Welcome to Project Laboratory

Our laboratory researches and supports various projects.
We are analyzing the structure of proteins related to histone modification, basic transcription, transcriptional activity, transcriptional repression, and heterochromatin formation in telomeres and centromeres using NMR.



"Three human RNA polymerases interact with TFIIH via a common RPB6 subunit." has been accepted in Nucleic Acids Research(2021 Jun 16)


"The N-terminal Tails of Histones H2A and H2B Adopt Two Distinct Conformations in the Nucleosome with Contact and Reduced Contact to DNA." has been accepted in Journal of Molecular Biology(2021 Jun 18)


"Difference of binding modes among three ligands to a receptor mSin3B corresponding to their inhibitory activities." has been accepted in Scientific Reports(2021 Mar 17)


"Mechanism of hERG inhibition by gating-modifier toxin, APETx1"Mechanism of hERG inhibition by gating-modifier toxin, APETx1, deduced by functional characterization." has been accepted in BMC Molecluar and Cell Biology(2021 Jan 7)


Dr. Okuda's art design covered the issue of NAR. "Structural and dynamical insights into the PH domain of p62 in human TFIIH." has been published in Nucleic Acids Research(Volume 49, Issue 5, 18 March 2021, Pages 2916–2930)


"Structural dynamics of double-stranded DNA with epigenome modification." has been accepted in Nucleic Acids Research(2020 Dec 19, Online)


"Partial replacement of nucleosomal DNA with human FACT induces dynamic exposure and acetylation of histone H3 N-terminal tails." has been accepted in iScience(2020 Oct 23, Online)


"Acetylated histone H4 tail enhances histone H3 tail acetylation by altering their mutual dynamics in the nucleosome." has been accepted in Proceedings of the National Academy of Sciences of the United States of America(2020 Aug 4, Online)


"The Eaf3 chromodomain acts as a pH sensor for gene expression by altering its binding affinity for histone methylated-lysine residues." has been accepted in Bioscience Reports(2020 Feb 7)


"Structural visualization of key steps in nucleosome reorganization by human FACT." has accepted in Scientific Reports(2019 Jul 15)


"Sertraline, chlorprothixene, and chlorpromazine characteristically interact with the REST-binding site of the corepressor mSin3, showing medulloblastoma cell growth inhibitory activities." has been accepted in Scientific Reports(2018 Sep 13, Online)


"Common TFIIH recruitment mechanism in global genome and transcription-coupled repair subpathways." has been accepted in Nucleic Acids Res.(2017 Dec 15)


"A mimetic of the mSin3-binding helix of NRSF/REST ameliorates abnormal pain behavior in chronic pain models" has been accepted in Bioorganic & Medicinal Chemistry Letters(2017 Oct 15)


"Impact of nucleic acid and methylated H3K9 binding activities of Suv39h1 on its heterochromatin assembly." has been accepted in eLIFE(2017 Aug 1)


"Crystal structure of the overlapping dinucleosome composed of hexasome and octasome." has been accepted in Science


"NMR Screening of mSin3B Binding Compounds for the Interaction Inhibition with a Neural Repressor, NRSF/REST" has been published in Modern Magnetic Resonance(Springer International Publishing, 2017)


"The Interaction Mode of the Acidic Region of the Cell Cycle Transcription Factor DP1 with TFIIH." has been accepted in Journal of Molecular Biology(2016 Dec 4)


"Dynamics of the Extended String-Like Interaction of TFIIE with the p62 Subunit of TFIIH." has been accepted in Biophysical Journal(2016 Sep 6)


"Solution structure of the isolated histone H2A-H2B heterodimer." has been accepted in Scientific Reports(2016 May 16)


"Extended string-like binding of the phosphorylated HP1α N-terminal tail to the lysine 9-methylated histone H3 tail" has been accepted in Scientific Reports(2016 Mar 3)



Dr. Okuda's art design covered the issue of STRUCTURE. "Structural Insight into the Mechanism of TFIIH Recognition by the Acidic String of the Nucleotide Excision Repair Factor XPC." has been published in STRUCTURE (2015 Oct 6)


Contact us

1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045 JAPAN
TEL +81-45-508-7211 (Dr. Nishimura's room [A111])
TEL +81-45-508-7381 (Staff room [A115], Laboratory[A113,A114])
FAX +81-45-508-7360