Anavex Life Sciences Corp (AVXL)

[XenaLives]

I just wrote the following message for someone who asked me why Anavex's drugs would work if Alzheimer's was caused by EMF. Personally I don't believe that "Alzheimer's" exists as a single disease. It was a catch all term to cover the fact that the medical profession didn't understand what was going on.

This was my response to that question:

I have flouroquinolone toxicity which has messed up my entire metabolism, including memory and cognition. EMF can also be a trigger for the same process:

Check out these searches:

https://www.google.com/search?q=SIGMAR1+and+muscarinic+receptors+%22taurine%22

https://www.google.com/search?q=SIGMAR1+and+muscarinic+receptors+%22tyrosine%22

https://www.google.com/search?q=sigmar1+and+muscarinic+receptors+%22glutamate+receptors%22

When studying the protein hydration shell as a crucial contributor to protein activity and structure, the protein itself has been considered to be transparent to terahertz radiation. However, in studies with a low hydration level and with frozen samples, it was demonstrated that the protein molecule contributes significantly to permittivity. In this case, the imaginary part of dielectric permittivity is a sum of products of resonant frequency with the imaginary part of permittivity for ice, bound water and the protein itself. By knowing the dielectric parameters for pure ice and the calculated contribution of the solute-bound water (only the fast component of water relaxation is important, and taking its value of 32 ps for unfrozen solute-associated water and the Arrhenius temperature dependence, it is possible to calculate the low-temperature relaxation time), one can isolate the protein component from the general terahertz response of the sample [199]. Another approach is to use spectroscopy. Sulfur atoms are heavier than carbon or oxygen and thus have their vibrational states in the terahertz range. Also, some amino acids like cysteine and methionine (homocysteine and taurine are not incorporated into proteins [200]) contain sulfur atoms and can form disulfide bridges which are critical for secondary and tertiary protein structure as well as linkage of the polypeptide chains [201]. There are three conformational states for disulfide bridges and for all three, the terahertz absorption spectra demonstrate several absorption peaks. The frequencies of the disulfide bridge stretching vibrations are very sensitive to minor variations in the dihedral angle of the bridge and thus can provide information about protein structure [202,203].

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5746568/


https://www.researchgate.net/publication/271530073_Role_of_sigma-1_receptors_in_neurodegenerative_diseases

Neurodegenerative diseases with distinct genetic etiologies and pathological phenotypes appear to share common mechanisms of neuronal cellular dysfunction, including excitotoxicity, calcium dysregulation, oxidative damage, ER stress and mitochondrial dysfunction. Glial cells, including microglia and astro-cytes, play an increasingly recognized role in both the promotion and prevention of neurodegeneration. Sigma receptors, particularly the sigma-1 receptor subtype, which are expressed in both neurons and glia of multiple regions within the central nervous system, are a unique class of intracellular proteins that can modulate many biological mechanisms associated with neurodegeneration. These receptors therefore represent compelling putative targets for pharmacologically treating neurodegenerative disorders. In this review, we provide an overview of the biological mechanisms frequently associated with neuro-degeneration, and discuss how sigma-1 receptors may alter these mechanisms to preserve or restore neuronal function. In addition, we speculate on their therapeutic potential in the treatment of various neurodegenerative disorders

https://www.researchgate.net/publication/271530073_Role_of_sigma-1_receptors_in_neurodegenerative_diseases