Great find.

Further to that - here is the article and it lists RVX-208 (see page 16).

Also...

https://www.biorxiv.org/content/10.1101/2020.03.22.002386v2.full.pdf

The article is 44 pages so I will not even try to duplicate it here. But here are a few tidbits, with apologies if someone has already posted this.  It has a long list of authors - including:

David E. Gordon1,2,3,4, Gwendolyn M. Jang1,2,3,4, Mehdi Bouhaddou1,2,3,4, Jiewei Xu1,2,3,4, Kirsten Obernier1,2,3,4,... Nevan J. Krogan1,2,3,4

A SARS-CoV-2-Human Protein-Protein Interaction Map Reveals Drug Targets and Potential Drug-Repurposing

Abstract:

An outbreak of the novel coronavirus SARS-CoV-2, the causative agent of COVID-19 respiratory disease, has infected over 290,000 people since the end of 2019, killed over 12,000, and caused worldwide social and economic disruption1,2. There are currently no antiviral drugs with proven efficacy nor are there vaccines for its prevention. Unfortunately, the scientific community has little knowledge of the molecular details of SARS-CoV-2 infection. To illuminate this, we cloned, tagged and expressed 26 of the 29 viral proteins in human cells and identified the human proteins physically associated with each using affinity-purification mass spectrometry (AP-MS), which identified 332 high confidence SARS-CoV-2-human protein-protein interactions (PPIs). Among these, we identify 67 druggable human proteins or host factors targeted by 69 existing FDA-approved drugs, drugs in clinical trials and/or preclinical compounds, that we are currently evaluating for efficacy in live SARS-CoV-2 infection assays. The identification of host dependency factors mediating virus infection may provide key insights into effective molecular targets for developing broadly acting antiviral therapeutics against SARS-CoV-2 and other deadly coronavirus strains

Exceprt: SARS-CoV-2 envelope interacts with bromodomain proteins

Surprisingly, we find that the transmembrane protein E binds to the bromodomain-containing proteins BRD2 and BRD4 (Fig. 4d, Extended Data Fig. 9), potentially disrupting BRD-histone binding by mimicking histone structure. BRD2 is a member of the bromodomain and extra-terminal (BET) domain family whose members bind acetylated histones to regulate gene transcription69. The N-terminus of histone 2A shares local sequence similarity over an alpha-helix of approximately 15 residues, some of which are in a transmembranesegment, of Protein E (Fig. 4d). Moreover, this matching region of the histone is spanned by acetylated lysine residues shown to bind BRD270. This analysis may suggest that Protein E mimics the histone to disrupt its interaction with BRD2, thus inducing changes in host's protein expression that are beneficial to the virus.For a more comprehensive overview of the virus-host interactions we detected, see Supplemental Discussion.

Also find RVX-208 listed on page 16 and in the supplemental information and diagrams on pages 41-44.