879 resultados para Administrator belonging to the family


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"Errata": leaf at end.

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"Supplementary history and personnel of towns belonging to the colony of New Haven": p. [593]-732, 749-767.

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Mode of access: Internet.

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The university never owned McMillan Hall but it did serve the campus community. "For many years the Y.M.C.A. had rented Sackett & McMillan Halls on State Street three blocks north of the campus, from the Presbyterian Church, ...[source: Encyclopedic Survey, pl 1669]. The Y.M.C.A. moved into Lane Hall upon its opening in 1917.

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Includes biographical notice of Gen. William Whipple and the Whipple family.

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Includes index.

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We compared the costs incurred by families attending outpatient appointments at the Royal Children's Hospital (RCH) in Brisbane with those incurred by families who had a consultation via videoconference in their regional area. In each category 200 families were interviewed. The median time spent travelling for videoconferences was 30 min compared with 80 min for face-to-face appointments. Families interviewed in the outpatient department had travelled a median distance of 70 km, while those who had a videoconference at the local hospital had travelled only 20 km. It cost these families much more to attend an appointment at the RCH than to attend a videoconference. Ninety-six per cent of families (193) reported at least one of the following types of expense: 150 families had expenses related to parking (median A$10), 156 had fuel expenses (median A$10) and 122 reported costs related to meals purchased at the RCH (median A$10). Only 21 families who had their appointment via local videoconference reported any additional costs. Specialist appointments via videoconference were a more convenient and cheaper option for families living in regional areas of Queensland than the conventional method of attending outpatient appointments at the specialist hospital in Brisbane.

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Sorting nexins are a large family of proteins that contain the phosphoinositide-binding Phox homology (PX) domain. A number of sorting nexins are known to bind to PtdIns(3)P, which mediates their localization to membranes of the endocytic pathway. We show here that sorting nexin 5 (SNX5) can be recruited to two distinct membrane compartments. In non-stimulated cells, the PX domain was independently targeted to endosomal structures and colocalized with full-length SNX5. The membrane binding of the PX domain was inhibited by the PI 3-kinase inhibitor, wortmannin. Although SNX5 colocalized with a fluid-phase marker and was found predominantly within a PtdIns(3)P-rich endosomal domain, very little colocalization was observed between SNX5 and the PtdIns(3)P-binding protein, EEA1. Using liposome-based binding assays, we have shown that the PX domain of SNX5 interacts not only with PtdIns(3)P but also with PtdIns(3,4)P-2. In response to EGF stimulation, either the SNX5-PX domain or full-length SNX5 was rapidly recruited to the plasma membrane. The localization of SNX1, which does not bind PtdIns(3,4)P-2, was unaffected by EGF signalling. Therefore, SNX5 is localized to a subdomain of the early endosome distinct from EEA1 and, following EGF stimulation and elevation of PtdIns(3,4)P-2, is also transiently recruited to the plasma membrane. These results indicate that SNX5 may have functions not only associated with endosomal sorting but also with the phosphoinositide-signalling pathway.

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The cadherin superfamily members play an important role in mediating cell-cell contact and adhesion (Takeichi, M., 1991. Cadherin cell adhesion receptors as a morphogenetic regulator. Science 251, 1451-1455). A distinct subfamily, neither belonging to the classical or protocadherins includes Fat, the largest member of the cadherin super-family. Fat was originally identified in Drosophila. Subsequently, orthologues of Fat have been described in man (Dunne, J., Hanby, A. M., Poulsom, R., Jones, T. A., Sheer, D., Chin, W. G., Da, S. M., Zhao, Q., Beverley, P. C., Owen, M. J., 1995. Molecular cloning and tissue expression of FAT, the human homologue of the Drosophila fat gene that is located on chromosome 4q34-q35 and encodes a putative adhesion molecule. Genomics 30, 207-223), rat (Ponassi, M., Jacques, T. S., Ciani, L., ffrench, C. C., 1999. Expression of the rat homologue of the Drosophila fat tumour suppressor gene. Mech. Dev. 80, 207-212) and mouse (Cox, B., Hadjantonakis, A. K., Collins, J. E., Magee, A. I., 2000. Cloning and expression throughout mouse development of mfat 1, a homologue of the Drosophila tumour suppressor gene fat [In Process Citation]. Dev. Dyn. 217, 233-240). In Drosophila, Fat has been shown to play an important role in both planar cell polarity and cell boundary formation during development. In this study we describe the characterization of zebrafish Fat, the first non-mammalian, vertebrate Fat homologue to be identified. The Fat protein has 64% amino acid identity and 80% similarity to human FAT and an identical domain structure to other vertebrate Fat proteins. During embryogenesis fat mRNA is expressed in the developing brain, specialised epithelial surfaces the notochord, ears, eyes and digestive tract, a pattern similar but distinct to that found in mammals. (c) 2005 Elsevier B.V. All rights reserved.

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A key component of the venom of many Australian snakes belonging to the elapid family is a toxin that is structurally and functionally similar to that of the mammalian prothrombinase complex. In mammals, this complex is responsible for the cleavage of prothrombin to thrombin and is composed of factor Xa in association with its cofactors calcium, phospholipids, and factor Va. The snake prothrombin activators have been classified on the basis of their requirement for cofactors for activity. The two major subgroups described in Australian elapid snakes, groups C and D, are differentiated by their requirement for mammalian coagulation factor Va. In this study, we describe the cloning, characterization, and comparative analysis of the factor X- and factor V-like components of the prothrombin activators from the venom glands of snakes possessing either group C or D prothrombin activators. The overall domain arrangement in these proteins was highly conserved between all elapids and with the corresponding mammalian clotting factors. The deduced protein sequence for the factor X-like protease precursor, identified in elapids containing either group C or D prothrombin activators, demonstrated a remarkable degree of relatedness to each other (80%-97%). The factor V-like component of the prothrombin activator, present only in snakes containing group C complexes, also showed a very high degree of homology (96%-98%). Expression of both the factor X- and factor V-like proteins determined by immunoblotting provided an additional means of separating these two groups at the molecular level. The molecular phylogenetic analysis described here represents a new approach for distinguishing group C and D snake prothrombin activators and correlates well with previous classifications.

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The 40 life history, myological, and osteological characters that Tibbetts (1992) used in his study of the hemiramphids are evaluated for both saury genera (Cololabis and Scomberesox) to determine if the Scomberesocidae are more closely related to the Zenarchopteridae, to the needlefishes (Belonidae), or to the halfbeaks (Hemiramphidae) and flyingfishes (Exocoetidae). Data were analyzed using PAUP*, and eight equally parsimonious trees were found (70 steps, CI 0.814, RI 0.938). This analysis indicates that sauries are most closely related to needlefishes, supporting the historical concept of the superfamily Scomberesocoidea as a monophyletic assemblage. A caudal displacement of the origin of the retractor dorsalis muscle is a tentative additional synapomorphy for all four saury species. Zenarchopteridae is strongly supported as a valid family sister to the Scomberesocoidea (decay index = 19, bootstrap = 100). Resolution of the internal structure of the Belonidae and the Hemiramphidae requires the identification of additional characters and examination of a greater number of taxa.