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Ischaemic concentrations of lactate increase TREK1 channel activity by interacting with a single histidine residue in the carboxy terminal domain

机译：乳酸的缺血浓度通过与羧基末端结构域中的单个组氨酸残基相互作用而提高了TREK1通道的活性

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期刊名称 The Journal of Physiology
作者
Swagata Ghatak; Aditi Banerjee; Sujit Kumar Sikdar;
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作者单位

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年(卷),期 2016(594),1
年度 2016
页码 59–81
总页数 23
原文格式 PDF
正文语种
中图分类神经科学;人体生理学;
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专利

1. Ischaemic concentrations of lactate increase TREK1 channel activity by interacting with a single histidine residue in the carboxy terminal domain [J] . The Journal of Physiology . 2016,第1期

机译：乳酸的缺血浓度通过与羧基末端结构域中的单个组氨酸残基相互作用而增加了TREK1通道的活性
2. Extracellular acidification exerts opposite actions on TREK1 and TREK2 potassium channels via a single conserved histidine residue [J] . Guillaume Sandoz, Dominique Douguet, Franck Chatelain, Proceedings of the National Academy of Sciences of the United States of America . 2009,第34期

机译：细胞外酸化通过一个保守的组氨酸残基对TREK1和TREK2钾通道产生相反的作用
3. SMRT recruitment by PPARgamma is mediated by specific residues located in its carboxy-terminal interacting domain. [J] . Sutanto MM, Symons MS, Cohen RN Molecular and Cellular Endocrinology . 2006,第1a2期

机译：PPARγ的SMRT募集是由位于其羧基末端相互作用域中的特定残基介导的。
4. Decision Feedback Channel Estimation Scheme Using Terminal Speed for Single-Carrier Frequency-Domain Equalization [C] . Mihara Hirotaka, Maehara Fumiaki IEEE Vehicular Technology Conference . 2015

机译：终端速度的单载波频域均衡决策反馈信道估计方案
5. A carboxy-terminal truncation of human alpha-galactosidase A in a heterozygous female with Fabry disease and modification of the enzymatic activity by the carboxy-terminal domain. Increased reduced or absent enzyme activity depending on number of amino acid residues deleted. [O] . N Miyamura, E Araki, K Matsuda, 1996

机译：在患有Fabry病的杂合雌性中人α-半乳糖苷酶A的羧基末端截短并通过羧基末端结构域修饰酶活性。增加减少或缺乏酶活性取决于缺失的氨基酸残基数量。
6. Ischaemic concentrations of lactate increase TREK1 channel activity by interacting with a single histidine residue in the carboxy terminal domain [O] . Ghatak, Swagata, Banerjee, Aditi, Sikdar, Sujit Kumar 2016

机译：乳酸的缺血浓度通过与羧基末端结构域中的单个组氨酸残基相互作用而提高了TREK1通道的活性
7. Evidence for the Participation of Histidine Residues Located in the 56 kDa C-Terminal Polypeptide Domain of ADP-Ribosyl Transferase in its Catalytic Activity [R] . Kun, E. 1990

机译：位于aDp核糖基转移酶56kDa C-末端多肽结构域的组氨酸残基参与其催化活性的证据

Ischaemic concentrations of lactate increase TREK1 channel activity by interacting with a single histidine residue in the carboxy terminal domain

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