메뉴 건너뛰기




Volumn 43, Issue 12, 2011, Pages 1792-1801

Shiga toxin 1 is more dependent on the P proteins of the ribosomal stalk for depurination activity than Shiga toxin 2

Author keywords

E. coli O157:H7; P protein; Ribosomal stalk; Ribosome inactivating protein; Shiga toxin

Indexed keywords

GLYCINE DEHYDROGENASE (DECARBOXYLATING); VEROTOXIN 1; VEROTOXIN 2;

EID: 80255123875     PISSN: 13572725     EISSN: 18785875     Source Type: Journal    
DOI: 10.1016/j.biocel.2011.08.018     Document Type: Article
Times cited : (32)

References (48)
  • 1
    • 0029686290 scopus 로고    scopus 로고
    • The large ribosomal subunit stalk as a regulatory element of the eukaryotic translational machinery
    • J.P. Ballesta, and M. Remacha The large ribosomal subunit stalk as a regulatory element of the eukaryotic translational machinery Prog Nucleic Acid Res Mol Biol 55 1996 157 193
    • (1996) Prog Nucleic Acid Res Mol Biol , vol.55 , pp. 157-193
    • Ballesta, J.P.1    Remacha, M.2
  • 3
    • 80051804184 scopus 로고    scopus 로고
    • Characterisation of the Escherichia coli strain associated with an outbreak of haemolytic uraemic syndrome in Germany, 2011: A microbiological study
    • M. Bielaszewska, A. Mellmann, W. Zhang, R. Kock, A. Fruth, and A. Bauwens Characterisation of the Escherichia coli strain associated with an outbreak of haemolytic uraemic syndrome in Germany, 2011: a microbiological study Lancet Infect Dis 11 2011 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
  • 5
    • 79956024966 scopus 로고    scopus 로고
    • The amino terminal end determines the stability and assembling capacity of eukaryotic ribosomal stalk proteins P1 and P2
    • H. Camargo, G. Nusspaumer, D. Abia, V. Briceno, M. Remacha, and J.P. Ballesta The amino terminal end determines the stability and assembling capacity of eukaryotic ribosomal stalk proteins P1 and P2 Nucleic Acids Res 39 2011 3735 3743
    • (2011) Nucleic Acids Res , vol.39 , pp. 3735-3743
    • Camargo, H.1    Nusspaumer, G.2    Abia, D.3    Briceno, V.4    Remacha, M.5    Ballesta, J.P.6
  • 6
    • 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
    • S.H. Chan, F.S. Hung, D.S. Chan, and P.C. Shaw Trichosanthin interacts with acidic ribosomal proteins P0 and P1 and mitotic checkpoint protein MAD2B Eur J Biochem 268 2001 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
  • 7
    • 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
    • D.S. Chan, L.O. Chu, K.M. Lee, P.H. Too, K.W. Ma, and K.H. Sze Interaction between trichosanthin, a ribosome-inactivating protein, and the ribosomal stalk protein P2 by chemical shift perturbation and mutagenesis analyses Nucleic Acids Res 35 2007 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
  • 8
    • 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
    • J.C. Chiou, X.P. Li, M. Remacha, J.P. Ballesta, and N.E. Tumer The ribosomal stalk is required for ribosome binding, depurination of the rRNA and cytotoxicity of ricin A chain in Saccharomyces cerevisiae Mol Microbiol 70 2008 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
  • 10
    • 79952359595 scopus 로고    scopus 로고
    • Identification of amino acids critical for the cytotoxicity of Shiga toxin 1 and 2 in Saccharomyces cerevisiae
    • R. Di, E. Kyu, V. Shete, H. Saidasan, P.C. Kahn, and N.E. Tumer Identification of amino acids critical for the cytotoxicity of Shiga toxin 1 and 2 in Saccharomyces cerevisiae Toxicon 57 2011 525 539
    • (2011) Toxicon , vol.57 , pp. 525-539
    • Di, R.1    Kyu, E.2    Shete, V.3    Saidasan, H.4    Kahn, P.C.5    Tumer, N.E.6
  • 11
    • 0023854742 scopus 로고
    • Site of action of a Vero toxin (VT2) from Escherichia coli O157:H7 and of Shiga toxin on eukaryotic ribosomes. RNA N-glycosidase activity of the toxins
    • Y. Endo, K. Tsurugi, T. Yutsudo, Y. Takeda, T. Ogasawara, and K. Igarashi Site of action of a Vero toxin (VT2) from Escherichia coli O157:H7 and of Shiga toxin on eukaryotic ribosomes. RNA N-glycosidase activity of the toxins Eur J Biochem 171 1988 45 50 (Pubitemid 18042873)
    • (1988) European Journal of Biochemistry , vol.171 , Issue.1-2 , pp. 45-50
    • Endo, Y.1    Tsurugi, K.2    Yutsudo, T.3    Takeda, Y.4    Ogasawara, T.5    Igarashi, K.6
  • 12
    • 0028961149 scopus 로고
    • Furin-induced cleavage and activation of Shiga toxin
    • O. Garred, B. van Deurs, and K. Sandvig Furin-induced cleavage and activation of Shiga toxin J Biol Chem 270 1995 10817 10821
    • (1995) J Biol Chem , vol.270 , pp. 10817-10821
    • Garred, O.1    Van Deurs, B.2    Sandvig, K.3
  • 13
    • 0037781517 scopus 로고    scopus 로고
    • The puzzling lateral flexible stalk of the ribosome
    • DOI 10.1016/S0248-4900(03)00034-0
    • P. Gonzalo, and J.P. Reboud The puzzling lateral flexible stalk of the ribosome Biol Cell 95 2003 179 193 (Pubitemid 36889220)
    • (2003) Biology of the Cell , vol.95 , Issue.3-4 , pp. 179-193
    • Gonzalo, P.1    Reboud, J.-P.2
  • 15
    • 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
    • E. Guarinos, C. Santos, A. Sanchez, D.Y. Qiu, M. Remacha, and J.P. Ballesta Tag-mediated fractionation of yeast ribosome populations proves the monomeric organization of the eukaryotic ribosomal stalk structure Mol Microbiol 50 2003 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
  • 16
    • 0025878152 scopus 로고
    • Preparation of VT1 and VT2 hybrid toxins from their purified dissociated subunits: Evidence for B subunit modulation of a subunit function
    • S.C. Head, M.A. Karmali, and C.A. Lingwood 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 1991 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
  • 17
    • 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
    • K.A. Hudak, B.A. Parikh, R. Di, M. Baricevic, M. Santana, and M. Seskar Generation of pokeweed antiviral protein mutations in Saccharomyces cerevisiae: evidence that ribosome depurination is not sufficient for cytotoxicity Nucleic Acids Res 32 2004 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
  • 18
    • 0029160529 scopus 로고
    • Isolation and characterization of pokeweed antiviral protein mutations in Saccharomyces cerevisiae: Identification of residues important for toxicity
    • Y. Hur, D.J. Hwang, O. Zoubenko, C. Coetzer, F.M. Uckun, and N.E. Tumer Isolation and characterization of pokeweed antiviral protein mutations in Saccharomyces cerevisiae: identification of residues important for toxicity Proc Natl Acad Sci U S A 92 1995 8448 8452
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 8448-8452
    • Hur, Y.1    Hwang, D.J.2    Zoubenko, O.3    Coetzer, C.4    Uckun, F.M.5    Tumer, N.E.6
  • 19
    • 0029020517 scopus 로고
    • Eukaryotic acidic phosphoproteins interact with the ribosome through their amino-terminal domain
    • M.P. Jose, H. Santana-Roman, M. Remacha, J.P. Ballesta, and S. Zinker Eukaryotic acidic phosphoproteins interact with the ribosome through their amino-terminal domain Biochemistry 34 1995 7941 7948
    • (1995) Biochemistry , vol.34 , pp. 7941-7948
    • Jose, M.P.1    Santana-Roman, H.2    Remacha, M.3    Ballesta, J.P.4    Zinker, S.5
  • 20
    • 67049119434 scopus 로고    scopus 로고
    • Assembly and stability of the Shiga toxins investigated by electrospray ionization mass spectrometry
    • E.N. Kitova, G.L. Mulvey, T. Dingle, I. Sinelnikov, S. Wee, and T.P. Griener Assembly and stability of the Shiga toxins investigated by electrospray ionization mass spectrometry Biochemistry 48 2009 5365 5374
    • (2009) Biochemistry , vol.48 , pp. 5365-5374
    • Kitova, E.N.1    Mulvey, G.L.2    Dingle, T.3    Sinelnikov, I.4    Wee, S.5    Griener, T.P.6
  • 21
    • 20444380695 scopus 로고    scopus 로고
    • Acquisition of a stable structure by yeast ribosomal P0 protein requires binding of P1A-P2B complex: In vitro formation of the stalk structure
    • DOI 10.1016/j.bbagen.2005.03.009, PII S0304416505000851
    • D. Krokowski, M. Tchorzewski, A. Boguszewska, and N. Grankowski Acquisition of a stable structure by yeast ribosomal P0 protein requires binding of P1A-P2B complex: in vitro formation of the stalk structure Biochim Biophys Acta 1724 2005 59 70 (Pubitemid 40799111)
    • (2005) Biochimica et Biophysica Acta - General Subjects , vol.1724 , Issue.1-2 , pp. 59-70
    • Krokowski, D.1    Tchorzewski, M.2    Boguszewska, A.3    Grankowski, N.4
  • 23
    • 0036439195 scopus 로고    scopus 로고
    • Characterization of interaction sites in the Saccharomyces cerevisiae ribosomal stalk components
    • DOI 10.1046/j.1365-2958.2002.03179.x
    • V.S. Lalioti, J. Perez-Fernandez, M. Remacha, and J.P. Ballesta Characterization of interaction sites in the Saccharomyces cerevisiae ribosomal stalk components Mol Microbiol 46 2002 719 729 (Pubitemid 35365607)
    • (2002) Molecular Microbiology , vol.46 , Issue.3 , pp. 719-729
    • Lalioti, V.S.1    Perez-Fernandez, J.2    Remacha, M.3    Ballesta, J.P.G.4
  • 24
    • 33845976010 scopus 로고    scopus 로고
    • Ribosome depurination is not sufficient for ricin-mediated cell death in Saccharomyces cerevisiae
    • DOI 10.1128/IAI.01295-06
    • X.P. Li, M. Baricevic, H. Saidasan, and N.E. Tumer Ribosome depurination is not sufficient for ricin-mediated cell death in Saccharomyces cerevisiae Infect Immun 75 2007 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
  • 25
    • 66149084818 scopus 로고    scopus 로고
    • A two-step binding model proposed for the electrostatic interactions of ricin a chain with ribosomes
    • X.P. Li, J.C. Chiou, M. Remacha, J.P. Ballesta, and N.E. Tumer A two-step binding model proposed for the electrostatic interactions of ricin a chain with ribosomes Biochemistry 48 2009 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
  • 26
    • 78650659145 scopus 로고    scopus 로고
    • Pentameric organization of the ribosomal stalk accelerates recruitment of ricin a chain to the ribosome for depurination
    • X.P. Li, P. Grela, D. Krokowski, M. Tchorzewski, and N.E. Tumer Pentameric organization of the ribosomal stalk accelerates recruitment of ricin a chain to the ribosome for depurination J Biol Chem 285 2010 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
  • 27
    • 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
    • A.J. McCluskey, G.M. Poon, E. Bolewska-Pedyczak, T. Srikumar, S.M. Jeram, and B. Raught 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 2008 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
  • 28
    • 0035900715 scopus 로고    scopus 로고
    • Kinetic analysis of binding between Shiga toxin and receptor glycolipid Gb3Cer by surface plasmon resonance
    • H. Nakajima, N. Kiyokawa, Y.U. Katagiri, T. Taguchi, T. Suzuki, and T. Sekino Kinetic analysis of binding between Shiga toxin and receptor glycolipid Gb3Cer by surface plasmon resonance J Biol Chem 276 2001 42915 42922
    • (2001) J Biol Chem , vol.276 , pp. 42915-42922
    • Nakajima, H.1    Kiyokawa, N.2    Katagiri, Y.U.3    Taguchi, T.4    Suzuki, T.5    Sekino, T.6
  • 29
    • 0034669118 scopus 로고    scopus 로고
    • N-terminal region of yeast ribosomal protein P1 mediate its degradation, which is prevented by protein P2
    • G. Nusspaumer, M. Remacha, J.P. Ballesta, and Phosphorylation N-terminal region of yeast ribosomal protein P1 mediate its degradation, which is prevented by protein P2 EMBO J 19 2000 6075 6084
    • (2000) EMBO J , vol.19 , pp. 6075-6084
    • Nusspaumer, G.1    Remacha, M.2    Ballesta, J.P.3    Phosphorylation4
  • 30
    • 35548955176 scopus 로고    scopus 로고
    • The Shiga toxin genotype rather than the amount of Shiga toxin or the cytotoxicity of Shiga toxin in vitro correlates with the appearance of the hemolytic uremic syndrome
    • DOI 10.1016/j.diagmicrobio.2007.04.013, PII S0732889307001812
    • D. Orth, K. Grif, A.B. Khan, A. Naim, M.P. Dierich, and R. Wurzner The Shiga toxin genotype rather than the amount of Shiga toxin or the cytotoxicity of Shiga toxin in vitro correlates with the appearance of the hemolytic uremic syndrome Diagn Microbiol Infect Dis 59 2007 235 242 (Pubitemid 350016692)
    • (2007) Diagnostic Microbiology and Infectious Disease , vol.59 , Issue.3 , pp. 235-242
    • Orth, D.1    Grif, K.2    Khan, A.B.3    Naim, A.4    Dierich, M.P.5    Wurzner, R.6
  • 31
    • 0036828767 scopus 로고    scopus 로고
    • Pokeweed antiviral protein regulates the stability of its own mRNA by a mechanism that requires depurination but can be separated from depurination of the α-sarcin/ricin loop of rRNA
    • DOI 10.1074/jbc.M205463200
    • B.A. Parikh, C. Coetzer, and N.E. Tumer Pokeweed antiviral protein regulates the stability of its own mRNA by a mechanism that requires depurination but can be separated from depurination of the alpha-sarcin/ricin loop of rRNA J Biol Chem 277 2002 41428 41437 (Pubitemid 35257444)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.44 , pp. 41428-41437
    • Parikh, B.A.1    Coetzer, C.2    Tumer, N.E.3
  • 32
    • 0031848112 scopus 로고    scopus 로고
    • Pathogenesis and diagnosis of Shiga toxin-producing Escherichia coli infections
    • J.C. Paton, and A.W. Paton Pathogenesis and diagnosis of Shiga toxin-producing Escherichia coli infections Clin Microbiol Rev 11 1998 450 479 (Pubitemid 28379095)
    • (1998) Clinical Microbiology Reviews , vol.11 , Issue.3 , pp. 450-479
    • Paton, J.C.1    Paton, A.W.2
  • 33
    • 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
    • M. Pierce, J.N. Kahn, J. Chiou, and N.E. Tumer 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 2011 201 210
    • (2011) RNA , vol.17 , pp. 201-210
    • Pierce, M.1    Kahn, J.N.2    Chiou, J.3    Tumer, N.E.4
  • 36
    • 20744450629 scopus 로고    scopus 로고
    • Delivery into cells: Lessons learned from plant and bacterial toxins
    • DOI 10.1038/sj.gt.3302525, Vector Traffic
    • K. Sandvig, and B. van Deurs Delivery into cells: lessons learned from plant and bacterial toxins Gene Ther 12 2005 865 872 (Pubitemid 40852204)
    • (2005) Gene Therapy , vol.12 , Issue.11 , pp. 865-872
    • Sandvig, K.1    Van Deurs, B.2
  • 37
    • 0028232189 scopus 로고
    • Ribosomal protein P0, contrary to phosphoproteins P1 and P2, is required for ribosome activity and Saccharomyces cerevisiae viability
    • C. Santos, and J.P. Ballesta Ribosomal protein P0, contrary to phosphoproteins P1 and P2, is required for ribosome activity and Saccharomyces cerevisiae viability J Biol Chem 269 1994 15689 15696
    • (1994) J Biol Chem , vol.269 , pp. 15689-15696
    • Santos, C.1    Ballesta, J.P.2
  • 38
    • 17144365102 scopus 로고    scopus 로고
    • Hemolytic uremic syndrome; pathogenesis, treatment, and outcome
    • DOI 10.1097/01.mop.0000152997.66070.e9
    • R. Siegler, and R. Oakes Hemolytic uremic syndrome; pathogenesis, treatment, and outcome Curr Opin Pediatr 17 2005 200 204 (Pubitemid 40516100)
    • (2005) Current Opinion in Pediatrics , vol.17 , Issue.2 , pp. 200-204
    • Siegler, R.1    Oakes, R.2
  • 39
    • 0042328609 scopus 로고    scopus 로고
    • Response to Shiga toxin 1 and 2 in a baboon model of hemolytic uremic syndrome
    • DOI 10.1007/s00467-002-1035-7
    • R.L. Siegler, T.G. Obrig, T.J. Pysher, V.L. Tesh, N.D. Denkers, and F.B. Taylor Response to Shiga toxin 1 and 2 in a baboon model of hemolytic uremic syndrome Pediatr Nephrol 18 2003 92 96 (Pubitemid 41490292)
    • (2003) Pediatric Nephrology , vol.18 , Issue.2 , pp. 92-96
    • Siegler, R.L.1    Obrig, T.G.2    Pysher, T.J.3    Tesh, V.L.4    Denkers, N.D.5    Taylor, F.B.6
  • 40
    • 0032910242 scopus 로고    scopus 로고
    • In vitro assessment of a chemically synthesized Shiga toxin receptor analog attached to Chromosorb P (Synsorb Pk) as a specific absorbing agent of Shiga toxin 1 and 2
    • T. Takeda, K. Yoshino, E. Adachi, Y. Sato, and K. Yamagata In vitro assessment of a chemically synthesized Shiga toxin receptor analog attached to chromosorb P (Synsorb Pk) as a specific absorbing agent of Shiga toxin 1 and 2 Microbiol Immunol 43 1999 331 337 (Pubitemid 29194202)
    • (1999) Microbiology and Immunology , vol.43 , Issue.4 , pp. 331-337
    • Takeda, T.1    Yoshino, K.-I.2    Adachi, E.3    Sato, Y.4    Yamagata, K.5
  • 41
    • 0034639256 scopus 로고    scopus 로고
    • Oligomerization properties of the acidic ribosomal P-proteins from Saccharomyces cerevisiae: Effect of P1A protein phosphorylation on the formation of the P1A-P2B hetero-complex
    • M. Tchorzewski, A. Boguszewska, P. Dukowski, and N. Grankowski Oligomerization properties of the acidic ribosomal P-proteins from Saccharomyces cerevisiae: effect of P1A protein phosphorylation on the formation of the P1A-P2B hetero-complex Biochim Biophys Acta 1499 2000 63 73
    • (2000) Biochim Biophys Acta , vol.1499 , pp. 63-73
    • Tchorzewski, M.1    Boguszewska, A.2    Dukowski, P.3    Grankowski, N.4
  • 42
    • 77949368508 scopus 로고    scopus 로고
    • Induction of apoptosis by Shiga toxins
    • V.L. Tesh Induction of apoptosis by Shiga toxins Future Microbiol 5 2010 431 453
    • (2010) Future Microbiol , vol.5 , pp. 431-453
    • Tesh, V.L.1
  • 44
    • 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
    • P.H. Too, M.K. Ma, A.N. Mak, Y.T. Wong, C.K. Tung, and G. Zhu 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 2009 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
  • 45
    • 0026035948 scopus 로고
    • Characterization of the yeast acidic ribosomal phosphoproteins using monoclonal antibodies. Proteins L44/L45 and L44′ have different functional roles
    • M.D. Vilella, M. Remacha, B.L. Ortiz, E. Mendez, and J.P. Ballesta Characterization of the yeast acidic ribosomal phosphoproteins using monoclonal antibodies. Proteins L44/L45 and L44′ have different functional roles Eur J Biochem 196 1991 407 414
    • (1991) Eur J Biochem , vol.196 , pp. 407-414
    • Vilella, M.D.1    Remacha, M.2    Ortiz, B.L.3    Mendez, E.4    Ballesta, J.P.5
  • 46
    • 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
    • Y. Yang, A.N. Mak, P.C. Shaw, and K.H. Sze 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 2010 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
  • 47
    • 0030739177 scopus 로고    scopus 로고
    • The exchangeable yeast ribosomal acidic protein YP2β shows characteristics of a partly folded state under physiological conditions
    • DOI 10.1021/bi9702400
    • J. Zurdo, J.M. Sanz, C. Gonzalez, M. Rico, and J.P. Ballesta The exchangeable yeast ribosomal acidic protein YP2beta shows characteristics of a partly folded state under physiological conditions Biochemistry 36 1997 9625 9635 (Pubitemid 27347004)
    • (1997) Biochemistry , vol.36 , Issue.31 , pp. 9625-9635
    • Zurdo, J.1    Sanz, J.M.2    Gonzalez, C.3    Rico, M.4    Ballesta, J.P.G.5
  • 48
    • 0034254658 scopus 로고    scopus 로고
    • Assembly of saccharomyces cerevisiae ribosomal stalk: Binding of p1 proteins is required for the interaction of p2 proteins
    • DOI 10.1021/bi000362j
    • J. Zurdo, P. Parada, A. van den Berg, G. Nusspaumer, A. Jimenez-Diaz, and M. Remacha Assembly of Saccharomyces cerevisiae ribosomal stalk: binding of P1 proteins is required for the interaction of P2 proteins Biochemistry 39 2000 8929 8934 (Pubitemid 30602803)
    • (2000) Biochemistry , vol.39 , Issue.30 , pp. 8929-8934
    • Zurdo, J.1    Parada, P.2    Van Den Berg, A.3    Nusspaumer, G.4    Jimenez-Diaz, A.5    Remacha, M.6    Ballesta, J.P.G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.