168 HOURS

Every person gets the same 168 hours each week. The surprising truth is that your bills don’t stop when you stop working. Your mortgage, rent, utilities, insurance, subscriptions, and everyday expenses continue 24 hours a day, 7 days a week. So why are so many people taught to earn money only 40 hours a week? On this episode of The Paul D. Jones Show, Paul D. Jones challenges the traditional way we’ve been taught to think about work and income. Learn why building income that continues b...