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VOLUME 9 ISSUE 5 (Oct, 2017)

Editorial
Review
Yanbo Fan, Haocheng Lu, Wenying Liang, Wenting Hu, Jifeng Zhang, and Y. Eugene Chen
Articles
Jun Lin, Chunwei Cao, Cong Tao, Rongcai Ye, Meng Dong, Qiantao Zheng, Chao Wang, Xiaoxiao Jiang, Guosong Qin, Changguo Yan, Kui Li, John R. Speakman, Yanfang Wang, Wanzhu Jin, and Jianguo Zhao
Jing Yan, Feng Jiang, Rong Zhang, Tongfu Xu, Zhou Zhou, Wei Ren, Danfeng Peng, Yong Liu, Cheng Hu, and Weiping Jia
Kejing Zeng, Lili Tian, Adam Sirek, Weijuan Shao, Ling Liu, Yu-Ting Chiang, Jonathan Chernoff, Dominic S. Ng, Jianping Weng, and Tianru Jin
Yanfen Cui, Yuanyuan Wang, Miao Liu, Li Qiu, Pan Xing, Xin Wang, Guoguang Ying, and Binghui Li
Lin Wang, Rui Zhang, Xue You, Huanhuan Zhang, Siying Wei, Tingting Cheng, Qianqian Cao, Zhenzhen Wang, and Yan Chen
Yan Luo, Bilian Liu, Xin Yang, Xiaoxiao Ma, Xing Zhang, Denis E. Bragin, Xuexian O. Yang, Wendong Huang, and Meilian Liu
  Collection: Metabolic Homeostasis: to Maintain or to Disrupt


Cover legend
In ß cells, the single chain precursor preproinsulin is cleaved of the signal peptide to produce proinsulin across the ER membrane. Wild-type proinsulin is then folded and delivered to the Golgi apparatus to form mature insulin, which is stored in secretory granules to be secreted (left). In contrast, the p.Ala2Thr mutation located at the signal peptide in INS gene results in an improperly cleaved proinslin, which is unfolded and retained in the ER to trigger ER stress, leading to impaired ß cell secretion function and resultant hyperglycemia (right). This causative mutation p.Ala2Thr in INS is responsible for MODY10 in Chinese population. See pages 376–383 by Yan et al. for details.
 
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