In recent years, the incidence of adenocarcinoma of esophagogastric junction (AEG) has increased gradually. Due to the unique anatomical location and the different biological features from esophageal cancer and gastric cancer, AEG cannot be simply equated with esophageal cancer or gastric cancer, and the definition, classification and treatment methods of AEG are still controversial. As a result, the study of AEG is becoming increasingly important. Using bibliometrics, the authors search English literatures from the Web of Science Core Collection database from the establishment to December 31, 2022, with the keyword adenocarcinoma of esophagogastric junc-tion. To systematically review the international literatures on AEG, EndNote and Excel are used to manage literatures and perform statistical analysis, and VOSviewer and CiteSpace are used to analyze the social network, time series of countries, institutions, authors and keywords, the co-citation of authors and the citation bursts of keywords. The authors summarize the research status and hot trends in this field, hoping to provide reference for future research.

OBJECTIVE：To study the effects and mechanism of oncolytic virus M 1（called M 1 virus for short ）inducing the apoptosis of cervical cancer C-33A cells. METHODS ：MTT assay was used to detect survival rate of C- 33A cells that were treated with different titers （0，0.001，0.01，0.1，1，10 PFU/cell）of M 1 virus. C- 33A cells were divided into control group （0 PFU/cell）， low-dose，medium-dose and high-dose groups of M 1 virus（0.001，0.01，0.1 PFU/cell）. After treated with corresponding titers of M1 virus for 48 h，flow cytometry was used to detect the apoptotic rate and infection rate of cells；Western blot was performed to detect the protein expression of C/EBP homologous proteins （CHOP），caspase-12，caspase-3 and cleaved-caspase- 3. RESULTS ： After treated with different titers of M 1 virus，the survival rate of C- 33A cells decreased significantly （P＜0.01），and showed a dose-dependent tr end. Compared with control group ，the apoptotic rate and infection rate of cells in M 1 virus groups as well as the protein expression of CHOP ，caspase-12 and cleaved-caspase- 3（except for medium-dose group ）in M 1 virus medium-dose and high-dose groups were increased significantly （P＜0.01）. CONCLUSIONS ：M1 virus can induce the apoptosis of cervical cancer C-33A cells ，and its mechanism may be related to the activation of endoplasmic reticulum stress pathway.

ObjectiveTo study the inhibitory effect of aloe-emodin （AE） on aluminum ion （Al³⁺）-induced β-amyloid protein 42 （Aβ₄₂） aggregation and its depolymerization on formed Aβ₄₂-Al³⁺ aggregates in vitro， and to investigate the effect of AE on the cytotoxicity of Aβ₄₂ aggregation in the presence of Al³⁺. MethodThe Aβ₄₂ group， Aβ₄₂+Al³⁺ group， Aβ₄₂+AE group， Aβ₄₂+Al³⁺+AE group and the depolymerization test group were set up in the experiment. The aggregation fibrosis process， aggregation morphology， aggregation size and cytotoxicity of Aβ₄₂ in each group were detected by thioflavin T （ThT） fluorescence assay， transmission electron microscopy （TEM）， dynamic light scattering （DLS） experiment and thiazolyl blue （MTT） cytotoxicity assay. ResultCompared with the Aβ₄₂ group， Al³⁺ could promote Aβ₄₂ aggregation， increase the fluorescence intensity of ThT by 124.48%， induce the aggregation of Aβ₄₂ to form fiber bundles with larger particle size， and significantly reduce the cell viability of human neuroblastoma SH-SY5Y cells （P<0.01）， thus reducing the cell survival rate to 51.05%. AE not only inhibited Aβ₄₂ aggregation， but also inhibited Al³⁺-induced Aβ₄₂ aggregation in a concentration-dependent manner. Compared with the Aβ₄₂+Al³⁺ group， high concentration of AE could reduce the ThT fluorescence intensity to 41.66%， and change the polypeptide aggregation pathway to form amorphous aggregates with small particle size. Besides， it significantly inhibited the cytotoxicity of Aβ₄₂ induced by Al³⁺ （P<0.01）， and restored the cell survival rate to 84.87%. Further depolymerization was conducted， AE could depolymerize Aβ₄₂-Al³⁺ aggregates to make the formed aggregates disappear and form some small-particle short fibers and amorphous structure aggregates with low toxicity. ConclusionAE can inhibit Aβ₄₂ aggregation and cytotoxicity in the presence of Al³⁺， depolymerize the formed Aβ₄₂-Al³⁺ aggregates and alleviate the cytotoxicity， thus laying the foundation for exploring the mechanism of AE in the treatment of Alzheimer's disease.