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Bin Zhang
Researcher at Zhejiang University
Publications - 7
Citations - 149
Bin Zhang is an academic researcher from Zhejiang University. The author has contributed to research in topics: NMDA receptor & Phosphorylation. The author has an hindex of 7, co-authored 7 publications receiving 115 citations.
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Journal ArticleDOI
Phosphorylation of Tyrosine 1070 at the GluN2B Subunit Is Regulated by Synaptic Activity and Critical for Surface Expression of N-Methyl-d-aspartate (NMDA) Receptors
Wen Lu,Weiqing Fang,Jian Li,Bin Zhang,Qian Yang,Xun-yi Yan,Lin Peng,Heng Ai,Jie-jie Wang,Xiao Liu,Jianhong Luo,Wei Yang +11 more
TL;DR: A tyrosine site on the GluN2B subunit, Tyr-1070, was identified, which was phosphorylated by a proto-oncogene tyosine-protein (Fyn) kinase and critical for the surface expression of Glu N2B-containing NMDARs, providing a new mechanism for regulating the surface Expression of NMD ARs with implications for synaptic plasticity.
Journal ArticleDOI
Activity-induced synaptic delivery of the GluN2A-containing NMDA receptor is dependent on endoplasmic reticulum chaperone Bip and involved in fear memory
Xiao-min Zhang,Xun-yi Yan,Bin Zhang,Qian Yang,Mao Ye,Wei Cao,Wen-bin Qiang,Lijun Zhu,Yong-lan Du,Xing-Xing Xu,Jia-sheng Wang,Fei Xu,Wei Lu,Shuang Qiu,Wei Yang,Jianhong Luo +15 more
TL;DR: A novel mechanism for the activity-dependent supply of synaptic GluN2A-containing NMDARs is uncovered, its relevance to memory formation is demonstrated, and intraperitoneal injection of the interfering peptide before training is disrupted.
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A novel phosphorylation site of N-methyl-d-aspartate receptor GluN2B at S1284 is regulated by Cdk5 in neuronal ischemia
TL;DR: NMDAR GluN2B S1284 was identified as a novel phosphorylation site regulated by Cdk5 with implication in neuronal ischemia, and no significant changes in the phosphorylated level of this site are found neither in chemical LTP stimulation in cultured hippocampal neurons nor fear conditioning in adult mice.
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UHRF2 regulates local 5-methylcytosine and suppresses spontaneous seizures
TL;DR: A unique role of U HRF2 in the maintenance of local 5mC levels in brain that is distinct from that of its paralog UHRF1 is revealed.
Journal ArticleDOI
Zinc Finger Protein 618 Regulates the Function of UHRF2 (Ubiquitin-like with PHD and Ring Finger Domains 2) as a Specific 5-Hydroxymethylcytosine Reader.
TL;DR: This study has identified zinc figure protein 618 (ZNF618) as a novel binding partner of UHRF2 and suggests that ZNF618 is a key protein that regulates U HRF2 function as a specific 5hmC reader in vivo.