structure of the transcriptional coactivator (2008)
Jun Ozaki, Ken-ichi Takemaru, Takahisa Ikegami, Masaki Mishima, Hitoshi Ueda, Susumu Hirose, ...
Identification of the core domain and the secondary
Studies of DNA recognition mechanism of transcription factor IRF-4 (2006)
Furuita, Kyoko, Ishizaki, Itsuko, Fukada, Harumi, Yamamoto, Kazuo, Matsuyama, Toshifumi, Nomura, Makoto, ...
Transcription factor IFN regulatory factor-4 (IRF-4) prefers a DNA sequence including CCGAAA, though the consensus DNA-binding sequence of the IRF family proteins is NNGAAA, and the crystal structure...
Solution structure of a small-molecular ligand complexed with CAG trinucleotide repeat DNA (2005)
Nakatani, Kazuhiko, Hagihara, Shinya, Goto, Yuki, Kobori, Akio, Hagihara, Masaki, Hayashi, Gosuke, ...
NMR structure of the first identified ligand, naphthyridine–azaquinolone (NA), complexed with the CAG-CAG triad is reported. The determined structure revealed the invasive ligands binding to the...
Tominaga, Yohei, Ushijima, Yasuhiro, Tsuchimoto, Daisuke, Mishima, Masaki, Shirakawa, Masahiro, Hirano, Seiki, ...
MutY homolog (MUTYH) excises adenine opposite 8-oxoguanine (8-oxoG) in DNA, thus preventing occurrence of G:C to T:A transversion. In cell-free extract prepared from the thymocytes of wild type but...
Tenno, Takeshi, Goda, Natsuko, Tateishi, Yukihiro, Tochio, Hidehito, Mishima, Masaki, Hayashi, Hidenori, ...
Fusion protein constructs for labeled peptides were generated with the 114 amino acid thioredoxin (TRX), coupled with the incorporation of a histidine tag for affinity purification. Two tandem AhdI...
Solution NMR study of DNA recognition mechanism of IRF4 protein (2004)
Ishizaki, Itsuko, Nomura, Makoto, Yamamoto, Kazuo, Matsuyama, Toshifumi, Mishima, Masaki, Kojima, Chojiro
Transcription factor IRF-4 prefers the DNA sequence including CCGAAA. The consensus sequence of the IRF family proteins is NNGAAA, and all crystal structures indicate the NN region does not interact...
Tenno, Takeshi, Goda, Natsuko, Tateishi, Yukihiro, Tochio, Hidehito, Mishima, Masaki, Hayashi, Hidenori, ...
Fusion protein constructs for labeled peptides were generated with the 114 amino acid thioredoxin (TRX), coupled with the incorporation of a histidine tag for affinity purification. Two tandem AhdI...
Tenno, Takeshi, Goda, Natsuko, Tateishi, Yukihiro, Tochio, Hidehito, Mishima, Masaki, Hayashi, Hidenori, ...
Fusion protein constructs for labeled peptides were generated with the 114 amino acid thioredoxin (TRX), coupled with the incorporation of a histidine tag for affinity purification. Two tandem AhdI...
Tominaga, Yohei, Ushijima, Yasuhiro, Tsuchimoto, Daisuke, Mishima, Masaki, Shirakawa, Masahiro, Hirano, Seiki, ...
MutY homolog (MUTYH) excises adenine opposite 8-oxoguanine (8-oxoG) in DNA, thus preventing occurrence of G:C to T:A transversion. In cell-free extract prepared from the thymocytes of wild type but...
Tominaga, Yohei, Ushijima, Yasuhiro, Tsuchimoto, Daisuke, Mishima, Masaki, Shirakawa, Masahiro, Hirano, Seiki, ...
MutY homolog (MUTYH) excises adenine opposite 8-oxoguanine (8-oxoG) in DNA, thus preventing occurrence of G:C to T:A transversion. In cell-free extract prepared from the thymocytes of wild type but...
Structural basis for tubulin recognition by cytoplasmic linker protein 170 and its autoinhibition
Mishima, Masaki, Maesaki, Ryoko, Kasa, Miyuki, Watanabe, Takashi, Fukata, Masaki, Kaibuchi, Kozo, ...
Cytoplasmic linker protein 170 (CLIP-170) is a prototype of the plus end-tracking proteins that regulate microtubule dynamics, but it is obscure how CLIP-170 recognizes the microtubule plus end and...