954 resultados para Bible Association of Friends in America


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General note: Title and date provided by Bettye Lane.

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The Catherwood Library, which serves Cornell's School of Industrial and Labor Relations, houses a complete set of the studies either published by or produced under the auspices of the Work in America Institute, Inc. These volumes were donated to the Catherwood Library by the Institute's Board of Directors through the initiative of Jay W. Waks, ILR '68, who succeeded Mr. Rosow as Chair of the Institute and who, for many years, sat on the Institute's Executive Committee with Mr. Rosow and Thomas R. Donahue, former Secretary-Treasurer and Interim President of the AFL-CIO. Each volume bears a bookplate with this message: "This volume was donated by the Work in America Institute, Inc. in honor of its founder, Jerome M. Rosow, 1919-2002." For additional information or to check on the availability of a document, please contact the Reference Department at 607-255-2277 or email us at ilrref@cornell.edu.

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The purpose of this document is to provide a single source of reference for every paper published in the journals directly related to research in Construction Management. It is indexed by author and keyword and contains the titles, authors, abstracts and keywords of every article from the following journals: • Building Research and Information (BRI) • Construction Management and Economics (CME) • Engineering, Construction and Architectural Management (ECAM) • Journal of Construction Procurement (JCP) • Journal of Construction Research (JCR) • Journal of Financial Management in Property and Construction (JFM) • RICS Research Papers (RICS) The index entries give short forms of the bibliographical citations, rather than page numbers, to enable annual updates to the abstracts. Each annual update will carry cumulative indexes, so that only one index needs to be consulted.

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The purpose of this document is to provide a single source of reference for every paper published in the journals directly related to research in Construction Management. This volume brings together articles published during 1999. It is indexed by author and keyword and contains the titles, authors, abstracts and keywords of every article from the following journals: • Building Research and Information (BRI) • Construction Management and Economics (CME) • Engineering, Construction and Architectural Management (ECAM) • Journal of Construction Procurement (JCP) • RICS Research Papers (RICS) The index entries give short forms of the bibliographical citations, rather than page numbers, to enable rapid reference to articles. A cumulative volume is available from the editor. Included in this volume is an appendix listing a wide range of journals associated with construction management research, giving details of frequency, editorial addresses and web sites, as well as whether each journal is international and/or refereed.

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Two radiolarian assemblages are distinguished: an equatorial sub-assemblage of the tropical assemblage in the East Pacific Ocean, which differs somewhat from association of radiolarians in the western part of the ocean, and an assemblage close to transitional one between the tropical and the boreal. The latter is characterized by presence of considerable number of species typical for cold-water regions. Some criteria are presented for distinguishing radiolarian associations in nearshore regions from similar associations in regions of the open ocean.

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In natural streptavidin, tryptophan 120 of each subunit makes contacts with the biotin bound by an adjacent subunit through the dimer-dimer interface. To understand quantitatively the role of tryptophan 120 and its intersubunit communication in the properties of streptavidin, a streptavidin mutant in which tryptophan 120 is converted to phenylalanine was produced and characterized. The streptavidin mutant forms a tetrameric molecule and binds one biotin per subunit, as does natural streptavidin, indicating that the mutation of tryptophan 120 to phenylalanine has no significant effect on the basic properties of streptavidin. However, its biotin-binding affinity was reduced substantially, to approximately 10(8) M-1, indicating that the contact made by tryptophan 120 to biotin has a considerable contribution to the extremely tight biotin binding by streptavidin. The mutant retained bound biotin over a wide pH range or with the addition of urea up to 6 M at neutral pH. However, bound biotin was efficiently released by the addition of excess free biotin due, presumably, to exchange reactions. Electrophoretic analysis revealed that the intersubunit contact made by tryptophan 120 to biotin through the dimer-dimer interface is the major interaction responsible for the biotin-induced, tighter subunit association of streptavidin. In addition, the mutant has weaker subunit association than natural streptavidin even in the absence of biotin, indicating that tryptophan 120 also contributes to the subunit association of tetramers in the absence of biotin.

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by Josephine A. Roche.

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Concerns a bill providing for the division of church property between traditional Friends and the Hicksite faction of Friends.

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Elevated levels of the calcium-binding protein S100A4 promote metastasis and in carcinoma cells are associated with reduced survival of cancer patients. S100A4 interacts with target proteins that affect a number of activities associated with metastatic cells. However, it is not known how many of these interactions are required for S100A4-promoted metastasis, thus hampering the design of specific inhibitors of S100A4-induced metastasis. Intracellular S100A4 exists as a homodimer through previously identified, well conserved, predominantly hydrophobic key contacts between the subunits. Here it is shown that mutating just one key residue, phenylalanine 72, to alanine is sufficient to reduce the metastasis-promoting activity of S100A4 to 50% that of the wild type protein, and just 2 or 3 specific mutations reduces the metastasis-promoting activity of S100A4 to less than 20% that of the wild type protein. These mutations inhibit the self-association of S100A4 in vivo and reduce markedly the affinity of S100A4 for at least two of its protein targets, a recombinant fragment of non-muscle myosin heavy chain isoform A, and p53. Inhibition of the self-association of S100 proteins might be a novel means of inhibiting their metastasis-promoting activities.

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General note: Title and date provided by Bettye Lane.

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Inscriptions: Verso: [stamped] Credit must be given to Freda Leinwand from Monkmeyer Press Photo Service.