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Fine-tuning large language models (LLMs) often exceeds GPU memory limits, prompting systems to offload model states to CPU memory. However, existing offloaded training frameworks like ZeRO-Offload treat all parameters equally and update the full model on the CPU, causing severe GPU stalls, where fast, expensive GPUs sit idle, waiting for slow CPU updates and limited-bandwidth PCIe transfers. We present ZenFlow, a new offloaded training framework that decouples updates between GPU and CPU by prioritizing important gradients. ZenFlow performs in-place updates of important gradients on GPU while offloading and accumulating less important ones on CPU without blocking training iterations, fully overlapping CPU work with GPU computation. To make this importance-aware design scalable, ZenFlow leverages a novel spatio-temporal locality of important gradients—concentrated in specific positions that remain stable across iterations—to make important gradient identification efficient and lightweight while preserving fidelity. Evaluation shows that ZenFlow achieves up to 5×end-to-end speedup, 2×lower PCIe traffic, 85% less GPU stalls, and up to 72% lower cloud GPU cost, all while preserving accuracy. 

ABSTRACT AST3-2 is the second of the three Antarctic Survey Telescopes, aimed at wide-field time-domain optical astronomy. It is located at Dome A, Antarctica, which is by many measures the best optical astronomy site on the Earth’s surface. Here we present the data from the AST3-2 automatic survey in 2016 and the photometry results. The median 5σ limiting magnitude in i-band is 17.8 mag and the light-curve precision is 4 mmag for bright stars. The data release includes photometry for over 7 million stars, from which over 3500 variable stars were detected, with 70 of them newly discovered. We classify these new variables into different types by combining their light-curve features with stellar properties from surveys such as StarHorse. 

Abstract Protein tyrosine O -sulfation (PTS) plays a crucial role in extracellular biomolecular interactions that dictate various cellular processes. It also involves in the development of many human diseases. Regardless of recent progress, our current understanding of PTS is still in its infancy. To promote and facilitate relevant studies, a generally applicable method is needed to enable efficient expression of sulfoproteins with defined sulfation sites in live mammalian cells. Here we report the engineering, in vitro biochemical characterization, structural study, and in vivo functional verification of a tyrosyl-tRNA synthetase mutant for the genetic encoding of sulfotyrosine in mammalian cells. We further apply this chemical biology tool to cell-based studies on the role of a sulfation site in the activation of chemokine receptor CXCR4 by its ligand. Our work will not only facilitate cellular studies of PTS, but also paves the way for economical production of sulfated proteins as therapeutic agents in mammalian systems.