Yongna Xing

3.3k total citations
43 papers, 2.4k citations indexed

About

Yongna Xing is a scholar working on Molecular Biology, Cell Biology and Reproductive Medicine. According to data from OpenAlex, Yongna Xing has authored 43 papers receiving a total of 2.4k indexed citations (citations by other indexed papers that have themselves been cited), including 31 papers in Molecular Biology, 7 papers in Cell Biology and 7 papers in Reproductive Medicine. Recurrent topics in Yongna Xing's work include Hypothalamic control of reproductive hormones (7 papers), Microtubule and mitosis dynamics (5 papers) and Enzyme Structure and Function (5 papers). Yongna Xing is often cited by papers focused on Hypothalamic control of reproductive hormones (7 papers), Microtubule and mitosis dynamics (5 papers) and Enzyme Structure and Function (5 papers). Yongna Xing collaborates with scholars based in United States, China and Sweden. Yongna Xing's co-authors include Nathan Wlodarchak, Philip D. Jeffrey, Yigong Shi, Zhu Li, Zheng Lin, Yanhui Xu, Chao Yang, Jeffry B. Stock, Stefan Strack and Li Jiang and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Yongna Xing

41 papers receiving 2.4k citations

Peers

Countries citing papers authored by Yongna Xing

Since Specialization

Citations

This map shows the geographic impact of Yongna Xing's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Yongna Xing with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Yongna Xing more than expected).

Fields of papers citing papers by Yongna Xing

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Yongna Xing. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Yongna Xing. The network helps show where Yongna Xing may publish in the future.

Co-authorship network of co-authors of Yongna Xing

This figure shows the co-authorship network connecting the top 25 collaborators of Yongna Xing. A scholar is included among the top collaborators of Yongna Xing based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Yongna Xing. Yongna Xing is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

#	Work	Indexed citations
1	Coupling to short linear motifs creates versatile PME-1 activities in PP2A holoenzyme demethylation and inhibition 2022 ·eLife ·(unknown), (unknown), (unknown), Cheng-Guo Wu, (unknown), Vikash Kumar Yadav, Ylva Ivarsson, Stefan Strack, Irina Novikova, Yongna Xing	8
2	Eya3 partners with PP2A to induce c-Myc stabilization and tumor progression 2018 ·Nature Communications ·Lingdi Zhang, Hengbo Zhou, Xueni Li, Rebecca L. Vartuli, (unknown), Yongna Xing, Pratyaydipta Rudra, Debashis Ghosh, Rui Zhao, Heide L. Ford	61
3	Trace derivatives of kynurenine potently activate the aryl hydrocarbon receptor (AHR) 2017 ·Journal of Biological Chemistry ·Seung‐Hyeon Seok, Zhi‐Xiong Ma, John B. Feltenberger, (unknown), Hui Chen, Cameron O. Scarlett, Ziqing Lin, Kenneth A. Satyshur, (unknown), Colin R. Jefcoate, Ying Ge, Weiping Tang, Christopher A. Bradfield, Yongna Xing	122
4	Methylation-regulated decommissioning of multimeric PP2A complexes 2017 ·Nature Communications ·Cheng-Guo Wu, Aiping Zheng, Li Jiang, (unknown), Vitali Stanevich, Hui Chen, (unknown), Kenneth A. Satyshur, Benjamin M. Johnson, Ting‐Jia Gu, Zuojia Liu, Yongna Xing	30
5	Purification of Target Proteins from Native Tissues: CCT Complex from Bovine Testes and PP2Ac from Porcine Brains 2017 ·Methods in molecular biology ·Feng Guo, Nathan Wlodarchak, (unknown), Yongna Xing	0
6	PP2A as a master regulator of the cell cycle 2016 ·Critical Reviews in Biochemistry and Molecular Biology ·Nathan Wlodarchak, Yongna Xing	268
7	MTDH-SND1 Interaction Is Crucial for Expansion and Activity of Tumor-Initiating Cells in Diverse Oncogene- and Carcinogen-Induced Mammary Tumors 2014 ·Cancer Cell ·Liling Wan, Xin Lü, Salina Yuan, Yong Wei, Feng Guo, Minhong Shen, Min Yuan, Rumela Chakrabarti, (unknown), Heath A. Smith, Andrés Blanco, Marina Chekmareva, Hao Wu, Roderick T. Bronson, Bruce G. Haffty, Yongna Xing, Yibin Kang	109
8	Structural Insights into the Tumor-Promoting Function of the MTDH-SND1 Complex 2014 ·Cell Reports ·Feng Guo, Liling Wan, Aiping Zheng, Vitali Stanevich, Yong Wei, Kenneth A. Satyshur, Minhong Shen, Woo‐Jong Lee, Yibin Kang, Yongna Xing	41
9	Centralspindlin assembly and 2 phosphorylations on MgcRacGAP by Polo-like kinase 1 initiate Ect2 binding in early cytokinesis 2014 ·Cell Cycle ·Hyun-Jung Kim, Feng Guo, (unknown), Yongna Xing, Mark E. Burkard	19
10	PR65A Phosphorylation Regulates PP2A Complex Signaling 2014 ·PLoS ONE ·Kumar Kotlo, Yongna Xing, (unknown), (unknown), (unknown), Randal A. Skidgel, R. John Solaro, Robert S. Danziger	7
11	SU5416, a VEGF Receptor Inhibitor and Ligand of the AHR, Represents a New Alternative for Immunomodulation 2012 ·PLoS ONE ·Joshua D. Mezrich, Linh P. Nguyen, (unknown), Manabu Nukaya, John H. Fechner, Xiaoji Zhang, Yongna Xing, Christopher A. Bradfield	37
12	The Structural Basis for Tight Control of PP2A Methylation and Function by LCMT-1 2011 ·Molecular Cell ·Vitali Stanevich, Li Jiang, Kenneth A. Satyshur, Yongfeng Li, Philip D. Jeffrey, Zhu Li, (unknown), M. F. SEMMELHACK, Yongna Xing	108
13	Structural Mechanism of Demethylation and Inactivation of Protein Phosphatase 2A 2008 ·Cell ·Yongna Xing, Zhu Li, Yu Chen, Jeffry B. Stock, Philip D. Jeffrey, Yigong Shi	154
14	Structural and biochemical insights into the regulation of protein phosphatase 2A by small t antigen of SV40 2007 ·Nature Structural & Molecular Biology ·(unknown), Yanhui Xu, Qing Bao, Yongna Xing, Zhu Li, Zheng Lin, Jeffry B. Stock, Philip D. Jeffrey, Yigong Shi	71
15	Structure of the Protein Phosphatase 2A Holoenzyme 2006 ·Cell ·Yanhui Xu, Yongna Xing, Yu Chen, Chao Yang, Zheng Lin, Eugene Fan, Jong W. Yu, Stefan Strack, Philip D. Jeffrey, Yigong Shi	351
16	Structure of Protein Phosphatase 2A Core Enzyme Bound to Tumor-Inducing Toxins 2006 ·Cell ·Yongna Xing, Yanhui Xu, Yu Chen, Philip D. Jeffrey, Chao Yang, Zheng Lin, Zhu Li, Stefan Strack, Jeffry B. Stock, Yigong Shi	269
17	Glycoprotein Hormone Assembly in the Endoplasmic Reticulum 2004 ·Journal of Biological Chemistry ·Yongna Xing, Rebecca V. Myers, Donghui Cao, (unknown), Mei Jiang, Michael P. Bernard, William R. Moyle	19
18	Glycoprotein Hormone Assembly in the Endoplasmic Reticulum 2004 ·Journal of Biological Chemistry ·Yongna Xing, Rebecca V. Myers, Donghui Cao, (unknown), Mei Jiang, Michael P. Bernard, William R. Moyle	19
19	Threading of a glycosylated protein loop through a protein hole: Implications for combination of human chorionic gonadotropin subunits 2001 ·Protein Science ·Yongna Xing, Christopher T. Williams, R. Keith Campbell, Stephanie Cook, Maria H. Knoppers, Theresa A. Addona, (unknown), William R. Moyle	20
20	Alternatively Folded Choriogonadotropin Analogs 2001 ·Journal of Biological Chemistry ·Yongna Xing, (unknown), Mei Jiang, Rebecca V. Myers, Donghui Cao, Michael P. Bernard, William R. Moyle	20

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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