Microprocessors  

Researchers at UC Davis have created a new microprocessor, called “KiloCore,” which is made up of 1,000 independent processors. Kilo core has a computed computation rate of 1.78 trillion instructions per second and contains 621 million transistors.

Researchers at California's UC Davis have created a microchip containing 1,000 independent programmable processors. The energy-efficient “KiloCore” chip has a maximum computation rate of 1.78 trillion instructions per second and contains 621 million transistors. The KiloCore was presented at the 2016 Symposium on VLSI Technology and Circuits in Honolulu this month.

“To the best of our knowledge, it is the world’s first 1,000-processor chip and it is the highest clock-rate processor ever designed in a university,” said Bevan Baas, professor of electrical and computer engineering, who led the team that designed the chip architecture. While other multiple-processor chips have been created, none exceed about 300 processors, according to an analysis by Baas’ team. Most were created for research purposes and few are sold commercially. The KiloCore chip was fabricated by IBM using their 32 nm CMOS technology.

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"To the best of our knowledge, it is the world’s first 1,000-processor chip and it is the highest clock-rate processor eve."

Each processor core can run its own small program independently of the others, which is a fundamentally more flexible approach than so-called Single-Instruction-Multiple-Data approaches utilized by processors such as GPUs; the idea is to break an application up into many small pieces, each of which can run in parallel on different processors, enabling high throughput with lower energy use, Baas said.

Each processor is independently clocked, it can shut itself down to further save energy when not needed, said graduate student Brent Bohnenstiehl, who developed the principal architecture. Cores operate at an average maximum clock frequency of 1.78 GHz, and they transfer data directly to each other rather than using a pooled memory area that can become a bottleneck for data.

The chip is the most energy-efficient “many-core” processor ever reported, Baas said. For example, the 1,000 processors can execute 115 billion instructions per second while dissipating only 0.7 Watts, low enough to be powered by a single AA battery. The KiloCore chip executes instructions more than 100 times more efficiently than a modern laptop processor.

Applications already developed for the chip include wireless coding/decoding, video processing, encryption, and others involving large amounts of parallel data such as scientific data applications and datacenter record processing.

The team has completed a compiler and automatic program mapping tools for use in programming the chip.

SOURCE  UC Davis

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 Biofuels  

Gasoline-like fuels can be made from cellulosic materials such as farm and forestry waste using a new process invented by chemists at the University of California, Davis. The process could open up new markets for plant-based fuels, beyond existing diesel substitutes.

Gasoline-like fuels can be made from cellulosic materials such as farm and forestry waste using a new process invented by chemists at the University of California, Davis. The process could open up new markets for plant-based fuels, beyond existing diesel substitutes.

"What's exciting is that there are lots of processes to make linear hydrocarbons, but until now nobody has been able to make branched hydrocarbons with volatility in the gasoline range," said Mark Mascal, professor of chemistry at UC Davis and lead author on the paper published  in the journal Angewandte Chemie.

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Traditional diesel fuel is made up of long, straight chains of carbon atoms, while the molecules that make up gasoline are shorter and branched. That means gasoline and diesel evaporate at different temperatures and pressures, reflected in the different design of diesel and gasoline engines.

Biodiesel, refined from plant-based oils, is already commercially available to run modified diesel engines. A plant-based gasoline replacement would open up a much bigger market for renewable fuels.

The feedstock for the new process is levulinic acid, which can be produced by chemical processing of materials such as straw, corn stalks or even municipal green waste. It's a cheap and practical starting point that can be produced from raw biomass with high yield, Mascal said.

"Essentially it could be any cellulosic material," Mascal said. Because the process does not rely on fermentation, the cellulose does not have to be converted to sugars first.

UC Davis has filed provisional patents on the process. Coauthors on the paper are postdoctoral researchers Saikat Dutta and Inaki Gandarias.


SOURCE  UC Davis

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 Medicine  

Blood clots play an unexpected role in protecting the body from the deadly effects of bacteria by absorbing bacterial toxins, researchers at UC Davis, have found. The discovery may shed light on the pathology of septic shock.

Blood clots play an unexpected role in protecting the body from the deadly effects of bacteria by absorbing bacterial toxins, researchers at the University of California, Davis, have discovered.

"It's a significant addition to the short list of defenses that animals use to protect themselves against toxin-induced sepsis," said Peter Armstrong, professor of molecular and cellular biology at UC Davis and senior author on the paper.

Even with modern antibiotics, septic shock from bacterial infections afflicts about 300,000 people a year in the U.S., with a mortality rate of 30 to 50 percent. Septic shock is caused by Gram-negative bacteria, which release a toxin called lipopolysaccharide or endotoxin. In small amounts, lipopolysaccharide triggers inflammation. When infections with these bacteria get out of hand, lipopolysaccharide courses through the bloodstream, causing catastrophic damage to organs and tissues.

The video above shows a mouse blood clot (red) capturing bacterial toxin (green). Yellow color shows toxin bound to the clot. Pieces of clot break off as blood flows past.

These toxins cause disease in a variety of animal species — lipopolysaccharide is also toxic to both horseshoe crabs and lobsters, separated from humans by hundreds of millions of years of evolution. In humans and other mammals, blood clots quickly form from a mix of specialized blood cells and protein fibers. Arthropods like horseshoe crabs and lobsters can also form clots in response to injury, with a different mix of cells and proteins.

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The research was published in the journal PLoS ONE.

Clots protect and help to seal wounds, prevent blood or body fluids from leaking out and form a physical barrier that entangles and blocks bacteria from entering the body. The new study shows that they also actively soak up lipopolysaccharide, reducing its release from the wound site into the body, where it could cause disease or even death.

Armstrong's laboratory had previously developed fluorescent labels to show that a lipopolysaccharide-like molecule is present in chloroplasts, structures inside cells of green plants that carry out photosynthesis and are thought to be descended from bacteria. As he also studies the role of blood clots in resisting infections, Armstrong decided to test the same techniques on blood clots that had been exposed to bacteria or to bacterial lipopolysaccharide. The fluorescent probes lit up the clots, showing that the clot fibers bound lipopolysaccharide to their surfaces.

"I was ecstatic," Armstrong said. "It was one of those moments that makes the rest of the slogging worthwhile."

Armstrong and colleagues Margaret Armstrong at UC Davis and Frederick Rickles at George Washington University looked at clots of blood, or its equivalent, from humans, mice, lobsters and horseshoe crabs. In all four species, they found that fluorescently tagged lipopolysaccharide was bound to the fibers of the blood clot. The toxin was too tightly attached to be readily removed by chemical treatments that remove weakly bound macromolecules from proteins.

One of the deadly consequences of septic shock is disseminated intravascular coagulation, when blood clots form rapidly throughout the body. But the new results suggest that on a small and local scale, this might be part of a protective mechanism against sepsis — these intravascular clots can soak up quantities of lipopolysaccharide from the blood. They also show that rather than being a simple physical barrier, blood clots play an active and dynamic role in protecting the body from infections.


SOURCE  UC Davis

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