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It's a fact that Americans are spending more than they earn, and they can only work 40 - 60 hours each week and it seems like it still comes short of making ends meet and some left to enjoy life.

The Answer is in front of us everyday right here on the Internet, but we don't seem to "get it" because of the stupid gossip about not trusting anything that costs even a dollar from some you don't know. Bunk ...

There's a new attitude among the people who have seen proof of what can be achieved by others, and then once proven we take the tour or ask for more details on how to get started.

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