{"id":276,"date":"2023-07-07T12:20:09","date_gmt":"2023-07-07T04:20:09","guid":{"rendered":"http:\/\/yuhongtaolab.com\/?post_type=publication&#038;p=276"},"modified":"2023-07-07T13:24:56","modified_gmt":"2023-07-07T05:24:56","slug":"276","status":"publish","type":"publication","link":"http:\/\/yuhongtaolab.com\/en\/publication\/276\/","title":{"rendered":"Publish papers in recent 5 years"},"content":{"rendered":"<p>1\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Li, S. et al. Prolonged activation of innate immune pathways by a polyvalent STING agonist. Nat Biomed Eng, doi:10.1038\/s41551-020-00675-9 (2021).<\/p>\n<p>2\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Shi, Z., Gao, H., Bai, X. C. &amp; Yu, H. Cryo-EM structure of the human cohesin-NIPBL-DNA complex. Science 368, 1454-1459, doi:10.1126\/science.abb0981 (2020).<\/p>\n<p>3\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Park, J. et al. Structure of human GABA(B) receptor in an inactive state. Nature 584, 304-309, doi:10.1038\/s41586-020-2452-0 (2020).<\/p>\n<p>4\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Li, F. et al. Cryo-EM structure of VASH1-SVBP bound to microtubules. eLife 9, doi:10.7554\/eLife.58157 (2020).<\/p>\n<p>5\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Kim, Y. &amp; Yu, H. Shaping of the 3D genome by the ATPase machine cohesin. Exp Mol Med 52, 1891-1897, doi:10.1038\/s12276-020-00526-2 (2020).<\/p>\n<p>6\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Hall, C., Yu, H. &amp; Choi, E. Insulin receptor endocytosis in the pathophysiology of insulin resistance. Exp Mol Med 52, 911-920, doi:10.1038\/s12276-020-0456-3 (2020).<\/p>\n<p>7\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Yang, H. et al. Mps1 regulates spindle morphology through MCRS1 to promote chromosome alignment. Molecular biology of the cell 30, 1060-1068, doi:10.1091\/mbc.E18-09-0546 (2019).<\/p>\n<p>8\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Uchikawa, E., Choi, E., Shang, G., Yu, H. &amp; Bai, X. C. Activation mechanism of the insulin receptor revealed by cryo-EM structure of the fully liganded receptor-ligand complex. eLife 8, doi:10.7554\/eLife.48630 (2019).<\/p>\n<p>9\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Li, J., Choi, E., Yu, H. &amp; Bai, X. C. Structural basis of the activation of type 1 insulin-like growth factor receptor. Nature communications 10, 4567, doi:10.1038\/s41467-019-12564-0 (2019).<\/p>\n<p>10\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Li, F., Raczynska, J. E., Chen, Z. &amp; Yu, H. Structural Insight into DNA-Dependent Activation of Human Metalloprotease Spartan. Cell reports 26, 3336-3346.e3334, doi:10.1016\/j.celrep.2019.02.082 (2019).<\/p>\n<p>11\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Li, F., Hu, Y., Qi, S., Luo, X. &amp; Yu, H. Structural basis of tubulin detyrosination by vasohibins. Nature structural &amp; molecular biology 26, 583-591, doi:10.1038\/s41594-019-0242-x (2019).<\/p>\n<p>12\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Kopp, F. et al. PUMILIO hyperactivity drives premature aging of Norad-deficient mice. eLife 8, doi:10.7554\/eLife.42650 (2019).<\/p>\n<p>13\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Kim, Y., Shi, Z., Zhang, H., Finkelstein, I. J. &amp; Yu, H. Human cohesin compacts DNA by loop extrusion. Science 366, 1345-1349, doi:10.1126\/science.aaz4475 (2019).<\/p>\n<p>14\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Choi, E. et al. Mitotic regulators and the SHP2-MAPK pathway promote IR endocytosis and feedback regulation of insulin signaling. Nature communications 10, 1473, doi:10.1038\/s41467-019-09318-3 (2019).<\/p>\n<p>15\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Zheng, G. &amp; Yu, H. Cyclin A Turns on Bora to Light the Path to Mitosis. Dev Cell 45, 542-543, doi:10.1016\/j.devcel.2018.05.017 (2018).<\/p>\n<p>16\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Zheng, G., Kanchwala, M., Xing, C. &amp; Yu, H. MCM2-7-dependent cohesin loading during S phase promotes sister-chromatid cohesion. eLife 7, doi:10.7554\/eLife.33920 (2018).<\/p>\n<p>17\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Yang, Y. &amp; Yu, H. Partner switching for Ran during the mitosis dance. Journal of molecular cell biology 10, 89-90, doi:10.1093\/jmcb\/mjx048 (2018).<\/p>\n<p>18\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Yang, Y. &amp; Yu, H. CENP-T bears the load in mitosis. Nature cell biology 20, 1335-1337, doi:10.1038\/s41556-018-0241-x (2018).<\/p>\n<p>19\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Petela, N. J. et al. Scc2 Is a Potent Activator of Cohesin&#8217;s ATPase that Promotes Loading by Binding Scc1 without Pds5. Molecular cell 70, 1134-1148.e1137, doi:10.1016\/j.molcel.2018.05.022 (2018).<\/p>\n<p>20\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Li, F. et al. The BUB3-BUB1 Complex Promotes Telomere DNA Replication. Molecular cell 70, 395-407.e394, doi:10.1016\/j.molcel.2018.03.032 (2018).<\/p>\n<p>21\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Lee, H. S. et al. The chromatin remodeler RSF1 controls centromeric histone modifications to coordinate chromosome segregation. Nature communications 9, 3848, doi:10.1038\/s41467-018-06377-w (2018).<\/p>\n<p>22\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Lee, C. C., Li, B., Yu, H. &amp; Matunis, M. J. Sumoylation promotes optimal APC\/C Activation and Timely Anaphase. eLife 7, doi:10.7554\/eLife.29539 (2018).<\/p>\n<p>23\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Lee, C. C., Li, B., Yu, H. &amp; Matunis, M. J. A Method for SUMO Modification of Proteins in vitro. Bio Protoc 8, doi:10.21769\/BioProtoc.3033 (2018).<\/p>\n<p>24\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Cortone, G. et al. Interaction of the Warsaw breakage syndrome DNA helicase DDX11 with the replication fork-protection factor Timeless promotes sister chromatid cohesion. PLoS genetics 14, e1007622, doi:10.1371\/journal.pgen.1007622 (2018).<\/p>\n<p>25\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Choi, E. &amp; Yu, H. Spindle Checkpoint Regulators in Insulin Signaling. Front Cell Dev Biol 6, 161, doi:10.3389\/fcell.2018.00161 (2018).<\/p>\n<p>26\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Zheng, G., Ouyang, Z. &amp; Yu, H. Biochemical and Functional Assays of Human Cohesin-Releasing Factor Wapl. Methods in molecular biology 1515, 37-53, doi:10.1007\/978-1-4939-6545-8_3 (2017).<\/p>\n<p>27\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Zhang, Q. et al. Ska3 Phosphorylated by Cdk1 Binds Ndc80 and Recruits Ska to Kinetochores to Promote Mitotic Progression. Current biology : CB 27, 1477-1484.e1474, doi:10.1016\/j.cub.2017.03.060 (2017).<\/p>\n<p>28\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Soardi, F. C. et al. Familial STAG2 germline mutation defines a new human cohesinopathy. NPJ Genom Med 2, 7, doi:10.1038\/s41525-017-0009-4 (2017).<\/p>\n<p>29\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Palozola, K. C. et al. Mitotic transcription and waves of gene reactivation during mitotic exit. Science 358, 119-122, doi:10.1126\/science.aal4671 (2017).<\/p>\n<p>30\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Ouyang, Z. &amp; Yu, H. Releasing the cohesin ring: A rigid scaffold model for opening the DNA exit gate by Pds5 and Wapl. Bioessays 39, doi:10.1002\/bies.201600207 (2017).<\/p>\n<p>31\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Ji, Z., Gao, H., Jia, L., Li, B. &amp; Yu, H. A sequential multi-target Mps1 phosphorylation cascade promotes spindle checkpoint signaling. eLife 6, doi:10.7554\/eLife.22513 (2017).<\/p>\n<p>32\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Brulotte, M. L. et al. Mechanistic insight into TRIP13-catalyzed Mad2 structural transition and spindle checkpoint silencing. Nature communications 8, 1956, doi:10.1038\/s41467-017-02012-2 (2017).<\/p>\n<p>33\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Sivakumar, S. et al. The human SKA complex drives the metaphase-anaphase cell cycle transition by recruiting protein phosphatase 1 to kinetochores. eLife 5, doi:10.7554\/eLife.12902 (2016).<\/p>\n<p>34\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Rong, Z., Ouyang, Z., Magin, R. S., Marmorstein, R. &amp; Yu, H. Opposing Functions of the N-terminal Acetyltransferases Naa50 and NatA in Sister-chromatid Cohesion. J Biol Chem 291, 19079-19091, doi:10.1074\/jbc.M116.737585 (2016).<\/p>\n<p>35\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Ouyang, Z., Zheng, G., Tomchick, D. R., Luo, X. &amp; Yu, H. Structural Basis and IP6 Requirement for Pds5-Dependent Cohesin Dynamics. Molecular cell 62, 248-259, doi:10.1016\/j.molcel.2016.02.033 (2016).<\/p>\n<p>36\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Lin, Z., Luo, X. &amp; Yu, H. Structural basis of cohesin cleavage by separase. Nature 532, 131-134, doi:10.1038\/nature17402 (2016).<\/p>\n<p>37\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Kikuchi, S., Borek, D. M., Otwinowski, Z., Tomchick, D. R. &amp; Yu, H. Crystal structure of the cohesin loader Scc2 and insight into cohesinopathy. Proceedings of the National Academy of Sciences of the United States of America 113, 12444-12449, doi:10.1073\/pnas.1611333113 (2016).<\/p>\n<p>38\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Choi, E., Zhang, X., Xing, C. &amp; Yu, H. Mitotic Checkpoint Regulators Control Insulin Signaling and Metabolic Homeostasis. Cell 166, 567-581, doi:10.1016\/j.cell.2016.05.074 (2016).<\/p>\n<p>&nbsp;<\/p>\n","protected":false},"featured_media":0,"template":"","class_list":["post-276","publication","type-publication","status-publish","hentry"],"acf":[],"_links":{"self":[{"href":"http:\/\/yuhongtaolab.com\/en\/wp-json\/wp\/v2\/publication\/276","targetHints":{"allow":["GET"]}}],"collection":[{"href":"http:\/\/yuhongtaolab.com\/en\/wp-json\/wp\/v2\/publication"}],"about":[{"href":"http:\/\/yuhongtaolab.com\/en\/wp-json\/wp\/v2\/types\/publication"}],"wp:attachment":[{"href":"http:\/\/yuhongtaolab.com\/en\/wp-json\/wp\/v2\/media?parent=276"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}