scispace - formally typeset
N

Naruhiko Adachi

Researcher at KEK

Publications -  42
Citations -  648

Naruhiko Adachi is an academic researcher from KEK. The author has contributed to research in topics: Chemistry & Medicine. The author has an hindex of 10, co-authored 31 publications receiving 390 citations. Previous affiliations of Naruhiko Adachi include University of Tokyo.

Papers
More filters
Journal ArticleDOI

Positive and negative regulation of the cardiovascular transcription factor KLF5 by p300 and the oncogenic regulator SET through interaction and acetylation on the DNA-binding domain.

TL;DR: A new pathway for regulation of a DNA-binding transcription factor on the DBD is suggested through interaction and coupled acetylation by two opposing regulatory factors of a coactivator/acetylase and a negative cofactor harboring activity to inhibit acetylations.
Journal ArticleDOI

Crystal Structure of the Human BRD2 Bromodomain INSIGHTS INTO DIMERIZATION AND RECOGNITION OF ACETYLATED HISTONE H4

TL;DR: The crystal structure of the N-terminal bromodomain (BD1, residues 74-194) of human BRD2 is reported, which is the first observation of a homodimer among the known bromidomain structures, through the buried hydrophobic core region at the interface.
Journal ArticleDOI

Discovery of non-squalene triterpenes

TL;DR: In this article , two fungal chimeric class I triterpene synthases, Talaromyces verruculosus talaropentaene synthase (TvTS) and Macrophomina phaseolina macrophomene synthesis (MpMS), were characterized.
Journal ArticleDOI

Discovery of non-squalene triterpenes

TL;DR: In this article , two fungal chimeric class I triterpene synthases, Talaromyces verruculosus talaropentaene synthase (TvTS) and Macrophomina phaseolina macrophomene synthesis (MpMS), were characterized.
Journal ArticleDOI

Structural analysis reveals TLR7 dynamics underlying antagonism

TL;DR: This work identifies the open conformation of the receptor and reveals the structural equilibrium between open and closed conformations that underlies TLR7 antagonism, as well as the detailed mechanism by which TLR 7-specific antagonists bind to their binding pocket inTLR7.