So I go to my email, and discover an email from Bob O'Hara telling me that Scientia Pro Publica 3: the Swine 'flu Edition is up! I follow the link (above) and discover (shock!) he's put my blog and post first. Thanks, again, Bob.
The very next blog/post was Brain Stimulant, where Mike had a post on Brain Synapse Computational Capacity. In a new paper (which I missed in my research), it's reported that literally hundreds of proteins in a single postsynaptic density (PSD) changed their phosphorylation status in response to activation of a single neurotransmitter receptor. See Mike's post (linked above) for more detaiil.
There's a great deal of synergy here with my posts on cellular intelligence, especially parts I and IV. In Part I: Enzymes as an Analog Computer I made the point that the interacting networks of enzymes constitute an analog computer of sorts, potentially much more powerful in its calculations than a digital computer composed of the same number of enzymes would be. In Part IV: Local Intelligence I extended that point to local conditions, especially in the synapse. While the potential was clear for a synapse to contain a network of hundreds of interacting enzymes, Coba et al., the paper Mike discusses, makes it clear that at least one type of neuron actually does this.
The point being that Mike's post makes my point stronger, and IMO my posts make his stronger as well. That's synergy.
Another example of synergy may be found at the Yahoo! Glue phosphatases page. I found this page while searching for the hundreds of links admiring readers must have made to my blog posts (Not!). The very first paper on it (then, and as I write) was From Promiscuity to Precision: Protein Phosphatases Get a Makeover by David M. Virshup and Shirish Shenolikar. To blockquote the abstract (which is all I can get to):
The control of biological events requires strict regulation using complex protein phosphorylation and dephosphorylation strategies. The bulk of serine-threonine dephosphorylations are catalyzed by a handful of phosphatase catalytic subunits, giving rise to the misconception that these phosphatases are promiscuous andunregulated enzymes invivo. The reality is much more nuanced: PP1 and PP2A, the most abundant serine-threonine phosphatases, are, in fact, families of hundreds of protein serine/threonine phosphatases, assembled from a few catalytic subunits in combination with a highly diverse array of regulators. As recent publications illustrate, these regulatory subunits confer specificity, selectivity, localization, and regulation on these important enzymes.
Here again, there's synergy: the precision of phosphatase activity becomes much more powerful if it's part of an analog computing network (rather than simply a digital one).
This kind of synergy is potentially a great boon that science blogging has to offer. The connection between ideas has only to be pointed out, it doesn't matter by whom. Scientists (and anyone else) can then use their own judgment as to the utility and implications of the connection.
Science blogging, then, could add an army of amateurs (including scientists out of their discipline) in support of the scientific community, many of whom are probably too narrowly focused on their immediate reseach (and publication of same) to fully investigate the possible interactions between their own work and others'.
Of course, to fully achieve this goal, Open Access is a necessity. Dr. Isis, in a recent post on her blog, asked Can There Be a Compromise to Open Access? My own response, as a science blogger (I believe I've paid my dues at this point), is a resounding NO! Open access is necessary for science to take full advantage of what the Internet offers in science blogging.