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Researchers from the Henry and Marilyn Taub Faculty of Computer Science have developed an AI-based method that accelerates DNA-based data retrieval by three orders of magnitude while significantly improving accuracy. The research team included Ph.D. student Omer Sabary, Dr. Daniella Bar-Lev, Dr. Itai Orr, Prof. Eitan Yaakobi, and Prof. Tuvi Etzion.

Imagine building a Lego tower with perfectly aligned blocks. Each block represents an atom in a tiny crystal, known as a quantum dot. Just like bumping the tower can shift the blocks and change its structure, external forces can shift the atoms in a quantum dot, breaking its symmetry and affecting its properties.

Scientists have learned that they can intentionally cause symmetry breaking—or symmetry restoration—in quantum dots to create new materials with unique properties. In a recent study, researchers at the U.S. Department of Energy’s (DOE) Argonne National Laboratory have discovered how to use light to change the arrangement of atoms in these minuscule structures.

Quantum dots made of semiconductor materials, such as lead sulfide, are known for their unique optical and due to their tiny size, giving them the potential to revolutionize fields such as electronics and medical imaging. By harnessing the ability to control symmetry in these quantum dots, scientists can tailor the materials to have specific light and electricity-related properties. This research opens up new possibilities for designing materials that can perform tasks previously thought impossible, offering a pathway to innovative technologies.

Ubiquitin marks proteins for degradation, whereby ubiquitin molecules can be combined in different types and numbers forming different chains. Researchers at the Max Planck Institute of Biochemistry (MPIB) have developed the new UbiREAD technology to decode the various combinations of ubiquitin molecules—the ubiquitin code—which determine how proteins are degraded in cells.

Using UbiREAD, scientists label with specific codes and track their degradation in cells. The study, published in Molecular Cell, revealed which ubiquitin code can or cannot induce intracellular protein degradation.

Proteins are the building blocks of life, maintaining cellular structure and function. However, when proteins become damaged, misfolded, or obsolete, they can lead to a range of diseases, from Alzheimer’s and Parkinson’s to cancer and muscular dystrophy. To prevent this, cells have developed a sophisticated system to mark unwanted proteins for degradation with a small protein called ubiquitin.

Terahertz (THz) waves are located between microwaves and infrared light in the electromagnetic spectrum. They can pass through many materials without causing damage, making them useful for security scanning, medical imaging, and high-speed wireless communication. Unlike visible light or radio waves, THz waves can reveal structural details of biological molecules and penetrate nonmetallic objects like clothing and paper.

THz waves hold great promise, but to harness them effectively, their polarization (the direction in which the waves vibrate) must be controlled. Polarization control is crucial for optimizing THz applications, from enhancing to improving imaging and sensing.

Unfortunately, existing THz polarization control methods rely on bulky external components like wave plates or metamaterials. These solutions are often inefficient, limited to narrow frequency ranges, and unsuitable for compact devices. To overcome these limitations, researchers have been exploring approaches to control THz polarization directly at the source.

Type 2 diabetes may quietly alter the brain in ways that mimic early Alzheimer’s, weakening reward perception and memory signals in a key brain area called the anterior cingulate cortex (ACC). In a rat study, diabetic animals still behaved normally but processed rewarding locations differently, s

Scientists at EMBL have captured how human chromosomes fold into their signature rod shape during cell division, using a groundbreaking method called LoopTrace. By observing overlapping DNA loops forming in high resolution, they revealed that large loops form first, followed by nested smaller loo

A research team led by Professor Hyung-Joon Shin from the Department of Materials Science and Engineering at UNIST has succeeded in elucidating the quantum phenomenon occurring within a triangular cluster of three water molecules. The work is published in the journal Nano Letters.

Their findings demonstrate that the collective rotational motion of water molecules enhances proton tunneling, a quantum mechanical effect where protons (H+) bypass energy barriers instead of overcoming them. This phenomenon has implications for and the stability of biomolecules such as DNA.

The study reveals that when the rotational motion of water molecules is activated, the distances between the molecules adjust, resulting in increased cooperativity and facilitating proton tunneling. This process allows the three protons from the water molecules to collectively surmount the energy barrier.

In an unprecedented move, precision medicine provider Human Longevity, Inc. (HLI) has effectively guaranteed its Executive Health Program members that it will prevent them from developing late stage prostate cancer. Such is the company’s belief in its preventive approach, it has announced it is committing $1 million for advanced treatment of any member diagnosed with stage four of the disease or higher while under its care.

Founded in 2013 by genomics pioneer Dr J Craig Venter, San Francisco-based Human Longevity Inc. (HLI) aims to extend human health and performance beyond the traditional focus on treating illness. By continuously analyzing health data from its clients, HLI seeks to identify potential health risks – such as prostate cancer – early, enabling targeted interventions to extend both healthspan and lifespan.

Leveraging data collected from more than 5,000 men over the past decade, HLI claims it has developed what it believes to be the most advanced algorithm for early prostate cancer detection. As preventive medicine continues to demonstrate its capacity to mitigate previously life-threatening conditions, will we see commitments of this nature emerging for more diseases?

The study is the first to use a cutting-edge technique called spatial transcriptomics on human clinical-trial brains with Alzheimer’s disease. The technique allows scientists to pinpoint the specific spatial location of gene activity inside a tissue sample.

By analyzing donated brain tissue from deceased people with Alzheimer’s disease who received amyloid-beta immunization and comparing it to those who did not, the scientists found that when these treatments work, the brain’s immune cells (called microglia) don’t just clear plaques — they also help restore a healthier brain environment.

But not all microglia are created equal. Some are quite effective at removing plaques, while others struggle, the study found. Also, microglia in treated brains adopt distinct states depending on the brain region and type of immunization. Lastly, certain genes, like TREM2 and APOE, are more active in microglia in response to treatment, helping these cells remove amyloid beta plaques, according to the findings.

“The idea is that in people who already have Alzheimer’s disease, yes, you can maybe remove amyloid, but if the tau spread has been set in motion, you are fighting an uphill battle,” the author said. “But maybe, if you treat people so early that they don’t yet have tau pathology, you can stop the domino effect from happening. Our study is the first to identify the mechanisms in microglia, the brain’s immune cells, that help limit the spread of amyloid in certain brain regions following treatment with amyloid-targeting drugs.


For more than three decades, scientists have been racing to stop Alzheimer’s disease by removing amyloid beta plaques — sticky clumps of toxic protein that accumulate in the brain. Now, a new study suggests a promising alternative: enhancing the brain’s own immune cells to clear these plaques more effectively.

The findings could reshape the future of Alzheimer’s treatments, shifting the focus from simply removing plaques to harnessing the brain’s natural defenses.

Earlier attempts at an Alzheimer’s vaccine failed when the immune system’s response caused dangerous brain swelling. Even today’s FDA-approved antibody treatments remain controversial, offering only modest benefits with potential side effects and high-price points.