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<title>Chemical Proteomic Approaches to Discover and Characterize Lysine Acetyltransferase Biology | NIH Research Festival</title>
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<article><div class="banner banner--gray banner--compact" style="--banner-background-image: url('/sites/default/files/media/image/2021-03/2015.jpg');--banner-background-focus: 50% 50%"><div class="banner__wrapper"><div class="banner__container"><h2 class="banner__heading">NIH Research Festival</h2><div class="banner__content"><p><strong><time datetime="2015-09-16">September 16</time> – <time datetime="2015-09-18">18, 2015</time></strong></p></div></div></div></div></article>
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<div class="section"><div data-drupal-messages-fallback class="hidden"></div></div><main role="main"><div id="main-content" tabindex="-1"></div><div class="section"><div class="content-sidebar"><div class="content-sidebar__main"><div class="content-sidebar__main-content"><div id="block-mainpagecontent-2"><article><h1>Chemical Proteomic Approaches to Discover and Characterize Lysine Acetyltransferase Biology</h1><div class="schedule"><div class="schedule__label"><div class="schedule__label-text"><time datetime="2015-09-17">Thursday, September 17, 2015</time>
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– Poster Session II
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</div></div><div class="schedule__content"><div class="schedule__item"><div class="schedule__time">12:00 – 1:30 p.m.</div><div class="schedule__description"><p><strong>FAES Terrace</strong></p></div><div class="schedule__description"><p><strong>NCI</strong></p></div><div class="schedule__description"><p><strong>CHEMBIO-8</strong></p></div></div></div></div><p><strong>FARE Award Winner</strong></p><h2>Authors</h2><ul><li>DC Montgomery</li><li>AW Sorum</li><li>JM Garlick</li><li>JL Meier</li></ul><h2>Abstract</h2><p>Lysine acetyltransferases (KATs) play a critical role in the regulation of central cellular functions such as gene expression and metabolism. However, while the disruption of acetylation-dependent signaling is an emerging paradigm in oncology, methods for the discovery and characterization of KAT inhibitors remain limited. To address this challenge, we have developed a chemoproteomic platform to enable global profiling of KAT activity in unfractionated proteomes. This approach utilizes cofactor-based affinity probes capable of reporting on the active-site occupancy of KAT enzymes in cellular contexts. Chemoproteomic profiling provides a read-out of class-wide KAT-ligand interactions in cellular contexts, circumventing the need for recombinant expression and purification of individual enzymes. This strategy facilitates analyses of inhibitor specificity, enables the biological study of KATs, and affords a high throughput platform for novel ligand discovery. By providing a powerful method to study the molecular interactions of KATs in native contexts, chemoproteomic profiling will aid investigations into the targetable role of KATs in cancer and other pathologies.</p><p><strong>Scientific Focus Area</strong>: Chemical Biology</p><p class="updated"><small>This page was last updated on Friday, March 26, 2021</small></p></article>
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