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Cheney

J S, I Morize, P R Menard, D L Cheney, C Hulme and R F Labaudiniere 1999. New 4-Point irmacophore Method for Molecular Similarity and Diversity Applications Overview of the thod and Applications, Including a Novel Approach to the Design of Combinatorial iraries Containing Privileged Substructures. Journal of Medicinal Chemistry 42 3251-3264. [Pg.740]

Another dynamic iastmment, the Scentometer, is the basis for odor regulations ia the states of Colorado, Illinois, Kentucky, Missouri, Nevada, and Wyoming, and ia the District of Columbia (324). The portable Scentometer (Bameby-Cheney) can produce dilution ratios up to 128 1 ia the field. The Scentometer blends two air streams, one of which has been deodorized with activated carbon. The dilution ratio is decreased until the odor becomes detectable (325). Improvements to dynamic methods have been recommended (326). [Pg.412]

J. A. Cheney, private communication, Airco Industrial Gases Division, Murray Hik, N.J., 1983. [Pg.19]

Cheney, E. W., and D. Kincaid. Numetical Mathematics and Computing, Brooks/Cole, Monlerey, CA (1980). [Pg.422]

The crude base is purified by converting 2g of base in toluene (3.3mL) into the acetate salt by heating at 65-70 with 0.46g of AcOH and the crystals are collected and dried (0.96g from two crops m 141-143 ). The acetate salt is dissolved in warm H2O, basified with aqueous NaOH and extracted with C6H6. The dried extract (MgS04) is evaporated in vacuum leaving a viscous oil which crystallises and can be distd. [Gottstein and Cheney J Org Chem 30 2072 1965.] The picrate has m 234-236 (from aq MeOH), and the formate has m 147-148° (from heptane). [Pg.185]

Figure 1. An unrooted phylogenetic tree of the myosins based on the amino acid sequence comparison of their head domains demonstrating the division of the myosin superfamily into nine classes. The lengths of the branches are proportional to the percent of amino acid sequence divergence and a calibration bar for 5% sequence divergence is shovk n. The different classes of myosins have been numbered using Roman numerals in rough order of their discovery and hypothetical models of the different myosin structures are shown. Question marks indicate either hypothetical or unknown structural features, and only a fraction of the known myosins are shown. (Taken, in modified form, from Cheney et al., 1993). Figure 1. An unrooted phylogenetic tree of the myosins based on the amino acid sequence comparison of their head domains demonstrating the division of the myosin superfamily into nine classes. The lengths of the branches are proportional to the percent of amino acid sequence divergence and a calibration bar for 5% sequence divergence is shovk n. The different classes of myosins have been numbered using Roman numerals in rough order of their discovery and hypothetical models of the different myosin structures are shown. Question marks indicate either hypothetical or unknown structural features, and only a fraction of the known myosins are shown. (Taken, in modified form, from Cheney et al., 1993).
The myosin-II group can be divided into two groups derived from striated muscle and non-muscle/smooth muscle (Cheney et al., 1993). The striated muscle subgroup can be further divided into the forms found in skeletal and cardiac muscles. The myosins from striated and cardiac muscles have different biochemical... [Pg.62]

Nonmuscle/smooth muscle myosins-Il are structurally similar to striated muscle myosin-II, but they have slower rates of ATP hydrolysis than do their striated muscle counterparts. Nonmuscle/smooth muscle myosin-II is also regulated differently than striated muscle myosin-II. Nonmuscle myosin-II is divided into the invertebrate and vertebrate branches (Cheney et al., 1993). This group is ubiquitous because it is present in most lower organisms, such as slime molds, amoeba, sea urchins, etc., and in virtually all mammalian nonmuscle cells. Smooth muscle myosin-II is also somewhat heterogeneous in that at least three separate forms of smooth muscle heavy chains, with molecular weights of 196,000, 200,000, and 204,000 have been identified (Kawamoto and Adelstein, 1987). The physiological properties of these separate myosin heavy chains are not yet known. [Pg.63]

Myosin-I molecules have several IQ sequences on or near the head and have light chains associated with them (Cheney and Mooseker, 1992 Cheney et al., 1993). Frequently, the light chains appear to be calmodulin molecules and some myosin-I molecules can bind three to four molecules of calmodulin at one time. Brush-border and adrenal myosin-I also bind calmodulin. Acanthamoeba myosin-I has a light chain that can be removed, in vitro, without adversely affecting the ATPase activity or the heavy chain phosphorylation (Korn and Hammer, 1988). The role of these calmodulin molecules in regulating myosin-I is complex and poorly understood. One possibility is that the calmodulin molecules dissociate from the heavy chains when calcium binds to the calmodulin, thereby imparting greater flexibility to the head of the myosin-I molecules. [Pg.70]

Chandler, V. Cheney, P. Thomas, P. Trabaud, L Williams, D. Forest Fire Management and Organization Fire in Forestry John Wiley Sons New York, NY, 1983 Vol. II. [Pg.455]

McPhaden, M. J., Busalacchi, A. J., Cheney, R. et al. (1998). The tropical ocean-global atmosphere observing system A decade of progress. /. Geophys. Res. 103,14169-14240. [Pg.277]

Mason JS, Morize 1, Menard PR, Cheney DL, Hulme C, Labaudiniere RF. New 4-point pharmacophore method for molecular similarity and diversity applications Overview of the method and applications, including a novel approach to the design of combinatorial libraries containing privileged substructures. I Med Chem 1999 42 3251-64. [Pg.207]


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See also in sourсe #XX -- [ Pg.377 , Pg.388 , Pg.392 ]




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