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Symposium Highlights
These articles highlight the main topics and discussion points from each Symposium session.
Articles marked with the microscope logo  are focused on specialized aspects of the topic, and are intended for a readership well-versed in the background literature.
Articles marked with binoculars  take an overview of the topic, and aim particularly to make the subject accessible to a broad audience. |
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Session 1: Technological challenges of studying protein folding
This session considered approaches to monitoring the folding of protein structures both in vitro and in vivo. The questions discussed were: What can we learn from studying model systems? How does mutational analysis help us to understand folding and disease? What methods are available to study structural details of proteins in vivo? Finally, the delegates discussed the link between protein folding and protein engineering and design.
 Protein folding - from in vitro to in vivo models
 Stuck in the middle |
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Session 2: Cell biology of protein folding
How does the crowded environment of the cell influence protein folding, and how, indeed, do misfolded proteins influence the cell? The key questions that were addressed included the role of chaperones in controlling the formation and fate of folded proteins, and how covalent modifications, both co-translational and post-translational, affect the process. The special role of the endoplasmic reticulum as a site of protein folding was discussed, as was the cellular responses to protein misfolding.
The cell's production line
Quality counts |
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| Session 3: Basic mechanisms of protein folding diseases
This session concentrated on the process of protein aggregation and the toxicity of the assemblies of misfolded proteins. In the pathogenesis of the amyloid diseases, such as Alzheimer's disease, how do the characteristic aggregates form? Would misfolded proteins that accumulate in the cytoplasm be expected to undergo a distinct kind of aggregation process to those in the extracellular space, and, if so, how might they differ? And most importantly, is it the early, intermediate or end-stage of the aggregation process that is responsible for the progressive neuronal degeneration in protein misfolding diseases?
Small, but deadly |
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| Session 4: Therapeutic strategies for protein folding diseases
What are the challenges for drug discovery in aggregation diseases? Key questions discussed were: What are the roles for antibodies versus small molecules? If, as some recent work indicates, the tendency to form b-sheet-rich aggregates is a generic property of polypeptides, will there be generic inhibitors of this process that could have pharmaceutical implications? What are the best systems for screening for inhibitors of aggregation? Finally, the delegates discussed how therapeutics for diseases such as familial amyloidotic polyneuropathy can be generalized to some of the more common diseases of protein aggregation.
Know your enemy |
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