Life Sciences Commons^™

Development Of High-Throughput Methods For Screening Venom Peptides, Tanya Napolitano

Dissertations, Theses, and Capstone Projects

Bioactive venom peptides are increasingly being explored as drug leads in pharmaceutical research because of their immense therapeutic potential, however there is a need to more efficiently screen and characterize these peptides to discover medicinal leads more quickly.1,2 The Holford lab has leveraged recent technological achievements in genomics, transcriptomics, and proteomics to produce a leap in the discovery of venom peptides from previously hard to characterize small and neglected venomous animals such as Terebridae, an understudied lineage of the Conoidea Superfamily.4, 5–7 With the rise of -omic technologies the floodgates have opened and venom researchers are awash with large datasets …

Sd2 Ptov1 Interactomics, Joshua Andersen

ScholarsArchive Data

PTOV1 interactome data

Sd1 14-3-3 Interactome For Ptov1 Manuscript, Joshua Andersen

ScholarsArchive Data

14-3-3 interactome

Sd1 14-3-3 Interactome For Ptov1 Manuscript, Joshua Andersen

ScholarsArchive Data

Excel data sheet of MS data from 14-3-3 interactomics

Mapping Ku70 Protein Interactions Using Proximity-Dependent Biotin Identification, Sanna Abbasi

Electronic Thesis and Dissertation Repository

The Ku heterodimer, composed of subunits Ku70 and Ku80, is a highly abundant protein complex, known for its affinity for double-stranded DNA ends. Accordingly, Ku is most well-studied for repairing double-stranded DNA breaks through the non-homologous end-joining (NHEJ) DNA repair pathway. Aside from NHEJ, Ku has also been implicated and studied in various other cellular processes including V(D)J recombination and telomere maintenance.

Numerous protein interactions have been mapped to the C-terminal region of Ku70, although few have been mapped to its N-terminal von Willebrand A-like (vWA) domain. Here, we used the high-throughput proteomic technique, proximity-dependent biotin identification (BioID, BioID2) to …

Uncovering The Ubiquitin Ligase Activity And Substrates Of The Human C-Terminal To Lish (Ctlh) Complex, Matthew E.R. Maitland

Electronic Thesis and Dissertation Repository

Ubiquitination is the transfer of a ubiquitin molecule to protein substrates by the sequential actions of E1 activating enzymes, E2 conjugating enzymes, and E3 ligases. It is a post-translational modification that controls the fate and function of the substrate protein. Substrate specificity in the ubiquitination reaction is conferred by the E3 ligases. Sequence homology suggests the human C-terminal to LisH (CTLH) complex could be an E3 ligase; however, very little is known about this complex. In this thesis, I characterize the human CTLH complex as a multi-subunit E3 ligase and define its activity, structure, and substrates. I demonstrate that the …

Characterization And Discovery Of Short Linear Motifs Mediating Protein Nuclear Import, Tanner M. Tessier

Electronic Thesis and Dissertation Repository

Protein-protein interactions (PPI) mediated through short linear motifs (SLiMs) are ubiquitous throughout the human proteome and are involved in many essential cellular processes. One such type of SLiM is the classical nuclear localization sequence (cNLS), which facilitates nuclear import by binding importin-α (Imp-α). This pathway is indispensable to many cellular processes and is extensively used by viral proteins that function within the nucleus of infected cells. Based on this, I demonstrated that the classical nuclear import pathway inhibitor, ivermectin, can inhibit replication of human adenovirus. Treatment with ivermectin blocks nuclear localization of the E1A protein, an essential viral nuclear protein …

Validation Of A Deployable Proteomic Assay For The Serological Screening Of Sexual Assault Samples, Catherine O'Sullivan Brown

Electronic Theses and Dissertations

Protein mass spectrometry (MS) has emerged as a technique to supplant traditional serological tests for body fluid identification. It was hypothesized that proteomic techniques would surpass the sensitivity and specificity of traditional serological techniques. An automated workflow coupled with protein MS has been developed for the confirmatory identification of five biological fluids. A developmental validation was completed, assessing parameters such as reproducibility, sensitivity, ion suppression, and limit of detection. Implementation was determined through tandem sample processing by MS, traditional serological tests, and standard DNA profiling methods. The MS approach offered superior detection limits while also providing true confirmatory results, producing …