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Rochester, NY, United States

The present invention relates to the use of small molecules as anti-HIV agents that disrupt self-association of the viral infectivity factor (Vif) found in HIV and other retroviruses. The present invention also relates to methods of identifying agents that disrupt VIf self-association and methods of using these agents, including methods of treating or preventing HIV infection.


Oyagen Inc. | Entity website

Aarhus University Hospital, Denmark announces clinical trial result at the International AIDS conference in Melbourne, Australia - that HDACi induce HIV viremia but did not decrease viral reservoirs. ...


Oyagen Inc. | Entity website

Aarhus University Hospital, Denmark announces clinical trial result at the International AIDS conference in Melbourne, Australia - that HDACi induce HIV viremia but did not decrease viral reservoirs. ...


Salter J.D.,Oyagen Inc. | Morales G.A.,Cogent | Smith H.C.,Oyagen Inc. | Smith H.C.,University of Rochester
Trends in Biochemical Sciences | Year: 2014

HIV-1 viral infectivity factor (Vif) is a viral accessory protein that is required for HIV-1 infection due largely to its role in recruiting antiretroviral factors of the APOBEC3 (apolipoprotein B editing catalytic subunit-like 3) family to an E3 ubiquitin ligase complex for polyubiquitylation and proteasomal degradation. The crystal structure of the (near) full-length Vif protein in complex with Elongin (Elo)B/C, core-binding factor (CBF)β and Cullin (Cul)5 revealed that Vif has a novel structural fold. In our opinion the structural data revealed not only the protein-protein interaction sites that determine Vif stability and interaction with cellular proteins, but also motifs driving Vif homodimerization, which are essential in Vif functionality and HIV-1 infection. Vif-mediated protein-protein interactions are excellent targets for a new class of antiretroviral therapeutics to combat AIDS. © 2014 Elsevier Ltd. Source


Salter J.D.,Oyagen Inc. | Bennett R.P.,Oyagen Inc. | Smith H.C.,Oyagen Inc. | Smith H.C.,University of Rochester
Trends in Biochemical Sciences | Year: 2016

The APOBEC (apolipoprotein B mRNA editing catalytic polypeptide-like) family of proteins have diverse and important functions in human health and disease. These proteins have an intrinsic ability to bind to both RNA and single-stranded (ss) DNA. Both function and tissue-specific expression varies widely for each APOBEC protein. We are beginning to understand that the activity of APOBEC proteins is regulated through genetic alterations, changes in their transcription and mRNA processing, and through their interactions with other macromolecules in the cell. Loss of cellular control of APOBEC activities leads to DNA hypermutation and promiscuous RNA editing associated with the development of cancer or viral drug resistance, underscoring the importance of understanding how APOBEC proteins are regulated. © 2016 Elsevier Ltd Source

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