Solution structure of an active mutant of maize ribosome-inactivating protein (MOD) and its interaction with the ribosomal stalk protein P2.

[1]  J. Ballesta,et al.  A two-step binding model proposed for the electrostatic interactions of ricin a chain with ribosomes. , 2009, Biochemistry.

[2]  G. Zhu,et al.  The C-terminal fragment of the ribosomal P protein complexed to trichosanthin reveals the interaction between the ribosome-inactivating protein and the ribosome , 2008, Nucleic acids research.

[3]  J. Gariépy,et al.  The catalytic subunit of shiga-like toxin 1 interacts with ribosomal stalk proteins and is inhibited by their conserved C-terminal domain. , 2008, Journal of molecular biology.

[4]  P. Shaw,et al.  1H, 13C and 15N backbone and side chain resonance assignments of a 28 kDa active mutant of maize ribosome-inactivating protein (MOD) , 2007, Biomolecular NMR assignments.

[5]  J. Piccirilli,et al.  Evidence for the importance of electrostatics in the function of two distinct families of ribosome inactivating toxins. , 2007, RNA.

[6]  P. Shaw,et al.  Structure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site , 2007, Nucleic acids research.

[7]  G. Zhu,et al.  Interaction between trichosanthin, a ribosome-inactivating protein, and the ribosomal stalk protein P2 by chemical shift perturbation and mutagenesis analyses , 2007, Nucleic acids research.

[8]  J. Piccirilli,et al.  The electrostatic character of the ribosomal surface enables extraordinarily rapid target location by ribotoxins , 2006, Nature Structural &Molecular Biology.

[9]  H. Bass,et al.  Maize ribosome-inactivating proteins (RIPs) with distinct expression patterns have similar requirements for proenzyme activation. , 2004, Journal of experimental botany.

[10]  F. Stirpe,et al.  Description, distribution, activity and phylogenetic relationship of ribosome-inactivating proteins in plants, fungi and bacteria. , 2004, Mini reviews in medicinal chemistry.

[11]  A. Monzingo,et al.  The structure of ribosome inactivating proteins. , 2004, Mini reviews in medicinal chemistry.

[12]  M. Motto,et al.  The genetics and properties of cereal ribosome-inactivating proteins. , 2004, Mini reviews in medicinal chemistry.

[13]  Peter Güntert,et al.  Automated NMR protein structure calculation , 2003 .

[14]  Roger L. Williams,et al.  Structural basis for the interaction of [E160A-E189A]-trichosanthin with adenine. , 2003, Toxicon : official journal of the International Society on Toxinology.

[15]  M. Tchórzewski The acidic ribosomal P proteins. , 2002, The international journal of biochemistry & cell biology.

[16]  Torsten Herrmann,et al.  Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. , 2002, Journal of molecular biology.

[17]  P. Shaw,et al.  Trichosanthin interacts with acidic ribosomal proteins P0 and P1 and mitotic checkpoint protein MAD2B. , 2001, European journal of biochemistry.

[18]  Liisa Holm,et al.  DaliLite workbench for protein structure comparison , 2000, Bioinform..

[19]  L. Federici,et al.  The crystal structure of saporin SO6 from Saponaria officinalis and its interaction with the ribosome , 2000, FEBS letters.

[20]  A. Bax,et al.  Protein backbone angle restraints from searching a database for chemical shift and sequence homology , 1999, Journal of biomolecular NMR.

[21]  J. Thornton,et al.  AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR , 1996, Journal of biomolecular NMR.

[22]  M. Billeter,et al.  MOLMOL: a program for display and analysis of macromolecular structures. , 1996, Journal of molecular graphics.

[23]  M. Hartley,et al.  The Action of Pokeweed Antiviral Protein and Ricin A-chain on Mutants in the α-Sarcin Loop ofEscherichia coli23S Ribosomal RNA , 1995 .

[24]  S. Grzesiek,et al.  NMRPipe: A multidimensional spectral processing system based on UNIX pipes , 1995, Journal of biomolecular NMR.

[25]  T. A. Walsh,et al.  Maize Ribosome-Inactivating Protein (b-32) (Homologs in Related Species, Effects on Maize Ribosomes, and Modulation of Activity by Pro-Peptide Deletions) , 1995, Plant physiology.

[26]  J. Lord,et al.  Structure, function and applications of ricin and related cytotoxic proteins , 1993 .

[27]  K. Kashiwagi,et al.  Comparison of the modes of action of a Vero toxin (a Shiga-like toxin) from Escherichia coli, of ricin, and of alpha-sarcin. , 1992, Archives of biochemistry and biophysics.

[28]  H. Bass,et al.  A maize ribosome-inactivating protein is controlled by the transcriptional activator Opaque-2. , 1992, The Plant cell.

[29]  F. Uckun,et al.  Pokeweed antiviral protein: ribosome inactivation and therapeutic applications. , 1992, Pharmacology & therapeutics.

[30]  T. A. Walsh,et al.  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. , 1991, The Journal of biological chemistry.

[31]  G. Legname,et al.  Single‐chain ribosome inactivating proteins from plants depurinate Escherichia coli 23S ribosomal RNA , 1991, FEBS letters.

[32]  A. Bolognesi,et al.  Ribosome-inactivating proteins from plants inhibit ribosome activity of Trypanosoma and Leishmania. , 1988, The Journal of protozoology.

[33]  K. Tsurugi,et al.  The RNA N-glycosidase activity of ricin A-chain. The characteristics of the enzymatic activity of ricin A-chain with ribosomes and with rRNA. , 1988, The Journal of biological chemistry.

[34]  H. Franz,et al.  The site of action of the A‐chain of mistletoe lectin I on eukaryotic ribosomes The RNA N‐glycosidase activity of the protein , 1988, FEBS letters.

[35]  K. Tsurugi,et al.  The site of action of six different ribosome-inactivating proteins from plants on eukaryotic ribosomes: the RNA N-glycosidase activity of the proteins. , 1988, Biochemical and biophysical research communications.

[36]  R. Ebert,et al.  The mechanism of action of barley toxin: a type 1 ribosome-inactivating protein with RNA N-glycosidase activity. , 1988, Biochimica et biophysica acta.

[37]  B. Svensson,et al.  Reduced turnover of the elongation factor EF-1 X ribosome complex after treatment with the protein synthesis inhibitor II from barley seeds. , 1986, Biochimica et biophysica acta.

[38]  W. Kabsch,et al.  Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.

[39]  D. Steiner,et al.  Post-translational proteolysis in polypeptide hormone biosynthesis. , 1982, Annual review of physiology.