Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
May 1 - 5, 2012
The meeting will feature advances in the areas of structure and mechanism of action of molecular chaperones; mechanisms of induction of the stress response; the role of chaperones in protein degradation, and chaperone function in disease, development and organellar homeostasis. Chaperones are intimately involved in basic biological processes such as protein translation, folding, complex assembly and disassembly, translocation across membranes and protein degradation. The contribution of heat shock proteins, to protein folding in vivo across the entire proteome will be described alongside function of specialized chaperones with more limited clientele. The interactions of chaperones and unfolded and misfolded proteins will be discussed in molecular and atomic detail. At the cellular level, the interactions between chaperones in the formation of protein folding networks will be discussed and at the physiological level the impact of altered chaperone buffering capacity on organellar, cellular and organismal function will be discussed. Sessions:
Protein Folding and Chaperone Biochemistry
Chaperone Networks in Development and Disease
Stress Signaling and Aging
Protein Folding and Disaggregation Machines
Therapeutics of Protein Misfolding
Chaperones and Proteolysis
Quality control and Protein Trafficking The format of the meeting will include morning and evening sessions consisting of 2/3 25 minute talks and between six to eight short talks per session, selected from the abstracts, principally on unpublished work. In addition, there will be three poster sessions, held in the afternoons. The organizers will decide the suitability of each abstract for oral or poster presentation, but please specify if you prefer a poster.
|
|