The long-term objective of the Scientific Core is to provide outstanding, state-of-the-art, cost-effective Core facilities and services that support all five projects of the Program. Core B is composed of a protein expression and purification facility, as well as other shared facilities including a darkroom, Phosphorlmager, ultracentrifuge, and liquid nitrogen freezers. The Core will also support the generation of retroviruses expressing variou~ shRNAs and microarray analysis of miRNA expression. The Phosphorlmager will be used for imaging and quantification of various results including primerextension assays, gel mobility shifts, and Westem blots. The protein expression and purification facility consists of a shaking incubator, a centrifuge, an FPLC, and protein expression vectors. It is used to express and purify proteins that are studied in each of the projects. In a new service, the Core will also generate shRNA constructs for the various projects. This will include design of shRNAs that target specific genes, cloning the inserts into retrovirus vectors, and generation of high-titer retrovirus stocks. The Core will also support the use of a Taqman microRNA microarray set-up by purchasing cassettes for the analysis. An Amaxa Nucleofector transfection apparatus will also be purchased for use by the projects. The Core also possesses liquid nitrogen freezers for the storage of cell lines and a gel documentation system. In addition, expertise is provided to all member laboratories by personnel who oversee the Core. This Scientific Core is essential to the success of the Program, and facilitates interaction between member laboratories.
This interdisciplinary Program consists of five projects using diverse, state-of-the-art approaches. However, several projects use the same technologies, which are most efficiently provided in a cost-effective manner by staff with specialized expertise. This Core will provide these scientific services to all of the projects.
|Zhang, Pengwei; Monteiro da Silva, Gabriel; Deatherage, Catherine et al. (2018) Cell-Penetrating Peptide Mediates Intracellular Membrane Passage of Human Papillomavirus L2 Protein to Trigger Retrograde Trafficking. Cell 174:1465-1476.e13|
|Inoue, Takamasa; Zhang, Pengwei; Zhang, Wei et al. (2018) ?-Secretase promotes membrane insertion of the human papillomavirus L2 capsid protein during virus infection. J Cell Biol 217:3545-3559|
|Vallery, Tenaya K; Withers, Johanna B; Andoh, Joana A et al. (2018) Kaposi's Sarcoma-Associated Herpesvirus mRNA Accumulation in Nuclear Foci Is Influenced by Viral DNA Replication and Viral Noncoding Polyadenylated Nuclear RNA. J Virol 92:|
|Hayes, Karen E; Barr, Jamie A; Xie, Mingyi et al. (2018) Immunoprecipitation of Tri-methylated Capped RNA. Bio Protoc 8:|
|Park, Richard; Miller, George (2018) Epstein-Barr Virus-Induced Nodules on Viral Replication Compartments Contain RNA Processing Proteins and a Viral Long Noncoding RNA. J Virol 92:|
|Lipovsky, Alex; Erden, Asu; Kanaya, Eriko et al. (2017) The cellular endosomal protein stannin inhibits intracellular trafficking of human papillomavirus during virus entry. J Gen Virol 98:2821-2836|
|Singh, Gatikrushna; Fritz, Sarah M; Ranji, Arnaz et al. (2017) Isolation of Cognate RNA-protein Complexes from Cells Using Oligonucleotide-directed Elution. J Vis Exp :|
|Martinez, Ivan; Hayes, Karen E; Barr, Jamie A et al. (2017) An Exportin-1-dependent microRNA biogenesis pathway during human cell quiescence. Proc Natl Acad Sci U S A 114:E4961-E4970|
|Pawlica, Paulina; Moss, Walter N; Steitz, Joan A (2016) Host miRNA degradation by Herpesvirus saimiri small nuclear RNA requires an unstructured interacting region. RNA 22:1181-9|
|Gorres, Kelly L; Daigle, Derek; Mohanram, Sudharshan et al. (2016) Valpromide Inhibits Lytic Cycle Reactivation of Epstein-Barr Virus. MBio 7:e00113|
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