So what is PCV, and why is it important for those with GBM

Here a little history regarding a recent drug treatment paradigm. If you want more specifics please provided comments!

https://www.linkedin.com/co…/the-brain-institute-of-america/

http://bit.ly/2RWX2w4

 

 

Advertisements

Why bother with social media?

When I first started my business all of my colleagues said Brian, you need to focus, you have some great ideas and you need to build a biomarker company ASAP and make a ton of money. Some of their advice rings true. I would love to be dining on something other than 25 cent ramen noodles and whatever the next BOGO deal is at the local shop. However I felt as if I wouldn’t be able to make much of a social impact if I only built a private business entity. 

That’s why we post!

Social media takes on so many different forms and flavors, it can be tough to keep up on these platforms. And it surely is a full time job to keep up with it. Yet there is a greater payoff in the end. That is to change the conversation in this country regarding what information is true, which is false, and how we should use that information to make more effective evidence-based policies in this country. 

Science seems to back this philosophy.

In a recent study, 110 academic scholars’ Twitter accounts were examined and some interesting bits of information were identified. The first is that people tend to flock together. So academics with under 500 followers are primarily having Twitter audiences of about 65% other scientists, 20% public forum, and 10% media organization as well as outreach groups.  And it takes about 1-2K followers to have an audience comprised of 40% public forum and 12% media outlets.

That’s a fairly sobering statistic for many of us young scientists. I started my Twitter account a year and a half ago and I have some 100 followers. However I haven’t been posting much content on Twitter either. By comparison my website gets about 8K views per year with around 2k being unique visitors, and I post way more content on my webpage.

Yet the point here is that the content you post has to be relevant and reach people outside your network, otherwise your just a bunch of academics talking amongst yourselves about making change. 

My group is pretty darn good at this, since many of my followers already are the outreach and advocacy groups who are the key groups that give out money to those lucky few researchers.  Now we turn our attention to the public forum and media sectors. The louder we get, the more we can inform our citizenry of the proper evidence-based information we should be discussing in order to make our communities happy healthier, and stronger.  This is why we post.

We thank you for the support!

– Let’s End This!

Written by Brian D. Adams, President, CEO, Director of Research, The Brain Institute of America

***Soon we will be launching individual blog channels for each of our content items. There you will have access to more in depth information regarding the topics we post. Meanwhile, for any comments or suggestions regarding our next segment please send us an email at brian.adams@braininstituteamerica.com ***

 

Structural insights of RNaseP helps scientists understand tRNA processing

A new wave of discoveries in the RNA field occurred in early November. Today the BIoA is highlighting updates made to ribonuclease P (RNaseP).  Why is this molecule so important? Why do scientists study this particular RNA enzyme? And how is this enzyme related at all with human health? 

Well to start off RNaseP is unlike any other enzyme because it operates on RNA molecules and the catalytic component of the enzyme is itself an RNA. Of course, there is one other enzyme that does this, and that is the ribosome! Since, Dr. Sidney Altman’s discovery that RNaseP is required for the processing of the 5′ leader sequence of tRNAs, scientists have shown RNaseP is essential for the proper transcription of a swath of noncoding RNA genes transcribed by RNA pol III, such as tRNA, rRNAs, and snRNAs.

The other fascinating finding is that RNaseP is found everywhere, in every cell, and in every organism. Such ultra conservation of a molecule indicates not only a crucial biological importance for RNaseP, it also implicates RNaseP as a living fossil of the much touted “RNA-world” that existed around the time life began on planet Earth. 

Apart from being an RNA fossil, why should I care about RNaseP?  If it is so ubiquitous, then why should I target it for any type of medicinal purposes… Well for one thing, dumb chemotherapies such as cisplatin that target the most ubiquitous biological process of DNA replication works quite well, despite some the toxic pitfalls (see our previous LinkedIn post on that concept). And secondly, scientists love to go after ubiquitous targets, but do not like to admit it. TP53, the protein that codes for P53, is a very distributed transcription factor expressed nearly everywhere, yet millions of dollars have been spent developing P53-based therapies. So the rationale is just in my mind for scientists to go after RNaseP as a drug target.

So which diseases? Well RNaseP enzymatically cleaves RNA, so why not develop therapies using RNaseP against RNA-mediated diseases such as herpes and influenza. In fact that is what is going on right now. Approximately 80,000 people will die of influenza this year, while ~45,000 women will die of breast cancer. So there is a clear clinical rationale for developing new and innovative RNA-based therapies for a number of these chronic or acute infections. 

Why do we care about RNaseP today? Well in Science, Lan et. al., reported some updated crystal structures of RNaseP from yeast (both in it’s isolated state, and in complex with tRNA). An old saying in the scientific community is “structure-function”. Essentially if you understand how an enzyme is built via structure, then you can develop smarter drugs that disrupt an interfered function. The study by Lan et. al., shows pretty convincingly that all forms of RNaseP (called ribozymes) share an RNA-based, substrate induced catalytic mechanism for the processing of pre-RNAs. In eukaryotes, the pre-RNA is the substrate, the RNaseP enzyme is controlled or regulated by proteins in the cell, and the catalytic activity of RNAseP is still RNA-based. 

So much like receptor tyrosine kinase inhibitors that are used in cancer therapy because they interfere with the enzymatic activity of the protein, so to should RNA-based therapies be developed so as to interfere with RNaseP activity for the betterment human health.

 

See references article below-

http://bit.ly/2SzoqQE

 

We thank you for the support!

 

Written by Brian D. Adams, President, CEO, Director of Research, The Brain Institute of America

 

– Let’s End This!

 

***Soon we will be launching individual blog channels for each of our content items. There you will have access to more in depth information regarding the topics we post. Meanwhile, for any comments or suggestions regarding our next segment please send us an email at brian.adams@braininstituteamerica.com ***