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Uchida","year":"2009","journal-title":"Microbiology"},{"key":"ref55","doi-asserted-by":"crossref","first-page":"4362","DOI":"10.1128\/IAI.00044-09","article-title":"Characterization of a unique ADP-ribosyltransferase of mycoplasma penetrans.","volume":"77","author":"C Johnson","year":"2009","journal-title":"Infect Immun"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"13525","DOI":"10.1074\/jbc.M109.077339","article-title":"Photox, a novel actin-targeting mono-ADP-ribosyltransferase from photorhabdus luminescens.","volume":"285","author":"DD Visschedyk","year":"2010","journal-title":"J Biol Chem"},{"key":"ref57","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1128\/JB.01260-09","article-title":"A type VI secretion system effector protein, VgrG1, from aeromonas hydrophila that induces host cell toxicity by ADP ribosylation of actin.","volume":"192","author":"G Suarez","year":"2010","journal-title":"J Bacteriol"},{"key":"ref58","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1007\/BF00731300","article-title":"Lectin domains in the toxin of bordetella pertussis: Selectin mimicry linked to microbial pathogenesis.","volume":"11","author":"J Sandros","year":"1994","journal-title":"Glycoconj J"},{"key":"ref59","doi-asserted-by":"crossref","first-page":"2342","DOI":"10.1001\/jama.294.18.2342","article-title":"Ricin poisoning: A comprehensive review.","volume":"294","author":"J Audi","year":"2005","journal-title":"JAMA"},{"key":"ref60","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1586\/14760584.7.5.561","article-title":"Vaccination with dukoral against travelers&apos; diarrhea (ETEC) and cholera.","volume":"7","author":"T Jelinek","year":"2008","journal-title":"Expert Rev Vaccines"},{"key":"ref61","doi-asserted-by":"crossref","first-page":"8449","DOI":"10.1073\/pnas.0402414101","article-title":"Identification of anthrax toxin genes in a bacillus cereus associated 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bacteriophage T4.","volume":"60","author":"H Rohrer","year":"1975","journal-title":"Eur J Biochem"},{"key":"ref75","doi-asserted-by":"crossref","first-page":"1221","DOI":"10.1038\/nsmb1317","article-title":"Structure of phage P22 cell envelope-penetrating needle.","volume":"14","author":"AS Olia","year":"2007","journal-title":"Nat Struct Mol Biol"},{"key":"ref76","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1111\/j.1462-5822.2004.00467.x","article-title":"Potentiation and cellular phenotypes of the insecticidal toxin complexes of photorhabdus bacteria.","volume":"7","author":"N Waterfield","year":"2005","journal-title":"Cell Microbiol"},{"key":"ref77","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.molcel.2008.08.009","article-title":"Substrate-assisted catalysis by PARP10 limits its activity to mono-ADP-ribosylation.","volume":"32","author":"H Kleine","year":"2008","journal-title":"Mol 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Liu","year":"2005","journal-title":"Proteomics"},{"key":"ref81","doi-asserted-by":"crossref","first-page":"527","DOI":"10.2174\/138920305774933231","article-title":"Computational methods for remote homolog identification.","volume":"6","author":"XF Wan","year":"2005","journal-title":"Curr Protein Pept Sci"},{"key":"ref82","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1093\/bib\/bbl032","article-title":"The WWWH of remote homolog detection: The state of the art.","volume":"8","author":"P Fariselli","year":"2007","journal-title":"Brief Bioinform"},{"key":"ref83","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1186\/1471-2105-8-314","article-title":"A comprehensive system for evaluation of remote sequence similarity detection.","volume":"8","author":"Y Qi","year":"2007","journal-title":"BMC Bioinformatics"},{"key":"ref84","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1007\/s12033-007-0032-2","article-title":"Classification of protein folds.","volume":"36","author":"RB Russell","year":"2007","journal-title":"Mol Biotechnol"},{"key":"ref85","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1016\/S0022-2836(05)80134-2","article-title":"SCOP: A structural classification of proteins database for the investigation of sequences and structures.","volume":"247","author":"AG Murzin","year":"1995","journal-title":"J Mol Biol"},{"key":"ref86","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1016\/S0969-2126(97)00260-8","article-title":"CATH\u2013a hierarchic classification of protein domain structures.","volume":"5","author":"CA Orengo","year":"1997","journal-title":"Structure"},{"key":"ref87","doi-asserted-by":"crossref","DOI":"10.4324\/9780203427828-11","article-title":"From structure-based genome annotation to understanding genes and proteins.","author":"SA Teichmann","year":"2003"},{"key":"ref88","first-page":"107","article-title":"ScanProsite: A reference implementation of a PROSITE scanning tool.","volume":"1","author":"A Gattiker","year":"2002","journal-title":"Appl Bioinformatics"},{"key":"ref89","doi-asserted-by":"crossref","first-page":"D26","DOI":"10.1093\/nar\/gkl993","article-title":"Entrez gene: Gene-centered information at NCBI.","volume":"35","author":"D Maglott","year":"2007","journal-title":"Nucleic Acids Res"},{"key":"ref90","doi-asserted-by":"crossref","first-page":"e1000437","DOI":"10.1371\/journal.pgen.1000437","article-title":"Bacterial toxin-antitoxin systems: More than selfish entities?","volume":"5","author":"L Van Melderen","year":"2009","journal-title":"PLoS Genet"},{"key":"ref91","doi-asserted-by":"crossref","first-page":"W604","DOI":"10.1093\/nar\/gkl092","article-title":"Expresso: Automatic incorporation of structural information in multiple sequence alignments using 3D-coffee.","volume":"34","author":"F Armougom","year":"2006","journal-title":"Nucleic Acids Res"},{"key":"ref92","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1093\/bioinformatics\/15.4.305","article-title":"ESPript: Analysis of multiple sequence alignments in PostScript.","volume":"15","author":"P Gouet","year":"1999","journal-title":"Bioinformatics"},{"key":"ref93","doi-asserted-by":"crossref","first-page":"W465","DOI":"10.1093\/nar\/gkn180","article-title":"Phylogeny.fr: Robust phylogenetic analysis for the non-specialist.","volume":"36","author":"A Dereeper","year":"2008","journal-title":"Nucleic Acids Res"},{"key":"ref94","doi-asserted-by":"crossref","first-page":"1188","DOI":"10.1101\/gr.849004","article-title":"WebLogo: A sequence logo generator.","volume":"14","author":"GE Crooks","year":"2004","journal-title":"Genome Res"},{"key":"ref95","first-page":"2.3.1","article-title":"Multiple sequence alignment using ClustalW and ClustalX.","author":"JD Thompson","year":"2002"},{"key":"ref96","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1093\/bioinformatics\/17.8.754","article-title":"MRBAYES: Bayesian inference of phylogenetic trees.","volume":"17","author":"JP Huelsenbeck","year":"2001","journal-title":"Bioinformatics"},{"key":"ref97","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1016\/j.sbi.2006.03.004","article-title":"Servers for protein structure prediction.","volume":"16","author":"D Fischer","year":"2006","journal-title":"Curr Opin Struct Biol"},{"key":"ref98","doi-asserted-by":"crossref","first-page":"1015","DOI":"10.1093\/bioinformatics\/btg124","article-title":"3D-jury: A simple approach to improve protein structure predictions.","volume":"19","author":"K Ginalski","year":"2003","journal-title":"Bioinformatics"},{"key":"ref99","doi-asserted-by":"crossref","first-page":"W369","DOI":"10.1093\/nar\/gkm319","article-title":"Pcons.net: Protein structure prediction meta server.","volume":"35","author":"B Wallner","year":"2007","journal-title":"Nucleic Acids Res"},{"key":"ref100","doi-asserted-by":"crossref","first-page":"3305","DOI":"10.1093\/nar\/gkg557","article-title":"GeneSilico protein structure prediction meta-server.","volume":"31","author":"MA Kurowski","year":"2003","journal-title":"Nucleic Acids Res"},{"key":"ref101","doi-asserted-by":"crossref","first-page":"3375","DOI":"10.1093\/nar\/gkm251","article-title":"LOMETS: A local meta-threading-server for protein structure prediction.","volume":"35","author":"S Wu","year":"2007","journal-title":"Nucleic Acids Res"},{"key":"ref102","doi-asserted-by":"crossref","first-page":"W485","DOI":"10.1093\/nar\/gkp368","article-title":"@TOME-2: A new pipeline for comparative modeling of protein-ligand complexes.","volume":"37","author":"JL Pons","year":"2009","journal-title":"Nucleic Acids Res"},{"key":"ref103","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1002\/prot.21675","article-title":"Assessment of predictions submitted for the CASP7 domain prediction category.","volume":"69","author":"M Tress","year":"2007","journal-title":"Proteins"},{"key":"ref104","doi-asserted-by":"crossref","first-page":"W354","DOI":"10.1093\/nar\/gkm390","article-title":"DOMAC: An accurate, hybrid protein domain prediction server.","volume":"35","author":"J Cheng","year":"2007","journal-title":"Nucleic Acids Res"},{"key":"ref105","doi-asserted-by":"crossref","first-page":"1611","DOI":"10.1016\/j.bbamem.2008.01.026","article-title":"Pore formation: An ancient yet complex form of attack.","volume":"1778","author":"I Iacovache","year":"2008","journal-title":"Biochim Biophys Acta"},{"key":"ref106","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1110\/ps.051892906","article-title":"A comparative study of available software for high-accuracy homology modeling: From sequence alignments to structural models.","volume":"15","author":"A Nayeem","year":"2006","journal-title":"Protein Sci"},{"key":"ref107","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1007\/978-1-60327-058-8_8","article-title":"Protein structure modeling with MODELLER.","volume":"426","author":"N Eswar","year":"2008","journal-title":"Methods Mol Biol"},{"key":"ref108","doi-asserted-by":"crossref","first-page":"3670","DOI":"10.1038\/sj.emboj.7600813","article-title":"Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme.","volume":"24","author":"A Pautsch","year":"2005","journal-title":"EMBO J"},{"key":"ref109","doi-asserted-by":"crossref","first-page":"1219","DOI":"10.1016\/j.str.2006.05.022","article-title":"A steric antagonism of actin polymerization by a salmonella virulence protein.","volume":"14","author":"SM Margarit","year":"2006","journal-title":"Structure"},{"key":"ref110","doi-asserted-by":"crossref","first-page":"45924","DOI":"10.1074\/jbc.M307719200","article-title":"The crystal structure of C3stau2 from staphylococcus aureus and its complex with NAD.","volume":"278","author":"HR Evans","year":"2003","journal-title":"J Biol Chem"},{"key":"ref111","doi-asserted-by":"crossref","first-page":"28713","DOI":"10.1074\/jbc.M109.043018","article-title":"Structural basis for substrate recognition in the enzymatic component of ADP-ribosyltransferase toxin CDTa from clostridium difficile.","volume":"284","author":"A Sundriyal","year":"2009","journal-title":"J Biol Chem"},{"key":"ref112","doi-asserted-by":"crossref","first-page":"10155","DOI":"10.1021\/bi034625w","article-title":"Substrate binding and catalysis of ecto-ADP-ribosyltransferase 2.2 from rat.","volume":"42","author":"H Ritter","year":"2003","journal-title":"Biochemistry"},{"key":"ref113","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1126\/science.1113398","article-title":"Structural basis for the activation of cholera toxin by human ARF6-GTP.","volume":"309","author":"CJ O'Neal","year":"2005","journal-title":"Science"},{"key":"ref114","doi-asserted-by":"crossref","first-page":"1731","DOI":"10.1021\/ja026939x","article-title":"HADDOCK: A protein-protein docking approach based on biochemical or biophysical information.","volume":"125","author":"C Dominguez","year":"2003","journal-title":"J Am Chem Soc"},{"key":"ref115","first-page":"273","article-title":"Structural quality assurance.","author":"RA Laskowski","year":"2003"},{"key":"ref116","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1186\/1471-2105-9-403","article-title":"MetaMQAP: A meta-server for the quality assessment of protein models.","volume":"9","author":"M Pawlowski","year":"2008","journal-title":"BMC Bioinformatics"},{"key":"ref117","doi-asserted-by":"crossref","first-page":"W375","DOI":"10.1093\/nar\/gkm216","article-title":"MolProbity: All-atom contacts and structure validation for proteins and nucleic acids.","volume":"35","author":"IW Davis","year":"2007","journal-title":"Nucleic Acids Res"},{"key":"ref118","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1093\/protein\/8.2.127","article-title":"LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions.","volume":"8","author":"AC Wallace","year":"1995","journal-title":"Protein Eng"},{"key":"ref119","doi-asserted-by":"crossref","first-page":"D266","DOI":"10.1093\/nar\/gki001","article-title":"PDBsum more: New summaries and analyses of the known 3D structures of proteins and nucleic acids.","volume":"33","author":"RA Laskowski","year":"2005","journal-title":"Nucleic Acids Res"},{"key":"ref120","doi-asserted-by":"crossref","first-page":"W416","DOI":"10.1093\/nar\/gkm228","article-title":"3dLOGO: A web server for the identification, analysis and use of conserved protein substructures.","volume":"35","author":"A Via","year":"2007","journal-title":"Nucleic Acids 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