Principles of cell signaling - UT Southwestern

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39057_ch14_cellbio.qxd 8/28/06 5:11 PM Page 640 Review Mangelsdorf, D. J. et al., 1995. The nuclear receptor superfamily: the second decade. Cell v. 83 p. 835–839. Smith, C. L. and O’Malley, B. W., 2004. Coregulator function: a key to understanding tissue specificity of selective receptor modulators. Endocr. Rev. v. 25 p. 45–71. Research Brzozowski A. M., Pike, A. C., Dauter, Z., Hubbard, R. E., Bonn, T., Engstrom, O., Ohman, L., Green, G. L., Gustafsson, J. A., and Carlquist, M., 1997. Molecular basis of agonism and antagonism in the oestrogen receptor. Nature v. 389 p. 753–758. 14.20 G protein signaling modules are widely used and highly adaptable Review Clapham, D. E. and Neer, E. J., 1997. G protein subunits. Annu. Rev. Pharmacol. Toxicol. v. 37 p. 167–203. Filipek, S., Teller, D. C., Palczewski, K., and Stenkamp, R., 2003. The crystallographic model of rhodopsin and its use in studies of other G protein-coupled receptors. Annu. Rev. Biophys. Biomol. Struct. v. 32 p. 375–397. Ross, E. M. and Wilkie, T. M., 2000. GTPaseactivating proteins for heterotrimeric G proteins: Regulators of G protein signaling (RGS) and RGS-like proteins. Annu. Rev. Biochem. v. 69 p. 795–827. Ross, E. M., 1989. Signal sorting and amplification through G protein-coupled receptors. Neuron v. 3 p. 141–152. Sprang, S. R., 1997. G proteins, effectors and GAPs: structure and mechanism. Curr. Opin. Struct. Biol. v. 7 p. 849–856. Sprang, S. R., 1997. G protein mechanisms: Insights from structural analysis. Annu. Rev. Biochem. v. 66 p. 639–678. Research Benke, T., Motoshima, C. A., Fox, H., Le Trong, B. A., Teller, I., Okada, D. C., Stenkamp, T., Yamamoto, R. E., and Miyano, M., 2000. Crystal structure of rhodopsin: A G protein-coupled receptor. Science v. 289 p. 739–745. Chen, C. -K., Burns, M. E., He, W., Wensel, T. G., Baylor, D. A., and Simon, M. I., 2000. Slowed recovery of rod photoresponse in mice lacking the GTPase acceleration protein RGS9-1. Nature, v. 403 p. 557–560. Palczewski, K., Kumasaka, T., Hori, T., Behnke , C. A., Motoshima, H., Fox, B. A., Le Trong, I., Teller, D. C., Okada, T., Stenkamp, R. E., Yamamoto, M., and Miyano, M., 2000. Crystal structure of rhodopsin: a G protein-coupled receptor. Science v. 289 p. 739–745. Wall, M. A., Coleman, D. E., Lee, E., Iniguez- Lluhi, J. A., Posner, B. A., Gilman, A. G., and Sprang, S. R., 1995. The structure of the G protein heterotrimer G i1 1 2 . Cell v. 83 p. 1047–1058. 14.23 Small, monomeric GTP-binding proteins are multiuse switches Review Bishop, A. L. and Hall, A., 2000. Rho GTPases and their effector proteins. Biochem. J. v. 348 pt. 2 p. 241–255. Kuersten, S., Ohno, M., and Mattaj, I. W., 2001. Nucleocytoplasmic transport: Ran, beta and beyond. Trends Cell Biol. v. 11 p. 497–503. Takai, Y., Sasaki, T., and Matozaki, T., 2001. Small GTP-binding proteins. Physiol. Rev. v. 81 p. 153–208. 14.24 Protein phosphorylation/dephosphorylation is a major regulatory mechanism in the cell Review Cohen, S., 1983. The epidermal growth factor (EGF). Cancer v. 51 p. 1787–1791. Fischer, E. H., 1997. “Protein phosphorylation and cellular regulation, II,” in Nobel Lectures, Physiology or Medicine 1991–1995, N., Ringertz, Ed., Singapore: World Scientific Publishing Co. Krebs, G., 1993. Protein phosphorylation and cellular regulation. Bioscience Reports v. 13 p. 127–142. Manning, G., Whyte, D. B., Martinez, R., Hunter, T., and Sudarsanam, S., 2002. The protein kinase complement of the human genome. Science v. 298 p. 1912–1934. Newton, A. C., 2003. Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm. Biochem. J. v. 370 p. 361–371. Nolen, B., Taylor, S., and Ghosh, G., 2004. Regulation of protein kinases; controlling activity through activation segment conformation. Mol. Cell v. 15 p. 661–675. Turk, B. E. and Cantley, L. C., 2003. Peptide libraries: at the crossroads of proteomics and bioinformatics. Curr. Opin. Chem. Biol. v. 7 p. 84–90. Research Canagarajah, B. J., Khokhlatchev, A., Cobb, M. H., and Goldsmith, E. J., 1997. Activation mechanism of the MAP kinase ERK2 by dual phosphorylation. Cell v. 90 p. 859–869. Ginty, D. D., Kornhauser, J. M., Thompson, 640 CHAPTER 14 Principles of cell signaling
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