https://www.bitchute.com/video/AXEAGQoUJ8o/

#StephanieSeneff, a senior #research scientist at the Massachusetts Institute of Technology (MIT), has been studying #glyphosate for years and has been a champion for helping to understand how and why glyphosate is so #dangerous.

The increase in glyphosate usage in the U.S., as well as in Canada, is extremely well correlated with the concurrent increase in the incidence of multiple diseases, including breast cancer, pancreatic cancer, kidney cancer, thyroid cancer, liver cancer, bladder cancer and myeloid leukemia.9

Research scientist Anthony Samsel is one of Seneff’s co-authors, and together they’ve suggested that one of the ways glyphosate is harmful is via disruption of glycine homeostasis. Glyphosate has a glycine molecule as part of its structure (hence the “gly” in glyphosate). Glycine is a very common amino acid your body uses to make proteins.

Samsel and Seneff believe your body can substitute glyphosate and its metabolite aminomethylphosphonic acid (AMPA) into peptides and proteins, which results in damaged peptides and proteins being produced. According to Seneff as she explains in the video above:

“I believe that in certain proteins, in certain spots, glyphosate is able to get into the protein by mistake in place of the amino acid glycine. And to understand that glyphosate is a complete glycine molecule. It's a perfect match to glycine. Except that it has extra materials stuck onto its nitrogen atom.

… the protein that's going to recognize glycine in order to put it into DNA has to leave the nitrogen atom outside of its pocket because the nitrogen has to hook up with the next amino acid. So the fact that the nitrogen has some stuff on it doesn't matter to it. It says, ‘Oh, I have to fit exactly glycine very tightly.’

Glycine is the smallest amino acid. And in order to distinguish glycine from all the other amino acids all I need to do is make sure that I make a tiny space that fits only glycine …

Glyphosate will fit because it's a perfect glycine molecule. Except the nitrogen is sticking outside of that pocket so that it could hook. So the extra stuff on nitrogen is not constrained. This is important because I think a lot of people think, ‘Oh, it can't happen.’”

Going back to EPSPS, the bacterial version of EPSPS inserted into glyphosate-resistant Roundup Ready crop has alanine instead of glycine. But, according to Seneff, if you change the glycine into alanine by adding one extra methyl group, it ruins the protein.

“This is absolutely terrifying,” Seneff says. “They knew, ‘First we've got to get rid of glycine.’ And then that takes a hit on the enzyme. The enzyme doesn't work as well because it's got alanine there. It's got that extra methyl group that's in the way — the same problem that glyphosate causes.”

The arguments for why glyphosate specifically disrupts proteins that depend on glycine for phosphate binding are described more fully in a paper Seneff published together with colleagues arguing that glyphosate is a major factor in kidney failure among young agricultural workers in Central America.10