Results 171 to 180 of about 37,262 (190)
Some of the next articles are maybe not open access.
Current Opinion in Chemical Biology, 2022
Lysine acetylation creates docking sites for epigenetic reader domains of BET bromodomain proteins that have emerged as principal regulators of linage specific gene transcription. The development of potent and highly selective inhibitors, that have been soon widely available, enabled mechanistic studies in a diversity of disease models leading to a ...
Martin P. Schwalm, Stefan Knapp
openaire +2 more sources
Lysine acetylation creates docking sites for epigenetic reader domains of BET bromodomain proteins that have emerged as principal regulators of linage specific gene transcription. The development of potent and highly selective inhibitors, that have been soon widely available, enabled mechanistic studies in a diversity of disease models leading to a ...
Martin P. Schwalm, Stefan Knapp
openaire +2 more sources
Bromodomain and extraterminal domain protein bromodomain inhibitor based cancer therapeutics
Current Opinion in Oncology, 2021Purpose of review Bromodomain and extraterminal domain (BET) proteins are evolutionarily conserved, multifunctional super-regulators that specifically recognize acetyl-lysine on histones and other proteins controlling gene transcription.
Tithi Ghosh, Halder +2 more
openaire +2 more sources
Bromodomain inhibitors and therapeutic applications
Current Opinion in Chemical Biology, 2023The bromodomain acts to recognize acetylated lysine in histones and transcription proteins and plays a fundamental role in chromatin-based cellular processes including gene transcription and chromatin remodeling. Many bromodomain proteins, particularly the bromodomain and extra terminal domain (BET) protein BRD4 have been implicated in cancers and ...
Bharath Kumar Gajjela, Ming-Ming Zhou
openaire +2 more sources
Bromodomain inhibitors revisited
Science, 2020Drug Discovery Bromodomain and extraterminal domain (BET) proteins contribute to the pathogenesis of cancer and immune diseases through their effects on transcriptional regulation. BET proteins contain two nearly identical bromodomains, BD1 and BD2, structural modules that have attracted great interest as targets for drug development.
openaire +1 more source
Bromodomain motifs and scaffolding
Frontiers in Bioscience, 2001Bromodomain-containing multiprotein complexes share some of the properties of signal transduction scaffolds. Insights from MAP kinase signaling scaffolds, for example, may provide useful perspectives for future studies of bromodomain proteins. The regulatory processes of modification (phosphorylation, acetylation, ubiquitination), turnover, nuclear ...
openaire +2 more sources
Bromodomains and Their Pharmacological Inhibitors
ChemMedChem, 2014AbstractOver 60 bromodomains belonging to proteins with very different functions have been identified in humans. Several of them interact with acetylated lysine residues, leading to the recruitment and stabilization of protein complexes. The bromodomain and extra‐terminal domain (BET) proteins contain tandem bromodomains which bind to acetylated ...
Daniel, Gallenkamp +3 more
openaire +2 more sources
BET bromodomain inhibitors in leukemia
Experimental Hematology, 2015The last few years have seen the identification of bromodomain and extraterminal (BET) proteins as critical mediators of transcription with effects on its direct control and cisregulation. This discovery is important in furthering our understanding of the mechanisms of normal transcriptional control. Subsequent work has shed light on the multiple roles
Faisal, Basheer, Brian J P, Huntly
openaire +2 more sources
Bromodomain Histone Readers and Cancer
Journal of Molecular Biology, 2017Lysine acetylation of histone proteins is a fundamental post-translational modification that regulates chromatin structure and plays an important role in gene transcription. Aberrant levels of histone lysine acetylation are associated with the development of several diseases.
Abhinav K, Jain, Michelle C, Barton
openaire +2 more sources