Lei Wang

Yanqi Dai, Huanran Hu, Lei Wang et al.

Recently, Role-Playing Agents (RPAs) have garnered increasing attention for their potential to deliver emotional value and facilitate sociological research. However, existing studies are primarily confined to the textual modality, unable to simulate humans' multimodal perceptual capabilities. To bridge this gap, we introduce the concept of Multimodal Role-Playing Agents (MRPAs), and propose a comprehensive framework, MMRole, for their development and evaluation, which comprises a personalized multimodal dataset and a robust evaluation approach. Specifically, we construct a large-scale, high-quality dataset, MMRole-Data, consisting of 85 characters, 11K images, and 14K single or multi-turn dialogues. Additionally, we present a robust evaluation approach, MMRole-Eval, encompassing eight metrics across three dimensions, where a reward model is designed to score MRPAs with the constructed ground-truth data for comparison. Moreover, we develop the first specialized MRPA, MMRole-Agent. Extensive evaluation results demonstrate the improved performance of MMRole-Agent and highlight the primary challenges in developing MRPAs, emphasizing the need for enhanced multimodal understanding and role-playing consistency. The data, code, and models are all available at https://github.com/YanqiDai/MMRole.

Wenbin Li, Ziyi, Wang et al.

Few-shot learning, especially few-shot image classification, has received increasing attention and witnessed significant advances in recent years. Some recent studies implicitly show that many generic techniques or ``tricks'', such as data augmentation, pre-training, knowledge distillation, and self-supervision, may greatly boost the performance of a few-shot learning method. Moreover, different works may employ different software platforms, backbone architectures and input image sizes, making fair comparisons difficult and practitioners struggle with reproducibility. To address these situations, we propose a comprehensive library for few-shot learning (LibFewShot) by re-implementing eighteen state-of-the-art few-shot learning methods in a unified framework with the same single codebase in PyTorch. Furthermore, based on LibFewShot, we provide comprehensive evaluations on multiple benchmarks with various backbone architectures to evaluate common pitfalls and effects of different training tricks. In addition, with respect to the recent doubts on the necessity of meta- or episodic-training mechanism, our evaluation results confirm that such a mechanism is still necessary especially when combined with pre-training. We hope our work can not only lower the barriers for beginners to enter the area of few-shot learning but also elucidate the effects of nontrivial tricks to facilitate intrinsic research on few-shot learning. The source code is available from https://github.com/RL-VIG/LibFewShot.

Xiaoqi Ling, Cheng Cai, Demin Kong et al.

Computational protein design (CPD) refers to the use of computational methods to design proteins. Traditional methods relying on energy functions and heuristic algorithms for sequence design are inefficient and do not meet the demands of the big data era in biomolecules, with their accuracy limited by the energy functions and search algorithms. Existing deep learning methods are constrained by the learning capabilities of the networks, failing to extract effective information from sparse protein structures, which limits the accuracy of protein design. To address these shortcomings, we developed an Efficient attention-based Models for Computational Protein Design using amino acid microenvironment (EMOCPD). It aims to predict the category of each amino acid in a protein by analyzing the three-dimensional atomic environment surrounding the amino acids, and optimize the protein based on the predicted high-probability potential amino acid categories. EMOCPD employs a multi-head attention mechanism to focus on important features in the sparse protein microenvironment and utilizes an inverse residual structure to optimize the network architecture. The proposed EMOCPD achieves over 80% accuracy on the training set and 68.33% and 62.32% accuracy on two independent test sets, respectively, surpassing the best comparative methods by over 10%. In protein design, the thermal stability and protein expression of the predicted mutants from EMOCPD show significant improvements compared to the wild type, effectively validating EMOCPD's potential in designing superior proteins. Furthermore, the predictions of EMOCPD are influenced positively, negatively, or have minimal impact based on the content of the 20 amino acids, categorizing amino acids as positive, negative, or neutral. Research findings indicate that EMOCPD is more suitable for designing proteins with lower contents of negative amino acids.