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Post-translational Modifications: From Protein Structure to Systems Biology

Wednesday, October 26, 2011 — Concurrent Symposia Session IV

Noon – 2:00 p.m.

Ruth L. Kirschstein Auditorium


  • Aleksandra Nita-Lazar, NIAID
  • Mark Knepper, NHLBI


Post-translational modifications (PTMs) modulate the activity of most proteins, therefore adding a layer of complexity to the analysis of cellular processes and extending the repertoire of protein functions. The analysis of PTMs has proven to be challenging because of their abundance, complexity and, often, dynamic character. Nevertheless, excellent, innovative, and highly significant research encompassing many different types of PTMs is being conducted at NIH. This mini-symposium aims at showcasing different approaches to the PTM discovery and functional interpretation. The reversible AMPylation is crucial for the pathogenicity of Legionella. Careful, comprehensive analysis can lead to the discovery and functional characterization of new PTMs, like β-methylthiolation of an E.coli protein. S-nitrosylation is an example of the PTM regulating human physiology with clinical relevance. Two examples of systematic analyses of phosphorylation-dependent signaling networks will be described: the vasopressin signaling network and TLR signaling network.

Phosphorylation Dynamics in the TLR Signaling Pathway
Virginie Sjoelund, NIAID

Systems Biology of G Protein-Coupled Receptor Signaling Revealed by Quantitative Phosphoproteomics
Jason Hoffert, NHLBI

A Proteomic and Transcriptomic Approach Reveals New Insight into Beta-Methylthiolation of Escherichia coli Ribosomal Protein S12
Michael Brad Strader, NIMH

The Role of S-Nitrosylation in Regulating Myocardial Cell Death and Protection
Elizabeth Murphy, NHLBI

Redox Modifications Play a Critical Role in Myocardial Ischemic Preconditioning *FARE Award Winner
Mark Kohr, NHLBI

Controlling Small GTPase Activity through Reversible AMPylation
Matthias Machner, NICHD

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