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Probing O-GlcNAc Modifications Via Metabolic Labeling Using Unnatural Sugars

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dc.contributor.advisor Carrico, Isaac S en_US
dc.contributor.author Rajaram, Lakshmi en_US
dc.contributor.other Department of Chemistry. en_US
dc.date.accessioned 2017-09-20T16:52:04Z
dc.date.available 2017-09-20T16:52:04Z
dc.date.issued 2015-08-01
dc.identifier.uri http://hdl.handle.net/11401/77145 en_US
dc.description 100 pg. en_US
dc.description.abstract Understanding the impact of post-translational modifications in the context of the complexity of the human proteome is extremely challenging. Part of the challenge lies in cataloging the proteins that are modified with any given post-translational modification, and how this list changes in response to changes in cellular/tissue physiology. The O-GlcNAc modification is one such modification that involves an addition of a single N-acetylglucosamine moiety onto serines and threonines of eukaryotic proteins. This dynamic modification is mediated via two enzymes: O-GlcNAc transferase (OGT) for installing the sugar and O-GlcNAcase (OGA) for cleaving the sugar off modified proteins. O-GlcNAcylation occurs mainly in nuclear and cytosolic proteins ranging from structural proteins and enzymes to transcription factors and tumor suppressors. The dynamic nature of the modification, which can be compared to phosphorylation, has emerged as an important player in signaling, regulation of metabolism, nutrient response and disease onset. Despite being implicated as a key regulator of cellular physiology, O-GlcNAc remains ill-defined due to a lack of effective analytical tools. In this context, the chemical reporter strategy, which installs a chemical handle that can be later modified and monitored, provides a potential solution. Here we detail efforts towards installing chemical reporter mimics of O-GlcNAc and using them to profile the repertoire of proteins modified with this post-translational modification. In particular, we chose to scrutinize the involvement of O-GlcNAc in the activation of T lymphocytes, which was prompted by the discovery that OGT is essential for T and B lymphocyte activation. en_US
dc.description.sponsorship This work is sponsored by the Stony Brook University Graduate School in compliance with the requirements for completion of degree. en_US
dc.format Monograph en_US
dc.format.medium Electronic Resource en_US
dc.language.iso en_US en_US
dc.publisher The Graduate School, Stony Brook University: Stony Brook, NY. en_US
dc.subject.lcsh Chemistry en_US
dc.subject.other bioorthogonal chemistry, chemical biology, O-GlcNAc, T-cell activation en_US
dc.title Probing O-GlcNAc Modifications Via Metabolic Labeling Using Unnatural Sugars en_US
dc.type Dissertation en_US
dc.mimetype Application/PDF en_US
dc.contributor.committeemember Drueckhammer, Dale en_US
dc.contributor.committeemember Koch, Stephen en_US
dc.contributor.committeemember Koller, Antonius. en_US

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