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Ben-Ge Xin on Muck Rack

Ben-Ge Xin

As seen in: The Journal of Biological Chemistry
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Articles

Structural insights into the N-terminal APHB domain of HrpA: mediating canonical and i-motif recognition

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By Ben-Ge Xin, Ling-Yun Huang, Na-Nv Liu, Ling-Gang Yuan
| hal.science
Article Dans Une Revue Nucleic Acids Research Année : 2024 Structural insights into the N-terminal APHB domain of HrpA: mediating canonical and i-motif recognition Origine : Fichiers éditeurs autorisés sur une archive ouverte hal-04472793 , version 1 (22-02-2024) Ben-Ge Xin, Ling-Yun Huang, Ling-Gang Yuan, Na-Nv Liu, Hai-Hong Li, et al.. Structural insights into the N-terminal APHB domain of HrpA: mediating canonical and i-motif recognition. Nucleic Acids Research, In press, ⟨10.1093/nar/gkae138⟩.
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The HRDC domain oppositely modulates the unwinding activity of E. coli RecQ helicase on duplex DNA and G-quadruplex

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By Fang-Yuan Teng, Ting-Ting Wang, Hai-Lei Guo, Ben-Ge Xin
| The Journal of Biological Chemistry Verified
Fang-Yuan Teng1,2,3, Ting-Ting Wang1, Hai-Lei Guo1, Ben-Ge Xin1, Bo Sun4, Shuo-Xing Dou5, Xu-Guang Xi1,6* and Xi-Miao Hou1* 1State Key Laboratory of Crop Stress Biology for Arid Areas and College of Life Sciences, Northwest A&F University, Yangling, Shaanxi, China 2Experimental Medicine Center, The Affiliated Hospital of Southwest Medical University, Luzhou, Sichuan, China 3Department of Endocrinology and Metabolism, and Cardiovascular and Metabolic Diseases Key Laboratory of Luzhou, and...
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The HRDC domain oppositely modulates the unwinding activity of E. coli RecQ helicase on duplex DNA and G-quadruplex

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By Ting-Ting Wang, Fang-Yuan Teng, Hai-Lei Guo, Ben-Ge Xin
| The Journal of Biological Chemistry Verified
Fang-Yuan Teng1, Ting-Ting Wang1, Hai-Lei Guo1, Ben-Ge Xin1, Bo Sun2, Shuo-Xing Dou3, Xu-Guang Xi1* and Xi-Miao Hou4 1Northwest A&F University, China 2ShanghaiTech University, China 3Chinese Academy of Sciences, China 4Northwest A & F University, China ↵* Corresponding author; email: xxi01{at}ens-cachan.fr Abstract RecQ family helicases are highly conserved from bacteria to humans and have essential roles in maintaining genome stability.
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