2,890 research outputs found
A Diffusion model for POI recommendation
Next Point-of-Interest (POI) recommendation is a critical task in
location-based services that aim to provide personalized suggestions for the
user's next destination. Previous works on POI recommendation have laid focused
on modeling the user's spatial preference. However, existing works that
leverage spatial information are only based on the aggregation of users'
previous visited positions, which discourages the model from recommending POIs
in novel areas. This trait of position-based methods will harm the model's
performance in many situations. Additionally, incorporating sequential
information into the user's spatial preference remains a challenge. In this
paper, we propose Diff-POI: a Diffusion-based model that samples the user's
spatial preference for the next POI recommendation. Inspired by the wide
application of diffusion algorithm in sampling from distributions, Diff-POI
encodes the user's visiting sequence and spatial character with two
tailor-designed graph encoding modules, followed by a diffusion-based sampling
strategy to explore the user's spatial visiting trends. We leverage the
diffusion process and its reversed form to sample from the posterior
distribution and optimized the corresponding score function. We design a joint
training and inference framework to optimize and evaluate the proposed
Diff-POI. Extensive experiments on four real-world POI recommendation datasets
demonstrate the superiority of our Diff-POI over state-of-the-art baseline
methods. Further ablation and parameter studies on Diff-POI reveal the
functionality and effectiveness of the proposed diffusion-based sampling
strategy for addressing the limitations of existing methods
5,5′-Selenobis(2-hydroxybenzaldehyde)
In the title molecule, C14H10O4Se, the dihedral angle between the two benzene rings is 74.6 (1)°. Both hydroxybenzaldehyde groups form intramolecular O—H⋯O hydrogen bonds. In the crystal, pairs of molecules are linked by pairs of weak C—H⋯π(arene) interactions, forming centrosymmetric dimers. In addition, molecules are linked by π–π stacking interactions, with a centroid–centroid distance of 3.785 (2) Å, forming chains along the c axis
Cell-based analysis of Chikungunya virus E1 protein in membrane fusion
<p>Abstract</p> <p>Background</p> <p>Chikungunya fever is a pandemic disease caused by the mosquito-borne Chikungunya virus (CHIKV). E1 glycoprotein mediation of viral membrane fusion during CHIKV infection is a crucial step in the release of viral genome into the host cytoplasm for replication. How the E1 structure determines membrane fusion and whether other CHIKV structural proteins participate in E1 fusion activity remain largely unexplored.</p> <p>Methods</p> <p>A bicistronic baculovirus expression system to produce recombinant baculoviruses for cell-based assay was used. Sf21 insect cells infected by recombinant baculoviruses bearing wild type or single-amino-acid substitution of CHIKV E1 and EGFP (enhanced green fluorescence protein) were employed to investigate the roles of four E1 amino acid residues (G91, V178, A226, and H230) in membrane fusion activity.</p> <p>Results</p> <p>Western blot analysis revealed that the E1 expression level and surface features in wild type and mutant substituted cells were similar. However, cell fusion assay found that those cells infected by CHIKV E1-H230A mutant baculovirus showed little fusion activity, and those bearing CHIKV E1-G91D mutant completely lost the ability to induce cell-cell fusion. Cells infected by recombinant baculoviruses of CHIKV E1-A226V and E1-V178A mutants exhibited the same membrane fusion capability as wild type. Although the E1 expression level of cells bearing monomeric-E1-based constructs (expressing E1 only) was greater than that of cells bearing 26S-based constructs (expressing all structural proteins), the sizes of syncytial cells induced by infection of baculoviruses containing 26S-based constructs were larger than those from infections having monomeric-E1 constructs, suggesting that other viral structure proteins participate or regulate E1 fusion activity. Furthermore, membrane fusion in cells infected by baculovirus bearing the A226V mutation constructs exhibited increased cholesterol-dependences and lower pH thresholds. Cells bearing the V178A mutation exhibited a slight decrease in cholesterol-dependence and a higher-pH threshold for fusion.</p> <p>Conclusions</p> <p>Cells expressing amino acid substitutions of conserved protein E1 residues of E1-G91 and E1-H230 lost most of the CHIKV E1-mediated membrane fusion activity. Cells expressing mutations of less-conserved amino acids, E1-V178A and E1-A226V, retained membrane fusion activity to levels similar to those expressing wild type E1, but their fusion properties of pH threshold and cholesterol dependence were slightly altered.</p
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