Allotopic Expression of Yeast COX2: A New Leap Forward for MitoSENS

Posted by Michael Rae on March 23, 2010 | Chief Science Officer's Team

To date, three of the thirteen OXPHOS genes still encoded in the mitochondria have been allotopically expressed (AE) in human cells with mutated versions of the same gene, thereby rescuing a respiratory defect. Now we have the first report of a new gene, COX2, being allotopically expressed in yeast, by mutating the gene to overcome the hydrophobicity of the mitochondrial membrane; a similar mutation has been shown to underlie the ability of the unusual case of the soybean COX2, which is a case of a native nuclear-encoded COX2 gene.

SENS researchers aim to increase effectiveness of A2E degrading enzymes

Posted by Lorenzo Albanello on March 15, 2010 | Degradation of A2E

SENS researchers have recently begun efforts to improve the effectiveness of the A2E degrading enzyme versatile peroxidase by developing a chimeric enzyme which also features an additional portion who is expected to be able to dramatically increase its activity. This project is currently in progress at the SENS Foundation research center in collaboration with the State University of New York at Plattsburgh.

Introducing Jacques

Posted by Jacques Mathieu on March 15, 2010 | Clearing cells of age-related wastes

It was early 2005 when I first read about SENS. I had already applied to several graduate schools at that time and was waiting to hear back, but as I delved into that article in Popular Science I knew this was something I wanted to be involved in. A lot of people were studying aging, but no one had a plan like this. I emailed Aubrey and it wasn't long before I was headed to Rice University in Houston; first to perform some preliminary research into the LysoSENS project, and then to begin a PhD studying microbial oxysterol degradation.

Refining Intravenous IgG Pools for AD Immunotherapy

Posted by Michael Rae on March 13, 2010 | Chief Science Officer's Team

Intravenously delivered immunoglobulin G (IVIgG) is a mixture of antibodies extracted from human blood which has demonstrated promising preliminary results in clearing the beta-amyloid (Abeta) deposits that drive the pathogenesis of Alzheimer's disease. A recent study compares multiple commercial sources of IVIgG and finds significant differences in their Abeta-binding activity, suggesting that results from impending clinical trials are likely to be highly dependent on the specific "brand" of IVIgG in use.

Pages