AIM: To analyze the research status and future development trends of intermittent exotropia(IXT)by bibliometric study.METHODS: Bibliometrics methods were used and the related literatures in the Web of Science Core Collection(WoSCC)database from 2003 to 2022 were retrieved. CiteSpace6.2.R2 software was used to conduct visualized analysis of publications of one year, countries, institutions, journals, authors, references and keywords.RESULTS: A total of 620 literatures on IXT were retrieved from 2003 to 2022, and there has been a progressive increase in the number of publications. South Korea and the United States, Mayo Clinc and Holmes JM were the most productive and impactful country, institution and author, respectively. The Journal of American Association for Pediatric Ophthalmology and Strabismus(J AAPOS)published the most manuscripts(78 publications). The keywords with the strongest citation burst were surgery, epidemiology, alignment and recurrence.CONCLUSION: Visualized analysis conducted by CiteSpace software could objectively show the quantity changes and distribution of literatures on IXT from 2003 to 2022. Furthermore, the research hotspot of IXT has gradually shifted from surgery and epidemiology to fusion and recurrence.

Studies on coat protein I (COPI) have contributed to a basic understanding of how coat proteins generate vesicles to initiate intracellular transport. The core component of the COPI complex is coatomer, which is a multimeric complex that needs to be recruited from the cytosol to membrane in order to function in membrane bending and cargo sorting. Previous structural studies on the clathrin adaptors have found that membrane recruitment induces a large conformational change in promoting their role in cargo sorting. Here, pursuing negative-stain electron microscopy coupled with single-particle analyses, and also performing CXMS (chemical cross-linking coupled with mass spectrometry) for validation, we have reconstructed the structure of coatomer in its soluble form. When compared to the previously elucidated structure of coatomer in its membrane-bound form we do not observe a large conformational change. Thus, the result uncovers a key difference between how COPI versus clathrin coats are regulated by membrane recruitment.
ADP-Ribosylation Factor 1 ; chemistry ; metabolism ; Animals ; Coatomer Protein ; chemistry ; metabolism ; Cytosol ; chemistry ; metabolism ; GTPase-Activating Proteins ; chemistry ; metabolism ; Humans ; Membranes, Artificial ; Rats