197,770 research outputs found
Letter from M. E. Trapp to Senator Josh Lee, dated June 7, 1937
No full textLetter from M. E. Trapp to Senator Josh Lee, dated June 7, 1937, defending and praising Cyrus Avery's work through the WPA.The Cyrus S. Avery Collection chronicles the life and times of Cyrus Stevens Avery. Known as the 'Father of Route 66', Avery served in government positions and elected offices as well as in highway associations that led him to have an influential impact on the planning and development of the initial American highway system. Through Avery's involvement with the City of Tulsa, Oklahoma and his own agricultural interests, the collection also documents a growing city and its' rural life in the early twentieth century
Marth Trapp, MSU M Club President, Senator John C. Stennis, Coy Hines Stennis, and Hank Mosley
No full textMarth Trapp, MSU M Club President, Senator John C. Stennis, Coy Hines Stennis, and Hank Mosley at MSU Alumni Association eventhttps://scholarsjunction.msstate.edu/ua-photo-collection/10135/thumbnail.jp
M. H. Crawford, C.R. Ligota and J.B. Trapp, Medals and Coins from Budé to Mommsen.
No full textGerin Dominique. M. H. Crawford, C.R. Ligota and J.B. Trapp, Medals and Coins from Budé to Mommsen.. In: Revue numismatique, 6e série - Tome 151, année 1996 pp. 380-386
“A hora das crianças: Narrativas radiofônicas de Walter Benjamin”, de Walter Benjamin, traducción de Aldo Medeiros
No full textReseña por Caroline Trapp de Queiro
“A hora das crianças: Narrativas radiofônicas de Walter Benjamin”, de Walter Benjamin, tradução de Aldo Medeiros
No full textResenha por Caroline Trapp de Queiro
The TRAPP Complex: Insights into its Architecture and Function
No full textVesicle-mediated transport is a process carried out by virtually every cell and is required for the proper targeting and secretion of proteins. As such, there are numerous players involved to ensure that the proteins are properly localized. Overall, transport requires vesicle budding, recognition of the vesicle by the target membrane and fusion of the vesicle with the target membrane resulting in delivery of its contents. The initial interaction between the vesicle and the target membrane has been referred to as tethering. Because this is the first contact between the two membranes, tethering is critical to ensuring that specificity is achieved. It is therefore not surprising that there are numerous 'tethering factors' involved ranging from multisubunit complexes, coiled-coil proteins and Rab guanosine triphosphatases. Of the multisubunit tethering complexes, one of the best studied at the molecular level is the evolutionarily conserved TRAPP complex. There are two forms of this complex: TRAPP I and TRAPP II. In yeast, these complexes function in a number of processes including endoplasmic reticulum-to-Golgi transport (TRAPP I) and an ill-defined step at the trans Golgi (TRAPP II). Because the complex was first reported in 1998 , there has been a decade of studies that have clarified some aspects of its function but have also raised further questions. In this review, we will discuss recent advances in our understanding of yeast and mammalian TRAPP at the structural and functional levels and its role in disease while trying to resolve some apparent discrepancies and highlighting areas for future study.X116979sciescopu
Crystal structure of bet3 reveals a novel mechanism for Golgi localization of tethering factor TRAPP
No full textTransport protein particle (TRAPP) is a large multiprotein complex involved in endoplasmic reticulum-to-Golgi and intra-Golgi traffic. TRAPP specifically and persistently resides on Golgi membranes. Neither the mechanism of the subcellular localization nor the function of any of the individual TRAPP components is known. Here, the crystal structure of mouse Bet3p (bet3), a conserved TRAPP component, reveals a dimeric structure with hydrophobic channels. The channel entrances are located on a putative membrane-interacting surface that is distinctively flat, wide and decorated with positively charged residues. Charge-inversion mutations on the flat surface of the highly conserved yeast Bet3p led to conditional lethality, incorrect localization and membrane trafficking defects. A channel-blocking mutation led to similar defects. These data delineate a molecular mechanism of Golgi-specific targeting and anchoring of Bet3p involving the charged surface and insertion of a Golgi-specific hydrophobic moiety into the channels. This essential subunit could then direct other TRAPP components to the Golgi.X114340sciescopu
THE DYNAMICS OF FEEDER CATTLE MARKET RESPONSES TO CORN PRICE CHANGE
No full textA feeder-calf price model is estimated which incorporates elements of break-even budget analysis, including estimates of placement weights, slaughter weights, ration cost, and feed-conversion rates. From this model, a corn price multiplier is calculated which quantifies the corn/feeder-calf price relationship. Because the multiplier includes information on cattle weight, feed conversion, and ration cost, it also provides insight into how feeding programs are altered in response to corn price changes. Changes in feeding programs which occur in response to corn price changes are illustrated with dynamic simulation based on weight, ration cost, and price models presented here.corn, corn price multiplier, dynamic simulation, feeder cattle, Demand and Price Analysis,
Mutational analysis of the yeast TRAPP subunit Trs20p identifies roles in endocytic recycling and sporulation
No full textTrs20p is a subunit of the evolutionarily conserved TRAPP (TRAnsport Protein Particle) complex that mediates various aspects of membrane trafficking. Three TRAPP complexes have been identified in yeast with roles in ER-to-Golgi trafficking, post-Golgi and endosomal-to-Golgi transport and in autophagy. The role of Trs20p, which is essential for viability and a component of all three complexes, and how it might function within each TRAPP complex, has not been clarified to date. To begin to address the role of Trs20p we generated different mutants by random mutagenesis but, surprisingly, no defects were observed in diverse anterograde transport pathways or general secretion in Trs20 temperature-sensitive mutants. Instead, mutation of Trs20 led to defects in endocytic recycling and a block in sporulation/meiosis. The phenotypes of different mutants appear to be separable suggesting that the mutations affect the function of Trs20 in different TRAPP complexes
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