UC SanDiego researchers are using AI and "virtual cells" based on 4D movies to predict how cells will respond to drugs, which could speed up drug discovery for cancer, Alzheimer’s and more.

Autism spectrum disorder (ASD) is associated with more than 1,200 risk genes, raising a fundamental question: Do these diverse genetic changes affect the brain in entirely different ways, or do they converge on shared biological mechanisms?

A research team led by Professor KIM Eunjoon of the Center for Synaptic Brain Dysfunctions within the Institute for Basic Science (IBS) has identified two opposing patterns of brain gene activity across mice carrying different autism-risk mutations. By analyzing more than 1,000 mouse brain transcriptomes, the researchers found that genetically distinct models could be grouped according to shared molecular changes, offering a new framework for investigating autism-related mechanisms and responses to experimental drugs.

The paper introduces three interconnected resources for the global scientific community:

LongevityBench, the first open benchmark designed to rigorously evaluate AI reasoning across multiple domains of aging biology;

Longevity-LLMs, a family of compact, open-source language models specifically trained on clinical and multi-omics aging data; and

Longevity Claw, an open-source agentic research platform that autonomously integrates specialized longevity tools to identify and prioritize potential therapeutic targets.

Researchers at the Icahn School of Medicine at Mount Sinai and collaborators have identified candidate treatment targets and potential prognostic markers for high-grade glioma, an aggressive brain cancer, in children, adolescents, and young adults. The study found that high-grade glioma varies by developmental stage and sex, showing distinct tumor biology and outcomes across patient groups. Using this information to guide clinical trial design and develop new therapies could advance more precise treatment strategies. The findings were published in Cell Reports Medicine.

Cells rely on complex signaling networks in which different molecular pathways communicate with one another. Small GTPases act as molecular switches in these networks, controlling diverse cellular processes such as intracellular transport and cell morphogenesis. Although crosstalk between different families of small GTPases is established in animal cells, whether and how such crosstalk occurs in plants has remained largely unknown.

A research team led by Associate Professor Emi Ito and Professor Takashi Ueda at the National Institute for Basic Biology (NIBB), together with collaborators at Ochanomizu University, Kyoto Prefectural University, Saitama University, Nagoya University, and RIKEN, has now uncovered a molecular mechanism that connects two distinct types of small GTPases in the model plant Arabidopsis thaliana. The study was published in Nature Plants.

The researchers identified a protein called REAP1/SWAP70 that links RAB5, a small GTPase involved in intracellular membrane trafficking, with ROP7, a member of the plant-specific ROP (Rho of Plants) family of small GTPases involved in processes such as cell morphogenesis. Their findings reveal a previously unknown RAB5–REAP1–ROP7 signaling pathway and show that this pathway plays an important role in normal pollen development.

Neurodegenerative diseases, cerebrovascular disorders and other age-related neurological conditions are major causes of long-term disability. A review published in SCIENCE CHINA Life Sciences by researchers from Huashan Hospital, Fudan University, examines how damaged nuclear DNA and mitochondrial DNA can become immune danger signals. The authors highlight cGAS-STING as a key molecular hub linking cellular damage, inflammaging and neuroimmune dysfunction, and discuss opportunities for more precise therapeutic intervention.

Researchers have uncovered an unexpected antiviral role for PGK1, an enzyme best known for its function in glucose metabolism. Acting through its non-canonical protein kinase activity, PGK1 phosphorylates the host protein heat shock protein 90-alpha (HSP90AA1), reduces its chaperone function, and promotes its proteasomal degradation. The resulting loss of viral protein stability restricts the replication of several RNA and DNA viruses, highlighting a potential host-directed antiviral strategy.