日期:
2020 年 — 2026 年
2020
2021
2022
2023
2024
2025
2026
影响因子:

CryoEM structures of Kv1.2 potassium channels, conducting and non-conducting.

Kv1.2钾通道的冷冻电镜结构,包括导电型和非导电型

Wu Yangyu, Yan Yangyang, Yang Youshan, Bian Shumin, Rivetta Alberto, Allen Ken, Sigworth Fred J

TMED10 mediates the trafficking of insulin-like growth factor 2 along the secretory pathway for myoblast differentiation

TMED10 介导胰岛素样生长因子 2 沿分泌途径的运输,促进成肌细胞分化

Tiantian Li #, Feng Yang #, Youshan Heng, Shaopu Zhou, Gang Wang, Jianying Wang, Jinhui Wang, Xianwei Chen, Zhong-Ping Yao, Zhenguo Wu, Yusong Guo

Expression, purification and functional reconstitution of slack sodium-activated potassium channels.

松弛钠激活钾通道的表达、纯化和功能重建

Yan Yangyang, Yang Youshan, Bian Shumin, Sigworth Fred J

Asp433 in the closing gate of ASIC1 determines stability of the open state without changing properties of the selectivity filter or Ca2+ block

ASIC1 的关闭门中的 Asp433 决定了其开放状态的稳定性,而不会改变选择性过滤器或 Ca2+ 阻断的特性。

Li, Tianbo; Yang, Youshan; Canessa, Cecilia M

Cloning and identification of tissue-specific expression of KCNN4 splice variants in rat colon

克隆和鉴定大鼠结肠中KCNN4剪接变体的组织特异性表达

Barmeyer, Christian; Rahner, Christoph; Yang, Youshan; Sigworth, Frederick J; Binder, Henry J; Rajendran, Vazhaikkurichi M

Two residues in the extracellular domain convert a nonfunctional ASIC1 into a proton-activated channel

胞外结构域中的两个残基可将无功能的ASIC1转化为质子激活通道。

Li, Tianbo; Yang, Youshan; Canessa, Cecilia M

Leu85 in the beta1-beta2 linker of ASIC1 slows activation and decreases the apparent proton affinity by stabilizing a closed conformation

ASIC1 的 β1-β2 连接子中的 Leu85 通过稳定闭合构象来减缓活化并降低表观质子亲和力。

Li, Tianbo; Yang, Youshan; Canessa, Cecilia M

Asn415 in the beta11-beta12 linker decreases proton-dependent desensitization of ASIC1

β11-β12连接区中的Asn415降低了ASIC1的质子依赖性脱敏作用。

Li, Tianbo; Yang, Youshan; Canessa, Cecilia M

Interaction of the aromatics Tyr-72/Trp-288 in the interface of the extracellular and transmembrane domains is essential for proton gating of acid-sensing ion channels

胞外结构域和跨膜结构域界面处的芳香族氨基酸残基Tyr-72/Trp-288的相互作用对于酸敏感离子通道的质子门控至关重要。

Li, Tianbo; Yang, Youshan; Canessa, Cecilia M