Results 31 to 40 of about 93,929 (281)

Fine mapping of posttranslational modifications of the linker histone H1 from Drosophila melanogaster. [PDF]

, 2008
The linker histone H1 binds to the DNA in between adjacent nucleosomes and contributes to chromatin organization and transcriptional control. It is known that H1 carries diverse posttranslational modifications (PTMs), including phosphorylation, lysine ...
Villar-Garea, Ana, Imhof, Axel, Axel Imhof, Ana Villar-Garea   +3 more
core   +1 more source

Apicomplexa and Histone Variants: What’s New? [PDF]

, 2019
Plasmodium spp. and Toxoplasma gondii present a conserved nucleosome composition based on canonical H3 and variants, H4, canonical H2A and variants, and H2B.
Sergio Oscar Angel, Ángel, Sergio Oscar, Laura Vanagas, Susana Marisol Contreras, Vanagas, Laura, Contreras, Susana Marisol   +5 more
core   +1 more source

Acetylated histone variant H2A.Z is involved in the activation of neo-enhancers in prostate cancer

Nature Communications, 2017
Acetylation of the histone variant H2A.Z at gene promoters is associated with oncogene activation; however, it is unclear if such modification has a role in regulating the function of enhancers.
Fátima Valdés-Mora, Cathryn M. Gould, Yolanda Colino-Sanguino, Wenjia Qu, Jenny Z. Song, Kylie M. Taylor, Fabian A. Buske, Aaron L. Statham, Shalima S. Nair, Nicola J. Armstrong, James G. Kench, Kenneth M. L. Lee, Lisa G. Horvath, Minru Qiu, Alexei Ilinykh, Nicole S. Yeo-Teh, David Gallego-Ortega, Clare Stirzaker, Susan J. Clark   +18 more
doaj   +1 more source

Acetylation of histone H3 at lysine 64 regulates nucleosome dynamics and facilitates transcription [PDF]

, 2014
Post-translational modifications of proteins have emerged as a major mechanism for regulating gene expression. However, our understanding of how histone modifications directly affect chromatin function remains limited.
Holzner, M. (M), Eleni Kallis, Holzner, M., Michaelis, J., Richter, F. (F) M. (M), Ryan, D. (D) P. (P), Feldmann, A. (A), Daniel P Ryan, Owen-Hughes, Tom; id_orcid, Kacem, S., Tropberger, Philipp, Di Cerbo, V., Bannister, A., Kallis, E. (E), Michaelis, Jens, Feldmann, A., Richter, Florian, Martin, Daujat, S. (Sylvain), Robert Schneider, Richter, F., Tropberger, P., Hoerner, Leslie, Richter, Florian Martin, Mittler, G. (G), Emilie Montellier, Di Cerbo, V. (V), Feil, Robert, Bannister, A. (A) J. (J), Vincenzo Di Cerbo, Ryan, D., Kallis, Eleni, Ryan, D. P., Di Cerbo, Vincenzo, Owen-Hughes, T. (T), Leslie Hoerner, Jens Michaelis, Kallis, E., Khochbin, S. (S), Saadi Khochbin, Schneider, Robert, Holzner, Monika, Monika Holzner, Feil, R. (R), Ryan, Daniel, P., Feldmann, Angelika, Tom Owen-Hughes, Owen-Hughes, T., Bannister, A. J., Feil, R., Mohn, F., Hoerner, L., Fabio Mohn, Richter, F. M., Montellier, E. (E), Mittler, G., Schuebeler, D., Montellier, Emilie, Mohn, F. (F), Tropberger, P. (P), Angelika Feldmann, Owen-Hughes, Tom, Kacem, Salim, Mittler, Gerhard, Daujat, Sylvain, Montellier, E., Schneider, R., Dirk Schuebeler, Schuebeler, D. (D), Bannister, Andrew J., Hoerner, L. (L), Khochbin, S., Schneider, R. (Robert), Schuebeler, Dirk, Salim Kacem, Philipp Tropberger, Mohn, Fabio, Florian Martin Richter, Kacem, S. (S), Sylvain Daujat, Ryan, Daniel P., Andrew J Bannister, Khochbin, Saadi, Gerhard Mittler, Michaelis, J. (J), Robert Feil, Daujat, S.   +85 more
core   +1 more source

Analysis of Jmjd6 cellular localization and testing for its involvement in histone demethylation. [PDF]

, 2010
Methylation of residues in histone tails is part of a network that regulates gene expression. JmjC domain containing proteins catalyze the oxidative removal of methyl groups on histone lysine residues.
Erck, C, Böttger, Angelika, Burrells Alison, Andreas Lengeling, Butler, Danica, Hahn, P., Erck, Christian, Wolf, A., Lengeling, A., Bottger, A., Jens Böse, Erck, C., Christopher J Schofield, Hahn, P, Wegener, Ivonne, Wegener Ivonne, Böse, Jens, Christian Erck, Angelika Böttger, Burrells, A, Ivonne Wegener, Butler, D, Butler Danica, Lengeling Andreas, Böse Jens, Burrells, A., Alexander Wolf, Hahn Phillip, Wolf, A, Bose, J., Lengeling, A, Erck Christian, Böttger Angelika, Danica Butler, Phillip Hahn, Butler, D., Wolf Alexander, Hahn, Phillip, Wolf, Alexander, Schofield, Christopher J, Alison Burrells, Schofield Christopher J., Böse, J, Lengeling, Andreas, Schofield, Christopher J., Wegener, I, Schofield, CJ, Wegener, I., Burrells, Alison, Schofield, Christopher, Böttger, A, Christopher J. Schofield   +51 more
core   +1 more source

The evolution and functional divergence of the histone H2B family in plants.

PLoS Genetics, 2020
Chromatin regulation of eukaryotic genomes depends on the formation of nucleosome complexes between histone proteins and DNA. Histone variants, which are diversified by sequence or expression pattern, can profoundly alter chromatin properties.
Danhua Jiang, Michael Borg, Zdravko J Lorković, Sean A Montgomery, Akihisa Osakabe, Ramesh Yelagandula, Elin Axelsson, Frédéric Berger   +7 more
doaj   +1 more source

HistoneDB 2.0: a histone database with variants—an integrated resource to explore histones and their variants [PDF]

Database, 2016
Compaction of DNA into chromatin is a characteristic feature of eukaryotic organisms. The core (H2A, H2B, H3, H4) and linker (H1) histone proteins are responsible for this compaction through the formation of nucleosomes and higher order chromatin aggregates.
Eli J. Draizen, Alexey K. Shaytan, Leonardo Mariño-Ramírez, Paul B. Talbert, David Landsman, Anna R. Panchenko   +5 more
openaire   +2 more sources

Mass spectrometry analysis of the variants of histone H3 and H4 of soybean and their post-translational modifications

BMC Plant Biology, 2009
Background Histone modifications and histone variants are of importance in many biological processes. To understand the biological functions of the global dynamics of histone modifications and histone variants in higher plants, we elucidated the variants
Lam Hon-Ming, Sun Sai-Ming, Wang Chunmei, Tsai Sau-Na, Yuan Tiezheng, Wu Tao, Ngai Sai-Ming   +6 more
doaj   +1 more source

Intrinsic elasticity of nucleosomes is encoded by histone variants and calibrated by their binding partners [PDF]

Proceedings of the National Academy of Sciences of the United States of America, 2019
Daniel P Melters, Mary Pitman, Tatini Rakshit   +2 more
exaly   +2 more sources

Systematic quantitative analysis of H2A and H2B variants by targeted proteomics

Epigenetics & Chromatin, 2018
Background Histones organize DNA into chromatin through a variety of processes. Among them, a vast diversity of histone variants can be incorporated into chromatin and finely modulate its organization and functionality.
Sara El Kennani, Annie Adrait, Olga Permiakova, Anne-Marie Hesse, Côme Ialy-Radio, Myriam Ferro, Virginie Brun, Julie Cocquet, Jérôme Govin, Delphine Pflieger   +9 more
doaj   +1 more source