Zobrazeno 1 - 1
of 1
pro vyhledávání: '"Acidic-rich domain"'
Autor:
Otake, K., Ohzeki, J. I., Shono, N., Kugou, K., Okazaki, K., Nagase, T., Yamakawa, H., Kouprina, N., Larionov, V., Kimura, Hiroshi, Earnshaw, W. C., Masumoto, H.
Publikováno v:
Journal of Cell Science
article-version (VoR) Version of Record
Otake, K, Ohzeki, J, Shono, N, Kugou, K, Okazaki, K, Nagase, T, Yamakawa, H, Kouprina, N, Larionov, V, Kimura, H, Earnshaw, W C & Masumoto, H 2020, ' CENP-B creates alternative epigenetic chromatin states permissive for CENP-A or heterochromatin assembly ', Journal of Cell Science, vol. 133, jcs.243303 . https://doi.org/10.1242/jcs.243303
article-version (VoR) Version of Record
Otake, K, Ohzeki, J, Shono, N, Kugou, K, Okazaki, K, Nagase, T, Yamakawa, H, Kouprina, N, Larionov, V, Kimura, H, Earnshaw, W C & Masumoto, H 2020, ' CENP-B creates alternative epigenetic chromatin states permissive for CENP-A or heterochromatin assembly ', Journal of Cell Science, vol. 133, jcs.243303 . https://doi.org/10.1242/jcs.243303
CENP-B binds to CENP-B boxes on centromeric satellite DNAs (known as alphoid DNA in humans). CENP-B maintains kinetochore function through interactions with CENP-A nucleosomes and CENP-C. CENP-B binding to transfected alphoid DNA can induce de novo C