The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

surE  -  stationary phase survival protein SurE

Escherichia coli O157:H7 str. EDL933

 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of surE

 

High impact information on surE

 

Chemical compound and disease context of surE

 

Biological context of surE

 

Anatomical context of surE

 

Associations of surE with chemical compounds

  • The parenchymal acid phosphatase isozymes hydrolyze preferentially AMP and CMP, while the sinusoidal isozyme hydrolyzes phenylphosphate [15].
  • Cloning and characterization of the pH 2.5 acid phosphatase gene, appA: cyclic AMP mediated negative regulation [22].
  • We show here that the interruption of the aphA reading frame by kanamycin resistance gene insertion, abolishes acid phosphatase (NAP) activity [23].
  • Results are reported for acid phosphatase, alkaline phosphatase, ATPase, and pectinase at different conditions of temperature, CO2 pressure, and treatment time (32-40 degrees C, 85-150 bar, 30-70 min) [24].
  • Different compounds derived from choline, and obtained by demethylation or by oxidation of the primary alcohol group with subsequent N-demethylation, were tested as inducer agents of acid phosphatase and cholinesterase in Ps. aeruginosa [11].
 

Other interactions of surE

 

Analytical, diagnostic and therapeutic context of surE

References

  1. Growth-phase-dependent transcriptional regulation of the pcm and surE genes required for stationary-phase survival of Escherichia coli. Li, C., Wu, P.Y., Hsieh, M. Microbiology (Reading, Engl.) (1997) [Pubmed]
  2. Intracellular survival of virulent Bordetella pertussis in human polymorphonuclear leukocytes. Steed, L.L., Setareh, M., Friedman, R.L. J. Leukoc. Biol. (1991) [Pubmed]
  3. In vivo and in vitro studies of bacterial endotoxin-membrane interactions and the effects of membrane-active agents. Garnett, M.E., Godin, D.V., Tuchek, J.M. Br. J. Pharmacol. (1984) [Pubmed]
  4. Characterization and sequence of PhoC, the principal phosphate-irrepressible acid phosphatase of Morganella morganii. Thaller, M.C., Berlutti, F., Schippa, S., Lombardi, G., Rossolini, G.M. Microbiology (Reading, Engl.) (1994) [Pubmed]
  5. PHO5-LACZ hybrid proteins block translocation of native acid phosphatase in Saccharomyces cerevisiae. Wolfe, P.B. J. Biol. Chem. (1988) [Pubmed]
  6. Hemi-methylated oriC DNA binding activity found in non-specific acid phosphatase. Reshetnyak, E., d'Alençon, E., Kern, R., Taghbalout, A., Guillaud, P., Kohiyama, M. Mol. Microbiol. (1999) [Pubmed]
  7. The nucleotide sequence of the yeast PHO5 gene: a putative precursor of repressible acid phosphatase contains a signal peptide. Arima, K., Oshima, T., Kubota, I., Nakamura, N., Mizunaga, T., Toh-e, A. Nucleic Acids Res. (1983) [Pubmed]
  8. Mechanistic implications for Escherichia coli cofactor-dependent phosphoglycerate mutase based on the high-resolution crystal structure of a vanadate complex. Bond, C.S., White, M.F., Hunter, W.N. J. Mol. Biol. (2002) [Pubmed]
  9. Selective depletion of macrophages prevents pituitary-adrenal activation in response to subpyrogenic, but not to pyrogenic, doses of bacterial endotoxin in rats. Derijk, R., Van Rooijen, N., Tilders, F.J., Besedovsky, H.O., Del Rey, A., Berkenbosch, F. Endocrinology (1991) [Pubmed]
  10. Inhibition of phosphatase and sulfatase by transition-state analogues. Stankiewicz, P.J., Gresser, M.J. Biochemistry (1988) [Pubmed]
  11. Pseudomonas aeruginosa acid phosphatase and cholinesterase induced by choline and its metabolic derivatives may contain a similar anionic peripheral site. Lisa, T.A., Garrido, M.N., Domenech, C.E. Mol. Cell. Biochem. (1984) [Pubmed]
  12. Macrophage function in deer. Cross, M.L., Thomson, A.J., Slobbe, L.J., Griffin, J.F., Buchan, G.S. Vet. Immunol. Immunopathol. (1996) [Pubmed]
  13. Expression of herpes simplex virus glycoprotein B gene in yeast. Nozaki, C., Makizumi, K., Kino, Y., Nakatake, H., Eto, T., Mizuno, K., Hamada, F., Ohtomo, N. Virus Res. (1985) [Pubmed]
  14. Acid phosphatases of Escherichia coli: molecular cloning and analysis of agp, the structural gene for a periplasmic acid glucose phosphatase. Pradel, E., Boquet, P.L. J. Bacteriol. (1988) [Pubmed]
  15. Effect of endotoxin on rat liver. Analysis of acid phosphatase isozymes in the liver of normal and endotoxin-treated rats. Hirata, K., Kaneko, A., Ogawa, K., Hayasaka, H., Onoé, T. Lab. Invest. (1980) [Pubmed]
  16. Effects of sigmaS and the transcriptional activator AppY on induction of the Escherichia coli hya and cbdAB-appA operons in response to carbon and phosphate starvation. Atlung, T., Knudsen, K., Heerfordt, L., Brøndsted, L. J. Bacteriol. (1997) [Pubmed]
  17. Isolation, characterization, and nucleotide sequence of appY, a regulatory gene for growth-phase-dependent gene expression in Escherichia coli. Atlung, T., Nielsen, A., Hansen, F.G. J. Bacteriol. (1989) [Pubmed]
  18. Hemocyte-mediated phagocytosis and melanization in the mosquito Armigeres subalbatus following immune challenge by bacteria. Hillyer, J.F., Schmidt, S.L., Christensen, B.M. Cell Tissue Res. (2003) [Pubmed]
  19. Ultrastructural and cytochemical evaluation of sepsis-induced changes in the rat pulmonary intravascular mononuclear phagocytes. Singh, B., Doane, K.J., Niehaus, G.D. J. Anat. (1998) [Pubmed]
  20. Depressant effects of ambroxol on lipopolysaccharide- or fMLP-stimulated free radical production and granule enzyme release by alveolar macrophages. Lee, C.S., Jang, Y.Y., Han, E.S. Pulmonary pharmacology & therapeutics. (1999) [Pubmed]
  21. Phagocytosis of bacteria by proximal tubular epithelium in experimental pyelonephritis. Iványi, B., Krenács, T., Petri, S. Virchows Arch., B, Cell Pathol. (1985) [Pubmed]
  22. Cloning and characterization of the pH 2.5 acid phosphatase gene, appA: cyclic AMP mediated negative regulation. Touati, E., Danchin, A. Mol. Gen. Genet. (1987) [Pubmed]
  23. Increased expression of a hemimethylated oriC binding protein, SeqA, in an aphA mutant. Kohiyama, M., Bahloul, A., Kern, R., Meury, J., Reshetnyak, E., Malki, A., Guha, S. Biochimie (1998) [Pubmed]
  24. A study on the inactivation of micro-organisms and enzymes by high pressure CO2. Bertoloni, G., Bertucco, A., De Cian, V., Parton, T. Biotechnol. Bioeng. (2006) [Pubmed]
  25. Identification of the gene (aphA) encoding the class B acid phosphatase/phosphotransferase of Escherichia coli MG1655 and characterization of its product. Thaller, M.C., Schippa, S., Bonci, A., Cresti, S., Rossolini, G.M. FEMS Microbiol. Lett. (1997) [Pubmed]
  26. The class C acid phosphatase of Helicobacter pylori is a 5' nucleotidase. Reilly, T.J., Calcutt, M.J. Protein Expr. Purif. (2004) [Pubmed]
 
WikiGenes - Universities