Correction to Small Molecule Inhibitors of Bromodomain–Acetyl-lysine Interactions

Brand, Michael; Measures, Angelina R; Wilson, Bryan; Cortopassi, Wilian A.; Alexander, Rikki; Höss, Matthias; Hewings, David S.; Rooney, Timothy P. C.; Paton, Robert S.; Conway, Stuart J.

doi:10.1021/acschembio.5b01065

Cited by 2 publications

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“…Bromodomain and extraterminal domain (BET) family proteins function as the “epigenetic readers” that recognize and bind to the acetylated lysine residues (AcK) of histones and other nonhistone acetylated proteins in the epigenetic mechanism. , BET proteins are comprised of four isoforms (BRD2, BRD3, BRD4, and BRDT), and each isoform contains two highly conserved homologous bromodomains (BD1 and BD2). , BRD2, BRD3, and BRD4 are ubiquitously expressed in human cells and tissues, while BRDT is primarily expressed in testis . The BET family proteins, especially BRD4, have attracted extensive research attention and emerged as one of the most studied protein families following the exploration of their roles in multiple diseases and the discovery of selective BET inhibitors. , …”

Section: Introductionmentioning

confidence: 99%

Synthesis and Characterization of a Positron Emission Tomography Imaging Probe Selectively Targeting the Second Bromodomain of Bromodomain Protein BRD4

et al. 2021

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Two tandem bromodomains (BD1 and BD2) of bromodomain and extraterminal domain (BET) family proteins have shown distinct roles in mediating gene transcription and expression. Inhibitors that interact with a specific bromodomain may contribute to a specific therapeutic potential with fewer side effects. However, little is known about this disease-related target. Positron emission tomography (PET) imaging could allow us to achieve in-depth knowledge of the BD2 bromodomain. Herein we describe the radiosynthesis and evaluation of [ 11 C]1 as a BRD4 BD2 bromodomain PET imaging radioligand. Our preliminary PET imaging results in rodents demonstrated that [ 11 C]1 had suitable biodistribution in peripheral organs and tissues. Further blocking studies indicated that [ 11 C]1 had good binding specificity toward the BD2 bromodomain. This study may pave the way for the development of a PET radioligand specifically targeting BD1/2 bromodomains as well as for the biological mechanism investigation of BD1/2 bromodomains.

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Section: Introductionmentioning

confidence: 99%

Synthesis and Characterization of a Positron Emission Tomography Imaging Probe Selectively Targeting the Second Bromodomain of Bromodomain Protein BRD4

et al. 2021

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“…2,3 There are four subtypes of BET proteins, including BRD2, BRD3, BRD4, and BRDT, and each of them contains BD1 and BD2 bromodomains. 4,5 In mammals, BRD2, BRD3, and BRD4 are widely expressed in cells and tissues, while BRDT is mainly found in the testis. 6 Due to their essential role in epigenetic regulation, BET family proteins have been regarded as promising therapeutic targets for a variety of diseases, such as oncology, inflammation, and infectious diseases.…”

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confidence: 99%

A positron emission tomography imaging probe selectively targeting the BD1 bromodomain and extra-terminal domain

et al. 2022

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Correction to Small Molecule Inhibitors of Bromodomain–Acetyl-lysine Interactions

Cited by 2 publications

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Synthesis and Characterization of a Positron Emission Tomography Imaging Probe Selectively Targeting the Second Bromodomain of Bromodomain Protein BRD4

Synthesis and Characterization of a Positron Emission Tomography Imaging Probe Selectively Targeting the Second Bromodomain of Bromodomain Protein BRD4

A positron emission tomography imaging probe selectively targeting the BD1 bromodomain and extra-terminal domain

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