arXiv:2505.22564v2 Announce Type: replace-cross Abstract: Video dataset condensation aims to reduce the immense computational cost of video processing. However, it faces a fundamental challenge regarding the inseparable interdependence between spatial appearance and temporal dynamics. Prior work follows a static/dynamic disentanglement paradigm where videos are decomposed into static content and auxiliary motion signals. This multi-stage approach often misrepresents the intrinsic coupling of real-world actions. We introduce Progressive Refinement and Insertion for Sparse Motion (PRISM), a holistic approach that treats the video as a unified and fully coupled spatiotemporal structure from the outset. To maximize representational efficiency, PRISM addresses the inherent temporal redundancy of video by avoiding fixed-frame optimization. It begins with minimal temporal anchors and progressively inserts key-frames only where linear interpolation fails to capture non-linear dynamics. These critical moments are identified through gradient misalignments. Such an adaptive process ensures that representational capacity is allocated precisely where needed, minimizing storage requirements while preserving complex motion. Extensive experiments demonstrate that PRISM achieves competitive performance across standard benchmarks while providing state-of-the-art storage efficiency through its sparse and holistically learned representation.

arXiv:2512.00126v2 Announce Type: replace-cross Abstract: Protein inverse folding, the design of an amino acid sequence based on a target protein structure, is a fundamental problem of computational protein engineering. Existing methods either generate sequences without leveraging external knowledge or relying on protein language models~(PLMs). The former omits the knowledge stored in natural protein data, while the latter is parameter-inefficient and inflexible to adapt to ever-growing protein data. To overcome the above drawbacks, in this paper we propose a novel method, called $\underline{\text{r}}$etrieval-$\underline{\text{a}}$ugmented $\underline{\text{d}}$enoising $\underline{\text{diff}}$usion~($\mbox{RadDiff}$), for protein inverse folding. In RadDiff, a novel retrieval-augmentation mechanism is designed to capture the up-to-date protein knowledge. We further design a knowledge-aware diffusion model that integrates this protein knowledge into the diffusion process via a lightweight module. Experimental results on the CATH, TS50, and PDB2022 datasets show that $\mbox{RadDiff}$ consistently outperforms existing methods, improving sequence recovery rate by up to 19\%. Experimental results also demonstrate that RadDiff generates highly foldable sequences and scales effectively with database size.