Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Kristoffer N, Jensen"'
Autor:
Benjamin J. E. Martin, Julie Brind’Amour, Anastasia Kuzmin, Kristoffer N. Jensen, Zhen Cheng Liu, Matthew Lorincz, LeAnn J. Howe
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-9 (2021)
Histone acetylation is a ubiquitous hallmark of transcription. Here the authors provide evidence that the majority of histone acetylation is dependent on transcription, specifically due to the requirement of RNAPII for the recruitment and activity of
Externí odkaz:
https://doaj.org/article/e1ac767224d040cd8a4977701af65c0d
Autor:
Aaron B. Bogutz, Julie Brind’Amour, Hisato Kobayashi, Kristoffer N. Jensen, Kazuhiko Nakabayashi, Hiroo Imai, Matthew C. Lorincz, Louis Lefebvre
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
Although many species-specific imprinted genes have been identified, how the evolutionary switch from biallelic to imprinted expression occurs is still unknown. Here authors find that lineage-specific ERVs active as oocyte promoters can induce de nov
Externí odkaz:
https://doaj.org/article/23eab72a42084803b96998d94acb4a07
Autor:
Zhen Cheng Liu, Matthew C. Lorincz, LeAnn J. Howe, Julie Brind’Amour, Anastasia Kuzmin, Kristoffer N. Jensen, Benjamin J. E. Martin
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-9 (2021)
Nature Communications
Nature Communications
Histone acetylation is a ubiquitous hallmark of transcription, but whether the link between histone acetylation and transcription is causal or consequential has not been addressed. Using immunoblot and chromatin immunoprecipitation-sequencing in S. c
Autor:
Vicki E. Maltby, Kristina L. McBurney, Julie Brind’Amour, LeAnn J. Howe, Benjamin J. E. Martin, Kristoffer N. Jensen
Publikováno v:
Genetics. 205:1113-1123
Histone post-translational modifications (PTMs) alter chromatin structure by promoting the interaction of chromatin-modifying complexes with nucleosomes. The majority of chromatin-modifying complexes contain multiple domains that preferentially inter
Autor:
Matthew C. Lorincz, Hiroo Imai, Hisato Kobayashi, Louis Lefebvre, Kazuhiko Nakabayashi, Julie Brind’Amour, Kristoffer N. Jensen, Aaron B. Bogutz
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
Nature Communications
Nature Communications
Imprinted genes are expressed from a single parental allele, with the other allele often silenced by DNA methylation (DNAme) established in the germline. While species-specific imprinted orthologues have been documented, the molecular mechanisms unde
Autor:
Matthew C. Lorincz, LeAnn J. Howe, Julie Brind’Amour, Zhen Cheng Liu, Anastasia Kuzmin, Kristoffer N. Jensen, Benjamin J. E. Martin
Histone acetylation is a ubiquitous hallmark of transcriptional activity, but whether the link is of a causal or consequential nature is still a matter of debate. In this study we resolve this question. Using both immunoblot analysis and chromatin im
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::674ad75d3d3a1a8f39be969e05f4686c
Publikováno v:
Nature. 557:640-641
A complex that includes the protein HP1 binds to specific regulatory DNA sequences to promote local compaction of genomic regions and inhibit associated genes that drive differentiation of specific cell lineages. A complex that includes the protein H
Autor:
LeAnn J. Howe, Julie Brind’Amour, Kristoffer N. Jensen, Vicki E. Maltby, Benjamin J. E. Martin, Kristina L. McBurney
Histone post-translational modifications (PTMs) alter chromatin structure by promoting the interaction of chromatin-modifying complexes with nucleosomes. The majority of chromatin-modifying complexes contain multiple domains that preferentially inter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a3d559eb1c585328dff5876e4b299d9
https://doi.org/10.1101/096511
https://doi.org/10.1101/096511
Autor:
Benjamin J E, Martin, Kristina L, McBurney, Vicki E, Maltby, Kristoffer N, Jensen, Julie, Brind'Amour, LeAnn J, Howe
Publikováno v:
Genetics. 205(3)
Histone post-translational modifications (PTMs) alter chromatin structure by promoting the interaction of chromatin-modifying complexes with nucleosomes. The majority of chromatin-modifying complexes contain multiple domains that preferentially inter