Rui-ming Xu, Ph.D
Affiliations: | 2009- | Institute of Biophysics | Chinese Academy of Sciences (CAS) |
Area:
Epigenetic control gene expressionWebsite:
http://www.ibp.cas.cn/xurmlab/Google:
"https://scholar.google.com/citations?hl=en&user=LEPnfzYAAAAJ&view_op=list_works&sortby=pubdate"Mean distance: (not calculated yet)
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Publications
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Li Z, Hua X, Serra-Cardona A, et al. (2020) DNA polymerase α interacts with H3-H4 and facilitates the transfer of parental histones to lagging strands. Science Advances. 6: eabb5820 |
Gou LT, Lim DH, Ma W, et al. (2020) Initiation of Parental Genome Reprogramming in Fertilized Oocyte by Splicing Kinase SRPK1-Catalyzed Protamine Phosphorylation. Cell |
Song X, Yang L, Wang M, et al. (2019) A higher-order configuration of the heterodimeric DOT1L-AF10 coiled-coil domains potentiates their leukemogenenic activity. Proceedings of the National Academy of Sciences of the United States of America |
Du W, Dong Q, Zhang Z, et al. (2019) Stella protein facilitates DNA demethylation by disrupting the chromatin association of the RING finger-type E3 ubiquitin ligase UHRF1. The Journal of Biological Chemistry |
Hou P, Huang C, Liu CP, et al. (2019) Structural Insights into Stimulation of Ash1L's H3K36 Methyltransferase Activity through Mrg15 Binding. Structure (London, England : 1993) |
Xiong C, Wen Z, Yu J, et al. (2018) UBN1/2 of HIRA complex is responsible for recognition and deposition of H3.3 at cis-regulatory elements of genes in mouse ES cells. Bmc Biology. 16: 110 |
Zhang L, Serra-Cardona A, Zhou H, et al. (2018) Multisite Substrate Recognition in Asf1-Dependent Acetylation of Histone H3 K56 by Rtt109. Cell |
Jin W, Wang Y, Liu CP, et al. (2016) Structural basis for snRNA recognition by the double-WD40 repeat domain of Gemin5. Genes & Development. 30: 2391-2403 |
Fang Q, Chen P, Wang M, et al. (2016) Correction: Human cytomegalovirus IE1 alters the higher-order chromatin structure by targeting the acidic patch of the nucleosome. Elife. 5 |
Fu W, Liu N, Qiao Q, et al. (2016) Structural Basis for Substrate Preference of SMYD3, A SET Domain-containing Protein Lysine Methyltransferase. The Journal of Biological Chemistry |