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Updates every hour. Last Updated: 20-Oct-2026 04:16 ET (20-Oct-2026 08:16 GMT/UTC)
Researchers at the Research Center for Materials Nanoarchitectonics (MANA), one of the centers under the National Institute for Materials Science (NIMS), Japan, discovered that atomic-scale steps can guide superconducting vortices in an ultrathin superconductor. Vortices moved more than 1,000 times more easily along the steps than across them, and this guiding effect could be tuned by temperature and magnetic field.
Humans stand apart from other great apes: we walk on two legs, carry unusually large brains, and have slender, distinctively shaped skeletons. Yet which changes in our DNA produced these features has remained one of biology’s great open questions. Human and chimpanzee genomes are more than 98% identical, and the genes themselves, the blueprints for proteins, barely differ. The changes that make us human are thought to hide instead in the DNA that controls when and where genes switch on.
A team led by Associate Professor Fumitaka Inoue and researcher Yizhi Yan at Kyoto University’s Institute for the Advanced Study of Human Biology (WPI-ASHBi), together with Principal Investigator David Gokhman and Nadav Mishol at the Weizmann Institute of Science, has now built the world’s first functional atlas of the human-specific gene-control changes behind our skeleton. Combining two powerful techniques (massively parallel reporter assays, or MPRA, and human-ape hybrid cells), they discovered that a family of molecules called glycosaminoglycans (GAGs), which cushion and maintain our cartilage, has been dialed down over the course of human evolution. The finding offers a new window onto how the human skeleton took its shape, and onto why we are so uniquely susceptible to skeletal disease.
The work will be published in Nature on 23 September 2026 at 11:00 EST.Researchers at the Nano Life Science Institute (WPI-NanoLSI) at Kanazawa University, Kyoto University, SOKENDAI, and the National Institute for Physiological Sciences have revealed how CaMKIIα—a key brain protein involved in learning and memory—organizes itself into chain-like structures. Their study, published in Science Advances, shows how activation causes these protein structures to grow and how a mutation associated with neurodevelopmental disorders changes their organization, findings that could deepen our understanding of memory formation and neurological disease.
As new memories form the connections between brain cells can become stronger. A protein called CaMKIIα plays an important part in this process and is found in especially large amounts at the points where brain cells communicate. Scientists have long known that more of this protein gathers at active connections, but they have not been able to see clearly how the individual protein molecules come together.
In the new study, a team led by Mikihiro Shibata, used high-speed atomic force microscopy, a technique that can visualize individual molecules at very high resolution, to observe how CaMKIIα molecules move and interact in real time. The researchers discovered that, under crowded conditions similar to those inside brain-cell connections, the molecules join together to form chain-like structures.Researchers have developed an AI-based system that automatically and objectively detects the moment when fish experience loss of equilibrium (LOE) due to temperature stress. The system combines DeepLabCut, a deep-learning AI that captures animal posture from video, with ResNet34, a deep-learning AI-based image-classification technology. Their system is expected to help predict the effects of climate change on fish. The research team was led by Specially Appointed Lecturer Tomoya Nakayama and Yoshiya Matsuo (a master’s student at the time) of the Institute of Transformative Bio-Molecules (WPI-ITbM) at Nagoya University, in collaboration with Associate Professor Tatsuto Hasegawa and Takuya Kato (a master’s student at the time) of the University of Fukui. Their research was published in the journal Scientific Reports on September 10, 2026.
A team led by the University of Osaka researchers discovered that cells producing IgG1 antibodies multiply more, are less prone to cell death in the spleen, and migrate more efficiently to the bone marrow, where long-lived antibody-producing cells can become established. Understanding how these cells gain these advantages could help researchers design vaccines that provide longer-lasting protection against infection.