The ng_ζ1 toxin of the gonococcal epsilon/zeta toxin/antitoxin system drains precursors for cell wall synthesis
暂无分享,去创建一个
[1] C. Broeckling,et al. The effector AvrRxo1 phosphorylates NAD in planta , 2017, PLoS pathogens.
[2] A. Rocker,et al. 3′-NADP and 3′-NAADP, Two Metabolites Formed by the Bacterial Type III Effector AvrRxo1 , 2016, The Journal of Biological Chemistry.
[3] W. Chan,et al. The Streptococcus pneumoniae pezAT Toxin–Antitoxin System Reduces β-Lactam Resistance and Genetic Competence , 2016, Front. Microbiol..
[4] F. García-del Portillo,et al. Toxin-antitoxins and bacterial virulence. , 2016, FEMS microbiology reviews.
[5] H. Ishihara,et al. AvrRxo1 Is a Bifunctional Type III Secreted Effector and Toxin-Antitoxin System Component with Homologs in Diverse Environmental Contexts , 2016, PloS one.
[6] Dae-Hee Lee,et al. Comparative genomics and experimental evolution of Escherichia coli BL21(DE3) strains reveal the landscape of toxicity escape from membrane protein overproduction , 2015, Scientific Reports.
[7] J. Tokuhisa,et al. Crystal Structure of Xanthomonas AvrRxo1-ORF1, a Type III Effector with a Polynucleotide Kinase Domain, and Its Interactor AvrRxo1-ORF2. , 2015, Structure.
[8] Shuai Le,et al. The chromosomal SezAT toxin–antitoxin system promotes the maintenance of the SsPI‐1 pathogenicity island in epidemic Streptococcus suis , 2015, Molecular microbiology.
[9] A. Rocker,et al. A cis‐acting antitoxin domain within the chromosomal toxin–antitoxin module EzeT of Escherichia coli quenches toxin activity , 2015, Molecular microbiology.
[10] Tanel Tenson,et al. Recent functional insights into the role of (p)ppGpp in bacterial physiology , 2015, Nature Reviews Microbiology.
[11] J. Alonso,et al. Toxin ζ Reversible Induces Dormancy and Reduces the UDP-N-Acetylglucosamine Pool as One of the Protective Responses to Cope with Stress , 2014, Toxins.
[12] L. Van Melderen,et al. Toxin-Antitoxin Systems as Multilevel Interaction Systems , 2014, Toxins.
[13] E. Rotem,et al. HipA-mediated antibiotic persistence via phosphorylation of the glutamyl-tRNA-synthetase , 2013, Nature Communications.
[14] Sang Jun Lee,et al. Inactivation of Metabolic Genes Causes Short- and Long-Range dys-Regulation in Escherichia coli Metabolic Network , 2013, PloS one.
[15] N. Zenkin,et al. Molecular mechanism of bacterial persistence by HipA. , 2013, Molecular cell.
[16] A. Garcia-Pino,et al. The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu , 2013, Nature chemical biology.
[17] U. Zielenkiewicz,et al. Regulation of toxin-antitoxin systems by proteolysis. , 2013, Plasmid.
[18] Peter C. Fineran,et al. Ribonucleases in bacterial toxin-antitoxin systems. , 2013, Biochimica et biophysica acta.
[19] R. Bertram,et al. Toxin-antitoxin systems are ubiquitous and versatile modulators of prokaryotic cell fate. , 2013, FEMS microbiology letters.
[20] S. Brantl. Bacterial type I toxin-antitoxin systems , 2012, RNA biology.
[21] K. Gerdes,et al. Bacterial persistence and toxin-antitoxin loci. , 2012, Annual review of microbiology.
[22] M. Inouye,et al. Toxin-antitoxin systems in bacteria and archaea. , 2011, Annual review of genetics.
[23] H. Mutschler,et al. ε/ζ systems: their role in resistance, virulence, and their potential for antibiotic development , 2011, Journal of Molecular Medicine.
[24] T. Wood,et al. Toxin-Antitoxin Systems Influence Biofilm and Persister Cell Formation and the General Stress Response , 2011, Applied and Environmental Microbiology.
[25] A. Leach,et al. A Variable Region within the Genome of Streptococcus pneumoniae Contributes to Strain-Strain Variation in Virulence , 2011, PloS one.
[26] Raphaël Leplae,et al. Diversity of bacterial type II toxin–antitoxin systems: a comprehensive search and functional analysis of novel families , 2011, Nucleic acids research.
[27] R. Shoeman,et al. A Novel Mechanism of Programmed Cell Death in Bacteria by Toxin–Antitoxin Systems Corrupts Peptidoglycan Synthesis , 2011, PLoS biology.
[28] Xiaoyuan Wang,et al. Lipopolysaccharide: Biosynthetic pathway and structure modification. , 2010, Progress in lipid research.
[29] C. van der Does,et al. Conjugative Plasmids of Neisseria gonorrhoeae , 2010, PloS one.
[30] Kevin Cowtan,et al. Recent developments in classical density modification , 2010, Acta crystallographica. Section D, Biological crystallography.
[31] Vincent B. Chen,et al. Correspondence e-mail: , 2000 .
[32] R. Lenski,et al. Understanding the differences between genome sequences of Escherichia coli B strains REL606 and BL21(DE3) and comparison of the E. coli B and K-12 genomes. , 2009, Journal of molecular biology.
[33] Seema Namboori,et al. Enzymatic analysis of uridine diphosphate N-acetyl-D-glucosamine. , 2008, Analytical biochemistry.
[34] Liisa Holm,et al. Searching protein structure databases with DaliLite v.3 , 2008, Bioinform..
[35] D. Blanot,et al. Cytoplasmic steps of peptidoglycan biosynthesis. , 2008, FEMS microbiology reviews.
[36] H. Rubin,et al. Characterization of Nucleotide Pools as a Function of Physiological State in Escherichia coli , 2007, Journal of bacteriology.
[37] A. Brunger. Version 1.2 of the Crystallography and NMR system , 2007, Nature Protocols.
[38] Randy J. Read,et al. Phaser crystallographic software , 2007, Journal of applied crystallography.
[39] Anton Meinhart,et al. Molecular and Structural Characterization of the PezAT Chromosomal Toxin-Antitoxin System of the Human Pathogen Streptococcus pneumoniae* , 2007, Journal of Biological Chemistry.
[40] W. Hunter,et al. Nucleotide substrate recognition by UDP-N-acetylglucosamine acyltransferase (LpxA) in the first step of lipid A biosynthesis. , 2007, Journal of molecular biology.
[41] U. Zielenkiewicz,et al. The Toxin-Antitoxin System of the Streptococcal Plasmid pSM19035 , 2005, Journal of bacteriology.
[42] K. Gerdes,et al. Prokaryotic toxin–antitoxin stress response loci , 2005, Nature Reviews Microbiology.
[43] K. Gerdes,et al. Toxin–antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes , 2005, Nucleic acids research.
[44] P. Berti,et al. UDP-N-acetylmuramic acid (UDP-MurNAc) is a potent inhibitor of MurA (enolpyruvyl-UDP-GlcNAc synthase). , 2005, Biochemistry.
[45] Kevin Cowtan,et al. research papers Acta Crystallographica Section D Biological , 2005 .
[46] M. W. van der Woude,et al. Phase and Antigenic Variation in Bacteria , 2004, Clinical Microbiology Reviews.
[47] Mitsuhiko Ikura,et al. MazF cleaves cellular mRNAs specifically at ACA to block protein synthesis in Escherichia coli. , 2003, Molecular cell.
[48] Anton Meinhart,et al. Crystal structure of the plasmid maintenance system ɛ/ζ: Functional mechanism of toxin ζ and inactivation by ɛ2ζ2 complex formation , 2003, Proceedings of the National Academy of Sciences of the United States of America.
[49] Måns Ehrenberg,et al. The Bacterial Toxin RelE Displays Codon-Specific Cleavage of mRNAs in the Ribosomal A Site , 2003, Cell.
[50] S. Walker,et al. The Kinetic Characterization of Escherichia coli MurG Using Synthetic Substrate Analogues , 1999 .
[51] G. Murshudov,et al. Refinement of macromolecular structures by the maximum-likelihood method. , 1997, Acta crystallographica. Section D, Biological crystallography.
[52] J. Alonso,et al. Analysis of the stabilization system of pSM19035-derived plasmid pBT233 in Bacillus subtilis. , 1993, Gene.
[53] L. Wyns,et al. The F plasmid CcdB protein induces efficient ATP-dependent DNA cleavage by gyrase. , 1993, Journal of molecular biology.
[54] J. Alonso,et al. Characterization of the effectors required for stable inheritance of Streptococcus pyogenes pSM19035-derived plasmids in Bacillus subtilis , 1993, Molecular and General Genetics MGG.
[55] Wolfgang Kabsch,et al. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants , 1993 .
[56] R F Standaert,et al. Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. , 1993, Journal of molecular biology.
[57] P. R. Sibbald,et al. The P-loop--a common motif in ATP- and GTP-binding proteins. , 1990, Trends in biochemical sciences.
[58] D. Mengin-Lecreulx,et al. Variations in UDP-N-acetylglucosamine and UDP-N-acetylmuramyl-pentapeptide pools in Escherichia coli after inhibition of protein synthesis , 1989, Journal of bacteriology.
[59] A. Bzowska,et al. Properties of two unusual, and fluorescent, substrates of purine-nucleoside phosphorylase: 7-methylguanosine and 7-methylinosine. , 1986, Biochimica et biophysica acta.
[60] S. Morse,et al. High-level tetracycline resistance in Neisseria gonorrhoeae is result of acquisition of streptococcal tetM determinant , 1986, Antimicrobial Agents and Chemotherapy.
[61] K. Gerdes,et al. Mechanism of postsegregational killing by the hok gene product of the parB system of plasmid R1 and its homology with the relF gene product of the E. coli relB operon. , 1986, The EMBO journal.
[62] W. H. Elliott,et al. Data for Biochemical Research , 1986 .
[63] Z. A. McGee,et al. Ability of monomeric peptidoglycan fragments from Neisseria gonorrhoeae to damage human fallopian-tube mucosa. , 1984, The Journal of infectious diseases.
[64] T. Ogura,et al. Mini-F plasmid genes that couple host cell division to plasmid proliferation. , 1983, Proceedings of the National Academy of Sciences of the United States of America.
[65] J. Heijenoort,et al. Pool levels of UDP N-acetylglucosamine and UDP N-acetylglucosamine-enolpyruvate in Escherichia coli and correlation with peptidoglycan synthesis , 1983, Journal of bacteriology.
[66] J. Heijenoort,et al. Cytoplasmic steps of peptidoglycan synthesis in Escherichia coli , 1982, Journal of bacteriology.
[67] R. Rosenthal. Release of soluble peptidoglycan from growing gonococci: hexaminidase and amidase activities , 1979, Infection and immunity.
[68] J. Berghäuser. A reactive arginine in adenylate kinase. , 1975, Biochimica et biophysica acta.
[69] Paul Doty,et al. Absorption spectra of nucleotides, polynucleotides, and nucleic acids in the far ultraviolet , 1963 .
[70] T. Arndt. Crystal , 2019, Springer Reference Medizin.
[71] G. Sheldrick. A short history of SHELX. , 2008, Acta crystallographica. Section A, Foundations of crystallography.
[72] W. Delano. The PyMOL Molecular Graphics System , 2002 .