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

traP  -  signal transduction protein

Staphylococcus aureus RF122

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 traP


High impact information on traP


Chemical compound and disease context of traP


Biological context of traP


Anatomical context of traP


Associations of traP with chemical compounds

  • These data suggest that anti-kappa R-(33-52) 1) does not interact with the effector binding site of the receptor, but sterically interferes with U50,488H binding to the receptor; and/or 2) the antiserum interacts with a secondary binding site that is important for ligand binding, but may not be involved in signal transduction [21].
  • Despite this anomaly, the B cells from group II were able to progress through the cell cycle after stimulation with a combination of phorbol ester and ionomycin in complete medium, suggesting an impairment in BCR and CD40 early signal transduction [22].
  • These observations suggest that the cell wall stress stimulon is induced by inhibition of the process of peptidoglycan biosynthesis, and the inhibitory effects of glycerol monolaurate indicate that gene expression is dependent on a signal transduction pathway [23].
  • An inhibitor of protein tyrosine kinase, genistein, reduced MAC-T internalization of S. aureus by 95%, indicating a requirement for a host signal transduction system in this process [24].
  • Signal transduction studies with different inhibitors suggest that this one-way synergism is caused by an interaction between the cAMP and the PIP2 signaling pathway [25].

Other interactions of traP

  • This study demonstrates the role of sarA as a signal transduction regulatory component in response to aeration stimuli and suggests that sarA functions as a major repressor of protease activity [26].
  • The P2 operon sequence, reported here, contains 4 open reading frames, agrA, C, D, and B, of which A and C appear to encode proteins of a classical 2-component signal transduction pathway [27].
  • Furthermore, SarA plays a role in signal transduction in response to microaerobic growth since levels of hla were much lower in a microaerobic environment than after aerobic growth in the sarA mutant [26].

Analytical, diagnostic and therapeutic context of traP


  1. Competence for transformation: a matter of taste. Tortosa, P., Dubnau, D. Curr. Opin. Microbiol. (1999) [Pubmed]
  2. Sulfatides trigger increase of cytosolic free calcium and enhanced expression of tumor necrosis factor-alpha and interleukin-8 mRNA in human neutrophils. Evidence for a role of L-selectin as a signaling molecule. Laudanna, C., Constantin, G., Baron, P., Scarpini, E., Scarlato, G., Cabrini, G., Dechecchi, C., Rossi, F., Cassatella, M.A., Berton, G. J. Biol. Chem. (1994) [Pubmed]
  3. A genomic analysis of two-component signal transduction in Streptococcus pneumoniae. Throup, J.P., Koretke, K.K., Bryant, A.P., Ingraham, K.A., Chalker, A.F., Ge, Y., Marra, A., Wallis, N.G., Brown, J.R., Holmes, D.J., Rosenberg, M., Burnham, M.K. Mol. Microbiol. (2000) [Pubmed]
  4. Quorum sensing by peptide pheromones and two-component signal-transduction systems in Gram-positive bacteria. Kleerebezem, M., Quadri, L.E., Kuipers, O.P., de Vos, W.M. Mol. Microbiol. (1997) [Pubmed]
  5. Role for plastin in host defense distinguishes integrin signaling from cell adhesion and spreading. Chen, H., Mocsai, A., Zhang, H., Ding, R.X., Morisaki, J.H., White, M., Rothfork, J.M., Heiser, P., Colucci-Guyon, E., Lowell, C.A., Gresham, H.D., Allen, P.M., Brown, E.J. Immunity (2003) [Pubmed]
  6. alpha-Toxin is a mediator of Staphylococcus aureus-induced cell death and activates caspases via the intrinsic death pathway independently of death receptor signaling. Bantel, H., Sinha, B., Domschke, W., Peters, G., Schulze-Osthoff, K., Jänicke, R.U. J. Cell Biol. (2001) [Pubmed]
  7. Discrete steps in sensing of beta-lactam antibiotics by the BlaR1 protein of the methicillin-resistant Staphylococcus aureus bacterium. Thumanu, K., Cha, J., Fisher, J.F., Perrins, R., Mobashery, S., Wharton, C. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  8. Superantigen staphylococcal enterotoxin B-induced T-helper cell activation is independent of CD4 molecules and phosphatidylinositol hydrolysis. Oyaizu, N., Chirmule, N., Yagura, H., Pahwa, R., Good, R.A., Pahwa, S. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  9. Equivalence of lauric acid and glycerol monolaurate as inhibitors of signal transduction in Staphylococcus aureus. Ruzin, A., Novick, R.P. J. Bacteriol. (2000) [Pubmed]
  10. The target of RNAIII-activating protein (TRAP) from Staphylococcus aureus: purification, crystallization and preliminary X-ray analysis. Han, Y.H., Kim, Y.G., Kim, D.Y., Ha, S.C., Lokanath, N.K., Kim, K.K. Biochim. Biophys. Acta (2005) [Pubmed]
  11. Gangliosides suppress tumor necrosis factor production in human monocytes. Ziegler-Heitbrock, H.W., Käfferlein, E., Haas, J.G., Meyer, N., Ströbel, M., Weber, C., Flieger, D. J. Immunol. (1992) [Pubmed]
  12. Regulation of Staphylococcus aureus pathogenesis via target of RNAIII-activating Protein (TRAP). Balaban, N., Goldkorn, T., Gov, Y., Hirshberg, M., Koyfman, N., Matthews, H.R., Nhan, R.T., Singh, B., Uziel, O. J. Biol. Chem. (2001) [Pubmed]
  13. Ceramide triggers meiotic cell cycle progression in Xenopus oocytes. A potential mediator of progesterone-induced maturation. Strum, J.C., Swenson, K.I., Turner, J.E., Bell, R.M. J. Biol. Chem. (1995) [Pubmed]
  14. Parasite accessory cell interactions in murine leishmaniasis. I. Evasion and stimulus-dependent suppression of the macrophage interleukin 1 response by Leishmania donovani. Reiner, N.E. J. Immunol. (1987) [Pubmed]
  15. Identification of a distinct pool of sphingomyelin involved in the sphingomyelin cycle. Linardic, C.M., Hannun, Y.A. J. Biol. Chem. (1994) [Pubmed]
  16. Phosphatidylinositol 3-kinase activation in normal human B lymphocytes. Aagaard-Tillery, K.M., Jelinek, D.F. J. Immunol. (1996) [Pubmed]
  17. Signal transduction events and Fc gamma R engagement in human neutrophils stimulated with immune complexes. Walker, B.A., Hagenlocker, B.E., Stubbs, E.B., Sandborg, R.R., Agranoff, B.W., Ward, P.A. J. Immunol. (1991) [Pubmed]
  18. Apoptosis but not other activation events is inhibited by a mutation in the transmembrane domain of T cell receptor beta that impairs CD3zeta association. Rodríguez-Tarduchy, G., Sahuquillo, A.G., Alarcón, B., Bragado, R. J. Biol. Chem. (1996) [Pubmed]
  19. Influence of lipoteichoic acid structure on recognition by the macrophage scavenger receptor. Greenberg, J.W., Fischer, W., Joiner, K.A. Infect. Immun. (1996) [Pubmed]
  20. Lipoteichoic acid selectively induces the ERK signaling pathway in the cornea. You, L., Kruse, F.E., Bacher, S., Schmitz, M.L. Invest. Ophthalmol. Vis. Sci. (2002) [Pubmed]
  21. Anti-human kappa opioid receptor antibodies: characterization of site-directed neutralizing antibodies specific for a peptide kappa R(33-52) derived from the predicted amino terminal region of the human kappa receptor. Buchner, R.R., Vogen, S.M., Fischer, W., Thoman, M.L., Sanderson, S.D., Morgan, E.L. J. Immunol. (1997) [Pubmed]
  22. Impairment of B-lymphocyte differentiation induced by dual triggering of the B-cell antigen receptor and CD40 in advanced HIV-1-disease. Conge, A.M., Tarte, K., Reynes, J., Segondy, M., Gerfaux, J., Zembala, M., Vendrell, J.P. AIDS (1998) [Pubmed]
  23. Regulation of the expression of cell wall stress stimulon member gene msrA1 in methicillin-susceptible or -resistant Staphylococcus aureus. Pechous, R., Ledala, N., Wilkinson, B.J., Jayaswal, R.K. Antimicrob. Agents Chemother. (2004) [Pubmed]
  24. Fibronectin binding protein and host cell tyrosine kinase are required for internalization of Staphylococcus aureus by epithelial cells. Dziewanowska, K., Patti, J.M., Deobald, C.F., Bayles, K.W., Trumble, W.R., Bohach, G.A. Infect. Immun. (1999) [Pubmed]
  25. One-way synergistic effect of low superantigen concentrations on lipopolysaccharide-induced cytokine production. Luhm, J., Kirchner, H., Rink, L. J. Interferon Cytokine Res. (1997) [Pubmed]
  26. Role of SarA in virulence determinant production and environmental signal transduction in Staphylococcus aureus. Chan, P.F., Foster, S.J. J. Bacteriol. (1998) [Pubmed]
  27. The agr P2 operon: an autocatalytic sensory transduction system in Staphylococcus aureus. Novick, R.P., Projan, S.J., Kornblum, J., Ross, H.F., Ji, G., Kreiswirth, B., Vandenesch, F., Moghazeh, S. Mol. Gen. Genet. (1995) [Pubmed]
  28. Monocyte deactivation in severe human sepsis or following cardiopulmonary bypass. Wilhelm, W., Grundmann, U., Rensing, H., Werth, M., Langemeyer, J., Stracke, C., Dhingra, D., Bauer, M. Shock (2002) [Pubmed]
  29. Quorum sensing and the regulation of virulence gene expression in pathogenic bacteria. Winzer, K., Williams, P. Int. J. Med. Microbiol. (2001) [Pubmed]
WikiGenes - Universities