Zhongju Yuan

Zhongju Yuan, Zhenkun Wang, Genghui Li

Few-shot relation extraction aims to recognize novel relations with few labeled sentences in each relation. Previous metric-based few-shot relation extraction algorithms identify relationships by comparing the prototypes generated by the few labeled sentences embedding with the embeddings of the query sentences using a trained metric function. However, as these domains always have considerable differences from those in the training dataset, the generalization ability of these approaches on unseen relations in many domains is limited. Since the prototype is necessary for obtaining relationships between entities in the latent space, we suggest learning more interpretable and efficient prototypes from prior knowledge and the intrinsic semantics of relations to extract new relations in various domains more effectively. By exploring the relationships between relations using prior information, we effectively improve the prototype representation of relations. By using contrastive learning to make the classification margins between sentence embedding more distinct, the prototype's geometric interpretability is enhanced. Additionally, utilizing a transfer learning approach for the cross-domain problem allows the generation process of the prototype to account for the gap between other domains, making the prototype more robust and enabling the better extraction of associations across multiple domains. The experiment results on the benchmark FewRel dataset demonstrate the advantages of the suggested method over some state-of-the-art approaches.

Zhongju Yuan, Tao Shen, Sheng Xu et al.

Deep learning-based approaches, such as AlphaFold2 (AF2), have significantly advanced protein tertiary structure prediction, achieving results comparable to real biological experimental methods. While AF2 has shown limitations in predicting the effects of mutations, its robustness against sequence mutations remains to be determined. Starting with the wild-type (WT) sequence, we investigate adversarial sequences generated via an evolutionary approach, which AF2 predicts to be substantially different from WT. Our experiments on CASP14 reveal that by modifying merely three residues in the protein sequence using a combination of replacement, deletion, and insertion strategies, the alteration in AF2's predictions, as measured by the Local Distance Difference Test (lDDT), reaches 46.61. Moreover, when applied to a specific protein, SPNS2, our proposed algorithm successfully identifies biologically meaningful residues critical to protein structure determination and potentially indicates alternative conformations, thus significantly expediting the experimental process.