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Schiffer, Celia
One or more keywords matched the following items that are connected to
Schiffer, Celia
Item Type
Name
Academic Article
Replacement of the P1 amino acid of human immunodeficiency virus type 1 Gag processing sites can inhibit or enhance the rate of cleavage by the viral protease.
Academic Article
Co-evolution of nelfinavir-resistant HIV-1 protease and the p1-p6 substrate.
Academic Article
Substrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes.
Academic Article
Context surrounding processing sites is crucial in determining cleavage rate of a subset of processing sites in HIV-1 Gag and Gag-Pro-Pol polyprotein precursors by viral protease.
Academic Article
Structure-based prediction of potential binding and nonbinding peptides to HIV-1 protease.
Academic Article
Mechanism of substrate recognition by drug-resistant human immunodeficiency virus type 1 protease variants revealed by a novel structural intermediate.
Academic Article
Structural analysis of human immunodeficiency virus type 1 CRF01_AE protease in complex with the substrate p1-p6.
Academic Article
Human immunodeficiency virus type 1 protease-correlated cleavage site mutations enhance inhibitor resistance.
Academic Article
Three residues in HIV-1 matrix contribute to protease inhibitor susceptibility and replication capacity.
Concept
gag Gene Products, Human Immunodeficiency Virus
Concept
Gene Products, gag
Academic Article
HIV-1 protease-substrate coevolution in nelfinavir resistance.
Academic Article
Structural basis and distal effects of Gag substrate coevolution in drug resistance to HIV-1 protease.
Academic Article
Development of a Novel Screening Strategy Designed to Discover a New Class of HIV Drugs.
Academic Article
Optimizing the refinement of merohedrally twinned P61 HIV-1 protease-inhibitor cocrystal structures.
Search Criteria
Gene Products gag