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Byrareddy S.N on Muck Rack

Byrareddy S.N

As seen in: Cell Press, Cell Reports, Cell Reports Physical Science, The Lancet, The Journal of the American Dental Association, The Journal of Biological Chemistry, European Urology, The Journal of Hospital Infection, Archives of Physical Medicine and Rehabilitation, International Journal of Infectious Disease and
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Articles

A short sequence in the tail of SARS-CoV-2 envelope protein controls accessibility of its PDZ Binding Motif to the cytoplasm.

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By Byrareddy S.N, Florence Larrous
| The Journal of Biological Chemistry Verified
Abstract The carboxy terminal tail of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) envelope protein (E) contains a PDZ-binding motif (PBM) which is crucial for coronavirus pathogenicity. During SARS-CoV-2 infection, the viral E protein is expressed within the Golgi apparatus membrane of host cells with its PBM facing the cytoplasm. In this work we study the molecular mechanisms controlling the presentation of the PBM to host PDZ (PSD-95/Dlg/ZO-1) domain-containing proteins.
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AKT Signaling Modulates Latent Viral Reservoir Viability in HIV-1-Infected Blood-Brain Barrier Pericytes

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By Byrareddy S.N, Silvia Torices, Paul Clifford
| The Journal of Biological Chemistry Verified
ABSTRACT Despite antiretroviral therapy (ART), chronic forms of HIV-associated neurocognitive disorders (HAND) affect an estimated 50% of individuals living with HIV, greatly impacting their quality of life. The prevailing theory of HAND progression posits that chronic inflammation arising from the activation of latent viral reservoirs leads to progressive damage in the central nervous system (CNS).
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mRNA display reveals a class of high-affinity bromodomain-binding motifs that are not found in the human proteome

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By Byrareddy S.N, Jason Low, Natasha Jones, Paul Solomon
| The Journal of Biological Chemistry Verified
ABSTRACT Bromodomains regulate gene expression by recognizing protein motifs containing acetyllysine. Although originally characterized as histone-binding proteins, it has since become clear that these domains interact with other acetylated proteins, perhaps most prominently transcription factors. The likely transient nature and low stoichiometry of such modifications, however, has made it challenging to fully define the interactome of any given bromodomain.
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