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scale The alternative is to accept that empirical evidence has shown the physical reasoning concluding stationarity to be invalid If, on the other hand, the scaling was concentrated at the lowest scales (high frequencies), that is, j1 1 with some upper cutoff j2 , then the scaling may best be understood as indicating the fractal nature of the sample path The observed a should then be reexpressed as h a 1 =2, the local regularity parameter Values of h in the range (0, 1], for example, would then be interpreted as indicating continuous but nondifferentiable sample paths (under Gaussian assumptions [28]), as observed in the leftmost alignment region in the Internet delay data in the left plot in Fig 24 The stationarity or otherwise of the data in such a case may then not be relevant.

Exposure of juvenile insects to methoprene results in various abnormalities associated with development and ultimately death. The environmental degradation product of methoprene, methoprenic acid was found to serve as an RXR agonist and speci cally activate genes responsive to RXR homodimers. In addition exposure of frog larvae to methoprenic acid caused developmental deformities consistent with those that have been observed in recent years in wild populations and consistent with those caused by exposure to retinoic acid under laboratory conditions. These observations indicate that methoprenic acid functions as an RXR agonist, and that this activity could contribute to the occurrence of amphibians deformities documented in the environment.

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83 Nanduri, S; Carpick, B W; Yang, Y; Williams, B R G; Qin, J Structure of the doublestranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation EMBO J 1998, 17, 5458 5465 84 Bycroft, M; Grunert, S; Murzin, A G; Proctor, M; St Johnston, D NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5 EMBO J 1995, 14, 3563 3571 85 Doyle, M; Jantsch, M F New and old roles of the double-stranded RNA-binding domain J Struct Biol 2002, 140(1 3), 147 53 86 Wu, H; Henras, A; Chanfreau, G; Feigon, J Structural basis for recognition of the AGNN tetraloop RNA fold by the double-stranded RNA-binding domain of Rnt1p RNase III Proc Natl Acad Sci.

Note that j 1 has been excluded from the leftmost alignment region in each plot in Fig 24 This is not in contradiction with interpretations of fractality, as it is known that the details at j 1 can be considerably polluted due to errors in the initialization of the multiresolution algorithm (see Section 2214) If scaling with a > 1 is found over all or almost all of the scales in the data, such as in the right-hand plot in Fig 22, then exact self-similarity could be chosen as a model, again with H a 1 =2 being the relevant exponent However, in this case one could equally well use the local regularity parameter h a 1 =2, with the interpretation that the fractal behavior at small scales is constant over time and happens to extend right up to the largest scales in the data.

While the estrogen receptor appears somewhat unique among vertebrate nuclear hormone receptors in its promiscuity toward receptor agonists, many nuclear hormone receptors have been shown to be susceptible to chemical antagonism. Receptor antagonists are de ned as chemicals that bind to a hormone receptor but do not activate the receptor. Rather, these chemicals inhibit receptor activity by preventing the endogenous hormone from binding to and activating the receptor.

Finally, more than one alignment region is certainly possible within a single logscale diagram, a phenomenon that we refer to as biscaling One could imagine, for example, fractal characteristics leading to an alignment at small scales with one exponent, and long-range dependence resulting in alignment at large scales with a separate scaling exponent Examples of this phenomenon are shown in Fig 24 in.

USA 2004, 101, 8307 8312 87 Bevilacgua, P C; Cech, T R Minor-groove recognition of double-stranded RNA by the double-stranded RNA-binding domain from the RNA-activated protein kinase PKR Biochemistry 1996, 35(31), 9983 9994 88 Ryter, N M; Schultz, S C Molecular basis of double-stranded RNA-protein interactions: structure of a dsRNA-binding domain complexed with dsRNA EMBO J 1998, 17(24), 7505 7513 89 Ramos, A; Bayer, P; Varani, G Determination of the structure of the RNA complex of a double-stranded RNA-binding domain from Drosophila staufen protein Biopolymers 2001, 52, 181 196 90 Fierro-Monti, I; Mathews, M B Proteins binding to duplexed RNA: one motif, multiple functions TIBS 2000, 25, 241 246 91 Rosenthal, S R; Merchlinsky, M; LKleppinger C; Goldenthal K L Developing New Smallpox Vaccines 2001 http://wwwcdcgov/ncidod/EID/eidhtm 92 Carroll, M W; Moss, B.

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