<?xml version="1.0" encoding="UTF-8"?>
<seminar>
  <abstract>&lt;p&gt;&amp;nbsp;&lt;/p&gt;
&lt;div style="margin: 2pt 0in 4.8pt"&gt;S-Nitrosothiols (RSNO) are metabolites of nitric oxide that have been implicated to participate in NO signaling pathways. RSNO can form on both low-molecular weight thiols (such as cysteine and glutathione) or on protein thiols and can exchange between thiol groups by a process referred to as transnitrosation. Despite a growing literature on the control of cellular signaling via S-nitrosation, the mechanisms by which NO transmits its signals through thiol groups are poorly understood. BY making use of the fact that S-nitrosocysteine is specifically transported into cells via amino-acid transport system L, we have investigated mechanisms of NO and RSNO-dependent protein modification and found that they can vary considerably. In addition, we have examined using novel proteomic methods the level and distribution of S-nitrosation at close to physiological levels of S-nitrosothiol. Finally we have investigated novel mechanisms of S-nitrosothiol synthesis. In total we are attempting to put a mechanistic framework behind the process of protein S-nitrosation within the context of the cellular environment.&lt;/div&gt;</abstract>
  <affiliation>Medical College of Wisconsin</affiliation>
  <created-at type="datetime">2009-09-10T18:30:12-07:00</created-at>
  <division type="integer" nil="true"></division>
  <host>Xian</host>
  <id type="integer">77</id>
  <location>Fulmer 438</location>
  <presenter>Prof. Neil Hogg</presenter>
  <time type="datetime">2009-11-09T16:10:00-08:00</time>
  <title>S-Nitrosothiols: Synthesis and Signaling</title>
  <updated-at type="datetime">2009-10-29T14:11:11-07:00</updated-at>
</seminar>
