Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Takaki, Momose"'
Autor:
Chiaki Handa, Yuki Yamazaki, Shigeru Yonekubo, Noritaka Furuya, Takaki Momose, Tomonaga Ozawa, Takayuki Furuishi, Kaori Fukuzawa, Etsuo Yonemochi
Publikováno v:
The Journal of steroid biochemistry and molecular biology. 222
Estrogen receptors (ERs) are ligand-activated transcription factors, with two subtypes ERα and ERβ. The endogenous ligand of ERs is the common 17β-estradiol, and the ligand-binding pocket of ERα and ERβ is very similar. Nevertheless, some ERβ-s
Publikováno v:
ACS Medicinal Chemistry Letters. 8:660-665
Photoaffinity labeling (PAL) is widely used for the identification of ligand-binding proteins and elucidation of ligand-binding sites. PAL has also been employed for the characterization of G protein-coupled receptors (GPCRs); however, a limited numb
Publikováno v:
ACS medicinal chemistry letters. 8(6)
Photoaffinity labeling (PAL) is widely used for the identification of ligand-binding proteins and elucidation of ligand-binding sites. PAL has also been employed for the characterization of G protein-coupled receptors (GPCRs); however, a limited numb
Publikováno v:
Photoaffinity Labeling for Structural Probing Within Protein ISBN: 9784431565680
Photoaffinity labeling (PAL) is a method that forms an irreversible covalent bond between photoreactive ligands and neighboring amino acids under the irradiation of light. PAL is utilized in the pharmacological and biochemical identification of ligan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::13d1830244dc741395431d10f2c060f1
https://doi.org/10.1007/978-4-431-56569-7_12
https://doi.org/10.1007/978-4-431-56569-7_12
Autor:
Toshiya Endo, Takaki Momose, Takehiro Sato, Keisuke Yagawa, Takaomi Oguro, Koji Yamano, Shin Kawano, Masahiro Maeda
Publikováno v:
Protein Science. 19:693-702
Point mutations in proteins can have different effects on protein stability depending on the mechanism of unfolding. In the most interesting case of I27, the Ig-like module of the muscle protein titin, one point mutation (Y9P) yields opposite effects
Autor:
Kayoko Terao, Shin Kawano, Mari Naoé, Shuh-ichi Nishikawa, Koji Yamano, Nobuhisa Watanabe, Toshiya Endo, Takaki Momose
Publikováno v:
Proceedings of the National Academy of Sciences. 106:14403-14407
The mitochondrial intermembrane space (IMS) contains many small cysteine-bearing proteins, and their passage across the outer membrane and subsequent folding require recognition and disulfide bond transfer by an oxidative translocator Tim40/Mia40 in
Publikováno v:
EMBO reports. 8:664-670
Mitochondrial heat-shock protein 70 (mtHsp70) and its partner proteins drive protein import into the matrix. Tim15/Zim17/Hep1 is a mtHsp70 partner protein on the matrix side of the inner mitochondrial membrane. We determined the nuclear magnetic reso
Autor:
Tadashi Makio, Mayumi Matsunaga, Daisuke Kohda, Hayashi Yamamoto, Alyson E. Aiken Hobbs, Mihoko Yokota, Takaki Momose, Masatoshi Esaki, Yoh Ichi Yatsukawa, Toshihiro Shodai, Nobuka Itoh, Toshiya Endo, Shin Kawano, Robert E. Jensen
Mitochondria import most of their resident proteins from the cytosol, and the import receptor Tom20 of the outer-membrane translocator TOM40 complex plays an essential role in specificity of mitochondrial protein import. Here we analyzed the effects
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::adf2dcf093fe7d47a661ca69bc1fb438
https://europepmc.org/articles/PMC3017135/
https://europepmc.org/articles/PMC3017135/
Autor:
Keisuke, Yagawa, Koji, Yamano, Takaomi, Oguro, Masahiro, Maeda, Takehiro, Sato, Takaki, Momose, Shin, Kawano, Toshiya, Endo
Publikováno v:
Protein science : a publication of the Protein Society. 19(4)
Point mutations in proteins can have different effects on protein stability depending on the mechanism of unfolding. In the most interesting case of I27, the Ig-like module of the muscle protein titin, one point mutation (Y9P) yields opposite effects
Publikováno v:
Journal of molecular biology. 385(3)
Protein import into mitochondria requires unfolding of the folded mature domain of precursor proteins. Here we compared the effects of amino-acid replacement between the core region and the N-terminal region of the titin I27 domain (the 27th Ig domai