- Home : Health: December 30, 2013
Excerpt: “…many scientists studying these topics are unaware of ways in which nutrients may behave differently in something like a cell culture or lab animal, compared to the human body. This raises special challenges with vitamin C research in particular.”
See also: Myths, Artifacts, and Fatal Flaws: Identifying Limitations and Opportunities in Vitamin C Research. (This article belongs to the Special Issue Vitamin C and Human Health)
My comment: Until there is a model of cause and effect that clearly establishes how nutrients link the epigenetic landscape to the physical landscape of DNA in the organized genomes of species from microbes to man, it is not likely that people will understand how their impact on seemingly futile cycles of thermodynamically regulated protein biosynthesis and degradation are involved in health and disease via epigenetic effects on organism level thermoregulation. Addressing the biophysical constraints on mutations is not possible when each advance requires attempts to inform evolutionary theorists who dismiss what they don’t understand about biology.
And, until evolutionary theorists dispense with the nonsense of mutation-driven natural selection, it will remain difficult to convince the majority of people that ecological adaptation is what we see when mutations are controlled by diet and the metabolism of nutrients to species-specific pheromones that control the physiology of reproduction.
James V. Kohl detailedl how quantized energy-dependent microRNA biogenesis links the pheromone-controlled physiology of reproduction to biophysically constrained viral latency and healthy longevity. Links from what organisms eat to the enzyme-dependent metabolism of food also link metabolic networks to microRNA-mediated genetic networks in the context of RNA interference. Drug therapies alter RNA interference by altering cell type differentiation in all cells of all individuals of all species. For comparison, during the past 26 years, Kohl has detailed how the chemistry of protein folding is biophysically constrained at every level of biological organization by conserved molecular mechanisms.