Lifeboat Foundation: Safeguarding Humanity
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Former Google CEO Eric Schmidt is taking over as the CEO of Relativity Space, a 9-year-old rocket startup, a company spokesperson confirmed in a statement to TechCrunch. This is Schmidt’s first CEO job since he left Google nearly 15 years ago.

On Monday, Schmidt told employees of Relativity Space that he made a significant investment and had taken a controlling stake in the company, The New York Times first reported.

Schmidt is succeeding the startup’s co-founder, Tim Ellis, as chief executive. In a post on X, Ellis noted he will continue to support Relativity Space as a director on the company’s board.

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An artificial nerve that is based on a vertical n-type organic electrochemical transistor with a gradient-intermixed bicontinuous structure can operate at high frequencies and mimic basic conditioned reflex behaviour in animals.

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Billions of people may be continuously running AI inference for their waking hours in the near future. Satisfying this demand requires relentless focus on efficiency to reduce the required quantities of two key inputs: energy and capital. The constraints on these inputs in conjunction with the slowing and/or stagnation of both Moore’s Law and Dennard Scaling has left hardware architects no choice but to pursue Domain Specific Architectures (DSAs) — architectures tailored to the task at hand.

The current dominance of GPUs in modern deep learning is largely accidental — it was pure serendipity that the computational workload of graphics and deep learning were similar. Remnants of their graphical heritage still persist in GPU architectures today. What would AI inference hardware look like if it was redesigned carte blanche? By working backwards from the AI inference workload, we can determine some optimal properties these DSAs should have. Furthermore, we will attempt to predict the direction the inference paradigm will shift over time — a crucial exercise for hardware architects and engineers alike to ensure return on investment.

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Epstein-Barr virus (EBV) is a common virus that causes mononucleosis, or mono for short, and is associated with some types of cancer and autoimmune diseases. Despite EBV’s known effects and potential to cause disease, there are few therapeutic options and no licensed vaccines targeting the virus. Looking for ways to counter EBV, NIAID researchers are examining how the virus recognizes and interacts with cells at the molecular level. New research published in Immunity reveals the high-resolution crystal structure of a protein on the surface of EBV in complex with the receptor it binds to on the surface of human immune cells, called B cells. The researchers also discovered antibodies that potently neutralize EBV and found that they recognize the viral surface protein using interactions similar to those between EBV and its receptor on host cells. This research identifies a vulnerable site on EBV that could lead to the design of much-needed interventions against the virus.

EBV, also known as human herpesvirus 4, is one of the most common human viruses—nine out of ten people have or will have EBV in their lifetime. After being infected with EBV, many people experience no symptoms, but some experience symptoms of mononucleosis, such as fever, sore throat and fatigue. These symptoms are often mild but can be more severe in teens or adults. After the early stages of infection, the virus hides in the body and can emerge later in life or when the immune system is weakened. Recent studies have also found that EBV is linked to several types of cancer, autoimmune diseases including lupus, and other disorders.

A key step in EBV infection is for the virus to enter a cell in the body, which begins with the virus binding to a protein on the cell’s surface. The researchers, led by Dr. Masaru Kanekiyo, chief of the Molecular Immunoengineering Section at NIAID’s Vaccine Research Center, examined the atomic-level structure of an EBV surface protein called gp350 when bound to a protein on the surface of B cells called complement receptor type 2 (CR2). Usually, CR2 binds to a protein fragment, or ligand, called complement component C3d as a part of the immune response following a viral infection. The researchers found that the EBV protein precisely bound to the cell surface protein CR2 at the region where its natural ligand C3d binds, revealing that there is structural similarity between EBV and C3d in recognizing CR2 and how the virus exploits this interaction to enter and infect a cell.

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Crewless tanks.

As the newest generation platform within the RIPSAW family of vehicles, the M3 inherits the proven functionality and reliability of its predecessor in a more modular, mission-capable system, enhancing both soldier safety and mission success, according to the company.

The vehicle incorporates the familiar large, open deck area from the RIPSAW M5 robotic vehicle, and 10kW of offload power provides the flexibility to support multiple lethality, RSTA, combat engineering, and logistics payloads. With a powerful hybrid electric drivetrain and novel suspension, the RIPSAW M3 provides unmatched mobility with over 180 miles of range.

The company has completed over 2,500 miles of pre-delivery durability testing and refinement to ensure a rugged, reliable platform.

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Getting seven experiments on the International Space Station requires a really good idea. Like a brand new way to attack tumors—one that you can only make in space.

Space has unique advantages for making medicines. Its very makes it possible to grow molecules in shapes and uniformity that are difficult to create on Earth. If they can be reliably and affordably produced, such molecules could have all kinds of novel uses in industry and medicine.

University of Connecticut engineer Yupeng Chen has been growing one such unusually rod-shaped nanoparticle, called a Janus base nanotube, on the International Space Station (ISS).

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Summary: New research highlights a critical link between antibodies produced against Epstein-Barr virus (EBV) and the development of multiple sclerosis (MS). Scientists discovered that these viral antibodies mistakenly target a protein called GlialCAM in the brain, triggering autoimmune responses associated with MS.

The study also revealed how combinations of genetic risk factors and elevated viral antibodies further increase the risk of developing MS. These insights may pave the way for improved diagnostics and targeted therapies, enhancing our understanding of the genetic and immunological interplay underlying this debilitating disease.

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