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

Culture method for promoting efficient ciliary growth in the Chlamydomonas pf23 mutant defective in dynein preassembly

促进衣藻pf23突变体(动力蛋白预组装缺陷)纤毛高效生长的培养方法

Yamamoto, Ryosuke; Kon, Takahide

Chlamydomonas FBB18 is a ubiquitin-like protein essential for the cytoplasmic preassembly of various ciliary dyneins

衣藻 FBB18 是一种类泛素蛋白,对多种纤毛动力蛋白的胞质预组装至关重要。

Yamamoto, Ryosuke; Sahashi, Yui; Shimo-Kon, Rieko; Sakato-Antoku, Miho; Suzuki, Miyuka; Luo, Leo; Tanaka, Hideaki; Ishikawa, Takashi; Yagi, Toshiki; King, Stephen M; Kurisu, Genji; Kon, Takahide

Chlamydomonas IC97, an intermediate chain of the flagellar dynein f/I1, is required for normal flagellar and cellular motility

衣藻IC97是鞭毛动力蛋白f/I1的中间链,是正常鞭毛和细胞运动所必需的。

Yamamoto, Ryosuke; Tanaka, Yui; Orii, Shunsuke; Shiba, Kogiku; Inaba, Kazuo; Kon, Takahide

Chlamydomonas dynein-preassembly-deficient mutants exhibit characteristic ciliary responses to viscous media

衣藻动力蛋白预组装缺陷突变体对粘性介质表现出特征性的纤毛反应

Yamamoto, Ryosuke; Kitamura, Yu; Kon, Takahide

Composition and function of ciliary inner-dynein-arm subunits studied in Chlamydomonas reinhardtii

对莱茵衣藻纤毛内动力蛋白臂亚基的组成和功能进行了研究

Yamamoto, Ryosuke; Hwang, Juyeon; Ishikawa, Takashi; Kon, Takahide; Sale, Winfield S

Mutations in PIH proteins MOT48, TWI1 and PF13 define common and unique steps for preassembly of each, different ciliary dynein

PIH蛋白MOT48、TWI1和PF13的突变决定了每种不同的纤毛动力蛋白预组装的共同和独特步骤。

Yamamoto, Ryosuke; Yanagi, Shiho; Nagao, Masahito; Yamasaki, Yuya; Tanaka, Yui; Sale, Winfield S; Yagi, Toshiki; Kon, Takahide

Chlamydomonas DYX1C1/PF23 is essential for axonemal assembly and proper morphology of inner dynein arms

衣藻 DYX1C1/PF23 对于轴丝组装和内动力蛋白臂的正常形态至关重要

Yamamoto, Ryosuke; Obbineni, Jagan M; Alford, Lea M; Ide, Takahiro; Owa, Mikito; Hwang, Juyeon; Kon, Takahide; Inaba, Kazuo; James, Noliyanda; King, Stephen M; Ishikawa, Takashi; Sale, Winfield S; Dutcher, Susan K

Elastic properties of dynein motor domain obtained from all-atom molecular dynamics simulations

通过全原子分子动力学模拟获得的动力蛋白马达结构域的弹性特性

Kamiya, Narutoshi; Mashimo, Tadaaki; Takano, Yu; Kon, Takahide; Kurisu, Genji; Nakamura, Haruki

A flipped ion pair at the dynein-microtubule interface is critical for dynein motility and ATPase activation

动力蛋白-微管界面处翻转的离子对对于动力蛋白的运动和ATPase的激活至关重要。

Uchimura, Seiichi; Fujii, Takashi; Takazaki, Hiroko; Ayukawa, Rie; Nishikawa, Yosuke; Minoura, Itsushi; Hachikubo, You; Kurisu, Genji; Sutoh, Kazuo; Kon, Takahide; Namba, Keiichi; Muto, Etsuko

Tug-of-war of microtubule filaments at the boundary of a kinesin- and dynein-patterned surface.

在驱动蛋白和动力蛋白图案化表面的边界处,微管丝发生拔河比赛

Ikuta Junya, Kamisetty Nagendra K, Shintaku Hirofumi, Kotera Hidetoshi, Kon Takahide, Yokokawa Ryuji