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Sarah E. St. John

Researcher at Purdue University

Publications -  8
Citations -  898

Sarah E. St. John is an academic researcher from Purdue University. The author has contributed to research in topics: Coronavirus & Protease. The author has an hindex of 6, co-authored 8 publications receiving 640 citations.

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The SARS-coronavirus papain-like protease: structure, function and inhibition by designed antiviral compounds.

TL;DR: Targeting papain-like protease with antiviral drugs may have an advantage in not only inhibiting viral replication but also inhibiting the dysregulation of signaling cascades in infected cells that may lead to cell death in surrounding, uninfected cells.
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Ligand-induced Dimerization of Middle East Respiratory Syndrome (MERS) Coronavirus nsp5 Protease (3CLpro) IMPLICATIONS FOR nsp5 REGULATION AND THE DEVELOPMENT OF ANTIVIRALS

TL;DR: Activation of Mers-CoV 3CLpro through ligand-induced dimerization appears to be unique within the genogroup 2c and may potentially increase the complexity in the development of MERS- coV 3clpro inhibitors as antiviral agents.
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Targeting zoonotic viruses: Structure-based inhibition of the 3C-like protease from bat coronavirus HKU4--The likely reservoir host to the human coronavirus that causes Middle East Respiratory Syndrome (MERS).

TL;DR: The X-ray structures and SAR analysis reveal critical insights into the structure and inhibition of HKU4-CoV 3CLpro, providing fundamental knowledge that may be exploited in the development of anti-coronaviral therapeutics for coronaviruses emerging from zoonotic reservoirs.
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Design, synthesis, biological and structural evaluation of functionalized resveratrol analogues as inhibitors of quinone reductase 2.

TL;DR: Several novel inhibitors of QR2 were successfully identified as well as a compound that inhibits QR2 with a novel binding orientation, which may protect cells against reactive intermediates and eventually cancer.
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X-ray structure and inhibition of the feline infectious peritonitis virus 3C-like protease: Structural implications for drug design.

TL;DR: The first X-ray crystal structure of FIPV-3CLpro in complex with the best inhibitor identified is determined to better understand the structural basis for inhibitor specificity and expands the current structural knowledge of coronaviral 3CLpro architecture.