Trimming Down Large Spiking Vision Transformers via Heterogeneous Quantization Search

Spiking Neural Networks (SNNs) are amenable to deployment on edge devices and neuromorphic hardware due to their lower dissipation. Recently, SNN-based transformers have garnered significant interest, incorporating attention mechanisms akin to their counterparts in Artificial Neural Networks (ANNs) while demonstrating excellent performance. However, deploying large spiking transformer models on resource-constrained edge devices such as mobile phones, still poses significant challenges resulted from the high computational demands of large uncompressed high-precision models. In this work, we introduce a novel heterogeneous quantization method for compressing spiking transformers through layer-wise quantization. Our approach optimizes the quantization of each layer using one of two distinct quantization schemes, i.e., uniform or power-of-two quantification, with mixed bit resolutions. Our heterogeneous quantization demonstrates the feasibility of maintaining high performance for spiking transformers while utilizing an average effective resolution of 3.14-3.67 bits with less than a 1% accuracy drop on DVS Gesture and CIFAR10-DVS datasets. It attains a model compression rate of 8.71x-10.19x for standard floating-point spiking transformers. Moreover, the proposed approach achieves a significant energy reduction of 5.69x, 8.72x, and 10.2x while maintaining high accuracy levels of 85.3%, 97.57%, and 80.4% on N-Caltech101, DVS-Gesture, and CIFAR10-DVS datasets, respectively.

DarkSAM: Fooling Segment Anything Model to Segment Nothing

Segment Anything Model (SAM) has recently gained much attention for its outstanding generalization to unseen data and tasks. Despite its promising prospect, the vulnerabilities of SAM, especially to universal adversarial perturbation (UAP) have not been thoroughly investigated yet. In this paper, we propose DarkSAM, the first prompt-free universal attack framework against SAM, including a semantic decoupling-based spatial attack and a texture distortion-based frequency attack. We first divide the output of SAM into foreground and background. Then, we design a shadow target strategy to obtain the semantic blueprint of the image as the attack target. DarkSAM is dedicated to fooling SAM by extracting and destroying crucial object features from images in both spatial and frequency domains. In the spatial domain, we disrupt the semantics of both the foreground and background in the image to confuse SAM. In the frequency domain, we further enhance the attack effectiveness by distorting the high-frequency components (i.e., texture information) of the image. Consequently, with a single UAP, DarkSAM renders SAM incapable of segmenting objects across diverse images with varying prompts. Experimental results on four datasets for SAM and its two variant models demonstrate the powerful attack capability and transferability of DarkSAM.

Joint Design of Protein Sequence and Structure based on Motifs

Designing novel proteins with desired functions is crucial in biology and chemistry. However, most existing work focus on protein sequence design, leaving protein sequence and structure co-design underexplored. In this paper, we propose GeoPro, a method to design protein backbone structure and sequence jointly. Our motivation is that protein sequence and its backbone structure constrain each other, and thus joint design of both can not only avoid nonfolding and misfolding but also produce more diverse candidates with desired functions. To this end, GeoPro is powered by an equivariant encoder for three-dimensional (3D) backbone structure and a protein sequence decoder guided by 3D geometry. Experimental results on two biologically significant metalloprotein datasets, including $\beta$-lactamases and myoglobins, show that our proposed GeoPro outperforms several strong baselines on most metrics. Remarkably, our method discovers novel $\beta$-lactamases and myoglobins which are not present in protein data bank (PDB) and UniProt. These proteins exhibit stable folding and active site environments reminiscent of those of natural proteins, demonstrating their excellent potential to be biologically functional.