Zobrazeno 1 - 10
of 65
pro vyhledávání: '"Hongda Huang"'
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-13 (2022)
The authors report several high-resolution functional snapshots of type III-E nuclease-protease Craspase complexes, revealing the mechanisms underlying target RNA cleavage and non-self RNA activated protease activities; and highlighting the potential
Externí odkaz:
https://doaj.org/article/90cc95d009f44d7da4d983e6b89696ae
Autor:
Huanhuan Cui, Hongyang Yi, Hongyu Bao, Ying Tan, Chi Tian, Xinyao Shi, Diwen Gan, Bin Zhang, Weizheng Liang, Rui Chen, Qionghua Zhu, Liang Fang, Xin Gao, Hongda Huang, Ruijun Tian, Silke R. Sperling, Yuhui Hu, Wei Chen
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-16 (2022)
The functional role of DPF3, a component of the SWI/SNF chromatin remodelling complex associated with clear cell renal cell carcinoma (ccRCC), remains unknown. Here, the authors characterise the mechanism by which DPF3 promotes metastasis via the act
Externí odkaz:
https://doaj.org/article/af754302317846bcb9106e92c8c0d336
Autor:
Hongyu Bao, Hongda Huang
Publikováno v:
eLife, Vol 11 (2022)
A newly discovered pathway suggests histone proteins H3 and H4 are imported into the nucleus as individual units rather than joined together as heterodimers as was previously thought.
Externí odkaz:
https://doaj.org/article/8b88d9ecf8dc4065bb40f4ab15dfb058
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-13 (2017)
The ATRX-DAXX histone chaperone complex incorporates H3.3 in heterochromatin in a replication-independent manner. Here, the authors present a high-resolution x-ray crystal structure of an interaction surface between ATRX and DAXX, and characterize AT
Externí odkaz:
https://doaj.org/article/0eb14fc947d44504ad5c2c9805c2cc49
Autor:
Hongda Huang, Zhong Deng, Olga Vladimirova, Andreas Wiedmer, Fang Lu, Paul M. Lieberman, Dinshaw J. Patel
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-10 (2016)
The Epstein-Barr virus tegument protein BNRF1 is required for the establishment of selective viral gene expression during latency and interacts with the histone chaperone DAXX. Here the authors provide structural insight into how BNRF1 hijacks the DA
Externí odkaz:
https://doaj.org/article/6d2925404a094e03b04d736dea4baa8d
Autor:
Chongping Li, Ying Li, Yuci Wang, Xiangrui Meng, Xiaoyan Shi, Yangyi Zhang, Nan Liang, Hongda Huang, Yue Li, Hui Zhou, Jiawei Xu, Wenqi Xu, Hao Chen
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America; 11/12/2024, Vol. 121 Issue 46, p1-12, 35p
Autor:
Yue Li, Hongda Huang
Publikováno v:
Biochemical and Biophysical Research Communications. 651:85-91
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f4e7534472c1ef7381afc99480b0a003
https://doi.org/10.1016/j.bbrc.2023.02.016
https://doi.org/10.1016/j.bbrc.2023.02.016
Publikováno v:
Journal of Integrative Plant Biology. 64:2309-2313
The structural basis for histone recognition by the histone chaperone nuclear autoantigenic sperm protein (NASP) remains largely unclear. Here, we showed that Arabidopsis thaliana AtNASP is a monomer and displays robust nucleosome assembly activity i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::620fb9aa87bdf92c24dca220e8de9102
https://doi.org/10.1111/jipb.13277
https://doi.org/10.1111/jipb.13277
Autor:
Yinpeng Xie, Ying Zhu, Na Wang, Min Luo, Tsuyoshi Ota, Ruipan Guo, Ikuo Takahashi, Zongjun Yu, Yalikunjiang Aizezi, Linlin Zhang, Yan Yan, Yujie Zhang, Hongyu Bao, Yichuan Wang, Ziqiang Zhu, Ancheng C. Huang, Yunde Zhao, Tadao Asami, Hongda Huang, Hongwei Guo, Kai Jiang
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 119, iss 49
Auxin inactivation is critical for plant growth and development. To develop plant growth regulators functioning in auxin inactivation pathway, we performed a phenotype-based chemical screen in Arabidopsis and identified a chemical, nalacin, that part
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4bac2d6e687f26cf5346e23cf0b7421
https://pubmed.ncbi.nlm.nih.gov/36454752
https://pubmed.ncbi.nlm.nih.gov/36454752
The RNA-targeting type III-E CRISPR-gRAMP effector forms a complex with a caspase-like protease TPR-CHAT, but the mechanistic details of their functional relationship remain unknown. Here, we report on cryo-EM structures of gRAMPcrRNA and gRAMPcrRNA-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d8e3e1e63327a3c27bb83b1ddc908323
https://doi.org/10.1101/2022.09.03.506347
https://doi.org/10.1101/2022.09.03.506347
