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.
Papers
More filters
Patent
Crystalline interferon alpha for pulmonary delivery and method for producing the same
Paul Reichert,Patricia C. Weber,Rowena F. Choudrie,Bruce O. Stuart,Tattanahalli L. Nagabhushan,Ashit K. Ganguly +5 more
TL;DR: A method to prepare crystalline interferon alpha suitable for aerosol formulation either for systemic or topical (inhaled) drug delivery is described in this paper. But this method requires the use of a pre-defined medium diameter.
Patent
Single-chain recombinant complexes of hepatitis C virus NS3 protease and NS4A cofactor peptide
TL;DR: In this paper, a Covalent HCV NS4A-NS3 complexes comprising the central hydrophobic domain of a peptide, a linker, and the NS3 serine protease domain were proposed.
Patent
Treatment of trypanosoma brucei with farnesyl protein transferase inhibitors
William T. Windsor,Patricia C. Weber,Corey Strickland,Rosalinda Syto,Viyyoor M. Girijavallabhan,James J. Kaminski,Zhuyan Guo +6 more
TL;DR: In this article, the Farnesyl Protein Transferase Inhibitor alone or in combination with an additional anti- Trypanosoma Brucei agent and/or an anti-Trypanosa brucei resistance reversing agent is used.
Journal ArticleDOI
Conserved C-Terminal Threonine of Hepatitis C Virus NS3 Regulates Autoproteolysis and Prevents Product Inhibition
Wenyan Wang,Frederick C. Lahser,Min Kyung Yi,Jacquelyn Wright-Minogue,Ellen Xia,Patricia C. Weber,Stanley M. Lemon,Bruce A. Malcolm +7 more
TL;DR: In vitro transcription-translation studies suggest that the threonine is conserved at position 631 because it serves two functions: (i) to slow processing at the NS3-4A cleavage site, ensuring proper intercalation of the NS4A cofactor with NS3 prior to polyprotein scission, and (ii) to prevent subsequent product inhibition by theNS3 C terminus.
Journal Article
Recent advances in the analysis of HCV NS5B RNA-dependent RNA polymerase.
TL;DR: The crystal structure of the NS5B apoenzyme revealed a globular shape unique among polymerases, and implicated new structural features important for binding the RNA template and cognate ribonucleotide substrates.