Editing Folding@home (section)

=== Cancer ===
More than half of all known cancers involve [[mutations]] of [[p53]], a [[tumor suppressor]] protein present in every cell which regulates the [[cell cycle]] and signals for [[cell death]] in the event of damage to [[DNA]]. Specific mutations in p53 can disrupt these functions, allowing an abnormal cell to continue growing unchecked, resulting in the development of [[tumors]]. Analysis of these mutations helps explain the root causes of p53-related cancers.<ref name="10.1126/science.1905840"/> In 2004, Folding@home was used to perform the first molecular dynamics study of the refolding of p53's [[protein dimer]] in an [[water model|all-atom simulation of water]]. The simulation's results agreed with experimental observations and gave insights into the refolding of the dimer that were formerly unobtainable.<ref name="10.1016/j.jmb.2004.10.083"/> This was the first [[peer review]]ed publication on cancer from a distributed computing project.<ref name="FAH publishes cancer results"/> The following year, Folding@home powered a new method to identify the amino acids crucial for the stability of a given protein, which was then used to study mutations of p53. The method was reasonably successful in identifying cancer-promoting mutations and determined the effects of specific mutations which could not otherwise be measured experimentally.<ref name="10.1016/j.jmb.2005.12.083"/>

Folding@home is also used to study [[chaperone (protein)|protein chaperones]],<ref name="diseases FAQ"/> [[heat shock protein]]s which play essential roles in cell survival by assisting with the folding of other proteins in the [[Macromolecular crowding|crowded]] and chemically stressful environment within a cell. Rapidly growing cancer cells rely on specific chaperones, and some chaperones play key roles in [[chemotherapy]] resistance. Inhibitions to these specific chaperones are seen as potential modes of action for efficient chemotherapy drugs or for reducing the spread of cancer.<ref name="10.1016/j.biopha.2011.04.025"/> Using Folding@home and working closely with the Center for Protein Folding Machinery, the Pande lab hopes to find a drug which inhibits those chaperones involved in cancerous cells.<ref name="typepad: nanomedicine ce"/> Researchers are also using Folding@home to study other molecules related to cancer, such as the enzyme [[Src kinase]], and some forms of the [[Engrailed (gene)|engrailed]] [[homeodomain]]: a large protein which may be involved in many diseases, including cancer.<ref name="typepad: protomol b4"/><ref name="description: 180"/> In 2011, Folding@home began simulations of the dynamics of the small [[Trefoil knot fold|knottin]] protein EETI, which can identify [[carcinoma]]s in [[medical imaging|imaging scan]]s by binding to [[cell surface receptor|surface receptor]]s of cancer cells.<ref name="forum: 7600 in beta"/><ref name="description: 7600"/>

[[Interleukin 2]] (IL-2) is a protein that helps [[T cell]]s of the [[immune system]] attack pathogens and tumors. However, its use as a cancer treatment is restricted due to serious side effects such as [[pulmonary edema]]. IL-2 binds to these pulmonary cells differently than it does to T cells, so IL-2 research involves understanding the differences between these binding mechanisms. In 2012, Folding@home assisted with the discovery of a mutant form of IL-2 which is three hundred times more effective in its immune system role but carries fewer side effects. In experiments, this altered form significantly outperformed natural IL-2 in impeding tumor growth. [[Pharmaceutical companies]] have expressed interest in the mutant molecule, and the [[National Institutes of Health]] are testing it against a large variety of tumor models to try to accelerate its development as a therapeutic.<ref name="scientists boost IL-2 potency"/><ref name="10.1038/nature10975"/>