Structural basis of Streptococcus pyogenes immunity to its NAD+ glycohydrolase toxin.
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[1] Joydeep Ghosh,et al. Characterization of Streptococcus pyogenes beta-NAD+ glycohydrolase: re-evaluation of enzymatic properties associated with pathogenesis. , 2010, The Journal of biological chemistry.
[2] H. Tsuge,et al. Structural basis of actin recognition and arginine ADP-ribosylation by Clostridium perfringens ι-toxin , 2008, Proceedings of the National Academy of Sciences.
[3] I. Tatsuno,et al. Characterization of the NAD-glycohydrolase in streptococcal strains. , 2007, Microbiology.
[4] B. Finlay,et al. Host–microbe interactions , 2007, Nature.
[5] Eric Blanc,et al. Automated structure solution with autoSHARP. , 2007, Methods in molecular biology.
[6] Joydeep Ghosh,et al. Specificity of Streptococcus pyogenes NAD+ glycohydrolase in cytolysin‐mediated translocation , 2006, Molecular microbiology.
[7] K. Acharya,et al. A family of killer toxins , 2006, The FEBS journal.
[8] Y. Yokota,et al. Genetic and Biochemical Properties of Streptococcal NAD-glycohydrolase Inhibitor* , 2006, Journal of Biological Chemistry.
[9] M. Wessels,et al. Enhancement of Streptolysin O Activity and Intrinsic Cytotoxic Effects of the Group A Streptococcal Toxin, NAD-Glycohydrolase* , 2006, Journal of Biological Chemistry.
[10] J. Pinkner,et al. A Novel Endogenous Inhibitor of the Secreted Streptococcal NAD-Glycohydrolase , 2005, PLoS Pathogens.
[11] A. Schwan,et al. Exotoxin A–eEF2 complex structure indicates ADP ribosylation by ribosome mimicry , 2005, Nature.
[12] J. Potempa,et al. Fighting an enemy within: cytoplasmic inhibitors of bacterial cysteine proteases , 2005, Molecular microbiology.
[13] K. Gerdes,et al. Prokaryotic toxin–antitoxin stress response loci , 2005, Nature Reviews Microbiology.
[14] Y. Yokota,et al. Molecular characterization of NADase-streptolysin O operon of hemolytic streptococci. , 2005, Biochimica et biophysica acta.
[15] K Henrick,et al. Electronic Reprint Biological Crystallography Secondary-structure Matching (ssm), a New Tool for Fast Protein Structure Alignment in Three Dimensions Biological Crystallography Secondary-structure Matching (ssm), a New Tool for Fast Protein Structure Alignment in Three Dimensions , 2022 .
[16] Kevin Cowtan,et al. research papers Acta Crystallographica Section D Biological , 2005 .
[17] M. Caparon,et al. Specificity of streptolysin O in cytolysin‐mediated translocation , 2004, Molecular microbiology.
[18] D. Szebenyi,et al. ADP-ribosyl cyclase; crystal structures reveal a covalent intermediate. , 2004, Structure.
[19] Finbarr Hayes,et al. Toxins-Antitoxins: Plasmid Maintenance, Programmed Cell Death, and Cell Cycle Arrest , 2003, Science.
[20] Naohiro Matsugaki,et al. Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal protein transport , 2003, Nature Structural Biology.
[21] Xiangyuan He,et al. Crystal structure of GGA2 VHS domain and its implication in plasticity in the ligand binding pocket , 2003, FEBS letters.
[22] Burkhard Rost,et al. The PredictProtein server , 2003, Nucleic Acids Res..
[23] George M Sheldrick,et al. Substructure solution with SHELXD. , 2002, Acta crystallographica. Section D, Biological crystallography.
[24] P. Salo,et al. ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization. , 2002, Molecular biology of the cell.
[25] Jérôme Gouzy,et al. ProDom: Automated Clustering of Homologous Domains , 2002, Briefings Bioinform..
[26] M. Wessels,et al. NAD+‐glycohydrolase acts as an intracellular toxin to enhance the extracellular survival of group A streptococci , 2002, Molecular microbiology.
[27] Thomas Earnest,et al. Structural basis for recognition of acidic-cluster dileucine sequence by GGA1 , 2002, Nature.
[28] J. Tainer,et al. The ARTT motif and a unified structural understanding of substrate recognition in ADP-ribosylating bacterial toxins and eukaryotic ADP-ribosyltransferases. , 2002, International journal of medical microbiology : IJMM.
[29] J. Bonifacino,et al. Structural Requirements for Function of Yeast GGAs in Vacuolar Protein Sorting, α-Factor Maturation, and Interactions with Clathrin , 2001, Molecular and Cellular Biology.
[30] N. Ruiz,et al. Cytolysin-Mediated Translocation (CMT) A Functional Equivalent of Type III Secretion in Gram-Positive Bacteria , 2001, Cell.
[31] J. Tainer,et al. Crystal structure and novel recognition motif of rho ADP-ribosylating C3 exoenzyme from Clostridium botulinum: structural insights for recognition specificity and catalysis. , 2001, Journal of molecular biology.
[32] D. Stevens,et al. Molecular epidemiology of nga and NAD glycohydrolase/ADP-ribosyltransferase activity among Streptococcus pyogenes causing streptococcal toxic shock syndrome. , 2000, The Journal of infectious diseases.
[33] M. Cunningham,et al. Pathogenesis of group A streptococcal infections. , 2000, Clinical microbiology reviews.
[34] J. Pflugrath,et al. The finer things in X-ray diffraction data collection. , 1999, Acta crystallographica. Section D, Biological crystallography.
[35] I. Vetter,et al. The crystal structure of rna1p: a new fold for a GTPase-activating protein. , 1999, Molecular cell.
[36] R J Read,et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. , 1998, Acta crystallographica. Section D, Biological crystallography.
[37] K Cowtan,et al. Miscellaneous algorithms for density modification. , 1998, Acta crystallographica. Section D, Biological crystallography.
[38] G. Murshudov,et al. Refinement of macromolecular structures by the maximum-likelihood method. , 1997, Acta crystallographica. Section D, Biological crystallography.
[39] C Sander,et al. Mapping the Protein Universe , 1996, Science.
[40] R. Rappuoli,et al. Three conserved consensus sequences identify the NAD‐binding site of ADP‐ribosylating enzymes, expressed by eukaryotes, bacteria and T‐even bacteriophages , 1996, Molecular microbiology.
[41] S. Nakamura,et al. NAD(+)-glycohydrolase from Streptococcus pyogenes shows cyclic ADP-ribose forming activity. , 1995, FEMS microbiology letters.
[42] Collaborative Computational,et al. The CCP4 suite: programs for protein crystallography. , 1994, Acta crystallographica. Section D, Biological crystallography.
[43] J. Zou,et al. Improved methods for building protein models in electron density maps and the location of errors in these models. , 1991, Acta crystallographica. Section A, Foundations of crystallography.
[44] W. B. Davis. Identification of a nicotinamide adenine dinucleotide glycohydrolase and an associated inhibitor in isoniazid-susceptible and -resistant Mycobacterium phlei , 1980, Antimicrobial Agents and Chemotherapy.
[45] K. E. Everse,et al. The pyridine nucleosidases from Bacillus subtilis and Neurospora crassa. Isolation and structural properties. , 1975, Archives of biochemistry and biophysics.
[46] N. Kaplan,et al. The pyridine nucleosidase from Bacillus subtilis. Kinetic properties and enzyme-inhibitor interactions. , 1975, Archives of biochemistry and biophysics.
[47] S. Shany,et al. Purification and properties of streptococcal nicotinamide adenine dinucleotide glycohydrolase , 1975, Journal of bacteriology.
[48] I. Mather,et al. A heat-stable nicotinamide adenine dinucleotidase from Pseudomonas fluorescens. , 1969, Journal of general microbiology.