Once we arrive at AGI (artificial general intelligence), the pursuit of ASI (artificial superintelligence) is next. Here is a speculated timeline 2040–2050.

While radiation treatments designed to kill cancer cells have come a long way, scientists and doctors are always exploring new ways to zap tumors more effectively. Recent tests at the U.S. Department of Energy’s (DOE) Brookhaven National Laboratory show that a small array of magnets designed as an offshoot of the Lab’s nuclear physics research could quite literally provide a path for such future cancer treatments.
The tests revealed that an arc of meticulously designed permanent magnets can transport beams of cancer-killing protons over a broad range of energies, from 50 to 250 million electron volts (MeV). “That’s the highest energy ever for this sort of beamline,” said Brookhaven Lab physicist Stephen Brooks, designer of the fixed-field magnets, and it’s an energy range that could enable more effective cancer treatment.
Specifically, the project is a step toward a possible future accelerator built using this technology, where physicians could rapidly switch among beam energies to deliver very fast lethal proton doses throughout a tumor’s depth.
How does America stack up with other civilized countries in it’s treatment of it’s workers… hint — it’s not pretty
A team of researchers from Utrecht University, Durham University, and other institutions have observed something remarkable at a chimpanzee sanctuary in Zambia. Several chimpanzees from one particular group were seen dangling blades of grass from their ear holes or their behinds, for no apparent reason. The behavior was not seen in other chimpanzee groups at the same sanctuary, despite similar living conditions.
Scientists have identified a new type of protein in bacteria that could change our understanding of how these organisms interact with their environments.
A new study, published in Nature Communications, focuses on a protein called PopA, found in the bacterial predator Bdellovibrio bacteriovorus. The protein forms a unique fivefold structure, unlike the usual single or three-part structures seen in similar proteins.
An international research team, led by University of Birmingham scientists, used advanced imaging techniques to reveal that PopA has a bowl-like shape that can trap parts of the bacterial membrane inside it.