Anyone interested -
Did you know that while you're sleeping, you could be helping Stanford research and possibly help find a cure for a number of diseases? A number of us are contributing to the project - it's free, there's no charge - you just sign up, install a small program, and let Stanford use your computer whenever you're not using it yourself.
A few of the things we're helping with are listed below. If anyone drops by and has any interest in joining us in the effort, please post that and we'll help you get started. If you venture forth - we're team 328 and the group is more than willing to answer questions or coach you through the process.
I knew a few of the things that that Stanford was studying, but I wasn't aware how the list had grown:
- Alzheimer's Disease (AD)
- Huntington's Disease (HD)
- Cancer and P53
- Chagas Disease
- Malaria
- Osteogenesis Imperfecta (OI)
- Diabetes
- Antibiotics
- Parkinson's Disease (PD)
- Viral diseases
And below are some of the steps forward that we've helped Stanford with - from their website:
2012 We're very excited to report on our progress towards our goal to develop new small molecule drug candidates for AD. In a paper just published in the Journal of Medicinal Chemistry, we report on tests of predictions from earlier Folding@home simulations, and how these predictions have led to a new strategy to fight Alzheimer's Disease. These results have been a long time in coming and in many ways represents a major achievement for Folding@home (FAH) in general. While this is not a cure, it is a major step towards our final goal, some light at the end of the tunnel. The next steps, now underway in our lab, are to take this lead compound and help push it towards a viable drug. We're very excited that the directions set out in this paper do appear to be bearing fruit in terms of a viable drug (not just a drug candidate). We hope to have more results in the coming months!
2012 Dr. Peter Kasson has been applying his work on viruses to cancer, as many cancers are virus-associated.
At FAHcon 2012, Dr. Xuhui Huang presented our recent results of the molecular mechanisms of gene transcription. Transcription is the first step in reading genomic DNA, and regulation of this process plays a key role in cell differentiation and other fundamental processes. Misregulation of transcription is a major factor in cancer and other human diseases. Our simulation results are able to provide dynamic information for the transcription, and this dynamic information is largely inaccessible to present experimental techniques.
We're studying the folding of ubiquitin, a small regulatory protein found in almost all cells in human body. It is part of a large regulatory system that labels other unneeded proteins for destruction. The ubiquitin system has an important role in regulating cellular growth and proliferation. As expected, alterations in the ubiquitin system could lead to uncontrolled accumulation of malignant proteins in cells and lead to cancer.
We are simulating many forms of Pin1 WW domain, a protein implicated in some cancers and Alzheimer's disease. Understanding the role of mutations on misfolding can have important biomedical consequences.
We assisted Chris Garcia's lab with their work with Interleukin 2 (IL-2), a protein which assists the immune system in fighting pathogens and cancer tumors. While injecting a patient with more IL-2 has been an effective cancer treatment, naturally occuring IL-2 has very serious side effects. We helped the Garcia lab to discover a form of IR-2 that was more "floppy", which greatly increased its cancer-fighting potency. This means that it's possible to admister theurapedic doses of it without causing the side effects. Stanford has applied for a patent, and several major pharmaceutical companies approached the Garcia lab about this discovery. Please see this paper and this article for more information.
And July 2012 - Our group [http://choderalab.org] is using Folding@Home to understand how some successful anti-cancer therapeutics (like imatinib) are able to selectively target the targeted disease-causing kinases while minimally interfering with other normally-functioning kinases. A deeper understanding of this selectivity would help recapitulate the success seen in treating some cancers by aiding the design of novel therapeutics targeting other cancers. Up to now, the origin of this selectivity has been elusive because it appears that highly selective drugs like imatinib can bind in essentially the same way to the highly similar Abl and Src kinases, despite the fact that it binds Abl well and Src poorly (see Figure). It is now believed these differences in binding are due to conformational preferences of the kinase for different geometries, something that had been traditionally hard to study but is well-suited to techniques we originally developed to study protein folding problems on Folding@Home.
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