Thesis advisor: Jianmin Gao / Thesis advisor: Eranthie Weerapana / Cysteine residues are known to perform an array of functional roles in proteins, including nucleophilic and redox catalysis, regulation, metal binding, and structural stabilization, on proteins across diverse functional classes. These functional cysteine residues often display hyperreactivity, and electrophilic chemical probes can be utilized to modify reactive cysteines and modulate their protein functions. A particular focus was placed on three peptide-based cysteine-reactive chemical probes (NJP2, NJP14. and NJP15) and their particular biological applications. NJP2 was discovered to be an apoptotic cell-selective inhibitor of glutathione S-transferase omega 1 and shows additional utility as an imaging agent of apoptosis. NJP14 aided in the development of a chemical-proteomic platform to detect Zn2+-cysteine complexes. This platform identified both known and unknown Zn2+-cysteine complexes across diverse protein classes and should serve as a valuable complement to existing methods to characterize functional Zn2+-cysteine complexes. Finally, NJP15 was part of a panel of site-selective cysteine-reactive inhibitors of protein disulfide isomerase A1 (PDIA1). These inhibitors show promise in clarifying the unique and redundant properties of PDIA1's dual active-sites, as well as interrogating the protein's role in cancer. Together, these case studies illustrate the potential of cysteine-reactive chemical probes to modulate protein activities, interrogate biological systems, and aid in the development of powerful therapeutic drugs. / Thesis (PhD) — Boston College, 2015. / Submitted to: Boston College. Graduate School of Arts and Sciences. / Discipline: Chemistry.

Thesis (Ph. D.)--University of Queensland, 2002. / Includes bibliographical references.

Dissertation (Ph.D.)--Auburn University, 2007. / Abstract. Vita. Includes bibliographic references.

Thesis (Ph. D.)--University of Washington, 2005. / Vita. Includes bibliographical references (leaves 167-186).

published_or_final_version / Botany / Doctoral / Doctor of Philosophy

No description available.

No description available.

Thesis advisor: Abhishek Chatterjee / Thesis advisor: Eranthie Weerapana / EGF signaling activates multiple pathways within the cell that lead towards proliferation, rendering this pathway of interest for cancer therapy. Recent studies focused on triple-negative breast cancer have shown that EGF-induced tumorigenesis strongly correlates with the up-regulation of FABP5, which shuttles fatty acids from the cytoplasm of cells to the nucleus. Our work began with the identification of redox active cysteine residues upon EGF activation in situ using a caged electrophile to perform live cell labeling. In these studies, the C120 residue of FABP5 was identified as a cysteine with high redox activity and thus became a subject of further interest. The characterization of redox active cysteine residues yields important information about protein structure and function. We have confirmed these results via in-gel fluorescence and developed fluorescence assays to probe the significance of C120 and C127 in FABP5. Two fatty acids were chosen based on their conformation in the FABP5 binding pocket. Upon the addition of a fatty acid, wild type protein showed a decrease in fluorescence indicating that the fatty acids were outcompeting the fluorophores used. Future studies will investigate both wild type and mutant versions of FABP5 with emphasis on determining potential disulfide bond formation via phosphoproteomics and western blotting techniques. / Thesis (MS) — Boston College, 2016. / Submitted to: Boston College. Graduate School of Arts and Sciences. / Discipline: Chemistry.

Bibliography : leaves 153-162. / xi, 162 leaves : ill. (chiefly col.) ; 30cm. / Title page, contents and abstract only. The complete thesis in print form is available from the University Library. / The objective of this project was to isolate follicle-derived cDNA clone(s) encoding putative L-cysteine transport proteins, and to determine their amino acid transport function in virto. / Thesis (Ph.D.)--University of Adelaide, Dept. of Animal Science, 2000

Sweet potato SPCP2 is a full-length cDNA isolated from senescent leaves and encodes a putative papain-like cysteine protease. The SPCP2 contained 1101 nucleotides (366 amino acids) in its open reading frame, and exhibited high amino acid sequence identities (ca. 68% to 83%) with plant cysteine proteases, including Actinidia deliciosa, Arabidopsis thaliana, Brassica oleracea, Phaseolus vulgaris, Pisum sativa, Vicia faba, Vicia sativa and Vigna mungo. SPCP2 gene expression was enhanced significantly in natural senescent leaves and in sprouting storage root. Transgenic Arabidopsis plants with ectopic constitutive SPCP2 expression showed earlier floral transition from vegetative to reproductive growth, reduced rosette leaves when flowering, enhanced germination percentage of transgenic progeny seeds in salt-containing MS medium, higher Fv/Fm value, higher relative water content and enhanced tolerance during drought treatment. Based on these results, we conclude that sweet potato papain-like cysteine protease, SPCP2, is a functional gene, and its expression causes altered developmental characteristics and enhances drought and salt stress responses in transgenic Arabidopsis plants.