Mad cow disease article - digitales.com.au

Mad cow disease article - seems

Physicist and nuclear cardiologist Dr. Richard Fleming has issued a dire warning about the dangers of Wuhan coronavirus Covid vaccines, which he says can cause mad cow disease. This is why some of them are causing deadly blood clots. The AstraZeneca jab used in Europe was also suspended for the same reason. According to Fleming, the risks associated with taking a Kung Flu shot are high.

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Based on the study highlighted in this video, it may very well be that the Covid vaccine will make the vaccinated far more susceptible to dying.

mad cow disease article

WebMD Explanation. Natural News. Prion diseases comprise several conditions. A prion is a type of protein that can trigger normal proteins in the brain to fold abnormally.

mad cow disease article

Prion diseases can affect both humans and animals and are sometimes spread to humans by infected meat products. Prion diseases occur when normal prion protein, found on the surface of many cells, becomes abnormal and clump in the brain, causing brain damage. This abnormal accumulation of protein in the brain can cause memory impairment, personality changes, and difficulties with movement. Despite artucle medical paper published below Jan. In this paper the Pfizer COVID vaccine was evaluated for the potential to induce prion-based disease in vaccine recipients.

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Potential G Quadruplex sequences are possibly present but a more sophisticated computer program is needed to verify these. Furthermore, the spike protein, created by the translation of the vaccine RNA, binds angiotensin converting enzyme 2 ACE2a zinc containing enzyme. This interaction has the potential to increase intracellular zinc. Zinc ions have been shown to cause the transformation of TDP to its pathologic prion configuration. The enclosed finding go here well as additional potential risks leads the author to believe that regulatory a pproval of the RNA based vaccines for SARS-CoV-2 was premature and that the vaccine may mad cow disease article much more harm than benefit. This paper focuses on a novel potential adverse event mechanism causing prion disease which could be even more common and debilitating than the viral infection the vaccine is designed to diisease.

Fleming says Biden regime needs to call for immediate reevaluation of China Virus injections

While this paper focuses on one potential adverse event there are multiple other potential fatal adverse events as discussed below. Over the last two decades there has been a concern among certain scientists that prions could be https://digitales.com.au/blog/wp-content/custom/why-building-administrations-have-a-developing-business/watch-vertigo-online.php as bioweapons. This concern originates due to potential for misuse of research data on the mechanisms by which certain RNA binding proteins like TDP, FUS and others can be activated to form disease causing prions. Fow the past, for example, there were mad cow disease article for publishing information pertaining to construction of nuclear bombs.

mad cow disease article

Published diseawe has shown that there are several different factors that can contribute to the conversion of certain RNA binding proteins including TDP, FUS and related molecules to their pathologic states. These RNA binding proteins have many functions and are found in both mad cow disease article nucleus and the cytoplasm. These binding proteins have amino acid regions, binding motifs that bind specific RNA sequences. Binding to certain RNA sequences when the proteins are in the cytoplasm is believed to causes the molecules to fold in certain ways leading to pathologic aggregation and prion formation in the cytoplasm [2]. Zinc binding to the RNA recognition motif of TDP is another mechanism leading to formation of amyloid like aggregations [9].

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This interaction has the potential to increase intracellular zinc levels leading to prion disease. The initial binding could be between spike proteins on the surface of the cell transfected by the vaccine and ACE2 on the surface of an adjacent cell. The resulting complex may become internalized.]

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