Matching Items (761)
ContributorsWard, Geoffrey Harris (Performer) / ASU Library. Music Library (Publisher)
Created2018-03-18
Description
The end of the nineteenth century was an exhilarating and revolutionary era for the flute. This period is the Second Golden Age of the flute, when players and teachers associated with the Paris Conservatory developed what would be considered the birth of the modern flute school. In addition, the founding in 1871 of the Société Nationale de Musique by Camille Saint-Saëns (1835-1921) and Romain Bussine (1830-1899) made possible the promotion of contemporary French composers. The founding of the Société des Instruments à Vent by Paul Taffanel (1844-1908) in 1879 also invigorated a new era of chamber music for wind instruments. Within this groundbreaking environment, Mélanie Hélène Bonis (pen name Mel Bonis) entered the Paris Conservatory in 1876, under the tutelage of César Franck (1822-1890). Many flutists are dismayed by the scarcity of repertoire for the instrument in the Romantic and post-Romantic traditions; they make up for this absence by borrowing the violin sonatas of Gabriel Fauré (1845-1924) and Franck. The flute and piano works of Mel Bonis help to fill this void with music composed originally for flute. Bonis was a prolific composer with over 300 works to her credit, but her works for flute and piano have not been researched or professionally recorded in the United States before the present study. Although virtually unknown today in the American flute community, Bonis's music received much acclaim from her contemporaries and deserves a prominent place in the flutist's repertoire. After a brief biographical introduction, this document examines Mel Bonis's musical style and describes in detail her six works for flute and piano while also offering performance suggestions.
ContributorsDaum, Jenna Elyse (Author) / Buck, Elizabeth (Thesis advisor) / Holbrook, Amy (Committee member) / Micklich, Albie (Committee member) / Schuring, Martin (Committee member) / Norton, Kay (Committee member) / Arizona State University (Publisher)
Created2013
ContributorsMatthews, Eyona (Performer) / Yoo, Katie Jihye (Performer) / Roubison, Ryan (Performer) / ASU Library. Music Library (Publisher)
Created2018-03-25
ContributorsHoeckley, Stephanie (Performer) / Lee, Juhyun (Performer) / ASU Library. Music Library (Publisher)
Created2018-03-24
ContributorsMcClain, Katelyn (Performer) / Buringrud, Deanna (Contributor) / Lee, Juhyun (Performer) / ASU Library. Music Library (Publisher)
Created2018-03-31
ContributorsHur, Jiyoun (Performer) / Lee, Juhyun (Performer) / ASU Library. Music Library (Publisher)
Created2018-03-01
ContributorsBolari, John (Performer) / ASU Library. Music Library (Publisher)
Created2018-10-04
Description
AMPylation is a post-translation modification that has an important role in the survival of many bacterial pathogens by affecting the host cell's molecular signaling. In the course of studying this intercellular manipulation, there has only been modest progression in the identification of the enzymes with AMPylation capabilities (AMPylators) and their respective targets. The reason for these minimal developments is the inability to analyze a large subset of these proteins. Therefore, to increase the efficiency of the identification and characterization of the proteins, Yu et al developed a high-throughput non-radioactive discovery platform using Human Nucleic Acid Programmable Protein Arrays (NAPPA) and a validation platform using bead-based assays. The large-scale unbiased screening of potential substrates for two bacterial AMPylators containing Fic domain, VopS and IbpAFic2, had been performed and dozens of novel substrates were identified and confirmed. With the efficiency of this method, the platform was extended to the identification of novel substrates for a Legionella virulence factor, SidM, containing a different adenylyl transferase domain. The screening was performed using NAPPA arrays comprising of 10,000 human proteins, the active AMPylator SidM, and its inactive D110/112A mutant as a negative control. Many potential substrates of SidM were found, including Rab GTPases and non-GTPase proteins. Several of which have been confirmed with the bead-based AMPylation assays.
ContributorsGraves, Morgan C. (Author) / LaBaer, Joshua (Thesis director) / Qiu, Ji (Committee member) / Yu, Xiaobo (Committee member) / Barrett, The Honors College (Contributor) / Department of Chemistry and Biochemistry (Contributor)
Created2013-05
ContributorsOftedahl, Paul (Performer) / ASU Library. Music Library (Publisher)
Created2018-09-29
ContributorsZaleski, Kimberly (Contributor) / Kazarian, Trevor (Performer) / Ryan, Russell (Performer) / IN2ATIVE (Performer) / ASU Library. Music Library (Publisher)
Created2018-09-28