Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Yong-Suk Che"'
Autor:
Yong-Suk Che, Takashi Sagawa, Yuichi Inoue, Hiroto Takahashi, Tatsuki Hamamoto, Akihiko Ishijima, Hajime Fukuoka
Publikováno v:
Biomolecules, Vol 10, Iss 11, p 1544 (2020)
Signal transduction utilizing membrane-spanning receptors and cytoplasmic regulator proteins is a fundamental process for all living organisms, but quantitative studies of the behavior of signaling proteins, such as their diffusion within a cell, are
Externí odkaz:
https://doaj.org/article/bcb98ac71b774d788b7a7209aae55b25
Autor:
Yumiko Uchida, Tatsuki Hamamoto, Yong-Suk Che, Hiroto Takahashi, John S. Parkinson, Akihiko Ishijima, Hajime Fukuoka
Publikováno v:
J Bacteriol
In isotropic environments, an Escherichia coli cell exhibits coordinated rotational switching of its flagellar motors, produced by fluctuations in the intracellular concentration of phosphorylated CheY (CheY-P) emanating from chemoreceptor signaling
Autor:
Takashi Sagawa, Akihiko Ishijima, Hajime Fukuoka, Yong-Suk Che, Tatsuki Hamamoto, Hiroto Takahashi, Yuichi Inoue
Publikováno v:
Biomolecules
Volume 10
Issue 11
Biomolecules, Vol 10, Iss 1544, p 1544 (2020)
Volume 10
Issue 11
Biomolecules, Vol 10, Iss 1544, p 1544 (2020)
Signal transduction utilizing membrane-spanning receptors and cytoplasmic regulator proteins is a fundamental process for all living organisms, but quantitative studies of the behavior of signaling proteins, such as their diffusion within a cell, are
Publikováno v:
Minorities and Small Numbers from Molecules to Organisms in Biology ISBN: 9789811320828
Escherichia coli and other bacteria are said to be the lowest forms of life in the biological world. Nevertheless, bacteria are magnificent organisms that can recognize the ambient environment, propagate ambient information into its body, and (in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::df94f1715ae3beb082f3e57e5e161e21
https://doi.org/10.1007/978-981-13-2083-5_16
https://doi.org/10.1007/978-981-13-2083-5_16
Autor:
Koichi D. Hiraoka, Mariko Ito, Yong-Suk Che, Tohru Minamino, Yusuke V. Morimoto, Keiichi Namba, Nobunori Kami-ike, Fan Bai
Publikováno v:
Molecular Microbiology. 91:1214-1226
The bacterial flagellar export apparatus is required for the construction of the bacterial flagella beyond the cytoplasmic membrane. The membrane-embedded part of the export apparatus, which consists of FlhA, FlhB, FliO, FliP, FliQ and FliR, is locat
Autor:
Tohru Minamino, Shuichi Nakamura, Keiichi Namba, Nobunori Kami-ike, Yong-Suk Che, Yusuke V. Morimoto
Publikováno v:
Molecular Microbiology. 91:175-184
The Salmonella flagellar motor consists of a rotor and about a dozen stator elements. Each stator element, consisting of MotA and MotB, acts as a proton channel to couple proton flow with torque generation. A highly conserved Asp33 residue of MotB is
Autor:
Yusuke V. Morimoto, Nobunori Kami-ike, David J. Castillo, Yong-Suk Che, Keiichi Namba, Seishi Kudo, Tohru Minamino, Shuichi Nakamura
Publikováno v:
Biophysics
The bacterial flagellar motor is made of a rotor and stators. In Salmonella it is thought that about a dozen MotA/B complexes are anchored to the peptidoglycan layer around the motor through the C-terminal peptidoglycan-binding domain of MotB to beco
Autor:
Yusuke V, Morimoto, Mariko, Ito, Koichi D, Hiraoka, Yong-Suk, Che, Fan, Bai, Nobunori, Kami-Ike, Keiichi, Namba, Tohru, Minamino
Publikováno v:
Molecular microbiology. 91(6)
The bacterial flagellar export apparatus is required for the construction of the bacterial flagella beyond the cytoplasmic membrane. The membrane-embedded part of the export apparatus, which consists of FlhA, FlhB, FliO, FliP, FliQ and FliR, is locat
Autor:
Yong-Suk, Che, Shuichi, Nakamura, Yusuke V, Morimoto, Nobunori, Kami-Ike, Keiichi, Namba, Tohru, Minamino
Publikováno v:
Molecular microbiology. 91(1)
The Salmonella flagellar motor consists of a rotor and about a dozen stator elements. Each stator element, consisting of MotA and MotB, acts as a proton channel to couple proton flow with torque generation. A highly conserved Asp33 residue of MotB is
Publikováno v:
FEBS letters. 584(6)
MotA and MotB form the proton-channel complex of the proton-driven bacterial flagellar motor. A plug segment of Escherichia coli MotB suppresses proton leakage through the MotA/B complex when it is not assembled into the motor. Using a ratiometric pH