메뉴 건너뛰기




Volumn 288, Issue 42, 2013, Pages 30270-30284

Arginine residues on the opposite side of the active site stimulate the catalysis of ribosome depurination by ricin A chain by interacting with the P-protein stalk

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ARGININE RESIDUE; DEPURINATION; P-PROTEIN; RICIN A CHAINS;

EID: 84886884229     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.510966     Document Type: Article
Times cited : (38)

References (69)
  • 1
    • 27744564219 scopus 로고    scopus 로고
    • Ricin poisoning. A comprehensive review
    • Audi, J., Belson, M., Patel, M., Schier, J., and Osterloh, J. (2005) Ricin poisoning. A comprehensive review. JAMA 294, 2342-2351
    • (2005) JAMA , vol.294 , pp. 2342-2351
    • Audi, J.1    Belson, M.2    Patel, M.3    Schier, J.4    Osterloh, J.5
  • 3
    • 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., and 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
  • 4
    • 0015801982 scopus 로고
    • Inhibition by ricin of protein synthesis in vitro. Ribosomes as the target of the toxin
    • Montanaro, L., Sperti, S., and Stirpe, F. (1973) Inhibition by ricin of protein synthesis in vitro. Ribosomes as the target of the toxin. Biochem. J. 136, 677-683
    • (1973) Biochem. J , vol.136 , pp. 677-683
    • Montanaro, L.1    Sperti, S.2    Stirpe, F.3
  • 5
    • 0016358276 scopus 로고
    • Mechanism of action of the toxic lectins abrin and ricin
    • Olsnes, S., Refsnes, K., and Pihl, A. (1974) Mechanism of action of the toxic lectins abrin and ricin. Nature 249, 627-631
    • (1974) Nature , vol.249 , pp. 627-631
    • Olsnes, S.1    Refsnes, K.2    Pihl, A.3
  • 6
    • 0023947126 scopus 로고
    • The RNA N-glycosidase activity of ricin A-chain. The characteristics of the enzymatic activity of ricin A-chain with ribosomes and with rRNA
    • Endo, Y., and Tsurugi, K. (1988) The RNA N-glycosidase activity of ricin A-chain. The characteristics of the enzymatic activity of ricin A-chain with ribosomes and with rRNA. J. Biol. Chem. 263, 8735-8739
    • (1988) J. Biol. Chem , vol.263 , pp. 8735-8739
    • Endo, Y.1    Tsurugi, K.2
  • 7
    • 0015801981 scopus 로고
    • Inhibition by ricin of protein synthesis in vitro. 60 S ribosomal subunit as the target of the toxin
    • Sperti, S., Montanaro, L., Mattioli, A., and Stirpe, F. (1973) Inhibition by ricin of protein synthesis in vitro. 60 S ribosomal subunit as the target of the toxin. Biochem. J. 136, 813-815
    • (1973) Biochem. J , vol.136 , pp. 813-815
    • Sperti, S.1    Montanaro, L.2    Mattioli, A.3    Stirpe, F.4
  • 8
    • 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., and 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
  • 9
    • 84860767838 scopus 로고    scopus 로고
    • Functional role of the sarcin-ricin loop of the 23S rRNA in the elongation cycle of protein synthesis
    • Shi, X., Khade, P. K., Sanbonmatsu, K. Y., and Joseph, S. (2012) Functional role of the sarcin-ricin loop of the 23S rRNA in the elongation cycle of protein synthesis. J. Mol. Biol. 419, 125-138
    • (2012) J. Mol. Biol. , vol.419 , pp. 125-138
    • Shi, X.1    Khade, P.K.2    Sanbonmatsu, K.Y.3    Joseph, S.4
  • 10
    • 0017396837 scopus 로고
    • Reciprocal interactions of ricin from Ricinus communis L. seeds with eukaryote ribosomes
    • Lugnier, A. A., Creppy, E. E., Le Meur, M. A., Gerlinger, P., and Dirheimer, G. (1977) Reciprocal interactions of ricin from Ricinus communis L. seeds with eukaryote ribosomes. FEBS Lett. 76, 166-172
    • (1977) FEBS Lett , vol.76 , pp. 166-172
    • Lugnier, A.A.1    Creppy, E.E.2    Le Meur, M.A.3    Gerlinger, P.4    Dirheimer, G.5
  • 11
    • 3042515159 scopus 로고    scopus 로고
    • Cytotoxicity and toxicity to animals and humans of ribosome-inactivating proteins
    • Battelli, M. G. (2004) Cytotoxicity and toxicity to animals and humans of ribosome-inactivating proteins. Mini Rev. Med. Chem. 4, 513-521
    • (2004) Mini Rev. Med. Chem. , vol.4 , pp. 513-521
    • Battelli, M.G.1
  • 13
    • 0018426962 scopus 로고
    • Protection and rescue of ribosomes from the action of ricin A chain
    • Cawley, D. B., Hedblom, M. L., and Houston, L. L. (1979) Protection and rescue of ribosomes from the action of ricin A chain. Biochemistry 18, 2648-2654
    • (1979) Biochemistry , vol.18 , pp. 2648-2654
    • Cawley, D.B.1    Hedblom, M.L.2    Houston, L.L.3
  • 14
    • 0036185561 scopus 로고    scopus 로고
    • Real-time kinetic analyses of the interaction of ricin toxin A-chain with ribosomes prove a conformational change involved in complex formation
    • Honjo, E., Watanabe, K., and Tsukamoto, T. (2002) Real-time kinetic analyses of the interaction of ricin toxin A-chain with ribosomes prove a conformational change involved in complex formation. J. Biochem. 131, 267-275
    • (2002) J. Biochem. , vol.131 , pp. 267-275
    • Honjo, E.1    Watanabe, K.2    Tsukamoto, T.3
  • 15
    • 0017168713 scopus 로고
    • The specific binding of ricin and its polypeptide chains to rat liver ribosomes and ribosomal subunits
    • Hedblom, M. L., Cawley, D. B., and Houston, L. L. (1976) The specific binding of ricin and its polypeptide chains to rat liver ribosomes and ribosomal subunits. Arch. Biochem. Biophys. 177, 46-55
    • (1976) Arch. Biochem. Biophys. , vol.177 , pp. 46-55
    • Hedblom, M.L.1    Cawley, D.B.2    Houston, L.L.3
  • 16
    • 0032581041 scopus 로고    scopus 로고
    • Shiga toxin attacks bacterial ribosomes as effectively as eucaryotic ribosomes
    • Suh, J. K., Hovde, C. J., and Robertus, J. D. (1998) Shiga toxin attacks bacterial ribosomes as effectively as eucaryotic ribosomes. Biochemistry 37, 9394-9398
    • (1998) Biochemistry , vol.37 , pp. 9394-9398
    • Suh, J.K.1    Hovde, C.J.2    Robertus, J.D.3
  • 17
    • 84863285459 scopus 로고    scopus 로고
    • Interaction of ricin and Shiga toxins with ribosomes
    • Tumer, N. E., and Li, X. P. (2012) Interaction of ricin and Shiga toxins with ribosomes. Curr. Top. Microbiol. Immunol. 357, 1-18
    • (2012) Curr. Top. Microbiol. Immunol. , vol.357 , pp. 1-18
    • Tumer, N.E.1    Li, X.P.2
  • 18
    • 66149084818 scopus 로고    scopus 로고
    • A two-step binding model proposed for the electrostatic interactions of ricin A chain with ribosomes
    • Li, X. P., Chiou, J. C., Remacha, M., Ballesta, J. P., and Tumer, N. E. (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
  • 19
    • 56749154533 scopus 로고    scopus 로고
    • The ribosomal stalk is required for ribosome binding, depurination of the rRNA and cytotoxicity of ricin A chain i
    • Chiou, J. C., Li, X. P., Remacha, M., Ballesta, J. P., and Tumer, N. E. (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) Saccharomyces Cerevisiae. 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
  • 20
    • 84867103425 scopus 로고    scopus 로고
    • The P1/P2 proteins of the human ribosomal stalk are required for ribosome binding and depurination by ricin in human cells
    • May, K. L., Li, X. P., Martínez-Azorin, F., Ballesta, J. P., Grela, P., Tchórzewski, M., and Tumer, N. E. (2012) The P1/P2 proteins of the human ribosomal stalk are required for ribosome binding and depurination by ricin in human cells. FEBS J. 279, 3925-3936
    • (2012) FEBS J. , vol.279 , pp. 3925-3936
    • May, K.L.1    Li, X.P.2    Martínez-Azorin, F.3    Ballesta, J.P.4    Grela, P.5    Tchórzewski, M.6    Tumer, N.E.7
  • 21
    • 78650659145 scopus 로고    scopus 로고
    • Pentameric organization of the ribosomal stalk accelerates recruitment of ricin a chain to the ribosome for depurination
    • Li, X. P., Grela, P., Krokowski, D., Tchórzewski, M., and Tumer, N. E. (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    Tchórzewski, M.4    Tumer, N.E.5
  • 22
    • 0035999791 scopus 로고    scopus 로고
    • Structure and function of the acidic ribosomal stalk proteins
    • Wahl, M. C., and Möller, W. (2002) Structure and function of the acidic ribosomal stalk proteins. Curr. Protein Pept. Sci. 3, 93-106
    • (2002) Curr. Protein Pept. Sci. , vol.3 , pp. 93-106
    • Wahl, M.C.1    Möller, W.2
  • 23
    • 0037781517 scopus 로고    scopus 로고
    • The puzzling lateral flexible stalk of the ribosome
    • Gonzalo, P., and Reboud, J. P. (2003) The puzzling lateral flexible stalk of the ribosome. Biol. Cell 95, 179-193
    • (2003) Biol. Cell , vol.95 , pp. 179-193
    • Gonzalo, P.1    Reboud, J.P.2
  • 25
    • 0142093587 scopus 로고    scopus 로고
    • Tag-mediated fractionation of yeast ribosome populations proves the monomeric organization of the eukaryotic ribosomal stalk structure
    • Guarinos, E., Santos, C., Sánchez, A., Qiu, D. Y., Remacha, M., and Ballesta, J. P. (2003) Tag-mediated fractionation of yeast ribosome populations proves the monomeric organization of the eukaryotic ribosomal stalk structure. Mol. Microbiol. 50, 703-712
    • (2003) Mol. Microbiol. , vol.50 , pp. 703-712
    • Guarinos, E.1    Santos, C.2    Sánchez, A.3    Qiu, D.Y.4    Remacha, M.5    Ballesta, J.P.6
  • 27
    • 0029135319 scopus 로고
    • The highly conserved protein P0 carboxyl end is essential for ribosome activity only in the absence of proteins P1 and P2
    • Santos, C., and Ballesta, J. P. (1995) The highly conserved protein P0 carboxyl end is essential for ribosome activity only in the absence of proteins P1 and P2. J. Biol. Chem. 270, 20608-20614
    • (1995) J. Biol. Chem. , vol.270 , pp. 20608-20614
    • Santos, C.1    Ballesta, J.P.2
  • 29
    • 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
    • Chan, D. S., Chu, L. O., Lee, K. M., Too, P. H., Ma, K. W., Sze, K. H., Zhu, G., Shaw, P. C., and Wong, K. B. (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
    • (2007) Nucleic Acids Res. , vol.35 , pp. 1660-1672
    • Chan, D.S.1    Chu, L.O.2    Lee, K.M.3    Too, P.H.4    Ma, K.W.5    Sze, K.H.6    Zhu, G.7    Shaw, P.C.8    Wong, K.B.9
  • 30
    • 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, A. J., Poon, G. M., Bolewska-Pedyczak, E., Srikumar, T., Jeram, S. M., Raught, B., and Gariépy, 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    Gariépy, J.7
  • 31
    • 84857098126 scopus 로고    scopus 로고
    • Charged and hydrophobic surfaces on the a chain of shiga-like toxin 1 recognize the C-terminal domain of ribosomal stalk proteins
    • McCluskey, A. J., Bolewska-Pedyczak, E., Jarvik, N., Chen, G., Sidhu, S. S., and Gariépy, J. (2012) Charged and hydrophobic surfaces on the a chain of shiga-like toxin 1 recognize the C-terminal domain of ribosomal stalk proteins. PLoS One 7, e31191
    • (2012) PLoS One , vol.7
    • McCluskey, A.J.1    Bolewska-Pedyczak, E.2    Jarvik, N.3    Chen, G.4    Sidhu, S.S.5    Gariépy, J.6
  • 32
    • 84885924558 scopus 로고    scopus 로고
    • Solution structure of human P1*P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosome
    • in press
    • Lee, K. M., Yusa, K., Chu, L. O., Wing-Heng Yu, C., Oono, M., Miyoshi, T., Ito, K., Shaw, P. C., Wong, K. B., and Uchiumi, T. (2013) Solution structure of human P1*P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosome. Nucleic Acids Res., in press
    • (2013) Nucleic Acids Res
    • Lee, K.M.1    Yusa, K.2    Chu, L.O.3    Wing-Heng Yu, C.4    Oono, M.5    Miyoshi, T.6    Ito, K.7    Shaw, P.C.8    Wong, K.B.9    Uchiumi, T.10
  • 33
    • 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, P. H., Ma, M. K., Mak, A. N., Wong, Y. T., Tung, C. K., Zhu, G., Au, S. W., Wong, K. B., and Shaw, P. C. (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
  • 34
    • 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, A. N., Shaw, P. C., and Sze, K. H. (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
  • 35
    • 84856080521 scopus 로고    scopus 로고
    • Convergent evolution led ribosome inactivating proteins to interact with ribosomal stalk
    • Lapadula, W. J., Sanchez-Puerta, M. V., and Ayub, M. J. (2012) Convergent evolution led ribosome inactivating proteins to interact with ribosomal stalk. Toxicon 59, 427-432
    • (2012) Toxicon , vol.59 , pp. 427-432
    • Lapadula, W.J.1    Sanchez-Puerta, M.V.2    Ayub, M.J.3
  • 37
    • 0023029307 scopus 로고
    • Involvement of arginine residues in inhibition of protein synthesis by ricin A-chain
    • Watanabe, K., and Funatsu, G. (1986) Involvement of arginine residues in inhibition of protein synthesis by ricin A-chain. FEBS Lett. 204, 219-222
    • (1986) FEBS Lett. , vol.204 , pp. 219-222
    • Watanabe, K.1    Funatsu, G.2
  • 38
    • 85007967644 scopus 로고
    • Effects of chemical modification of arginine residues outside the active site cleft of ricin A-chain on its RNA N-glycosidase activity for ribosomes
    • Watanabe, K., Dansako, H., Asada, N., Sakai, M., and Funatsu, G. (1994) Effects of chemical modification of arginine residues outside the active site cleft of ricin A-chain on its RNA N-glycosidase activity for ribosomes. Biosci. Biotechnol. Biochem. 58, 716-721
    • (1994) Biosci. Biotechnol. Biochem , vol.58 , pp. 716-721
    • Watanabe, K.1    Dansako, H.2    Asada, N.3    Sakai, M.4    Funatsu, G.5
  • 39
    • 0032189770 scopus 로고    scopus 로고
    • Involvement of the amino acids outside the active-site cleft in the catalysis of ricin A chain
    • Kitaoka, Y. (1998) Involvement of the amino acids outside the active-site cleft in the catalysis of ricin A chain. Eur. J. Biochem. 257, 255-262
    • (1998) Eur. J. Biochem. , vol.257 , pp. 255-262
    • Kitaoka, Y.1
  • 42
    • 77957601374 scopus 로고    scopus 로고
    • Folding domains within the ricin toxin A subunit as targets of protective antibodies
    • O'Hara, J. M., Neal, L. M., McCarthy, E. A., Kasten-Jolly, J. A., Brey, R. N., 3rd, and Mantis, N. J. (2010) Folding domains within the ricin toxin A subunit as targets of protective antibodies. Vaccine 28, 7035-7046
    • (2010) Vaccine , vol.28 , pp. 7035-7046
    • O'hara, J.M.1    Neal, L.M.2    McCarthy, E.A.3    Kasten-Jolly, J.A.4    Brey, R.N.5    Mantis III, N.J.6
  • 43
    • 84857812737 scopus 로고    scopus 로고
    • Immunity to ricin. Fundamental insights into toxin-antibody interactions
    • O'Hara, J. M., Yermakova, A., and Mantis, N. J. (2012) Immunity to ricin. Fundamental insights into toxin-antibody interactions. Curr. Top. Microbiol. Immunol. 357, 209-241
    • (2012) Curr. Top. Microbiol. Immunol. , vol.357 , pp. 209-241
    • O'hara, J.M.1    Yermakova, A.2    Mantis, N.J.3
  • 44
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy. Methods and reference databases
    • Whitmore, L., and Wallace, B. A. (2008) Protein secondary structure analyses from circular dichroism spectroscopy. Methods and reference databases. Biopolymers 89, 392-400
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 45
    • 33747855587 scopus 로고    scopus 로고
    • A reference database for circular dichroism spectroscopy covering fold and secondary structure space
    • Lees, J. G., Miles, A. J., Wien, F., and Wallace, B. A. (2006) A reference database for circular dichroism spectroscopy covering fold and secondary structure space. Bioinformatics 22, 1955-1962
    • (2006) Bioinformatics , vol.22 , pp. 1955-1962
    • Lees, J.G.1    Miles, A.J.2    Wien, F.3    Wallace, B.A.4
  • 46
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher, S. W., and Glöckner, J. (1981) Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20, 33-37
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glöckner, J.2
  • 47
    • 78650458476 scopus 로고    scopus 로고
    • Development of a quantitative RT-PCR assay to examine the kinetics of ribosome depurination by ribosome inactivating proteins using Saccharomyces cerevisiae as a model
    • Pierce, M., Kahn, J. N., Chiou, J., and Tumer, N. E. (2011) Development of a quantitative RT-PCR assay to examine the kinetics of ribosome depurination by ribosome inactivating proteins using Saccharomyces cerevisiae as a model. RNA 17, 201-210
    • (2011) RNA , vol.17 , pp. 201-210
    • Pierce, M.1    Kahn, J.N.2    Chiou, J.3    Tumer, N.E.4
  • 49
    • 65249171997 scopus 로고    scopus 로고
    • Detecting ricin. Sensitive luminescent assay for ricin A-chain ribosome depurination kinetics
    • Sturm, M. B., and Schramm, V. L. (2009) Detecting ricin. Sensitive luminescent assay for ricin A-chain ribosome depurination kinetics. Anal Chem. 81, 2847-2853
    • (2009) Anal Chem. , vol.81 , pp. 2847-2853
    • Sturm, M.B.1    Schramm, V.L.2
  • 51
    • 0019320458 scopus 로고
    • Pyruvate phosphate dikinase. Sequence of the histidyl peptide, the pyrophosphoryl and phosphoryl carrier
    • Goss, N. H., Evans, C. T., and Wood, H. G. (1980) Pyruvate phosphate dikinase. Sequence of the histidyl peptide, the pyrophosphoryl and phosphoryl carrier. Biochemistry 19, 5805-5809
    • (1980) Biochemistry , vol.19 , pp. 5805-5809
    • Goss, N.H.1    Evans, C.T.2    Wood, H.G.3
  • 52
    • 34548348189 scopus 로고    scopus 로고
    • Evidence for the importance of electrostatics in the function of two distinct families of ribosome inactivating toxins
    • Korennykh, A. V., Correll, C. C., and Piccirilli, J. A. (2007) Evidence for the importance of electrostatics in the function of two distinct families of ribosome inactivating toxins. RNA 13, 1391-1396
    • (2007) RNA , vol.13 , pp. 1391-1396
    • Korennykh, A.V.1    Correll, C.C.2    Piccirilli, J.A.3
  • 53
    • 33745090478 scopus 로고    scopus 로고
    • The electrostatic character of the ribosomal surface enables extraordinarily rapid target location by ribotoxins
    • Korennykh, A. V., Piccirilli, J. A., and Correll, C. C. (2006) The electrostatic character of the ribosomal surface enables extraordinarily rapid target location by ribotoxins. Nat. Struct. Mol. Biol. 13, 436-443
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 436-443
    • Korennykh, A.V.1    Piccirilli, J.A.2    Correll, C.C.3
  • 54
    • 84867229684 scopus 로고    scopus 로고
    • N-Glycosylation does not affect the catalytic activity of ricin a chain but stimulates cytotoxicity by promoting its transport out of the endoplasmic reticulum. Traffic 13, 1508-1521
    • Yan, Q., Li, X. P., and Tumer, N. E. (2012) N-Glycosylation does not affect the catalytic activity of ricin a chain but stimulates cytotoxicity by promoting its transport out of the endoplasmic reticulum
    • (2012) Traffic , vol.13 , pp. 1508-1521
    • Yan, Q.1    Li, X.P.2    Tumer, N.E.3
  • 55
    • 0018339835 scopus 로고
    • The interpretation of near-ultraviolet circular dichroism
    • Kahn, P. C. (1979) The interpretation of near-ultraviolet circular dichroism. Methods Enzymol. 61, 339-378
    • (1979) Methods Enzymol. , vol.61 , pp. 339-378
    • Kahn, P.C.1
  • 56
    • 0032544216 scopus 로고    scopus 로고
    • Ricin A-chain. Kinetics, mechanism, and RNA stem-loop inhibitors
    • Chen, X. Y., Link, T. M., and Schramm, V. L. (1998) Ricin A-chain. Kinetics, mechanism, and RNA stem-loop inhibitors. Biochemistry 37, 11605-11613
    • (1998) Biochemistry , vol.37 , pp. 11605-11613
    • Chen, X.Y.1    Link, T.M.2    Schramm, V.L.3
  • 57
    • 0032486270 scopus 로고    scopus 로고
    • Free ricin A chain, proricin, and native toxin have different cellular fates when expressed in tobacco protoplasts
    • Frigerio, L., Vitale, A., Lord, J. M., Ceriotti, A., and Roberts, L. M. (1998) Free ricin A chain, proricin, and native toxin have different cellular fates when expressed in tobacco protoplasts. J. Biol. Chem. 273, 14194-14199
    • (1998) J. Biol. Chem. , vol.273 , pp. 14194-14199
    • Frigerio, L.1    Vitale, A.2    Lord, J.M.3    Ceriotti, A.4    Roberts, L.M.5
  • 58
    • 0024756611 scopus 로고
    • Role of glutamic acid 177 of the ricin toxin A chain in enzymatic inactivation of ribosomes
    • Schlossman, D., Withers, D., Welsh, P., Alexander, A., Robertus, J., and Frankel, A. (1989) Role of glutamic acid 177 of the ricin toxin A chain in enzymatic inactivation of ribosomes. Mol. Cell. Biol. 9, 5012-5021
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 5012-5021
    • Schlossman, D.1    Withers, D.2    Welsh, P.3    Alexander, A.4    Robertus, J.5    Frankel, A.6
  • 59
    • 0025224121 scopus 로고
    • Role of arginine 180 and glutamic acid 177 of ricin toxin A chain in enzymatic inactivation of ribosomes
    • Frankel, A., Welsh, P., Richardson, J., and Robertus, J. D. (1990) Role of arginine 180 and glutamic acid 177 of ricin toxin A chain in enzymatic inactivation of ribosomes. Mol. Cell. Biol. 10, 6257-6263
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 6257-6263
    • Frankel, A.1    Welsh, P.2    Richardson, J.3    Robertus, J.D.4
  • 60
    • 0025986909 scopus 로고
    • Site-directed mutagenesis of ricin A-chain and implications for the mechanism of action
    • Ready, M. P., Kim, Y., and Robertus, J. D. (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
  • 61
    • 0027050799 scopus 로고
    • Analysis of several key active site residues of ricin A chain by mutagenesis and x-ray crystallography
    • Kim, Y., and Robertus, J. D. (1992) Analysis of several key active site residues of ricin A chain by mutagenesis and x-ray crystallography. Protein Eng. 5, 775-779
    • (1992) Protein Eng. , vol.5 , pp. 775-779
    • Kim, Y.1    Robertus, J.D.2
  • 62
    • 0026469648 scopus 로고
    • X-ray analysis of substrate analogs in the ricin A-chain active site
    • Monzingo, A. F., and Robertus, J. D. (1992) X-ray analysis of substrate analogs in the ricin A-chain active site. J. Mol. Biol. 227, 1136-1145
    • (1992) J. Mol. Biol. , vol.227 , pp. 1136-1145
    • Monzingo, A.F.1    Robertus, J.D.2
  • 63
    • 0032905173 scopus 로고    scopus 로고
    • Free energy determinants of binding the rRNA substrate and small ligands to ricin A-chain
    • Olson, M. A., and Cuff, L. (1999) Free energy determinants of binding the rRNA substrate and small ligands to ricin A-chain. Biophys. J. 76, 28-39
    • (1999) Biophys. J. , vol.76 , pp. 28-39
    • Olson, M.A.1    Cuff, L.2
  • 64
    • 1642539986 scopus 로고    scopus 로고
    • The effect of mutations surrounding and within the active site on the catalytic activity of ricin A chain
    • Marsden, C. J., Fülöp, V., Day, P. J., and Lord, J. M. (2004) The effect of mutations surrounding and within the active site on the catalytic activity of ricin A chain. Eur. J. Biochem. 271, 153-162
    • (2004) Eur. J. Biochem. , vol.271 , pp. 153-162
    • Marsden, C.J.1    Fülöp, V.2    Day, P.J.3    Lord, J.M.4
  • 65
    • 0031032729 scopus 로고    scopus 로고
    • Ricin A-chain structural determinant for binding substrate analogues. A molecular dynamics simulation analysis
    • Olson, M. A. (1997) Ricin A-chain structural determinant for binding substrate analogues. A molecular dynamics simulation analysis. Proteins 27, 80-95
    • (1997) Proteins , vol.27 , pp. 80-95
    • Olson, M.A.1
  • 66
    • 0026682830 scopus 로고
    • Determination by systematic deletion of the amino acids essential for catalysis by ricin A chain
    • Morris, K. N., and Wool, I. G. (1992) Determination by systematic deletion of the amino acids essential for catalysis by ricin A chain. Proc. Natl. Acad. Sci. U.S.A. 89, 4869-4873
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 4869-4873
    • Morris, K.N.1    Wool, I.G.2
  • 67
    • 78149302861 scopus 로고    scopus 로고
    • The mechanism for activation of GTP hydrolysis on the ribosome
    • Voorhees, R. M., Schmeing, T. M., Kelley, A. C., and Ramakrishnan, V. (2010) The mechanism for activation of GTP hydrolysis on the ribosome. Science 330, 835-838
    • (2010) Science , vol.330 , pp. 835-838
    • Voorhees, R.M.1    Schmeing, T.M.2    Kelley, A.C.3    Ramakrishnan, V.4
  • 69
    • 84857880542 scopus 로고    scopus 로고
    • How ricin and Shiga toxin reach the cytosol of target cells. Retrotranslocation from the endoplasmic reticulum
    • Spooner, R. A., and Lord, J. M. (2012) How ricin and Shiga toxin reach the cytosol of target cells. Retrotranslocation from the endoplasmic reticulum. Curr. Top. Microbiol. Immunol. 357, 19-40
    • (2012) Curr. Top. Microbiol. Immunol. , vol.357 , pp. 19-40
    • Spooner, R.A.1    Lord, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.