009) Biochemistry , vol.48 , pp. 3853-3863
    • Li, X.P.1    Chiou, J.C.2    Remacha, M.3    Ballesta, J.P.4    Tumer, N.E.5
  • 62
    • 78650659145 scopus 로고    scopus 로고
    • Pentameric organization of the ribosomal stalk accelerates recruitment of ricin a chain to the ribosome for depurination
    • Li XP, Grela P, Krokowski D, Tchorzewski M, Tumer NE (2010) Pentameric organization of the ribosomal stalk accelerates recruitment of ricin a chain to the ribosome for depurination. J Biol Chem 285:41463-41471
    • (2010) J Biol Chem , vol.285 , pp. 41463-41471
    • Li, X.P.1    Grela, P.2    Krokowski, D.3    Tchorzewski, M.4    Tumer, N.E.5
  • 64
    • 41249097425 scopus 로고    scopus 로고
    • The catalytic subunit of Shiga-like toxin 1 interacts with ribosomal stalk proteins and is inhibited by their conserved C-terminal domain
    • McCluskey AJ, Poon GM, Bolewska-Pedyczak E, Srikumar T, Jeram SM, Raught B, Gariepy J (2008) The catalytic subunit of Shiga-like toxin 1 interacts with ribosomal stalk proteins and is inhibited by their conserved C-terminal domain. J Mol Biol 378:375-386
    • (2008) J Mol Biol , vol.378 , pp. 375-386
    • McCluskey, A.J.1    Poon, G.M.2    Bolewska-Pedyczak, E.3    Srikumar, T.4    Jeram, S.M.5    Raught, B.6    Gariepy, J.7
  • 65
    • 0037108102 scopus 로고    scopus 로고
    • GTPase activation of elongation factors Tu and G on the ribosome
    • Mohr D, Wintermeyer W, Rodnina MV (2002) GTPase activation of elongation factors Tu and G on the ribosome. Biochemistry 41:12520-12528
    • (2002) Biochemistry , vol.41 , pp. 12520-12528
    • Mohr, D.1    Wintermeyer, W.2    Rodnina, M.V.3
  • 66
    • 0016441396 scopus 로고
    • Inhibition by ricin of protein synthesis in vitro: Inhibition of the binding of elongation factor 2 and of adenosine diphosphate-ribosylated elongation factor 2 to ribosomes
    • Montanaro L, Sperti S, Mattioli A, Testoni G, Stirpe F (1975) Inhibition by ricin of protein synthesis in vitro: inhibition of the binding of elongation factor 2 and of adenosine diphosphate-ribosylated elongation factor 2 to ribosomes. Biochem J 146:127-131
    • (1975) Biochem J , vol.146 , pp. 127-131
    • Montanaro, L.1    Sperti, S.2    Mattioli, A.3    Testoni, G.4    Stirpe, F.5
  • 67
    • 0030774277 scopus 로고    scopus 로고
    • The ribosome-in-pieces: Binding of elongation factor EF-G to oligoribonucleotides that mimic the sarcin/ricin and thiostrepton domains of 23S ribosomal RNA
    • Munishkin A, Wool IG (1997) The ribosome-in-pieces: binding of elongation factor EF-G to oligoribonucleotides that mimic the sarcin/ricin and thiostrepton domains of 23S ribosomal RNA. Proc Nat Acad Sci USA 94:12280-12284
    • (1997) Proc Nat Acad Sci USA , vol.94 , pp. 12280-12284
    • Munishkin, A.1    Wool, I.G.2
  • 68
    • 77951179786 scopus 로고    scopus 로고
    • Structural basis for translation factor recruitment to the eukaryotic/archaeal ribosomes
    • Naganuma T, Nomura N, Yao M, Mochizuki M, Uchiumi T, Tanaka I (2010) Structural basis for translation factor recruitment to the eukaryotic/archaeal ribosomes. J Biol Chem 285: 4747-4756
    • (2010) J Biol Chem , vol.285 , pp. 4747-4756
    • Naganuma, T.1    Nomura, N.2    Yao, M.3    Mochizuki, M.4    Uchiumi, T.5    Tanaka, I.6
  • 71
    • 0035780977 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins: A plant perspective
    • Nielsen K, Boston RS (2001) Ribosome-inactivating proteins: a plant perspective. Annu Rev Plant Physiol Plant Mol Biol 52:785-816 (Pubitemid 33720055)
    • (2001) Annual Review of Plant Biology , vol.52 , pp. 785-816
    • Nielsen, K.1    Boston, R.S.2
  • 72
    • 0017294568 scopus 로고
    • The binding of tritiated elongation-factors 1 and 2 to ribosomes from Krebs II mouse ascites-tumore cells: The influence of various antibiotics and toxins
    • Nolan RD, Grasmuk H, Drews J (1976) The binding of tritiated elongation-factors 1 and 2 to ribosomes from Krebs II mouse ascites-tumore cells: the influence of various antibiotics and toxins. Eur J Biochem 64:69-75
    • (1976) Eur J Biochem , vol.64 , pp. 69-75
    • Nolan, R.D.1    Grasmuk, H.2    Drews, J.3
  • 73
    • 0034669118 scopus 로고    scopus 로고
    • Phosphorylation and N-terminal region of yeast ribosomal protein P1 mediate its degradation, which is prevented by protein P2
    • Nusspaumer G, Remacha M, Ballesta JP (2000) Phosphorylation and N-terminal region of yeast ribosomal protein P1 mediate its degradation, which is prevented by protein P2. EMBO J 19:6075-6084
    • (2000) EMBO J , vol.19 , pp. 6075-6084
    • Nusspaumer, G.1    Remacha, M.2    Ballesta, J.P.3
  • 74
    • 0024514137 scopus 로고
    • Characterization of the ribosomal properties required for formation of a GTPase active complex with the eukaryotic elongation factor 2
    • DOI 10.1111/j.1432-1033.1989.tb14589.x
    • Nygard O, Nilsson L (1989) Characterization of the ribosomal properties required for formation of a GTPase active complex with the eukaryotic elongation factor 2. Eur J Biochem 179:603-608 (Pubitemid 19062336)
    • (1989) European Journal of Biochemistry , vol.179 , Issue.3 , pp. 603-608
    • Nygard, O.1    Nilsson, L.2
  • 75
    • 0021683078 scopus 로고
    • Shiga-like toxin-converting phages from Escherichia coli strains that cause hemorrhagic colitis or infantile diarrhea
    • O'Brien AD, Newland JW, Miller SF, Holmes RK, Smith HW, Formal SB (1984) Shiga-like toxin-converting phages from Escherichia coli strains that cause hemorrhagic colitis or infantile diarrhea. Science 226:694-696 (Pubitemid 15202147)
    • (1984) Science , vol.226 , Issue.4675 , pp. 694-696
    • O'Brien, A.D.1    Newland, J.W.2    Miller, S.F.3
  • 77
    • 4043074939 scopus 로고    scopus 로고
    • The history of ricin, abrin and related toxins
    • DOI 10.1016/j.toxicon.2004.05.003, PII S0041010104001898
    • Olsnes S (2004) The history of ricin, abrin and related toxins. Toxicon 44:361-370 (Pubitemid 39070638)
    • (2004) Toxicon , vol.44 , Issue.4 , pp. 361-370
    • Olsnes, S.1
  • 78
    • 0015523431 scopus 로고
    • Inhibition of peptide chain elongation
    • Olsnes S, Pihl A (1972a) Inhibition of peptide chain elongation. Nature 238:459-461
    • (1972) Nature , vol.238 , pp. 459-461
    • Olsnes, S.1    Pihl, A.2
  • 79
    • 0041022096 scopus 로고
    • Ricin-a potent inhibitor of protein synthesis
    • Olsnes S, Pihl A (1972b) Ricin-a potent inhibitor of protein synthesis. FEBS Lett 20:327-329
    • (1972) FEBS Lett , vol.20 , pp. 327-329
    • Olsnes, S.1    Pihl, A.2
  • 80
    • 3042522611 scopus 로고    scopus 로고
    • Antiviral activity of ribosome inactivating proteins in medicine
    • Parikh BA, Tumer NE (2004) Antiviral activity of ribosome inactivating proteins in medicine. Mini Rev Med Chem 4:523-543 (Pubitemid 38842613)
    • (2004) Mini-Reviews in Medicinal Chemistry , vol.4 , Issue.5 , pp. 523-543
    • Parikh, B.A.1    Tumer, N.E.2
  • 81
    • 0031848112 scopus 로고    scopus 로고
    • Pathogenesis and diagnosis of Shiga toxin-producing Escherichia coli infections
    • Paton JC, Paton AW (1998) Pathogenesis and diagnosis of Shiga toxin-producing Escherichia coli infections. Clin Microbiol Rev 11:450-479 (Pubitemid 28379095)
    • (1998) Clinical Microbiology Reviews , vol.11 , Issue.3 , pp. 450-479
    • Paton, J.C.1    Paton, A.W.2
  • 82
    • 0028270884 scopus 로고
    • Hemolytic-uremic syndrome and enterohemorrhagic Escherichia coli
    • quiz 476
    • Pickering LK, Obrig TG, Stapleton FB (1994) Hemolytic-uremic syndrome and enterohemorrhagic Escherichia coli. Pediatr Infect Dis J 13:459-475quiz 476
    • (1994) Pediatr Infect Dis J , vol.13 , pp. 459-475
    • Pickering, L.K.1    Obrig, T.G.2    Stapleton, F.B.3
  • 83
    • 79953727280 scopus 로고    scopus 로고
    • The ribotoxin restrictocin recognizes its RNA substrate by selective engagement of active site residues
    • Plantinga MJ, Korennykh AV, Piccirilli JA, Correll CC (2011) The ribotoxin restrictocin recognizes its RNA substrate by selective engagement of active site residues. Biochemistry 50:3004-3013
    • (2011) Biochemistry , vol.50 , pp. 3004-3013
    • Plantinga, M.J.1    Korennykh, A.V.2    Piccirilli, J.A.3    Correll, C.C.4
  • 84
    • 0035968204 scopus 로고    scopus 로고
    • Binding interactions between the active center cleft of recombinant pokeweed antiviral protein and the alpha-sarcin/ricin stem loop of ribosomal RNA
    • Rajamohan F, Mao C, Uckun FM (2001a) Binding interactions between the active center cleft of recombinant pokeweed antiviral protein and the alpha-sarcin/ricin stem loop of ribosomal RNA. J Biol Chem 276:24075-24081
    • (2001) J Biol Chem , vol.276 , pp. 24075-24081
    • Rajamohan, F.1    Mao, C.2    Uckun, F.M.3
  • 85
    • 0035822657 scopus 로고    scopus 로고
    • Active center cleft residues of pokeweed antiviral protein mediate its high-affinity binding to the ribosomal protein L3
    • DOI 10.1021/bi002851p
    • Rajamohan F, Ozer Z, Mao C, Uckun FM (2001b) Active center cleft residues of pokeweed antiviral protein mediate its high-affinity binding to the ribosomal protein L3. Biochemistry 40:9104-9114 (Pubitemid 32730031)
    • (2001) Biochemistry , vol.40 , Issue.31 , pp. 9104-9114
    • Rajamohan, F.1    Ozer, Z.2    Mao, C.3    Uckun, F.M.4
  • 86
    • 0025986909 scopus 로고
    • Site-directed mutagenesis of ricin A-chain and implications for the mechanism of action
    • Ready MP, Kim Y, Robertus JD (1991) Site-directed mutagenesis of ricin A-chain and implications for the mechanism of action. Proteins 10:270-278
    • (1991) Proteins , vol.10 , pp. 270-278
    • Ready, M.P.1    Kim, Y.2    Robertus, J.D.3
  • 89
    • 0029909329 scopus 로고    scopus 로고
    • Endocytosis, intracellular transport, and cytotoxic action of Shiga toxin and ricin
    • Sandvig K, van Deurs B (1996) Endocytosis, intracellular transport, and cytotoxic action of Shiga toxin and ricin. Physiol Rev 76:949-966 (Pubitemid 26346812)
    • (1996) Physiological Reviews , vol.76 , Issue.4 , pp. 949-966
    • Sandvig, K.1    Van Deurs, B.2
  • 90
    • 0037010141 scopus 로고    scopus 로고
    • Transport of protein toxins into cells: Pathways used by ricin, cholera toxin and Shiga toxin
    • DOI 10.1016/S0014-5793(02)03182-4, PII S0014579302031824
    • Sandvig K, van Deurs B (2002) Transport of protein toxins into cells: pathways used by ricin, cholera toxin and Shiga toxin. FEBS Lett 529:49-53 (Pubitemid 35283911)
    • (2002) FEBS Letters , vol.529 , Issue.1 , pp. 49-53
    • Sandvig, K.1    Van Deurs, B.2
  • 91
    • 20744450629 scopus 로고    scopus 로고
    • Delivery into cells: Lessons learned from plant and bacterial toxins
    • DOI 10.1038/sj.gt.3302525, Vector Traffic
    • Sandvig K, van Deurs B (2005) Delivery into cells: lessons learned from plant and bacterial toxins. Gene Ther 12:865-872 (Pubitemid 40852204)
    • (2005) Gene Therapy , vol.12 , Issue.11 , pp. 865-872
    • Sandvig, K.1    Van Deurs, B.2
  • 92
  • 96
    • 33747229123 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins: Progress and problems
    • Stirpe F, Battelli MG (2006) Ribosome-inactivating proteins: progress and problems. Cell Mol Life Sci 63:1850-1866
    • (2006) Cell Mol Life Sci , vol.63 , pp. 1850-1866
    • Stirpe, F.1    Battelli, M.G.2
  • 97
    • 0032581041 scopus 로고    scopus 로고
    • Shiga toxin attacks bacterial ribosomes as effectively as eucaryotic ribosomes
    • DOI 10.1021/bi980424u
    • Suh JK, Hovde CJ, Robertus JD (1998) Shiga toxin attacks bacterial ribosomes as effectively as eucaryotic ribosomes. Biochemistry 37:9394-9398 (Pubitemid 28307694)
    • (1998) Biochemistry , vol.37 , Issue.26 , pp. 9394-9398
    • Suh, J.-K.1    Hovde, C.J.2    Robertus, J.D.3
  • 98
    • 0028953727 scopus 로고
    • The sarcin/ricin loop, a modular RNA
    • Szewczak AA, Moore PB (1995) The sarcin/ricin loop, a modular RNA. J Mol Biol 247:81-98
    • (1995) J Mol Biol , vol.247 , pp. 81-98
    • Szewczak, A.A.1    Moore, P.B.2
  • 99
    • 0028446541 scopus 로고
    • Correlation between the activities of five ribosome-inactivating proteins in depurination of tobacco ribosomes and inhibition of tobacco mosaic virus infection
    • Taylor S, Massiah A, Lomonossoff G, Roberts LM, Lord JM, Hartley M (1994) Correlation between the activities of five ribosome-inactivating proteins in depurination of tobacco ribosomes and inhibition of tobacco mosaic virus infection. Plant J 5:827-835
    • (1994) Plant J , vol.5 , pp. 827-835
    • Taylor, S.1    Massiah, A.2    Lomonossoff, G.3    Roberts, L.M.4    Lord, J.M.5    Hartley, M.6
  • 100
    • 0344405681 scopus 로고    scopus 로고
    • Structural characterization of yeast acidic ribosomal P proteins forming the P1A - P2B heterocomplex
    • DOI 10.1021/bi0206006
    • Tchorzewski M, Krokowski D, Boguszewska A, Liljas A, Grankowski N (2003) Structural characterization of yeast acidic ribosomal P proteins forming the P1A-P2B heterocomplex. Biochemistry 42:3399-3408 (Pubitemid 36368633)
    • (2003) Biochemistry , vol.42 , Issue.12 , pp. 3399-3408
    • Tchorzewski, M.1    Krokowski, D.2    Boguszewska, A.3    Liljas, A.4    Grankowski, N.5
  • 102
    • 59649126993 scopus 로고    scopus 로고
    • The C-terminal fragment of the ribosomal P protein complexed to trichosanthin reveals the interaction between the ribosome-inactivating protein and the ribosome
    • Too PH, Ma MK, Mak AN, Wong YT, Tung CK, Zhu G, Au SW, Wong KB, Shaw PC (2009) The C-terminal fragment of the ribosomal P protein complexed to trichosanthin reveals the interaction between the ribosome-inactivating protein and the ribosome. Nucleic Acids Res 37:602-610
    • (2009) Nucleic Acids Res , vol.37 , pp. 602-610
    • Too, P.H.1    Ma, M.K.2    Mak, A.N.3    Wong, Y.T.4    Tung, C.K.5    Zhu, G.6    Au, S.W.7    Wong, K.B.8    Shaw, P.C.9
  • 104
    • 0025096660 scopus 로고
    • Monoclonal antibodies against acidic phosphoproteins P0, P1, and P2 of eukaryotic ribosomes as functional probes
    • Uchiumi T, Traut RR, Kominami R (1990) Monoclonal antibodies against acidic phosphoproteins P0, P1, and P2 of eukaryotic ribosomes as functional probes. J Biol Chem 265:89-95
    • (1990) J Biol Chem , vol.265 , pp. 89-95
    • Uchiumi, T.1    Traut, R.R.2    Kominami, R.3
  • 105
    • 0033600919 scopus 로고    scopus 로고
    • Replacement of L7/L12.L10 protein complex in Escherichia coli ribosomes with the eukaryotic counterpart changes the specificity of elongation factor binding
    • Uchiumi T, Hori K, Nomura T, Hachimori A (1999) Replacement of L7/L12.L10 protein complex in Escherichia coli ribosomes with the eukaryotic counterpart changes the specificity of elongation factor binding. J Biol Chem 274:27578-27582
    • (1999) J Biol Chem , vol.274 , pp. 27578-27582
    • Uchiumi, T.1    Hori, K.2    Nomura, T.3    Hachimori, A.4
  • 106
    • 0037040229 scopus 로고    scopus 로고
    • Translation elongation by a hybrid ribosome in which proteins at the GTPase center of the Escherichia coli ribosome are replaced with rat counterparts
    • DOI 10.1074/jbc.M107730200
    • Uchiumi T, Honma S, Nomura T, Dabbs ER, Hachimori A (2002) Translation elongation by a hybrid ribosome in which proteins at the GTPase center of the Escherichia coli ribosome are replaced with rat counterparts. J Biol Chem 277:3857-3862 (Pubitemid 34968636)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.6 , pp. 3857-3862
    • Uchiumi, T.1    Honma, S.2    Nomura, T.3    Dabbs, E.R.4    Hachimori, A.5
  • 107
    • 0029013242 scopus 로고
    • Ricin A chain can be chemically cross-linked to the mammalian ribosomal proteins L9 and L10e
    • Vater CA, Bartle LM, Leszyk JD, Lambert JM, Goldmacher VS (1995) Ricin A chain can be chemically cross-linked to the mammalian ribosomal proteins L9 and L10e. J Biol Chem 270:12933-12940
    • (1995) J Biol Chem , vol.270 , pp. 12933-12940
    • Vater, C.A.1    Bartle, L.M.2    Leszyk, J.D.3    Lambert, J.M.4    Goldmacher, V.S.5
  • 108
  • 109
    • 0024299352 scopus 로고
    • Globotriosyl ceramide is specifically recognized by the Escherichia coli verocytotoxin 2
    • Waddell T, Head S, Petric M, Cohen A, Lingwood C (1988) Globotriosyl ceramide is specifically recognized by the Escherichia coli verocytotoxin 2. Biochem Biophys Res Commun 152(2):674-679
    • (1988) Biochem Biophys Res Commun , vol.152 , Issue.2 , pp. 674-679
    • Waddell, T.1    Head, S.2    Petric, M.3    Cohen, A.4    Lingwood, C.5
  • 110
    • 0035999791 scopus 로고    scopus 로고
    • Structure and function of the acidic ribosomal stalk proteins
    • DOI 10.2174/1389203023380756
    • Wahl MC, Moller W (2002) Structure and function of the acidic ribosomal stalk proteins. Curr Protein Pept Sci 3:93-106 (Pubitemid 34520655)
    • (2002) Current Protein and Peptide Science , vol.3 , Issue.1 , pp. 93-106
    • Wahl, M.C.1    Moller, W.2
  • 111
    • 0026349475 scopus 로고
    • Characterization and molecular cloning of a proenzyme form of a ribosome-inactivating protein from maize: Novel mechanism of proenzyme activation by proteolytic removal of a 2.8-kilodalton internal peptide segment
    • Walsh TA, Morgan AE, Hey TD (1991) Characterization and molecular cloning of a proenzyme form of a ribosome-inactivating protein from maize: novel mechanism of proenzyme activation by proteolytic removal of a 2.8-kilodalton internal peptide segment. J Biol Chem 266:23422-23427 (Pubitemid 21908810)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.34 , pp. 23422-23427
    • Walsh, T.A.1    Morgan, A.E.2    Hey, T.D.3
  • 112
    • 0026690643 scopus 로고
    • Ribotoxin recognition of ribosomal RNA and a proposal for the mechanism of translocation
    • Wool IG, Gluck A, Endo Y (1992) Ribotoxin recognition of ribosomal RNA and a proposal for the mechanism of translocation. Trends Biochem Sci 17:266-269
    • (1992) Trends Biochem Sci , vol.17 , pp. 266-269
    • Wool, I.G.1    Gluck, A.2    Endo, Y.3
  • 113
    • 0034760104 scopus 로고    scopus 로고
    • Crystal structures of restrictocin-inhibitor complexes with implications for RNA recognition and base flipping
    • DOI 10.1038/nsb1101-968
    • Yang X, Gerczei T, Glover LT, Correll CC (2001) Crystal structures of restrictocin-inhibitor complexes with implications for RNA recognition and base flipping. Nat Struct Biol 8:968-973 (Pubitemid 33032366)
    • (2001) Nature Structural Biology , vol.8 , Issue.11 , pp. 968-973
    • Yang, X.1    Gerczei, T.2    Glover, L.3    Correll, C.C.4
  • 114
    • 73649148999 scopus 로고    scopus 로고
    • Solution structure of an active mutant of maize ribosome-inactivating protein (MOD) and its interaction with the ribosomal stalk protein P2
    • Yang Y, Mak AN, Shaw PC, Sze KH (2010) Solution structure of an active mutant of maize ribosome-inactivating protein (MOD) and its interaction with the ribosomal stalk protein P2. J Mol Biol 395:897-907
    • (2010) J Mol Biol , vol.395 , pp. 897-907
    • Yang, Y.1    Mak, A.N.2    Shaw, P.C.3    Sze, K.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.