A Segmentation Method Based on PDNet for Chest X-rays with Targets in Different Positions and Directions

To assess the impact of the relative displacement between machines and subjects, the machine angle and the fine-tuning of the subject posture on the segmentation accuracy of chest X-rays, this paper proposes a Position and Direction Network (PDNet) for chest X-rays with different angles and positions that provides more comprehensive information for cardiac image diagnosis and guided surgery. The implementation of PDnet was as follows: First, the extended database image was sent to a traditional segmentation network for training to prove that the network does not have linear invariant characteristics. Then, we evaluated the performance of the mask in the middle layers of the network and added a weight mask that identifies the position and direction of the object in the middle layer, thus improving the accuracy of segmenting targets at different positions and angles. Finally, the active-shape model (ASM) was used to postprocess the network segmentation results, allowing the model to be effectively applied to 2014 × 2014 or higher definition chest X-rays. The experimental comparison of LinkNet, ResNet, U-Net, and DeepLap networks before and after the improvement shows that its segmentation accuracy (MIoU) are 5%, 6%, 20%, and 13% better. Their differences of losses are 11.24%, 21.96%, 18.53%, and 13.43% and F-scores also show the improved networks are more stable.

Expedient Synthesis of Ubiquitin‐like Protein ISG15 Tools through Chemo‐Enzymatic Ligation Catalyzed by a Viral Protease Lbpro

Ubiquitin (Ub)‐like protein ISG15 (interferon‐stimulated gene 15) regulates innate immunity and links with the evasion of host response by viruses such as SARS‐CoV‐2. Dissecting ISGylation pathways recently received increasing attention which can inform related disease interventions, but such studies necessitate the preparation and development of various ISG15 protein tools. Here, we find that the leader protease (Lbpro) encoded by foot‐and‐mouth disease virus can promote ligation reactions between recombinant ISG15 and synthetic glycyl compounds, generating protein tools such as ISG15‐propargylamide and ISG15‐rhodamine110, which are needed for cellular proteomic studies of deISGylases, and the screening and evaluation of inhibitors against SARS‐CoV‐2 papain‐like protease (PLpro). Furthermore, this strategy can be also used to load ISG15 onto the lysine of a synthetic peptide through an isopeptide bond, and prepare Ub and NEDD8 (ubiquitin‐like protein Nedd8) protein tools.

Expedient Synthesis of Ubiquitin-like Protein ISG15 Tools through Chemo-Enzymatic Ligation Catalyzed by a Viral Protease Lbpro.

Ubiquitin (Ub)-like protein ISG15 (interferon-stimulated gene 15) regulates innate immunity and links with the evasion of host response by viruses such as SARS-CoV-2. Dissecting ISGylation pathways recently received increasing attention which can inform related disease interventions, but such studies necessitate the preparation and development of various ISG15 protein tools. Here, we find that the leader protease (Lbpro ) encoded by foot-and-mouth disease virus can promote ligation reactions between recombinant ISG15 and synthetic glycyl compounds, generating protein tools such as ISG15-propargylamide and ISG15-rhodamine110, which are needed for cellular proteomic studies of deISGylases, and the screening and evaluation of inhibitors against SARS-CoV-2 papain-like protease (PLpro). Furthermore, this strategy can be also used to load ISG15 onto the lysine of a synthetic peptide through an isopeptide bond, and prepare Ub and NEDD8 (ubiquitin-like protein Nedd8) protein tools.