P
Patricia C. Weber
Researcher at Schering-Plough
Publications - 44
Citations - 3491
Patricia C. Weber is an academic researcher from Schering-Plough. The author has contributed to research in topics: NS3 & Protease. The author has an hindex of 20, co-authored 44 publications receiving 3419 citations. Previous affiliations of Patricia C. Weber include Duke University.
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Journal ArticleDOI
Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site
Charles A. Lesburg,Michael B. Cable,Eric Ferrari,Zhi Hong,Anthony F. Mannarino,Patricia C. Weber +5 more
TL;DR: The HCV NS5B apoenzyme structure reported here can accommodate a template:primer duplex without global conformational changes, supporting the hypothesis that this structure is essentially preserved during the reaction pathway.
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Structure of the hepatitis C virus RNA helicase domain.
Nanhua Yao,Thomas Hesson,Michael B. Cable,Zhi Hong,Ann D. Kwong,Hung V. Le,Patricia C. Weber +6 more
TL;DR: In this paper, a resolution structure of the HCV helicase from the positive-stranded RNA hepatitis C virus reveals a molecule with distinct NTPase and RNA binding domains, and the structure supports a mechanism of helicase activity involving initial recognition of the requisite 3' singlestranded region on the nucleic acid substrate by a conserved arginine-rich sequence on the RNA binding domain.
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Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation.
Thierry O. Fischmann,Alan Hruza,Xiaoda Niu,James Fossetta,Charles A. Lunn,Edward Dolphin,Andrew Prongay,Paul Reichert,Daniel Lundell,Satwant K. Narula,Patricia C. Weber +10 more
TL;DR: The high-resolution, refined structures of eNOS and iNOS reveal an unexpected structural zinc situated at the intermolecular interface and coordinated by four cysteines, two from each monomer.
Journal ArticleDOI
Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease–helicase
TL;DR: The scNS3-NS4A structure provides the first atomic view of polyprotein cis processing, and suggests autoinhibition and substrate-induced activation mechanisms for regulation of NS3 protease activity.
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Microwave-enhanced enzyme reaction for protein mapping by mass spectrometry: A new approach to protein digestion in minutes
Birendra N. Pramanik,Urooj A. Mirza,Y.H. Ing,Yan-Hui Liu,Peter L. Bartner,Patricia C. Weber,Ajay K. Bose +6 more
TL;DR: The efficacy of this technique for protein mapping was demonstrated by the mass spectral analyses of the peptide fragmentation of several biologically active proteins, including cytochrome c, ubiquitin, lysozyme, myoglobin, and interferon α‐2b.