978 resultados para Halifax, George Savile, Marquis of, 1633-1695.


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Works, and Appendix of attributed works: v. 2, p. 269-541.

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Forms part of the Royal historical society's Publications, Camden third series, vol.XIII.

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Mode of access: Internet.

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Mode of access: Internet.

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Vols. 1 and 3 edited by J. J. Cartwright and J. M. Rigg; v. 2, by Mrs. S. C. Lomas; v. 4, by Marjorie Blatcher; v. 5, by G. Dyfnallt Owen.

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Letter to George Rykert (president of the Port Dalhousie and Thorold Railway), engineer from William Danforth, civil engineer in which he states that the preliminary survey has been made between Port Dalhousie and Centreville at which point it may intersect with the Great Western Railway. The estimate is included (2 pages, handwritten), July 25, 1853.

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Indenture of Bargain and Sale (vellum) between Captain George Salmon, formerly of Upper Canada and now of Middlesex, England and Charles Hampden Turner of Surrey, England for 1,200 acres lying in the Township of Windham in the County of Norfolk in the province of Upper Canada, May 5, 1819.

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Resumen: Descripción: retrato de niño de tres cuartos de figura mirando de frente

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myr 5 is an unconventional myosin (class IX) from rat that contains a Rho-family GTPase-activating protein (GAP) domain. Herein we addressed the specificity of the myr 5 GAP activity, the molecular mechanism by which GAPs activate GTP hydrolysis, the consequences of myr 5 overexpression in living cells, and its subcellular localization. The myr 5 GAP activity exhibits a high specificity for Rho. To achieve similar rates of GTPase activation for RhoA, Cdc42Hs, and Rac1, a 100-fold or 1000-fold higher concentration of recombinant myr 5 GAP domain was needed for Cdc42Hs or Rac1, respectively, as compared with RhoA. Cell lysates from Sf9 insect cells infected with recombinant baculovirus encoding myr 5 exhibited increased GAP activity for RhoA but not for Cdc42Hs or Rac1. Analysis of Rho-family GAP domain sequences for conserved arginine residues that might contribute to accelerate GTP hydrolysis revealed a single conserved arginine residue. Mutation of the corresponding arginine residue in the myr 5 GAP domain to a methionine (M1695) virtually abolished Rho-GAP activity. Expression of myr 5 in Sf9 insect cells induced the formation of numerous long thin processes containing occasional varicosities. Such morphological changes were dependent on the myr 5 Rho-GAP activity, because they were induced by expressing the myr 5 tail or just the myr 5 Rho-GAP domain but not by expressing the myr 5 myosin domain. Expression of myr 5 in mammalian normal rat kidney (NRK) or HtTA-1 HeLa cells induced a loss of actin stress fibers and focal contacts with concomitant morphological changes and rounding up of the cells. Similar morphological changes were observed in HtTA-1 HeLa cells expressing just the myr 5 Rho-GAP domain but not in cells expressing myr 5 M1695. These morphological changes induced by myr 5 were inhibited by coexpression of RhoV14, which is defective in GTP hydrolysis, but not by RhoI117. myr 5 was localized in dynamic regions of the cell periphery, in the perinuclear region in the Golgi area, along stress fibers, and in the cytosol. These results demonstrate that myr 5 has in vitro and in vivo Rho-GAP activity. No evidence for a Rho effector function of the myr 5 myosin domain was obtained.