SUMOYLATION

作品数:87被引量:165H指数:7
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相关领域:医药卫生生物学更多>>
相关作者:龚宇彭章龙张简尤圣武廖书胜更多>>
相关机构:中南大学上海交通大学华东师范大学中国科学院大学更多>>
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相关基金:国家自然科学基金广东省自然科学基金国家重点基础研究发展计划北京市自然科学基金更多>>
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KIF17 Modulates Epileptic Seizures and Membrane Expression of the NMDA Receptor Subunit NR2B
《Neuroscience Bulletin》2022年第8期841-856,共16页Yan Liu Xin Tian Pingyang Ke Juan Gu Yuanlin Ma Yi Guo Xin Xu Yuanyuan Chen Min Yang Xuefeng Wang Fei Xiao 
This work was supported by grants from the National Natural Science Foundation of China(81873788,81922023,82001378,and 82171440);the Chongqing Natural Science Foundation Project(cstc2019jcyj-msxmX0184);the Fifth Senior Medical Talents Program of Chongqing for Young and Middle-aged.
Epilepsy is a common and severe brain disease affecting>65 million people worldwide.Recent studies have shown that kinesin superfamily motor protein 17(KIF17)is expressed in neurons and is involved in regulating the d...
关键词:EPILEPSY KIF17 NR2B SUMOYLATION 
SUMOylation of Fragile X Mental Retardation Protein: A Critical Mechanism of FMRP-Mediated Neuronal Function
《Neuroscience Bulletin》2018年第6期1100-1102,共3页Mingzhu Tang Liqun Lu Feng Xie Linxi Chen 
supported by the National Natural Science Foundation of China (81503074)
Recently, Khayachi et al.;showed that fragile X mental retardation protein (FMRP) is an active substrate of the small ubiquitin-like modifier (SUMO) pathway in neurons.FMRP SUMOylation is induced by the activation...
关键词:FXS AD In SUMOylation of Fragile X Mental Retardation Protein 
The role of post-translational modifications of huntingtin in the pathogenesis of Huntington's disease
《Neuroscience Bulletin》2010年第2期153-162,共10页王雁 林芳 秦正红 
supported by grants from the National Natural Science Foundation of China (No.30600197)
Post-translational modifications are rapid, effective and reversible ways to regulate protein stability, localization, function, and their interactions with other molecules. Post-translational modifications usually oc...
关键词:Huntington's disease HUNTINGTIN modification SUMOYLATION PHOSPHORYLATION PALMITOYLATION ACETYLATION 
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