Effects of Bienzyme Complex Formation of Cysteine Synthetase from Escherichia coli on Some Properties and Kinetics
- K. Mino, T. Yamanoue, T. Sakiyama, N. Eisaki, A. Matsuyama, K. Nakanishi
- BiologyBioscience, biotechnology and biochemistry
- 1 January 2000
The role and significance of a complex formation for the cysteine synthetase is discussed and changes in the stability of the wild-type SAT by the complex formation are discussed.
Identification of cell-active lysine specific demethylase 1-selective inhibitors.
- Rie Ueda, Takayoshi Suzuki, N. Miyata
- Biology, ChemistryJournal of the American Chemical Society
- 16 November 2009
The first small-molecule LSD1-selective inhibitors are identified and show in vivo H3K4-methylating activity and antiproliferative activity and should be useful as lead structures for anticancer drugs and as tools for studying the biological roles of LSD1.
Identification of SAP155 as the target of GEX1A (Herboxidiene), an antitumor natural product.
- M. Hasegawa, Tatsuhiro Miura, T. Mizukami
- Biology, ChemistryACS Chemical Biology
- 13 January 2011
GEX1A serves as a novel splicing inhibitor that specifically impairs the SF3b function by binding to SAP155 protein, a subunit ofSF3b responsible for pre-mRNA splicing.
Design, synthesis, enzyme-inhibitory activity, and effect on human cancer cells of a novel series of jumonji domain-containing protein 2 histone demethylase inhibitors.
- Shohei Hamada, Takayoshi Suzuki, N. Miyata
- Chemistry, BiologyJournal of Medicinal Chemistry
- 14 July 2010
Findings suggest that combination treatment with JMJD2 inhibitors and LSD1 inhibitors may represent a novel strategy for anticancer chemotherapy.
Characteristics of Serine Acetyltransferase from Escherichia coli Deleting Different Lengths of Amino Acid Residues from the C-Terminus
- K. Mino, K. Hiraoka, K. Nakanishi
- Biology, ChemistryBioscience, biotechnology and biochemistry
- 1 January 2000
It was indicated that 10 amino acid residues or fewer from the C-terminus of the wild-type SAT are responsible for the complex formation with OASS-A.
A novel O‐phospho‐L‐serine sulfhydrylation reaction catalyzed by O‐acetylserine sulfhydrylase from Aeropyrum pernix K1
- K. Mino, K. Ishikawa
- Chemistry, BiologyFEBS Letters
- 11 September 2003
Characterization of a Novel Thermostable O-Acetylserine Sulfhydrylase from Aeropyrum pernix K1
- K. Mino, K. Ishikawa
- Biology, ChemistryJournal of Bacteriology
- 1 April 2003
ABSTRACT An O-acetylserine sulfhydrylase (OASS) from the hyperthermophilic archaeon Aeropyrum pernix K1, which shares the pyridoxal 5′-phosphate binding motif with both OASS and cystathionine…
Structural basis of Ets1 cooperative binding to palindromic sequences on stromelysin-1 promoter DNA
- N. Babayeva, P. Wilder, T. Tahirov
- ChemistryCell Cycle
- 1 August 2010
Ets1 is a member of the Ets family of transcription factors that binds to EMTs and acts as a “spatially aggregating force” to knock down the number of “bad” genes in the immune system.
Identification of ryuvidine as a KDM5A inhibitor
- Eishin Mitsui, Shogo Yoshida, T. Mizukami
- Biology, ChemistryScientific Reports
- 9 July 2019
Ryuvidine may serve as a lead compound for KDM5 targeted therapeutics after it was found that ryuvidine prevented generation of gefitinib-tolerant human small-cell lung cancer PC9 cells and also inhibited the growth of the drug-Tolerant cells at concentrations that did not affect thegrowth of parentalPC9 cells.
Identification of the KDM2/7 Histone Lysine Demethylase Subfamily Inhibitor and its Antiproliferative Activity
- Takayoshi Suzuki, Hiroki Ozasa, N. Miyata
- Chemistry, BiologyJournal of Medicinal Chemistry
- 21 August 2013
While inhibitors of KDM4s did not show any effect on cancer cells tested, the KDM2/7-subfamily inhibitor 9 exerted antiproliferative activity, indicating the potential for KDM 2/7 inhibitors as anticancer agents.
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