Writers and readers of histone acetylation: structure, mechanism, and inhibition

R Marmorstein, MM Zhou - Cold Spring Harbor …, 2014 - cshperspectives.cshlp.org
Histone acetylation marks are written by histone acetyltransferases (HATs) and read by
bromodomains (BrDs), and less commonly by other protein modules. These proteins …

[HTML][HTML] The role of human bromodomains in chromatin biology and gene transcription

R Sanchez, MM Zhou - Current opinion in drug discovery & …, 2009 - ncbi.nlm.nih.gov
The acetylation of histone lysine is central to providing the dynamic regulation of chromatin-
based gene transcription. The bromodomain (BRD), which is the conserved structural …

The Brd4 extraterminal domain confers transcription activation independent of pTEFb by recruiting multiple proteins, including NSD3

S Rahman, ME Sowa, M Ottinger, JA Smith… - … and cellular biology, 2011 - Taylor & Francis
Bromodomain protein 4 (Brd4) plays critical roles in development, cancer progression, and
virus-host pathogenesis. To gain mechanistic insight into the various biological functions of …

Bromo-and extraterminal domain chromatin regulators serve as cofactors for murine leukemia virus integration

SS Gupta, T Maetzig, GN Maertens, A Sharif… - Journal of …, 2013 - Am Soc Microbiol
Retroviral integrase (IN) proteins catalyze the permanent integration of proviral genomes
into host DNA with the help of cellular cofactors. Lens epithelium-derived growth factor …

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 …

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 …

Bromodomain and extra-terminal (BET) family proteins: New therapeutic targets in major diseases

B Padmanabhan, S Mathur, R Manjula, S Tripathi - Journal of biosciences, 2016 - Springer
The bromodomains and extra-terminal domain (BET) family proteins recognize acetylated
chromatin through their bromodomains (BDs) and help in regulating gene expression. BDs …

[HTML][HTML] Brd4 engagement from chromatin targeting to transcriptional regulation: selective contact with acetylated histone H3 and H4

CM Chiang - F1000 biology reports, 2009 - ncbi.nlm.nih.gov
Abstract Bromodomain-containing protein 4 (Brd4) contains two tandem bromodomains
(BD1 and BD2) that bind preferentially to acetylated lysine residues found in histones and …

A structural basis for BRD2/4-mediated host chromatin interaction and oligomer assembly of Kaposi sarcoma-associated herpesvirus and murine gammaherpesvirus …

J Hellert, M Weidner-Glunde, J Krausze… - PLoS …, 2013 - journals.plos.org
Kaposi sarcoma-associated herpesvirus (KSHV) establishes a lifelong latent infection and
causes several malignancies in humans. Murine herpesvirus 68 (MHV-68) is a related γ2 …

The Latency-Associated Nuclear Antigen, a Multifunctional Protein Central to Kaposi's Sarcoma-Associated Herpesvirus Latency

ME Ballestas, KM Kaye - Future microbiology, 2011 - Taylor & Francis
Latency-associated nuclear antigen (LANA) is encoded by the Kaposi's sarcoma (KS)-
associated herpesvirus (KSHV) open reading frame 73. LANA is expressed during latent …