Results 11 to 20 of about 5,681,501 (240)

The Expanding Constellation of Histone Post-Translational Modifications in the Epigenetic Landscape. [PDF]

Genes (Basel), 2021
Cavalieri V.
europepmc   +2 more sources

Assessing the in vitro Binding Specificity of Histone Modification Reader Proteins Using Histone Peptide Arrays

Bio-Protocol, 2021
In the field of chromatin biology, a major goal of understanding the roles of histone post-translational modifications is to identify the proteins and domains that recognize these modifications.
Mark Soo, Arneet Saltzman
doaj   +1 more source

Histone Post-Translational Modifications and CircRNAs in Mouse and Human Spermatozoa: Potential Epigenetic Marks to Assess Human Sperm Quality. [PDF]

J Clin Med, 2020
Chioccarelli T, Pierantoni R, Manfrevola F, Porreca V, Fasano S, Chianese R, Cobellis G.   +6 more
europepmc   +2 more sources

PTMViz: a tool for analyzing and visualizing histone post translational modification data

BMC Bioinformatics, 2021
Background Histone post-translational modifications (PTMs) play an important role in our system by regulating the structure of chromatin and therefore contribute to the regulation of gene and protein expression. Irregularities in histone PTMs can lead to
Kevin Chappell, Stefan Graw, Charity L. Washam, Aaron J. Storey, Chris Bolden, Eric C. Peterson, Stephanie D. Byrum   +6 more
doaj   +1 more source

Histone modifications in neurodifferentiation of embryonic stem cells

Heliyon, 2022
Post-translational modifications of histone proteins regulate a long cascade of downstream cellular activities, including transcription and replication.
Min Huang, Xiaoxiao Xiao, Guanxu Ji, Qiang Wu   +3 more
doaj   +1 more source

Histone modifications during the life cycle of the brown alga Ectocarpus

Genome Biology, 2021
Background Brown algae evolved complex multicellularity independently of the animal and land plant lineages and are the third most developmentally complex phylogenetic group on the planet.
Simon Bourdareau, Leila Tirichine, Bérangère Lombard, Damarys Loew, Delphine Scornet, Yue Wu, Susana M. Coelho, J. Mark Cock   +7 more
doaj   +1 more source

Mitotic post-translational modifications of histones promote chromatin compaction in vitro [PDF]

Open Biology, 2017
How eukaryotic chromosomes are compacted during mitosis has been a leading question in cell biology since the nineteenth century. Non-histone proteins such as condensin complexes contribute to chromosome shaping, but appear not to be necessary for ...
Alisa Zhiteneva, Juan Jose Bonfiglio, Alexandr Makarov, Thomas Colby, Paola Vagnarelli, Eric C. Schirmer, Ivan Matic, William C. Earnshaw   +7 more
doaj   +1 more source

The function of histone methylation and acetylation regulators in GBM pathophysiology

Frontiers in Oncology, 2023
Glioblastoma (GBM) is the most common and lethal primary brain malignancy and is characterized by a high degree of intra and intertumor cellular heterogeneity, a starkly immunosuppressive tumor microenvironment, and nearly universal recurrence.
Colin McCornack, Timothy Woodiwiss, Timothy Woodiwiss, Angela Hardi, Hiroko Yano, Hiroko Yano, Albert H. Kim, Albert H. Kim   +7 more
doaj   +1 more source

Opposing functions of the Hda1 complex and histone H2B mono-ubiquitylation in regulating cryptic transcription in Saccharomyces cerevisiae

G3: Genes, Genomes, Genetics, 2021
Maintenance of chromatin structure under the disruptive force of transcription requires cooperation among numerous regulatory factors. Histone post-translational modifications can regulate nucleosome stability and influence the disassembly and reassembly
Margaret K Shirra, Rachel A Kocik, Mitchell A Ellison, Karen M Arndt   +3 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