Xueying Yuan
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Sororin locks the DNA-exit gate of cohesin to preserve sister-chromatid cohesion
Abstract The cohesin complex mediates sister-chromatid cohesion by topologically entrapping DNA within an SMC1-SMC3-RAD21 ring, yet how Sororin preserves cohesion beyond its known role of antagonizing Pds5 binding to the release factor Wapl has remained unclear. Here, we show that the extreme C-terminal region (CTR) of Sororin functions as a direct structural lock for cohesin’s DNA-exit gate by engaging the RAD21-SMC3 interface.
Asymmetric Surface Charge Engineering Regulates Solvation Structure and Ionic Conductivity in Confined Polymer Electrolytes
Conflicts of Interest The authors declare no conflict of interest. Data Availability Statement The data that support the findings of this study are available from the corresponding author upon reasonable request. Supporting Information Filename Description smll72472-sup-0001-SuppMat.pdf740.8 KB Supporting File: smll72472-sup-0001-SuppMat.pdf. References 1, , and , “Towards Practical Lithium-Metal Anodes,” Chemical Society Reviews 49 (2020): 3040–3071, http://doi.org/10.1039/C9CS00838A.
CREB-Binding Protein/P300 Bromodomain Inhibition Reduces Neutrophil Accumulation and Activates Antitumor Immunity in Triple-Negative Breast Cancer
10.1172/jci.insight.182621 Post-print Triple Negative Breast Neoplasms, Female, Humans, Animals, Neutrophils, Mice, CREB-Binding Protein, Cell Line, Tumor, Xenograft Model Antitumor Assays, E1A-Associated p300 Protein, Cell Proliferation, Antineoplastic Agents, Immunology, Oncology, Breast cancer, Cellular immune response, Epigenetics yes Yuan, Xueying; Hao, Xiaoxin; Chan, Hilda L; et al., "CREB-Binding Protein/P300 Bromodomain Inhibition Reduces Neutrophil Accumulation and Activates...
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