TY - JOUR
T1 - Nuclear receptor mediated gene regulation through chromatin remodeling and histone modifications
AU - Kishimoto, Masahiko
AU - Fujiki, Ryoji
AU - Takezawa, Shinichiro
AU - Sasaki, Yasumasa
AU - Nakamura, Takashi
AU - Yamaoka, Kazuyoshi
AU - Kitagawa, Hirochika
AU - Kato, Shigeaki
PY - 2006
Y1 - 2006
N2 - Nuclear steroid/thyroid vitamin A/D receptor genes form a gene superfamily and encode DNA-binding transcription factors that control the transcription of target genes in a ligand-dependent manner. It has become clear that chromatin remodeling and the modification of histones, the main components of chromatin, play crucial roles in gene transcription, and many distinct classes of NR-interacting co-regulators have been identified that perform significant roles in gene transcription. Since NR dysfunction can lead to the onset or progression of endocrine disease, elucidation of the mechanisms of gene regulation mediated by NRs, as well as the identification and characterization of co-regulator complexes (especially chromatin remodeling and histone-modifying complexes), is essential not only for better understanding of NR ligand function, but also for pathophysiological studies and the development of therapeutic interventions in humans.
AB - Nuclear steroid/thyroid vitamin A/D receptor genes form a gene superfamily and encode DNA-binding transcription factors that control the transcription of target genes in a ligand-dependent manner. It has become clear that chromatin remodeling and the modification of histones, the main components of chromatin, play crucial roles in gene transcription, and many distinct classes of NR-interacting co-regulators have been identified that perform significant roles in gene transcription. Since NR dysfunction can lead to the onset or progression of endocrine disease, elucidation of the mechanisms of gene regulation mediated by NRs, as well as the identification and characterization of co-regulator complexes (especially chromatin remodeling and histone-modifying complexes), is essential not only for better understanding of NR ligand function, but also for pathophysiological studies and the development of therapeutic interventions in humans.
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U2 - 10.1507/endocrj.53.157
DO - 10.1507/endocrj.53.157
M3 - Review article
C2 - 16618973
AN - SCOPUS:33645877393
SN - 0918-8959
VL - 53
SP - 157
EP - 172
JO - Endocrine Journal
JF - Endocrine Journal
IS - 2
ER -