Targeting bromodomains: epigenetic readers of lysine acetylation
P Filippakopoulos, S Knapp - Nature reviews Drug discovery, 2014 - nature.com
Lysine acetylation is a key mechanism that regulates chromatin structure; aberrant
acetylation levels have been linked to the development of several diseases. Acetyl-lysine …
acetylation levels have been linked to the development of several diseases. Acetyl-lysine …
The bromodomain: from epigenome reader to druggable target
R Sanchez, J Meslamani, MM Zhou - Biochimica et Biophysica Acta (BBA) …, 2014 - Elsevier
Lysine acetylation is a fundamental post-translational modification that plays an important
role in the control of gene transcription in chromatin in an ordered fashion. The …
role in the control of gene transcription in chromatin in an ordered fashion. The …
Dual kinase-bromodomain inhibitors for rationally designed polypharmacology
Concomitant inhibition of multiple cancer-driving kinases is an established strategy to
improve the durability of clinical responses to targeted therapies. The difficulty of discovering …
improve the durability of clinical responses to targeted therapies. The difficulty of discovering …
BET and HDAC inhibitors induce similar genes and biological effects and synergize to kill in Myc-induced murine lymphoma
J Bhadury, LM Nilsson… - Proceedings of the …, 2014 - National Acad Sciences
The bromodomain and extraterminal (BET) domain family of proteins binds to acetylated
lysines on histones and regulates gene transcription. Recently, BET inhibitors (BETi) have …
lysines on histones and regulates gene transcription. Recently, BET inhibitors (BETi) have …
Acetyl-lysine binding site of bromodomain-containing protein 4 (BRD4) interacts with diverse kinase inhibitors
Members of the bromodomain and extra terminal (BET) family of proteins are essential for
the recognition of acetylated lysine (KAc) residues in histones and have emerged as …
the recognition of acetylated lysine (KAc) residues in histones and have emerged as …
Bromodomain protein BRD4 is required for estrogen receptor-dependent enhancer activation and gene transcription
S Nagarajan, T Hossan, M Alawi, Z Najafova… - Cell reports, 2014 - cell.com
The estrogen receptor α (ERα) controls cell proliferation and tumorigenesis by recruiting
various cofactors to estrogen response elements (EREs) to control gene transcription. A …
various cofactors to estrogen response elements (EREs) to control gene transcription. A …
Cancer epigenetics drug discovery and development: the challenge of hitting the mark
RM Campbell, PJ Tummino - The Journal of clinical …, 2014 - Am Soc Clin Investig
Over the past several years, there has been rapidly expanding evidence of epigenetic
dysregulation in cancer, in which histone and DNA modification play a critical role in tumor …
dysregulation in cancer, in which histone and DNA modification play a critical role in tumor …
Affinity map of bromodomain protein 4 (BRD4) interactions with the histone H4 tail and the small molecule inhibitor JQ1
M Jung, M Philpott, S Müller, J Schulze… - Journal of biological …, 2014 - ASBMB
Bromodomain protein 4 (BRD4) is a member of the bromodomain and extra-terminal domain
(BET) protein family. It binds to acetylated histone tails via its tandem bromodomains BD1 …
(BET) protein family. It binds to acetylated histone tails via its tandem bromodomains BD1 …
Bromodomains and their pharmacological inhibitors
D Gallenkamp, KA Gelato, B Haendler… - …, 2014 - Wiley Online Library
Over 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 …
identified in humans. Several of them interact with acetylated lysine residues, leading to the …
BET bromodomain inhibitors: a patent review
JM Garnier, PP Sharp, CJ Burns - Expert opinion on therapeutic …, 2014 - Taylor & Francis
Introduction: The bromodomain (BRD) and extra-C terminal domain (BET) protein family
consists of four members (BRD2, BRD3, BRD4 and BRDT). These “epigenetic readers” bind …
consists of four members (BRD2, BRD3, BRD4 and BRDT). These “epigenetic readers” bind …