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Rong Li, Di-Dong Xie, Jun-hong Dong, Hui Li, Kang-shuai Li, Jing Su, Lai-Zhong Chen, Yun-Fei Xu, Hong-Mei Wang, Zheng Gong, Guo-Ying Cui, Xiao Yu, Kai Wang, Wei Yao, Tao Xin, Min-Yong Li, Kun-Hong Xiao, Xiao-fei An, Yuqing Huo, Zhi-gang Xu, Jin-Peng Sun and Qi Pang Molecular mechanism of ERK dephosphorylation by striatal-enriched protein tyrosine phosphatase Journal of Neurochemistry 128

Version of Record online: 31 OCT 2013 | DOI: 10.1111/jnc.12463

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Regulation of phospho-ERK by STEP underlies important neuronal activities. A detailed enzymologic characterisation and cellular studies of STEP revealed that specific residues in KIM and active site mediated ERK recognition. Structural differences between the KIM-ERK interfaces and the active site among different ERK phosphatases could be targeted to develop specific STEP inhibitor, which has therapeutic potential for neurological disorders. PKA, protein kinase A & NGF, nerve growth factor.

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