Richard A. Quick
Johns Hopkins University School of Medicine
5 Papers
Richard A. Quick is an academic researcher from Johns Hopkins University School of Medicine. The author has contributed to research in topics: Nitric oxide & Nitric oxide synthase. The author has an hindex of 5, co-authored 5 publications. Previous affiliations of Richard A. Quick include Johns Hopkins University.
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Papers
The role of inducible nitric oxide synthase in the host response to Coxsackievirus myocarditis
Carlos Zaragoza,Christopher J. Ocampo,Marta Saura,Michelle K. Leppo,Xiao-Qing Wei,Richard A. Quick,Salvador Moncada,Foo Y. Liew,Charles J. Lowenstein +8 more
TL;DR: It is shown that Coxsackievirus replicates to higher titers in NOS2(-/-) mice, that the host lacking N OS2 clears virus more slowly than the wild-type host, and that myocarditis is much more severe in infected Nos2(- +/-) mice.
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Nitric Oxide Regulates Exocytosis by S-Nitrosylation of N-ethylmaleimide-Sensitive Factor
Kenji Matsushita,Craig N. Morrell,Béatrice Cambien,Shui Xiang Yang,Munekazu Yamakuchi,Clare Bao,Makoto R. Hara,Richard A. Quick,Wangsen Cao,Brian O'Rourke,John M. Lowenstein,Jonathan Pevsner,Denisa D. Wagner,Charles J. Lowenstein +13 more
TL;DR: It is shown that NO inhibits exocytosis of Weibel-Palade bodies, endothelial granules that mediate vascular inflammation and thrombosis, by regulating the activity of N-ethylmaleimide-sensitive factor (NSF).
Kalirin inhibition of inducible nitric-oxide synthase.
Edward A. Ratovitski,M. Rashidul Alam,Richard A. Quick,Audrey McMillan,Clare Bao,Chaim Kozlovsky,T. Hand,Richard C. Johnson,Richard E. Mains,Betty A. Eipper,Charles J. Lowenstein +10 more
TL;DR: Kalirin may play a neuroprotective role during inflammation of the central nervous system by inhibiting iNOS activity by preventing the formation of iN OS homodimers.
An Antiviral Mechanism of Nitric Oxide: Inhibition of a Viral Protease
Marta Saura,Carlos Zaragoza,Audrey McMillan,Richard A. Quick,Christine Hohenadl,John M. Lowenstein,Charles J. Lowenstein +6 more
TL;DR: S-nitrosylates the cysteine residue in the active site of protease 3C, inhibiting protease activity and interrupting the viral life cycle, and may be a general mechanism of antimicrobial host defenses.
An Inducible Nitric-oxide Synthase (NOS)-associated Protein Inhibits NOS Dimerization and Activity
Edward A. Ratovitski,Clare Bao,Richard A. Quick,Audrey McMillan,Chaim Kozlovsky,Charles J. Lowenstein +5 more
TL;DR: It is shown that murine macrophages express a 110-kDa protein that interacts with NOS2, which is called NOS-associated protein-110 kDa (NAP110), which directly interacts with the amino terminus of N OS2, and inhibits NOS catalytic activity by preventing formation of NOS 2 homodimers.