The only thing worse than genocide is irreversibly compromising the human genetics with incalculable consequences for all current and future generations.
And, once again, we bring proof they are knowingly doing this, and where there’s awareness, there’s also intention.
So this video below should open the Nuremberg 2 trials.

The WEF published this video in 2016, one year prior to Moderna’s Tal Zaks video for TED that we’ve already manage to make quite viral.
This crucial issue is hugely underrated and most people still are not so sure what to believe simply because The Military Biotech Complex is burning the books through its Big Tech arm.
Hopefully the video before clarifies the issue for good.

Before we further discuss this, please see this “prequel” for very important context:

SCANDALOUS! YOUTUBE JUST SCRUBBED MODERNA CHIEF SCIENTIST’S TED TALK ABOUT MRNA AND GENES. FOR “MEDICAL MISINFORMATION”

Actually, one of our first videos deleted by YouTube was just scientists describing their work in the field of epigenetics and epitratrascriptomics, a whole science dedicated to editing DNA using RNA as a screwdriver. See:

RNA USED TO ALTER DNA, BRAIN FUNCTIONS AND BEHAVIOR (BIOHACKING P.2)

And then came these:

WE WRITE NEW DNA USING RNA ONLY – FATHER OF THE HUMAN GENOME PROJECT FINANCED BY EPSTEIN, DARPA AND SCHWAB’S WYSS INST.

BREAKING! PFIZER IS PARTNERING WITH GENE-EDITING COMPANIES TO CORRECT YOUR DNA – CEO ALBERT BOURLA

Now that we are on the same page, in terms of information, I’d like to go back to our new video, there’s a few key points that I’d like to stress:

• They’ve been in the know since Day 1, this is not a surprising side effect, it’s the effect they pursued.
• The above implies intention
• Obviously they have no clue what this will lead to, other than genetic chaos. In the words of Bill Gates “If you want to see the effects after two years, you need to wait two years”. How about 20 or 200 years?
• Cherry on the cake – the newest revelations: 50% truncated mRNA that no one has any clue what it does
• All of the above is potentially irreversible, definitive and transmissible to the future generations. We have no clue what’s going to happen, but your grand-grand-grand kids may all suffer from it. Even if you’re a pure blood, you can get contaminated a million ways.
  AND THAT’S WHAT’S WORSE THEN GENOCIDING A GENERATION IN ONE COUNTRY OR ANOTHER.

Which brings me to another crucial question I launched in the public square long ago, without any satisfactory response:

You all know DNA is described as made of two protein spirals. If you take one and you break it to pieces, the result is hardly different from RNA or their description of a virus.
In which case I would love an expert to explain:

What happens to the DNA debris resulted from cell death, where does it go and can it be mistaken for viruses? Are infections and diseases actually auto-immune attacks?

Here’s a possible starting point:

Mechanisms and physiology of the clearance of dead cells by efferocytosis

Emilio Boada-Romero,¹ Jennifer Martinez,² Bradlee L. Heckmann,^1,† and Douglas R. Green^1,†

Nat Rev Mol Cell Biol. 2020 Jul; 21(7): 398–414.

Published online 2020 Apr 6. doi: 10.1038/s41580-020-0232-1

“Unlike PAMPs, which are derived from microbes, damage-associated molecular patterns (DAMPs) are of cellular origin and can be liberated upon cell death. DAMPs trigger inflammatory responses, and may also serve as chemoattractants for macrophages. DAMPs are metabolically diverse entities, including genomic and mitochondrial DNA, nuclear proteins (HMGB, histones)²⁵, cytoplasmic proteins (S100), cytokines (IL-1α, IL-33, IL-36), and other small molecules (ATP, UTP, uric acid crystals) (Table 1)²⁶. In addition, inflammasome [G] -mediated caspase-1 activation generates inflammatory cytokines IL-1β and IL-18 during pyroptosis (see Box 1) that lead to inflammatory immune activation after cellular demise.²⁷ Below, we review the relevance of DAMPs during efferocytosis, the ability of DAMPs to modulate inflammation, and specific DAMPs and their effects.

DNA as a DAMP. 

Several mechanisms ensure low DNA burden following apoptotic death and contribute to its immune-silent phenotype. In healthy cells, caspase-activated DNase (CAD) exists in complex with its inhibitory chaperone ICAD and remains constitutively inactive in the cytosol^28,29. Active caspase-3 cleaves ICAD^28,30, promoting CAD homodimerization, nuclear translocation, and DNA hydrolysis between nucleosomes. Nuclear pieces are then neatly packaged with cytoplasm into apoptotic bodies that are eventually digested during efferocytosis³¹. In contrast, nuclear and mitochondrial DNA (mtDNA), as well as pathogen-derived DNA molecules in those cells dying due to an infection, can be released to the extracellular environment from non-apoptotic dying cells. Toll-like receptor 9 (TLR9) is activated by unmethylated CpG sequences such as those found in mtDNA or bacterial DNA (Table 1), and activation of TLR9 triggers downstream inflammatory responses. circulating DNA DAMPs can accumulate in the body in cases where non-apoptotic cell death is widespread; for example, mtDNA was found to be elevated in the plasma of trauma patients³², likely as a result of injury-induced cell death.

DNA in the extracellular environment is processed by DNase-I³³, while DNase-III (also known as TREX1) clears cytoplasmic DNA³⁴, and DNase-II processes DNA from dying cells in the phagocyte’s lysosomes to help maintain negligible levels of DNA following efferocytosis. Should DNA escape to the cytosol, it can be recognized by cytosolic DNA sensors³⁵, including cyclic GMP-AMP synthase (cGAS) and the inflammasome component AIM2. cGAS is activated upon cytosolic DNA binding and subsequently catalyzes a reaction between GTP and ATP to form cyclic GMP-AMP (cGAMP)³⁶. The newly synthesized cGAMP binds to and activates the stimulator of interferon genes protein (STING), leading to TANK binding kinase 1 (TBK1)-dependent phosphorylation of the interferon regulatory factor IRF3³⁷. These events trigger the IRF3-mediated activation of a Type I interferon response.

DNase-II-deficient or DNase III-deficient mice die during embryogenesis and this embryonic lethality can be prevented if the response to misplaced DNA is abrogated through deletion of cGAS, STING, or the Type-I interferon receptor (IFNAR)^38–41. It is possible that these DNases function to limit cytosolic DNA following efferocytosis during development, thereby preventing this lethal interferonopathy, although how the DNA of engulfed corpses might be released from the phagosome or lysosome to become cytosolic, triggering such responses, remains unknown.

Similarly, recognition of cytosolic DNA by AIM2 causes AIM2 to recruit and activate caspase-1, resulting in IL-1β processing and release, contributing to inflammation^42,43. Again, when and how defects in the clearance of DNA during efferocytosis may engage AIM2 remains unclear.

Protein DAMPs. 

High mobility group protein B1 (HMGB1) is a nuclear protein that binds to DNA and assists replication, repair and transcription^44,45,46. Although some HMGB1 can be released to the extracellular milieu under steady state conditions⁴⁷ or during apoptosis⁴⁸, it is predominantly released during forms of immunogenic cell death²⁵. Efficient efferocytosis can thus limit the release of HMGB1. Based on its redox status, HMGB1 can function as a chemotactic agent (reduced) or as an inflammatory agent (oxidized)⁴⁹. In its reduced form, HMGB1 can prevent the induction of immune tolerance [G] to antigens associated with the dying cell⁴⁸. Reduced HMGB1 may bind to TLRs or the receptor for advanced glycation end products (RAGE) (Table 1)⁵⁰, leading to immune cell activation and cytokine production. Recently, binding of reduced HMGB1 to the chemokine receptor CXCR4 was observed during tissue regeneration following injury⁵¹, highlighting the possible importance of this molecule in the response to dying cells. S100 proteins can also be released from dying cells⁵², and efferocytosis can limit the release of these proteins from dying cells. Again, TLRs and RAGE appear to be the primary receptors on macrophages that promote inflammatory activation in response to S100 proteins.”

I keep my expectations low, but please surprise me!

To be continued?
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! Articles can always be subject of later editing as a way of perfecting them