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Eukaryotic receptors

Sinclair, J. F., and O Brien, A. D. (2002). Cell surface-localized nucleolin is a eukaryotic receptor for the adhesin intimin-gamma of enterohemorrhagic Escherichia coli 0157 H7. [Pg.157]

Kim, K.-P., Jagadeesan, B., Burkholder, K. M., Jaradat, Z. W., Wampler, J. L., Lathrop, A. A., Morgan, M. T., and Bhunia, A. K. (2006a). Adhesion characteristics of Listeria adhesion protein (LAP)-expressing Escherichia coli to Caco-2 cells and of recombinant LAP to eukaryotic receptor Flsp60 as examined in a surface plasmon resonance sensor. FEMS Microbiol. Lett. 256,324-332. [Pg.38]

The genome contains about 1500 genes, 300 of which encode membrane proteins, many with as yet unknown functions [15]. The sequences encoding for membrane proteins comprise genes such as the FiFq ATP synthase complex and various oxido-reductases such as cytochrome o, several transporters and a variety of two-component signaling systems (the equivalent of eukaryotic receptors). Some of the recognized transporters are illustrated in Figure 2. [Pg.120]

Figure S.21 The hemaggiutinin moiecuie is formed from three subunits. Each of these subunits Is anchored In the membrane of the influenza vims. The globular heads contain the receptor sites that bind to sialic acid residues on the surface of eukaryotic cells. A major part of the subunit interface is formed by the three long intertwining helices, one from each subunit. (Adapted from I. Wilson et al.. Nature 289 366-373, 1981.)... Figure S.21 The hemaggiutinin moiecuie is formed from three subunits. Each of these subunits Is anchored In the membrane of the influenza vims. The globular heads contain the receptor sites that bind to sialic acid residues on the surface of eukaryotic cells. A major part of the subunit interface is formed by the three long intertwining helices, one from each subunit. (Adapted from I. Wilson et al.. Nature 289 366-373, 1981.)...
In cyclic nucleotide-regulated channels, this domain serves as a high-affinity binding site for 3-5 cyclic monophosphates. The CNBD of channels has a significant sequence similarity to the CNBD of most other classes of eukaryotic cyclic nucleotide receptors and to the CNBD of the prokaryotic catabolite activator protein (CAP). The primary sequence of CNBDs consists of approximately 120 amino acid residues forming three a-helices (oA-aC) and eight (3-strands ( 31- 38). [Pg.399]

Ono Y, Fujibuchi W, Suwa M. Automatic gene collection system for genome-scale overview of G-protein coupled receptors in eukaryotes. Gene 2005 364 63-73. [Pg.48]

Gentz, R., Hayes, A., Grau, N. et al. (1992) Analysis of soluble human and mouse interferon-gamma receptors expressed in eukaryotic cells. European Journal of Biochemistry, 210 (2), 545-554. [Pg.58]

Figure 7.4 (a) IREs in eukaryotic mRNAs the secondary structures of ferritin and transferrin receptor IREs. (b) The IRE localization in mRNAs the translation/ribosome binding element in the 5 -UTR of ferritin mRNA is above, that of the stability/ turnover element in the 3 -UTR of transferrin receptor mRNA is below. Adapted from Theil, 1998, by courtesy of Marcel Dekker, Inc. [Pg.217]


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